diff --git a/public/404.html b/public/404.html
index b0b62588368fce70e123c9a706023a2501fba1ce..802eb5328dbbc0224f38de55e5ebf9b62e0007ef 100644
--- a/public/404.html
+++ b/public/404.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -105,6 +105,12 @@
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/LICENSE.html b/public/LICENSE.html
index 49262c271f9148167b743ca40e0078841b8828e6..30b49152aadc84479e1f33921f32b39484155c11 100644
--- a/public/LICENSE.html
+++ b/public/LICENSE.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item expanded "><a href="LICENSE.html" class="active">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item expanded "><a href="LICENSE.html" class="active">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -440,6 +440,12 @@ licenses.</p>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/attributions.html b/public/attributions.html
index 126a7b872805bbe06590b0d2b5c74a221d90bc52..49620d1a097853019dcb5df55e08c1d60226e894 100644
--- a/public/attributions.html
+++ b/public/attributions.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item expanded "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item expanded "><a href="attributions.html" class="active">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item expanded "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item expanded "><a href="attributions.html" class="active">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -99,11 +99,14 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="attributions"><a class="header" href="#attributions">Attributions</a></h1>
+<div class="h1-bg">
+ <h1 class>Attributions</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/attributions-bg.png" />
+</div>
<h2 id="biology-team"><a class="header" href="#biology-team">Biology team</a></h2>
<h3 id="yixuan-wu-lisa"><a class="header" href="#yixuan-wu-lisa">Yixuan Wu (Lisa)</a></h3>
<p>Biology Team leader.
-In charge of wet lab organization and human practice organizations.
+In charge of wet lab organization, human practice organizations and wiki construction.
Designed the overall topic and approach of the problem to tackle
with synthetic biology design. Designer of E.coli csgA surface display
and lab experiments of the E.<em>coli</em> group.</p>
@@ -116,7 +119,7 @@ Also assisted in Wiki writing and expert interview.</p>
writing.
Hosted journal clubs and science lectures for human practice.</p>
<h3 id="zhujun-yao"><a class="header" href="#zhujun-yao">Zhujun Yao</a></h3>
-<p>Designed lactococcus lab procedures and in charge of lactococcus and yeast lab experiments.
+<p>Designed <em>Lactococcus</em> lab procedures and in charge of <em>Lactococcus</em> and yeast lab experiments.
Conducted expert interviews for human practice.</p>
<h3 id="chang-shen"><a class="header" href="#chang-shen">Chang Shen</a></h3>
<p>Proposed the project topic, participated in plasmid design and workflow design
@@ -178,11 +181,11 @@ Modelled growth of chosen microbe model computationally.</p>
<h3 id="jiani-chen"><a class="header" href="#jiani-chen">Jiani Chen</a></h3>
<p>Oversee wet lab experiments and overall project advising.</p>
<h3 id="yang-yu"><a class="header" href="#yang-yu">Yang Yu</a></h3>
-<p>Oversee wet lab experiments, helped optimize lab protocols and troubleshooting. </p>
+<p>Oversee wet lab experiments, helped optimize lab protocols and troubleshooting.</p>
<h2 id="funding-support"><a class="header" href="#funding-support">Funding support</a></h2>
-<p>Thanks to the generous funding support of
-Duke Kunshan University Natural Science Divisions,
-Wang-Cai Biochemistry Lab,
+<p>Thanks to the generous funding support of
+Duke Kunshan University Natural Science Divisions,
+Wang-Cai Biochemistry Lab,
Synear Food Molecular Biology Lab,
DKU Innovation and Entrepreneurship Initiative,
and Marcia B. France, DKU Dean of Undergraduate Studies.
@@ -190,14 +193,20 @@ Thanks to free licenses provided by SnapGene.</p>
<h2 id="communications-support"><a class="header" href="#communications-support">Communications support</a></h2>
<p>Thanks to Dr. Floyd
Beckford and Dr. Huansheng Cao at Duke Kunshan University,
-Dr. Neel Joshi from Northwestern University,
-and Dr. Jisheng Lin at Sinovac Biotech CO.,LTD. for providing effective advice on
+Dr. Neel Joshi from Northwestern University,
+and Dr. Jisheng Lin at Sinovac Biotech CO.,LTD. for providing effective advice on
our project design and development.</p>
</main>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/book.js b/public/book.js
index 0bb78c9842ed2f98301f693af7c4418f1d40ef76..823be3a0784b937df3ed3d53804f9c36f82ace04 100644
--- a/public/book.js
+++ b/public/book.js
@@ -99,8 +99,8 @@ const create_ambient = async () => {
x[_] += x_speed[_];
y[_] += y_speed[_];
r[_] += r_speed[_];
- image.style.left = (Math.floor(x[_]) % window.innerWidth) + "px";
- image.style.top = (Math.floor(y[_]) % window.innerHeight) + "px";
+ image.style.left = (x[_] % window.innerWidth) + "px";
+ image.style.top = (y[_] % window.innerHeight) + "px";
image.style.transform = `rotate(${r[_]}deg)`;
}
setTimeout(update_ambient, 30);
@@ -108,33 +108,78 @@ const create_ambient = async () => {
update_ambient();
};
-const rotate_home_logo = async () => {
+const snap_home_articles = () => {
+ let snapping = false;
+ let current_scroll = window.scrollY;
+ let scroll_up = true;
+ const articles = document.querySelectorAll(
+ "main > article, #promotion_video"
+ );
+ const first_article = articles[0];
+ const last_article = articles[articles.length - 1];
+ const window_middle = () => window.innerHeight / 2 + window.scrollY;
+ const article_middle = (article) =>
+ article.offsetHeight / 2 + article.offsetTop;
+ const scroll_to = (article) =>
+ window.scrollTo(0, article_middle(article) - window.innerHeight / 2);
+ const snap = () => {
+ scroll_up = window.scrollY < current_scroll;
+ current_scroll = window.scrollY;
+ if (snapping) {
+ return;
+ }
+ snapping = true;
+ if (
+ window_middle() <= article_middle(first_article) ||
+ window_middle() >= article_middle(last_article)
+ ) {
+ return;
+ }
+ let index = 0;
+ let article = last_article;
+ for (; index < articles.length; index++) {
+ const relative_y =
+ article_middle(articles[index]) - window_middle();
+ if (relative_y >= 0) {
+ article = scroll_up ? articles[index - 1] : articles[index];
+ break;
+ }
+ }
+ scroll_to(article);
+ };
+ const not_snapping = () => (snapping = false);
+ return [snap, not_snapping];
+};
+
+const rotate_home_logo = () => {
const logo = document.getElementById("home_logo");
if (logo === null) {
- return;
+ return () => 0;
}
- create_ambient();
let timer = null;
let old_offset = window.scrollY;
const rotate = (offset) => (logo.style.transform = `rotate(${offset}deg)`);
+ const [snap, not_snapping] = snap_home_articles();
const reset_rotation = () => {
rotate(0);
old_offset = window.scrollY;
+ not_snapping();
};
const apply_rotation = async () => {
if (timer !== null) {
clearTimeout(timer);
}
+ snap();
rotate(window.scrollY - old_offset);
timer = setTimeout(reset_rotation, 100);
};
- window.addEventListener("scroll", apply_rotation);
+ return apply_rotation;
};
const add_toc = () => {
const h2s = document.querySelectorAll("h2");
if (h2s.length < 2) {
- return;
+ return () => 0;
}
const current_page_candidates = document.querySelectorAll(
".chapter li.chapter-item.expanded"
@@ -167,15 +212,12 @@ const add_toc = () => {
const toc_li = document.createElement("li");
toc_li.append(toc_ol);
current_page.after(toc_li);
- let highlight_scheduled = false;
- let highlight_active = false;
- const highlight_current_h2 = () => {
- highlight_scheduled = false;
+ const highlight_current_h2 = async () => {
let found_current_h2 = false;
let last_passed_toc = null;
for (const [h2, toc] of h2_w_toc) {
if (!found_current_h2) {
- if (window.scrollY > h2.offsetTop) {
+ if (window.innerHeight / 3 + window.scrollY > h2.offsetTop) {
last_passed_toc = toc;
} else {
found_current_h2 = true;
@@ -190,21 +232,8 @@ const add_toc = () => {
// The last h2 is the one to highlight
last_passed_toc.classList.add("expanded");
}
- if (highlight_scheduled) {
- schedule_highlight();
- } else {
- highlight_active = false;
- }
- };
- const schedule_highlight = async () => {
- if (highlight_active) {
- highlight_scheduled = true;
- } else {
- highlight_active = true;
- setTimeout(highlight_current_h2, 200);
- }
};
- window.addEventListener("scroll", schedule_highlight);
+ return highlight_current_h2;
};
const hide_loading = () => {
@@ -214,6 +243,57 @@ const hide_loading = () => {
main_loading.style.display = "none";
};
+const fade_in = () => {
+ let text_blocks = [];
+ for (const block of document.querySelectorAll("main > *")) {
+ if (block.style?.opacity !== undefined) {
+ text_blocks.push(block);
+ }
+ }
+ const set_all_opacity = async () => {
+ for (const block of text_blocks) {
+ if (
+ window.scrollY <= block.offsetTop + block.offsetHeight &&
+ window.scrollY + window.innerHeight >= block.offsetTop
+ ) {
+ block.style.opacity = 1;
+ } else {
+ block.style.opacity = 0;
+ }
+ }
+ };
+ return set_all_opacity;
+};
+
+const scrolling_effect = () => {
+ let active = false;
+ let scheduled = false;
+ const rotate_logo = rotate_home_logo();
+ const update_toc = add_toc();
+ const fade = fade_in();
+ fade();
+ const apply = () => {
+ scheduled = false;
+ update_toc();
+ rotate_logo();
+ fade();
+ if (scheduled) {
+ setTimeout(apply, 50);
+ } else {
+ active = false;
+ }
+ };
+ const schedule = () => {
+ if (active) {
+ scheduled = true;
+ } else {
+ active = true;
+ setTimeout(apply, 50);
+ }
+ };
+ window.addEventListener("scroll", schedule);
+};
+
const load = () => {
sidebar_aria();
codeSnippets();
@@ -223,9 +303,9 @@ const load = () => {
clipboard();
scrollToTop();
controllMenu();
- rotate_home_logo();
- add_toc();
+ create_ambient();
hide_loading();
+ scrolling_effect();
};
window.addEventListener("load", load);
diff --git a/public/collaborations.html b/public/collaborations.html
index 157c85e24e79a472baf1e94525b176436ad5a898..fd3420525278db2971bcfa80c0dcf5ce18cb9a0e 100644
--- a/public/collaborations.html
+++ b/public/collaborations.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item expanded "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item expanded "><a href="collaborations.html" class="active">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item expanded "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item expanded "><a href="collaborations.html" class="active">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -99,13 +99,37 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="collaborations"><a class="header" href="#collaborations">Collaborations</a></h1>
-<p>We collaborated with LZU, another iGEM team focusing on probiotics, on education. We found that there are many misleading claims about probiotics and their effects in the market, so we planned to conduct science promotion in local areas to improve people's understanding of probiotics. We chose a local international university to give a lecture on science popularization, and more than 300 middle and high school students and teachers attended.</p>
+<div class="h1-bg">
+ <h1 class>Collaborations</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/collab-title.jpg" />
+</div>
+<h2 id="collaboration-with-duke-igem"><a class="header" href="#collaboration-with-duke-igem">Collaboration with Duke iGEM</a></h2>
+<p>Duke-DKU iGEM History
+Duke Kunshan University (DKU) is our sister school in Kunshan, China. Like Duke, DKU set out to provide a transformative and innovative education to students around the world. In addition, students are given the opportunity to study abroad in both semesters, further cementing our status as sister schools. Since taking its inaugural class of undergraduate students in 2018, DKU only had its very first iGEM team. Duke, on the other hand, has competed in the competition ever since 2006. Thus, when we learned about their interest in iGEM, we were beyond happy and excited to build a strong partnership between our teams.</p>
+<p>Our Partnership
+Since DKU iGEM only started in 2021, we continued to look to Duke iGEM for support and guidance. This year, we are still able to meet on the Duke campus and give each other suggestions. We shared the trouble shooting processes of our wet labs and reached mutual agreement to construct a PCR trouble shooting guide for future iGEM teams to use. </p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/dku-duke-group0.jpeg" alt="dku-duke-group0" /></p>
+<h2 id="ccic-meetup"><a class="header" href="#ccic-meetup">CCiC Meetup</a></h2>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/dkucciccertificate.jpg" alt="CCiC certificate" /></p>
+<p>In order to carry out science communications on a larger scale, we participated
+the 9th CCiC Conference (Conference of China iGEMer Community), which is a
+national summit independently initiated by Chinese iGEM teams, aiming to
+provide a platform for iGEM teams to share resources and promote mutual
+learning and communication. We made poster and presented at the conference,
+answering questions from the audience and judges. After the conference, we
+collaborated with team LZU on science popularization about probiotics.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/ccic-meeting.png" alt="CCiC photo" /></p>
</main>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/communication.html b/public/communication.html
index 2745dbc1ea2b243ddd6bc5af9d19563aaceff132..ae008a4105d379252e7da4ec5a044e18c0deb9bd 100644
--- a/public/communication.html
+++ b/public/communication.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html" class="active">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item expanded "><a href="communication.html" class="active">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html" class="active">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item expanded "><a href="communication.html" class="active">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -99,13 +99,18 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="communication"><a class="header" href="#communication">Communication</a></h1>
+<div class="h1-bg">
+ <h1 class>Communications</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/communi-bg.jpg" />
+</div>
<h2 id="overview"><a class="header" href="#overview">Overview</a></h2>
-<p>We had science communications during different stages of our project. We
-designed these communications to have different manner, audience and scope,
-aiming at informing, educating, raising awareness of the topic of
-Gastrointestinal health, and increasing the sense of wonder about fighting
-against antibiotic resistance.</p>
+<p>We had science communications during different stages of our project.
+Firstly, we designed a socially-oriented questionnaire to find out how much the
+public knows about shigella.
+Then,throughout expert interviews, we managed to gain insights of our project feasibility
+and possible future directions. Finally,
+we participated in on-campus communication to let more people know about shigella
+and surface display technology.</p>
<h2 id="socially-oriented-questionnaire"><a class="header" href="#socially-oriented-questionnaire">Socially-Oriented Questionnaire</a></h2>
<p>Before the experiment, we designed and published a questionnaire about
antibiotic treatment and dysentery on social network platform, and obtained
@@ -115,51 +120,259 @@ dysentery, do not know how it is transmitted or the bacteria that causes it.
This makes us realize the importance of science popularization. Meanwhile,
people have different levels of concern about antibiotic resistance, which
means it is necessary for us to focus on antibiotic therapy replacement.</p>
-<!-- todo: add pic of questionnaire -->
+<p><img src="https://static.igem.wiki/teams/4161/wiki/fig-wenjuan.png"
+/></p>
+<h2 id="interview-with-prof-cao"><a class="header" href="#interview-with-prof-cao">Interview with Prof. Cao</a></h2>
+<p>We interviewed Huansheng Cao,
+Assistant professor of Environmental Science at Duke Kunshan University
+for suggestions on our initial lab plans.</p>
+<p>In the interview, team members Yuxin Wang and Chang Shen presented
+the main design, bacterial surface display, to consult Prof Cao on its feasibility.
+After confirming the rich research foundations of our plan, he encouraged us to add computational elements
+to our lab design.</p>
+<p>As a scientist working in computational biology and bioinformatics, he
+pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody
+and the antigen unit. As a well-trained
+biologist, he also suggested fitting our design to more than one model
+organisms, which shows integration in our drug design.</p>
+<p>The interview was full of enthusiasm, so we were able to come across many other topics.
+We discussed the trends in bioinformatics and biotechnology, including bacteria-based
+bioelectricity, and the relationship between human longevity and gut microbiota.</p>
+<p>This interview was both encouraging and informative, and contributed
+greatly to the first stage of human practice.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/prof-cao-interview1.jpg"
+/></p>
+<h2 id="interview-with-prof-beckford"><a class="header" href="#interview-with-prof-beckford">Interview with Prof. Beckford</a></h2>
+<p>After we successfully predicted the 3d structure of fusion protein-antibody
+complex by using Robetta and Alphafold2, the focus shift to how the fusion
+protein will influence the binding (docking) between antibody and antigen. We
+plan to get some insights about this from computer modeling before the wet lab
+begins.</p>
+<p>We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University
+for suggestions on our protein docking simulation.</p>
+<p>At the beginning, team leader Lisa Wu introduced the synthetic biology part of
+our project. Modeling team leader Zhenyu Xu introduced the progress of protein
+structure prediction and the need for protein docking simulation.</p>
+<p>As a scientist working in modern medicine, Prof. Floyd pointed us to some
+useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These
+software are powerful at predicting the docking scenario and are used by many
+researchers, with many online teaching resources accessible.</p>
+<p>To improve the speed of computer modeling, Prof. Floyd emphasized the
+preprocessing of protein structures. Namely, the antigen structure. He
+suggested us delete the floating molecules outside the binding sites and keep
+those inside, since we only care about the binding scenario. He also pointed
+that virtual screening could help if we want to do more mutations to the
+binding sites. Concerning the fusion protein-antibody complex models, since
+they are the optimal prediction given by Robetta and Alphafold2, we assume
+these models do not need preprocessing anymore.</p>
+<p>For docking, he suggested us try rigid docking first, and then flexible docking
+if we want to get closer to reality.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/fig-floyd.jpg"
+/></p>
+<h2 id="interview-with-dr-neel-joshi"><a class="header" href="#interview-with-dr-neel-joshi">Interview with Dr. Neel Joshi</a></h2>
+<p><strong>Introduction</strong></p>
+<p>Dr. Neel Joshi is an expert in bioengineering
+with tracks in human disease and new therapies.
+In his 2019 and 2021 literature,
+he and his team described genetically engineering <em>E. coli</em> Nissle 1917
+to treat some gastrointestinal diseases like bowel inflammation,
+which provide essential references for our project.
+To further understand the logics and advantages of this bioengineered model,
+we invited Dr. Joshi for an interview.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/dr-joshi-interview1.png" alt="Dr. Joshi interview photo 1" /></p>
+<p><strong>Interview Content</strong></p>
+<p><strong>Q:</strong>
+What stimulated you and your team to develop
+the surface-displaced single domain antibodies?
+What practical problems do you think this model can solve?</p>
+<p><strong>A:</strong>
+Although the nanobodies have great potentials in treating gastrointestinal diseases,
+it is somewhat hard to deliver those nanobodies directly to the digestive track.
+Therefore,
+the probiotics can serve as a scaffold to make the delivery of nanobodies easy.</p>
+<p><strong>Q:</strong>
+But why did you choose to display the nanobodies on the surface?
+Why not directly make the bacteria synthesize nanobodies and release them?</p>
+<p><strong>A:</strong>
+The surface display resolution has the property of multi-valency.
+By displaying the nanobodies on the surface,
+we would have the potential to space the binding domains together
+to bind to a pathogen surface.
+It could increase binding affinity and decrease the dissociation constant.
+It can also diffusion into different directions and increase the local concentration.</p>
+<p><strong>Q:</strong>
+What about the method of drug delivery?
+That is to say,
+how do you decide to send the engineered probiotics to human gastrointestinal track?
+And could you explain why you use that delivery method?</p>
+<p><strong>A:</strong>
+We only proposed an approach of micro biological therapy.
+But to deliver the bacteria,
+I think it can be freeze-dried to produce a freeze-dried product.
+Because a large portion of the geographical locations
+that suffered from these gut problems are the poor areas,
+and those areas do not have the condition
+to store the bacteria that require a very low temperature.
+The freeze-dried products do not require that strict storage conditions,
+so they are more available in those areas.</p>
+<p><strong>Q:</strong>
+Why pBbB8k plasmid backbone with kanamycin selection marker?
+(what's the difference between pUC19,
+which is our choice,
+and pBbB8K?)</p>
+<p><strong>A:</strong>
+pBbB8k is a rather arbitrary choice,
+we simply chose it
+because it was used due to antibiotics incompatibility in the previous experiment.
+When doing in vivo studies,
+we engineered plasmids from the original <em>E. coli</em> Nissle genome,
+the pMUT plasmids.
+These plasmids are more stable than the pBbB8K.
+For pUC19,
+I don’t see problems with the expression of pUC19 plasmid.
+However,
+you do need to consider if your antibiotic resistant marker
+in the plasmid is compatible with the shigella testing.
+If shigella is killed due to the antibiotic selecting E. coli,
+it can be a problem.</p>
+<p><strong>Q:</strong>
+What are the setbacks of
+the Probiotic-associated therapeutic curli hybrids (PATCH) system?</p>
+<p><strong>A:</strong>
+The first is safety concerns of curli fibers.
+It has been known that curli fibers induce various types of diseases,
+including neurological diseases,
+etc.
+The other is inherit disadvantages for <em>E. coli</em> to produce curli fibers in vivo.
+However,
+we have been able to shown effective production of curli fiber in vivo
+by measuring the amount of curli fibers coming from the fecal samples.</p>
+<p><strong>Q:</strong>
+What if the <em>E. coli</em> went out of control and grow infinitely in the gut,
+disrupting the original gastrointestinal microorganism environment?</p>
+<p><strong>A:</strong>
+This is a very popular question when it comes to distributing microbes to gut.
+Actually,
+we could use some of the auxotrophic strains to limit the growth of the bacteria.
+And I think there are many “switchesâ€
+that can turn on the suicide program of those bacteria.
+But in this case,
+I think <em>E. coli</em> Nissle 1917 is a very safe bacteria,
+it has already been identified as a harmless bacterium,
+so there should be less safety issues of this strain.</p>
+<p><strong>Q&A Section</strong></p>
+<p><strong>Q:</strong>
+Is it possible to apply magnetic triggers to shigella infection
+and cooperate this into the PATCH system?</p>
+<p><strong>A:</strong>
+Magnetic triggers are mostly applied in cancer treatment.
+This is because in cancer,
+you know the spot of the disease.
+In bacterial infection it’s hard to locate.</p>
+<p><strong>Q:</strong>
+In Barta et al.,
+the authors described the different indexes of the nanobodies,
+including binding domains and neutralization effects.
+What is your rationale when choosing the nanobodies?</p>
+<p><strong>A:</strong>
+It really depends on how you generate the nanobodies.
+When different parts of the pathogen are used in Alpaca immunizations,
+the nanobodies will vary.
+When displaying the nanobodies,
+some work and others don’t.
+We assume this is because of folding problems,
+but we did not figure out the exact reason.</p>
+<p><strong>Q:</strong>
+What do you think about sequence optimization in silica?
+Do you have experience working with this?
+Do you have any suggestions?</p>
+<p><strong>A:</strong>
+I would suggest generating different mutations in the sequence
+and do some docking analysis.
+Then generate the mutations and do wet labs.</p>
+<p><strong>Q:</strong>
+Our project aims to tackle the antibiotic resistance problem worldwide.
+Would the PATCH system generate drug resistance issues?</p>
+<p><strong>A:</strong>
+This is possible.
+For example,
+a mutation in the binding domain of the antigen might cause binding problems.
+However,
+I would say the selective pressure by the nanobody is smaller
+compared to that of the antibiotic.
+This is because antibiotic kills the pathogen,
+while PATCH only binds to the pathogen,
+keeping it from invasive activities.</p>
+<p><strong>Q:</strong>
+We are worried
+that the proteins in the GI tract environment would coat the surface of the probiotic,
+which would cause dysfunction of the nanobodies.
+How did your team encounter this problem?</p>
+<p><strong>A:</strong>
+The animal model was effective,
+which was sufficient to show
+that the GI tract environment did not inhibit the binding activity.
+The curli production is continuous in vivo,
+which provides adequate chance for the binding to occur.
+However,
+the proteases in the GI tract is something to consider.</p>
+<p><strong>Summary and Reflection</strong></p>
+<p>Dr. Joshi provided lots of perspectives from a brand-new aspect,
+which were extra inspirable for the whole team.
+First,
+Dr. Joshi elaborated on the practical problems
+that this model could potentially resolve.
+That the probiotic expression system could
+make the delivery of nanobodies easier expanded our understanding of
+the model as the delivery problem does not only exist in the step of bacteria delivery,
+it starts from the delivery of the essential nanobodies.</p>
+<p>Next,
+the freeze-dry delivery approach gives
+a less stricter storage condition of this drug,
+making it more available in poor areas,
+which corresponds with our assumed delivery method.
+As for the safety problem that the public is most interested in,
+Dr. Joshi proposed to use some molecular switches
+to eliminate those bacteria in addition to using safe strains like Nissle,
+giving important clue and indication for our project design.</p>
+<p>In the Q&A section,
+questions regarding drug localization,
+drug resistance,
+choice of nanobodies were mentioned by team members.
+Dr. Joshi gave many valuable advices depending on the questions.
+Overall,
+the interview was successful,
+and we were able to arm ourselves with adequate knowledge for the wet lab.</p>
+<h3 id="interview-with-sinovac"><a class="header" href="#interview-with-sinovac">Interview with SINOVAC</a></h3>
+<p><a href="entrepreneurship.html">See Entrepreneurship.</a></p>
<h2 id="on-campus-communication"><a class="header" href="#on-campus-communication">On-Campus Communication</a></h2>
<p>As an undergraduate team, we participated in the 2022's College Student
Innovation and Entrepreneurship Training Program—a national training program
for college students on innovation and entrepreneurship. In this way, we can
better promote the topic of synthetic biology to the DKU community and attract
more fresh blood to participate in innovation. We made posters and participated
-in project exhibitions, and were regularly inspected by the jury on campus. In
-addition, we have established a journal club, where different members of the
-team introduce cutting-edge knowledge about synthetic biology every two weeks,
-and we are happy to see many freshmen participating.</p>
-<!-- todo: add pic of poster, journal club, club expo -->
-<h2 id="ccic-igem-community-in-china"><a class="header" href="#ccic-igem-community-in-china">CCiC: iGEM community in China</a></h2>
-<p>In order to carry out science communications on a larger scale, we participated
-the 9th CCiC Conference (Conference of China iGEMer Community), which is a
-national summit independently initiated by Chinese iGEM teams, aiming to
-provide a platform for iGEM teams to share resources and promote mutual
-learning and communication. We made poster and presented at the conference,
-answering questions from the audience and judges. After the conference, we
-collaborated with team LZU on science popularization about probiotics.</p>
-<!-- todo: add pic of meeting and video -->
-<h2 id="local-school-education"><a class="header" href="#local-school-education">Local School Education</a></h2>
-<p>In the later stage of the experiment, in order to better promote the knowledge
-of synthetic biology and gastrointestinal health in the local area, we
-contacted a local international high school and successfully delivered popular
-science lectures to more than 330 middle and high school students and
-teachers.We distributed science manuals to everyone in the audience and
-introduced the GI tract, dysentery, probiotic therapy, and antibiotic
-resistance.</p>
-<!-- todo: add pic of manual and meeting -->
+in project exhibitions, and were regularly inspected by the jury on campus.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/fig-on-campus-communication.png"
+/></p>
<h2 id="summary"><a class="header" href="#summary">Summary</a></h2>
<p>Throughout the project, we never stopped science communication with different
groups. The social questionnaire allowed us to identify the need for the
program; the school publicity has attracted a batch of fresh blood to join the
-research and innovation of synthetic biology; the communication and cooperation
-with other Chinese IGEM teams enabled us to learn more knowledge, and also to
-understand the current issues of synthetic biology in China that deserve
-attention. The science popularization and education in local schools also gave
-us the opportunity to communicate with middle and high school students,
-understand their ideas and answer their doubts.</p>
+research and innovation of synthetic biology; the expert interviews enabled us to
+reflect on the feasibility and future directions of our lab design.
+These science communication helped us be more clear about the direction of the experiment
+and the significance of this project.</p>
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diff --git a/public/contribution.html b/public/contribution.html
index 63e9a58fe54b262db4cf946bb0e03de99ad5ed6c..75881d691d4160715568314fb8b8e24fb999c7ef 100644
--- a/public/contribution.html
+++ b/public/contribution.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item expanded "><a href="contribution.html" class="active">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item expanded "><a href="contribution.html" class="active">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
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<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
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@@ -99,7 +99,10 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h2 id="contribution"><a class="header" href="#contribution">Contribution</a></h2>
+<div class="h1-bg">
+ <h1 class>Contribution</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/contri-bg.jpg" />
+</div>
<p>We designed cell surface display platforms for probiotics including yeast,
E.<em>coli</em> Nissle 1917, and L.<em>lactis</em>. To be specific, the yeast Aga2 surface
display platform for nanobodies were developed, We also designed a novel way
@@ -107,7 +110,8 @@ to detect protein surface expression by using flow cytometry. Another
contribution is protein modeling protocol. We designed an integrated protocol
involving the usage of PyMol, RobeTTA, and Alphafold2. Through literature
review, we were able to determine multiple parameters that measure the accuracy
-of the protein model, and conducted evaluation on our protein design.</p>
+of the protein model, and conducted evaluation on our protein design. We also contributed
+to previous parts by designing our parts with imporvement based on past iGEM teams.</p>
<h3 id="cell-surface-display-platforms"><a class="header" href="#cell-surface-display-platforms">Cell surface display platforms</a></h3>
<p>Cell surface display platforms can be utilized to cater to many protein
engineering and therapeutic drug design purposes. In our case, the therapeutic
@@ -122,12 +126,20 @@ to model the structures of our protein, and used HADDOCK to visualize the
docking structure. Evaluation focuses on different parameters: Ramachandran
plot, Overall G-factors, Atomic Z-score RMS, Percentage of the amino acids
having scored >= 0.2 in the 3D/1D profile, Overall quality factor, and Z-score.
-These parameters determine whether a certain structure is stable.</p>
+These parameters determine whether a certain structure is stable. More details please see our <a href="model.html">Modeling Page</a></p>
+<h3 id="improvement-of-parts"><a class="header" href="#improvement-of-parts">Improvement of parts</a></h3>
+<p><a href="improve.html">See Improvement</a></p>
</main>
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+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
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diff --git a/public/description.html b/public/description.html
index 3780a6267fb7aa2bf015dd4ec54aef4322905dff..09f52276f72b886cde6c64389e4b520f61dcfadf 100644
--- a/public/description.html
+++ b/public/description.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
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-<h2 id="project-description"><a class="header" href="#project-description">Project Description</a></h2>
-<p>The Shigella species is listed as one of the eight dangerous drug resistant bacteria<sup class="footnote-reference"><a href="#CDC,2019">1</a></sup>, with associated mortalities projected to rise to 10 million globally by 2050. The use of conventional antibiotics aggravates the multidrug resistance of most Shigella strains. Besides aiding in the selection of resistant pathogens, antibiotics reduce intestinal species diversity and population, and disrupt the defensive, metabolic, and trophic functions of interdependent microbes <sup class="footnote-reference"><a href="#Francino,2016">2</a></sup>. Engineered probiotics with cell surface display systems are promising in tackling this problem due to a weaker selective pressure and specific binding proteins that are less likely to disrupt the host gut microbiome. Through literature review, E.<em>coli</em> Nissle 1917, yeast and L.<em>lactis</em> are chosen for expression because their probiotic nature present no known harm to the GI tract and the convenience in lab culturing.</p>
-<div class="footnote-definition" id="CDC,2019"><sup class="footnote-definition-label">1</sup>
-<p>Centers for Disease Control and Prevention. (2019). 2019 AR
-Threats Report. <a href="https://www.cdc.gov/drugresistance/biggest-threats.html">https://www.cdc.gov/drugresistance/biggest-threats.html</a></p>
-</div>
-<div class="footnote-definition" id="Francino,2016"><sup class="footnote-definition-label">2</sup>
-<p>Francino, M. P. (2016, January 1). Antibiotics and the human
-gut microbiome: Dysbioses and accumulation of resistances. Frontiers. Retrieved
-March 28, 2022, from
-<a href="https://www.frontiersin.org/articles/10.3389/fmicb.2015.01543/full">https://www.frontiersin.org/articles/10.3389/fmicb.2015.01543/full</a></p>
+<div class="h1-bg">
+ <h1 class>Project Description</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/wetlab9-for-bg.png" />
</div>
+<h2 id="background"><a class="header" href="#background">Background</a></h2>
+<p>The Shigella species is listed as one of the eight dangerous drug resistant bacteria<sup class="footnote-reference"><a href="#Langdon2016">1</a></sup>, with associated mortalities projected to rise to 10 million globally by 2050, if not properly addressed<sup class="footnote-reference"><a href="#ONeill2014">2</a></sup>.
+In the United States alone, over 77,000 antibiotic resistant cases were reported annually and 90% of overall Shigella cases were found to be resistant to the first choice medication ciprofloxacin<sup class="footnote-reference"><a href="#CDC2015">3</a></sup>.
+Shigella, as a highly infective, enteroinvasive and occasionally toxin-releasing<sup class="footnote-reference"><a href="#Carayol2013">4</a></sup> <sup class="footnote-reference"><a href="#Gray2015">5</a></sup>
+bacterial genus, may cause severe infection and bacterial dysentery in the colorectal mucosa even with as low a dose as 10 - 100 organisms<sup class="footnote-reference"><a href="#Garcia2014">6</a></sup>.
+Shigella-related infections thereby spread rapidly, particularly in low-resource populations<sup class="footnote-reference"><a href="#Hussen2019">7</a></sup> and among vulnerable groups including children in care facilities, the homeless, and returned travelers<sup class="footnote-reference"><a href="#CDC2020">8</a></sup> <sup class="footnote-reference"><a href="#Huruy2018">9</a></sup> <sup class="footnote-reference"><a href="#Casabonne2016">10</a></sup> <sup class="footnote-reference"><a href="#Gray2015">5</a></sup>.</p>
+<p>The use of conventional antibiotics aggravates the multidrug resistance of most Shigella strains. Besides aiding in the selection of resistant pathogens, antibiotics reduce intestinal species diversity and population, and disrupt the defensive, metabolic, and trophic functions of interdependent microbes <sup class="footnote-reference"><a href="#Francino2016">11</a></sup>.
+Although antibiotics are able to prevent and treat infections, antibiotic exposure to the intestinal microbiota can lead to loss of colonization resistance, rendering the host more susceptible to future invasion<sup class="footnote-reference"><a href="#Kim2017">12</a></sup> <sup class="footnote-reference"><a href="#Shad2021">13</a></sup>.</p>
+<p>Engineered probiotics with cell surface display systems are an especially promising alternative that improve Shigella eradication rates without heavy reliance on antibiotics.
+Single VH domain (VHH) antibodies displayed on the probiotic surface reduce virulent activity of Shigella<sup class="footnote-reference"><a href="#Roehrich2013">14</a></sup> through probiotic-pathogen binding while minimizing toxicity to non-targets<sup class="footnote-reference"><a href="#Barta2017">15</a></sup> <sup class="footnote-reference"><a href="#Tremblay2013">16</a></sup>. Specifically, these antibodies recognize and target epitopes within the tip complex that is conserved across all pathogens that utilize type III secretion system (T3SS) to translocate effector proteins into the host cells<sup class="footnote-reference"><a href="#Barta2017">15</a></sup>.
+Innovations in VHH-ipaD binding not only offer a solution that preserves the potency of antibiotics and microbial composition of the gut microbiome, but also illuminates targeted approaches to treat related T3SS bacteria like Salmonella and enterohemorrhagic E. coli, and other novel opportunities for passive immunization<sup class="footnote-reference"><a href="#Greve2019">17</a></sup>.</p>
+<p>Engineered probiotics with cell surface display systems are an especially promising alternative that improve Shigella eradication rates without heavy reliance on antibiotics. Single VH domain (VHH) antibodies displayed on the probiotic surface reduce virulent activity of Shigella<sup class="footnote-reference"><a href="#Roehrich2013">14</a></sup> through probiotic-pathogen binding while minimizing toxicity to non-targets<sup class="footnote-reference"><a href="#Barta2017">15</a></sup> <sup class="footnote-reference"><a href="#Tremblay2013">16</a></sup>. Specifically, these antibodies recognize and target epitopes within the tip complex that is conserved across all pathogens that utilize type III secretion system (T3SS) to translocate effector proteins into the host cells<sup class="footnote-reference"><a href="#Barta2017">15</a></sup>. Innovations in VHH-ipaD binding not only offer a solution that preserves the potency of antibiotics and microbial composition of the gut microbiome, but also illuminates targeted approaches to treat related T3SS bacteria like Salmonella and enterohemorrhagic E. coli, and other novel opportunities for passive immunization<sup class="footnote-reference"><a href="#Greve2019">17</a></sup>.</p>
+<h2 id="design"><a class="header" href="#design">Design</a></h2>
+<h3 id="yeast"><a class="header" href="#yeast">Yeast</a></h3>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-design.png" alt="Y_Design" /></p>
+<h4 id="idea-of-probiotics"><a class="header" href="#idea-of-probiotics">Idea of probiotics</a></h4>
+<p>Saccharomyces cerevisiae, or baker’s yeast, is widely used in food industry and scientific research.
+Its facultative anaerobic feature enables it to make fluffy bread<sup class="footnote-reference"><a href="#Sicard2011">18</a></sup>.
+Also, its variable metabolism pathways make it a good agent for alcohol fermentation and wine production<sup class="footnote-reference"><a href="#Holt2019">19</a></sup>.
+Last but not least, the already-annotated genome makes it an excellent model organism for molecular biology research<sup class="footnote-reference"><a href="#Piskur2004">20</a></sup>.
+With all these features, yeasts have been considered to be safe by Food and Drug Administration for a long time.
+Apart from our treatment strategy, this probiotic has been engineered as new conceptual drugs for other diseases treatment, such as vaginal infections, diarrhea, and irritable bowel syndrome (IBS)<sup class="footnote-reference"><a href="#Gaziano2020">21</a></sup> <sup class="footnote-reference"><a href="#Palma2015">22</a></sup>.
+Compared to other prokaryotic probiotics, the eukaryotic yeast could support more complex protein folding, which is favorable for the generation of antibodies of interest.
+Moreover, previous works have successfully developed a mature Aga proteins yeast surface display system, which have been put in practical use in vaccine selection and sorting<sup class="footnote-reference"><a href="#Boder1997">23</a></sup> <sup class="footnote-reference"><a href="#Chao2006">24</a></sup>.
+This established surface display system largely reduces the engineering difficulty and increases the reliability of our engineering.
+Take all the considerations above, we put yeasts into our plan list.</p>
+<h4 id="design-of-pyd1-20ipad-plasmid-for-therapeutic-yeast-engineering"><a class="header" href="#design-of-pyd1-20ipad-plasmid-for-therapeutic-yeast-engineering">Design of pYD1-20ipaD plasmid for therapeutic yeast engineering</a></h4>
+<p>One of the most important proteins in type III secretion system (T3SS) of pathogenic Shigella called ipaD is our attack target<sup class="footnote-reference"><a href="#Wagner2020">25</a></sup>.
+Because ipaD is the primary trigger to form translocon pores within the host cell membrane, the inhibition of it would probably inhibit the invasion of Shigella and thus treat the infection<sup class="footnote-reference"><a href="#Dickenson2011">26</a></sup> <sup class="footnote-reference"><a href="#Epler2009">27</a></sup>.
+Several single domain antibodies (nanobodies) have been previously reported to target ipaD, the most efficient of which is 20ipaD.
+Therefore, 20ipaD was chosen for further engineering.
+To have the yeasts displayed 20ipaD on surface, we adopted the strategy of Aga2 yeast surface display system.
+Aga2 is a membrane protein of S. cerevisiae, which would be sealed on membrane by the interaction with Aga16.
+By fusing the Aga2 protein with 20ipaD, the nanobody could thus be brought to the membrane, and that was what we designed as shown in the figure.
+Additionally, we introduced 3xFLAG tag behind 20ipaD for expression assays like immunofluorescent microscopic imaging, western blot, and FACS.
+The whole expression module was designed under the control of GAL1 promotor that can be induced by galactose to control the expression of the proteins of interest.
+We used pYD1 vector as the backbone which contains ampicillin resistance marker, <em>E. coli</em> replication origin, and tryptophan deficiency marker.
+These features enable us to store the recombinant plasmids in E. coli, and easily select the yeasts after transformation.</p>
+<h4 id="design-of-pyd1-ipad-plasmid-for-efficiency-detection"><a class="header" href="#design-of-pyd1-ipad-plasmid-for-efficiency-detection">Design of pYD1-ipaD plasmid for efficiency detection</a></h4>
+<p>Shigella is one of the most infectious pathogens characterized by CDC<sup class="footnote-reference"><a href="#CDC2020">8</a></sup>.
+Considering the health risks that could be risen during the experiments, we replace the real Shigella by yeasts anchored with the targeted epitope protein ipaD.
+The construction strategy of pYD1-ipaD was same as the pYD1-20ipaD discussed above except for the replacement of FLAG tag with HA tag.
+The yeasts containing pYD1-ipaD could display the antigen ipaD on their surfaces to mimic Shigella.
+With this pathogen analog, the binding affinity of the engineered therapeutic yeasts between the fake pathogens could be measured by whole cell ELISA and other binding affinity assays.</p>
+<h4 id="design-of-high-production-and-high-binding-affinity-plasmids-for-efficiency-optimization"><a class="header" href="#design-of-high-production-and-high-binding-affinity-plasmids-for-efficiency-optimization">Design of high production and high binding affinity plasmids for efficiency optimization</a></h4>
+<p>After the proving the construction and binding capacity of the engineered yeast, optimization would be done to increase the efficiency of the product.
+Expression efficiency and binding affinity would be the two main aspects of optimization.
+To increase the expression efficiency of the nanobody, previously reported strong promoters, including SSA1 and PGK1, would be introduced to replace GAL1 promoter<sup class="footnote-reference"><a href="#Peng2015">28</a></sup>.
+The expression abundancy would be compared, and the optimized promoter would be chosen.
+To increase the binding affinity of the nanobody, random mutations would be introduced to the 20ipaD sequence by error-prone PCR.
+The library would be screened for the optimization of nanobody targeting.</p>
+<h4 id="design-of-delivery-of-the-engineered-therapeutic-yeasts-by-shellac-based-microcapsules"><a class="header" href="#design-of-delivery-of-the-engineered-therapeutic-yeasts-by-shellac-based-microcapsules">Design of delivery of the engineered therapeutic yeasts by Shellac-based microcapsules</a></h4>
+<p>Microbes, especially yeasts, are hard to preserve for a long time under room temperature.
+Besides, the acidic and digestive environment inside the gut prevents most organisms from getting to the intestine where Shigella locates in.
+In order to preserve the engineered yeasts and deliver them into the intestine with smallest deficiency, we designed the shellac-cased microcapsules.
+Shellac is a natural material that can be used as encapsulating material for microcapsules that can wrap and package molecular matters like drugs and cells<sup class="footnote-reference"><a href="#Huang2020">29</a></sup>.
+The properties of shellac include high intensity, which can protect the encapsuled matters; hydrophobicity, making it easier for storage; only disintegrate at basic solution, which means that the microcapsules would not disintegrate in the acidic environment of stomach, but only dissolve in basic environment of small intestine where the target pathogen resides<sup class="footnote-reference"><a href="#Huang2019">30</a></sup>.
+Previous research has proven the efficiency of shellac microcapsules delivery of probiotics<sup class="footnote-reference"><a href="#Mei2018">31</a></sup> <sup class="footnote-reference"><a href="#Gately2017">32</a></sup> <sup class="footnote-reference"><a href="#Hamad2013">33</a></sup>.
+With the light of this, we also designed the capsulation for the engineered yeasts.
+By producing the microcapsule powder of yeasts, they can be subsequently packaged into macro capsule entities and be productized.</p>
+<h3 id="lactococcus"><a class="header" href="#lactococcus">Lactococcus</a></h3>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/l-design.png" alt="L_Design" /></p>
+<h4 id="idea-of-probiotics-1"><a class="header" href="#idea-of-probiotics-1">Idea of probiotics</a></h4>
+<p>The target probiotics, <em>Lactococcus lactis (L. lactis)</em>, is a lactic acid-producing Gram-positive species of bacteria that is used extensively in the food fermentation industry like the production of cheese and yoghurt.
+Therefore, it is generally considered as safe (GRAS) status by the Food and Drug Administration<sup class="footnote-reference"><a href="#Song2017">34</a></sup>.
+Apart from its important function in making food, <em>L. lactis</em> is often applied as the genetically modified organism for disease treatment of animals and humans<sup class="footnote-reference"><a href="#Braat2006">35</a></sup> <sup class="footnote-reference"><a href="#Moreno2016">36</a></sup>.
+In many parts, it acts as an alternative for the gram positive to Bacillus subtilis and Lactobacillus plantarum, while it can also substitute the gram-negative counterpart, Escherichia coli[GarcÃa2012]. The small genome size (2.3 Mbp) that has been fully sequenced, plus the development of successfully compatible tools including cloning and expression systems with customizable options, have turned _L. lactis_into a desirable model for genetic engineering<sup class="footnote-reference"><a href="#Song2017">34</a></sup>.</p>
+<h4 id="design-of-20ipad-plasmid"><a class="header" href="#design-of-20ipad-plasmid">Design of 20ipad plasmid</a></h4>
+<p>Due to the wide use of antibiotics, various types of bacteria have developed antibiotic resistance, thus providing great challenge to human health and therapy design.
+Our team’s target pathogen, the Shigella spp., is no exception.
+To overcome the issue of antibiotic resistance, we would like to engineer the probiotics to make it an effective tool for the treatment of shigella infections.
+Through literature review, it is identified that in the process of shigellosis (also named bacillary dysentery), Shigella uses the type III secretion system (T3SS) to invade colonic epithelial cells.
+Importantly, one important feature of T3SS is the existence of an extracellular needle with an associated tip complex responsible for assembly of a pore-forming translocon in the host cell membrane<sup class="footnote-reference"><a href="#Barta2017">15</a></sup>.
+For Shigella flexneri, the tip complex contains invasion plasmid antigen D (IpaD) that not only regulates secretion but also provides the physical platform for the translocon pore<sup class="footnote-reference"><a href="#Barta2017">15</a></sup> <sup class="footnote-reference"><a href="#Muthuramalingam2021">37</a></sup>.
+To explore the potential therapeutic avenues for managing infections of Shigella, researchers have developed single-VH domain antibodies (VHHs) that are capable of recognizing distinct epitopes within the antigen IpaD<sup class="footnote-reference"><a href="#Barta2017">15</a></sup>, where one of such VHHs is the 20ipaD applied by our team.
+In order to have our probiotics <em>L. lactis</em> express the 20ipaD, we firstly constructed the 20ipaD plasmid.
+For plasmid design, the Usp45 signal peptide was included for secretion to the growth medium, while AcmA3b was included for surface anchoring of the expressed 20ipaD to <em>L. lactis</em><sup class="footnote-reference"><a href="#Plavec2019">38</a></sup>.
+Flag-tag was added for the convenience of purification.
+Sequence of 20ipaD was surrounded by two restriction sites (BamHI and SacI respectively).
+The aim for such a design is that ideally, through the digestion of restriction enzymes, 20ipaD sequence could be obtained.</p>
+<h4 id="design-of-control-group-3flag-tag-with-flag-tag-sequence"><a class="header" href="#design-of-control-group-3flag-tag-with-flag-tag-sequence">Design of control group (3*Flag tag) with Flag-tag sequence</a></h4>
+<p>In our future stage, we would fuse the <em>Lactococcus lactis</em> expression vector pNZ8148 with control flag-tag<em>3 to benefit the examination procedures, here the plasmid containing control group (3</em>Flag tag) with Flag-tag sequence was designed so that we could get the sequence of control flag-tag<em>3 from the plasmid.
+Construction of the plasmid was similar to that of 20ipaD, with Usp45 signal peptide (indicated in yellow) and AcmA3b (indicated in green) included.
+The sequence of control flag-tag</em>3 is shown in blue. Two restriction sites for the enzyme NcoI (indicated in dark green) and HindIII (indicated in dark blue) were designed so that during enzymatic digestion, sequence of control flag-tag*3 would be obtained.</p>
+<h3 id="e-coli"><a class="header" href="#e-coli">E. coli</a></h3>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/e-design.png" alt="E_design" /></p>
+<p><em>E. coli</em> Nissle 1917, as a probiotic first isolated from the GI tract of healthy soldiers in WWI, has been proven to impose positive impacts on the human GI tract by supression and inhibition of GI tract pathogens.
+The current trend in developing Nissle for therapeutics is based on the fact that <em>E. coli</em> is one of the most developed model organisms for scientific research.
+It has a small genome, stability of expression, and is easy to culture.</p>
+<p>The detailed design of the <em>E. coli</em> surface display system is as follows. Through literature review, We have targeted two different display systems.
+One is based on <em>E. coli</em> curli operon.
+The curli fiber is a component of biofilm.
+The PATCH system developed form previous studies have been effective in displaying protiens of interest.
+Furthermore, the large capacity of the curli fiber presents multivalency, making it possible to display multiple proteins at arbitrarily close distance to bind simultaneously for the drug effective to take place.
+The plasmid design referenced the pM1s3ATScsg-Etag plasmid on Addgene (Plasmid #137946) from Neel Joshi Lab with the optimized synthetic curli operon.
+The other option is based on intimin.
+Intimin in <em>E. coli</em> has a trans-outer membrane region and a C-terminal repeat of Ig-like and lectin domains that can be used as a potential fusion site for protein display<sup class="footnote-reference"><a href="#Sadana2017">39</a></sup>.
+In some earlier studies, the researchers successfully inserted a fragment of EHEC intimin into a known plasmid vector with a VHH fusing to it and had it successfully express and display the VHH on the bacteria surface<sup class="footnote-reference"><a href="#Salema2013">40</a></sup>.
+To fully exploit the multivalency advantage of the baterial surface display system, we plan to display more than on kind of nanobodies, so the probiotic can bind to a larger range of pathogens, or it can bind different antigens of the pathogen.
+It is also important to mention that the target antigen IpaD is highly conservative and exists in all strains of shigella.
+Also, previous studies have constructed a library of anti-IpaD VHH including VHH 20ipaD, JMKH2, and JPSG3 are found specifically bind to the epitopes in IpaD protein<sup class="footnote-reference"><a href="#Barta2017">15</a></sup> <sup class="footnote-reference"><a href="#Sierocki2017">41</a></sup>. The affinity of this antigen-VHH pair is considerable when using 20ipaD and JMKH2<sup class="footnote-reference"><a href="#Sierocki2017">41</a></sup>.</p>
+<h2 id="references"><a class="header" href="#references">References</a></h2>
+<p><sup class="footnote-reference"><a href="#Carayol2013">4</a></sup> Carayol, N. and Guy Nhieu. (2013). The Inside Story of Shigella Invasion of Intestinal Epithelial Cells. Cold Spring Harbor Perspectives in Medicine. Retrieved March 28, 2022, from <a href="http://perspectivesinmedicine.cshlp.org/content/3/10/a016717.full">http://perspectivesinmedicine.cshlp.org/content/3/10/a016717.full</a></p>
+<p><sup class="footnote-reference"><a href="#Garcia2014">6</a></sup> Zaidi, M. B., & Estrada-GarcÃa, T. (2014, June 1). shigella: A highly virulent and elusive pathogen. Current tropical medicine reports. Retrieved March 28, 2022, from <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4126259/">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4126259/</a></p>
+<p><sup class="footnote-reference"><a href="#ONeill2014">2</a></sup> O' Neill, J. (2014, December). Antimicrobial resistance: Tackling a crisis for the health and wealth of nations . Retrieved March 28, 2022, from <a href="https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf">https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf</a></p>
+<p><sup class="footnote-reference"><a href="#Langdon2016">1</a></sup> Langdon, A., Crook, N., & Dantas, G. (2016). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome Medicine, 8(1). <a href="https://doi.org/10.1186/s13073-016-0294-z">https://doi.org/10.1186/s13073-016-0294-z</a></p>
+<p><sup class="footnote-reference"><a href="#CDC2015">3</a></sup> Centers for Disease Control and Prevention. (2015, April 2). Multidrug-resistant shigellosis spreading in the United States.</p>
+<p><sup class="footnote-reference"><a href="#CDC2020">8</a></sup> Centers for Disease Control and Prevention. (2020, October 8). Antibiotic resistance and Shigella infections. Centers for Disease Control and Prevention. Retrieved March 28, 2022, from <a href="https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html">https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html</a></p>
+<p><sup class="footnote-reference"><a href="#Hussen2019">7</a></sup> Hussen, S., Mulatu, G., & Yohannes Kassa, Z. (2019). Prevalence of shigella species and its drug resistance pattern in Ethiopia: A systematic review and meta-analysis. Annals of Clinical Microbiology and Antimicrobials, 18(1). <a href="https://doi.org/10.1186/s12941-019-0321-1">https://doi.org/10.1186/s12941-019-0321-1</a></p>
+<p><sup class="footnote-reference"><a href="#Gray2015">5</a></sup> Gray, M. D., Lacher, D. W., Leonard, S. R., Abbott, J., Zhao, S., Lampel, K. A., Prothery, E., Gouali, M., Weill, F.-X., & Maurelli, A. T. (2015, May 14). Prevalence of shiga toxin-producing Shigella species isolated from French travellers returning from the Caribbean: An emerging pathogen with international implications. Clinical Microbiology and Infection. Retrieved March 28, 2022, from <a href="https://www.sciencedirect.com/science/article/pii/S1198743X15004437">https://www.sciencedirect.com/science/article/pii/S1198743X15004437</a></p>
+<p><sup class="footnote-reference"><a href="#Huruy2008">42</a></sup> Huruy, K., Kassu, A., Mulu, A., Gebretsadik, S., Andargie, G., Tadesse, T., Birhan, W., Worku, N., Ghebreselassie, D., Belyhun, Y., Yifru, S., Adugna, S., & Tiruneh, M. (2008). High Level of Antimicrobial Resistance in Shigella Species Isolated From Diarrhoeal Patients in University of Gondar Teaching Hospital, Gondar, Ethiopia . Retrieved March 28, 2022, from <a href="https://pharmacologyonline.silae.it/files/archives/2008/vol2/29_Huruy.pdf">https://pharmacologyonline.silae.it/files/archives/2008/vol2/29_Huruy.pdf</a></p>
+<p><sup class="footnote-reference"><a href="#Casabonne2016">10</a></sup> Casabonne, C., González, A., Aquili, V., & Balagué, C. (2016, November 22). Prevalence and virulence genes of Shigella spp.. isolated from patients with diarrhea in Rosario, Argentina. Japanese Journal of Infectious Diseases. Retrieved March 28, 2022, from <a href="https://www.jstage.jst.go.jp/article/yoken/69/6/69_JJID.2015.459/_article/-char/ja/">https://www.jstage.jst.go.jp/article/yoken/69/6/69_JJID.2015.459/_article/-char/ja/</a>
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+<p><sup class="footnote-reference"><a href="#ONeill2014">2</a></sup> O' Neill, J. (2014, December). Antimicrobial resistance: Tackling a crisis for the health and wealth of nations . Retrieved March 28, 2022, from <a href="https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf">https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf</a></p>
+<p><sup class="footnote-reference"><a href="#CDC2015">3</a></sup> Centers for Disease Control and Prevention. (2015, April 2). Multidrug-resistant shigellosis spreading in the United States.</p>
+<p><sup class="footnote-reference"><a href="#CDC2020">8</a></sup> Centers for Disease Control and Prevention. (2020, October 8). Antibiotic resistance and Shigella infections. Centers for Disease Control and Prevention. Retrieved March 28, 2022, from <a href="https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html">https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html</a></p>
+<p><sup class="footnote-reference"><a href="#Hussen2019">7</a></sup> Hussen, S., Mulatu, G., & Yohannes Kassa, Z. (2019). Prevalence of shigella species and its drug resistance pattern in Ethiopia: A systematic review and meta-analysis. Annals of Clinical Microbiology and Antimicrobials, 18(1). <a href="https://doi.org/10.1186/s12941-019-0321-1">https://doi.org/10.1186/s12941-019-0321-1</a></p>
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+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item expanded "><a href="education.html" class="active">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item expanded "><a href="education.html" class="active">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
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<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
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@@ -99,8 +99,27 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="education"><a class="header" href="#education">Education</a></h1>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/education1.jpg" alt="photo" /></p>
+<div class="h1-bg">
+ <h1 class>Education</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/education1.jpg" />
+</div>
+<p><strong>Overview:</strong></p>
+<p>We conduct popular science education both on and off campus.</p>
+<ul>
+<li>
+<p>On campus, we have established a journal club, where different members of the
+team introduce cutting-edge knowledge about synthetic biology every two weeks,
+and we are happy to see many freshmen participating. We also cohosted a Biology Seminar Series,
+inviting Prof. Dong Hyun Jo, from Seoul National University College of Medicine
+to give a talk on therapeutic revolution for the DKU community.</p>
+</li>
+<li>
+<p>Off campus, we contacted a local international high school and successfully delivered popular science lectures
+to more than 330 middle and high school students and teachers about our project
+and synthetic biology.</p>
+</li>
+</ul>
+<h3 id="off-campus-education"><a class="header" href="#off-campus-education">Off campus education</a></h3>
<p>Although iGEM competition has a solid audience base in <strong>universities</strong>,
students in high schools have little knowledge of iGEM competition or give up
because of their limitation of conducting wetlabs. There is an increasing trend
@@ -114,25 +133,61 @@ presentation. <strong>In the introduction of iGEM</strong>, we introduced biolog
modelling team, wiki team and human practice team, including their
responsibility and collaborations between different subgroups.</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/education3.jpg" alt="photo" /></p>
-<p><strong>In GI tract</strong>, we introduced the process of digesting. Functions of each
+<p><strong>For GI tract</strong>, we introduced the process of digesting. Functions of each
human organ and different intestinal floras were explained in detail. Along
with knowledge, we provided two fun facts——“Mom passes gut microbiota to
baby†and “Having stomachache and diarrhea before examsâ€. Besides GI
tract, we also mentioned the harm that using antibiotics can do to
gastrointestinal tract.</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/education4.jpg" alt="photo" /></p>
-<p><strong>In probiotics</strong>, we popularized basic knowledge of probiotics, pointed out
+<p><strong>For probiotics</strong>, we popularized basic knowledge of probiotics, pointed out
issues that taking probiotics improperly will lead to and give our advice.
After the speech, 330 high school students and teachers had a better
understanding of choosing probiotic products. Students and teachers interested
in participating in iGEM competition consulted with us about the future iGEM
cooperations.</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/education5.jpg" alt="photo" /></p>
+<h3 id="on-campus-education"><a class="header" href="#on-campus-education">On campus education</a></h3>
+<h4 id="wang-cai-biology-seminar-series"><a class="header" href="#wang-cai-biology-seminar-series">Wang-Cai Biology Seminar Series</a></h4>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/wang-cai-talk.jpeg" alt="Wang-Cai Talk" /></p>
+<p>In this Wang-Cai biology seminar series, the DKU iGEM team was honored to co-host the speech delivered by Prof. Dong Hyun Jo from Seoul National University College of Medicine. The talk was titled “Therapeutic Revolution: Application of Novel Technologiesâ€, where Dr Jo introduced the brief history and therapeutic development for one specific type of cancer, retinoblastoma. </p>
+<p>Dr Jo is the assistant professor of Seoul National University College of Medicine in Republic of Korea. He had his medical degree at Seoul National University in 2007. In 2012, Dr Jo received residency at the Department of Ophthalmology, Seoul National University Hospital, and in 2016, he received his PhD at Seoul National University. Dr Jo’s research interest focuses on 3 aspects. The first is the development of novel therapeutic approaches against retinal diseases. The second is the molecular mechanisms of physiological and pathological angiogenesis in the retina and associated organs, the third is translational research on retinoblastoma. </p>
+<p>At the end of the talk. Dr. Jo shared his career pathway as both a physician and a researcher. The devotion he made to the clinical therapy of retinoblastoma and the improvement of the health of his patients made him feel that biomedical sciences are not limited to theoretical knowledge, but rather quite practical and can benefit the whole population. The experience and thoughts expressed by Dr. Jo greatly inspired us, which allow us to have more understanding of graduate choices and future career plans. </p>
+<h4 id="journal-club"><a class="header" href="#journal-club">Journal club</a></h4>
+<p>In order to have better educational effect and promote our project , we
+organized the Journal Club activity in the Duke Kunshan community.</p>
+<p>The first Journal Club was held on April 30th, 2022. At the very beginning of
+the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us
+and introduced in detail what systems biology is and the basic methods of
+studying systems biology. This journal club event mainly focused on COVID-19
+and then developed into three sub-topics including the antigen test for
+SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray
+presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the
+iGEM team, around 10 freshman students with various backgrounds participated in
+the sharing and raised many inspiring questions.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/fig-journal-club-poster.jpg"
+/>
+<img src="https://static.igem.wiki/teams/4161/wiki/fig-1st-journal-club.jpg"
+/></p>
+<h3 id="summary"><a class="header" href="#summary">Summary</a></h3>
+<p>We have devoted in several education activities.
+On-campus education allows us to better transfer knowledge about synthetic
+biology and shigella treatment to our students, as well as gather fresh
+blood for the next year's team.
+The science popularization and education in local school also gives
+us the opportunity to communicate with middle and high school students,
+understand their ideas and answer their doubts.</p>
</main>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/engineering.html b/public/engineering.html
index ac6ddfb32a0e94248cd479661c66ef11fa106e33..4e5f9cc781339b23b68612414ba1904f417aceb5 100644
--- a/public/engineering.html
+++ b/public/engineering.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item expanded "><a href="engineering.html" class="active">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item expanded "><a href="engineering.html" class="active">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
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@@ -99,69 +99,71 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="engineering-cycle"><a class="header" href="#engineering-cycle">Engineering Cycle</a></h1>
+<div class="h1-bg">
+ <h1 class>Engineering Cycle</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/wetlab3-for-bg.png" />
+</div>
<h2 id="introduction"><a class="header" href="#introduction">Introduction</a></h2>
-<p>This page will give a detailed explanation about the engineering cycle. To make yeast capable of displaying the target nanobody 20ipaD on the cell surface, 20ipaD gene was inserted behind the yeast membrane-sealed protein <em>Aga</em>2; therefore, <em>Aga</em>2 would bring the nanobody to the cell surface. The recombinant plasmid pYD1-20ipaD was successfully built, which was supported by PCR amplification data and sequencing data. Apart from yeast, <em>Lactococcus lactis</em> and <em>Escherichia coli</em> were also chosen as probiotics for surface displace of nanobodies at the beginning, where 20ipaD/JPS-G3 and control 3xFLAG tags were inserted into pNZ8148 (L. lactis) and pET30a (E. coli) for expression respectively. However, due to failure in transformation and plasmid construction, only yeast was selected as the final product. </p>
-<h2 id="engineering-cycle-1"><a class="header" href="#engineering-cycle-1">Engineering Cycle</a></h2>
+<p>This page will give a detailed explanation about the engineering cycle. To make yeast capable of displaying the target nanobody 20ipaD on the cell surface, 20ipaD gene was inserted behind the yeast membrane-sealed protein <em>Aga</em>2; therefore, <em>Aga</em>2 would bring the nanobody to the cell surface. The recombinant plasmid pYD1-20ipaD was successfully built, which was supported by PCR amplification data and sequencing data. Apart from yeast, <em>Lactococcus lactis</em> and <em>Escherichia coli</em> were also chosen as probiotics for surface displace of nanobodies at the beginning, where 20ipaD/JPS-G3 and control 3xFLAG tags were inserted into pNZ8148 (L. lactis) and pET30a (E. coli) for expression respectively. However, due to failure in transformation and plasmid construction, only yeast was selected as the final product.</p>
+<h2 id="engineering-cycle"><a class="header" href="#engineering-cycle">Engineering Cycle</a></h2>
<h3 id="yeast"><a class="header" href="#yeast">Yeast</a></h3>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-engineering-cycle-high-resolution.png" alt="y-engineering-cycle-high-resolution" /></p>
<h4 id="cycle-1"><a class="header" href="#cycle-1">Cycle 1</a></h4>
<h5 id="design"><a class="header" href="#design">Design</a></h5>
-<p>We located a single-domain antibody (VHH) named 20ipaD from the database, whose binding ability with the needle tip protein ipaD of <em>Shigella</em> type III secretion system has be testified (Barta et al., 2017; Sierocki et al., 2021). Peptide sequences of 20ipaD from Barta et al (2017). Codon optimization was performed to get DNA sequences. Two flank sequences containing XhoI and ApaI cutting sites as well as C-terminal Flag-tag were added to the ipaD DNA sequence. </p>
+<p>We located a single-domain antibody (VHH) named 20ipaD from the database, whose binding ability with the needle tip protein ipaD of <em>Shigella</em> type III secretion system has be testified <sup class="footnote-reference"><a href="#Barta,2017">1</a></sup> <sup class="footnote-reference"><a href="#Sierocki,2021">2</a></sup>. Peptide sequences of 20ipaD from Barta et al (2017). Codon optimization was performed to get DNA sequences. Two flank sequences containing XhoI and ApaI cutting sites as well as C-terminal Flag-tag were added to the ipaD DNA sequence.</p>
<h5 id="build"><a class="header" href="#build">Build</a></h5>
<p>Designed 20ipaD sequences were chemically de novo synthesized and sent in pUC19. XhoI and ApaI double-digestion enabled us to ligate the 20ipaD DNA sequence into pYD1, a plasmid allowing the surface display of the gene it carries in yeast. The ligation of 20ipaD into pYD1 generates a DNA sequencing coding a recombinant protein of 20ipaD and Aga2, a yeast extracellular membrane protein. pYD1 also contained a replication origin recognized by bacteria and an ampicillin resistance gene. After plasmid ligation, recombinant plasmids were transferred into <em>E. coli</em> to get a clone via ampicillin selection. Cloned plasmids were then transferred into yeast cells. Yeast cells containing the plasmid were selected by tryptophane-deficient medium. Expression of the recombinant protein was induced by add galactose.</p>
<h5 id="test"><a class="header" href="#test">Test</a></h5>
<p>After transformation of recombinant plasmid into <em>E. coli</em> and single colony collection, we perform enzyme digestion and gel electrophoresis to check if the ligation and transformation is successful. For expression assay, we incubated induced yeast cells with anti-flag-tag primary antibody. After incubating with FITC conjugated secondary antibody, cells were examined under florescence microscopy and flow cytometry.</p>
<h5 id="learn"><a class="header" href="#learn">Learn</a></h5>
-<p>Recombinant proteins were observed to express on the cell surfaces on a portion of the cell population. We therefore planned to further testify the effectiveness of our recombinant protein. Though previous modeling through Rosetta suggested that the recombinant Aga2 region as well as the linkers sequences do not undermine the correct folding of the VHH part, we still sought for a experimental support as well as a way to quantify the binding affinity. </p>
+<p>Recombinant proteins were observed to express on the cell surfaces on a portion of the cell population. We therefore planned to further testify the effectiveness of our recombinant protein. Though previous modeling through Rosetta suggested that the recombinant Aga2 region as well as the linkers sequences do not undermine the correct folding of the VHH part, we still sought for a experimental support as well as a way to quantify the binding affinity.</p>
<h4 id="cycle-2"><a class="header" href="#cycle-2">Cycle 2</a></h4>
<h5 id="design-1"><a class="header" href="#design-1">Design</a></h5>
<p>In this cycle, we aimed to test binding affinity between the recombinant nanobody and the ipaD epitopes. ipaD were retrieved from NCBI database. Codon optimization was also performed to collect the DNA sequence. Similar to 20ipaD, flank regions were inserted into ipaD except the substitution of Flag-tag to HA-tag.</p>
<h5 id="build-1"><a class="header" href="#build-1">Build</a></h5>
<p>Synthesized ipaD sequences were got from the same company. Using the same method, we expressed ipaD recombinant protein of the yeast surface.</p>
-<h5 id="test-1"><a class="header" href="#test-1">Test</a></h5>
-<h5 id="learn-1"><a class="header" href="#learn-1">Learn</a></h5>
<h4 id="cycle-3"><a class="header" href="#cycle-3">Cycle 3</a></h4>
<h5 id="design-2"><a class="header" href="#design-2">Design</a></h5>
-<p>In this cycle, we aims to improve the expression level of the recombinant protein. Energy flows within the yeast cells would be controlled to concentrate more on protein production rather than other metabolic activities. We started by looking for a strong and continuously expressed promoter to drive the expression of 20ipaD recombinant protein. At the same time, we also tried to reduce other cellular activities. </p>
+<p>In this cycle, we aims to improve the expression level of the recombinant protein. Energy flows within the yeast cells would be controlled to concentrate more on protein production rather than other metabolic activities. We started by looking for a strong and continuously expressed promoter to drive the expression of 20ipaD recombinant protein. At the same time, we also tried to reduce other cellular activities.</p>
<h4 id="cycle-4"><a class="header" href="#cycle-4">Cycle 4</a></h4>
<h5 id="design-3"><a class="header" href="#design-3">Design</a></h5>
<p>In this cycle, we aims to improve the binding affinity of the recombinant protein with the antigen epitope. We would perform error prone PCRs to introduce mutations into 20ipaD sequences. Concentrations of the nucleotide analogs would be controlled so that only point mutants would be produced. All mutants would be screened to identify binding affinity improvements. To reduce the workload of screening, we would perform a modeling prescreen. In the prescreen, we would predict how single amino acid change influence the binding affinity between 20ipaD and ipaD.</p>
<h3 id="lactococcus-lactis"><a class="header" href="#lactococcus-lactis"><em>Lactococcus lactis</em></a></h3>
<h4 id="cycle-1-1"><a class="header" href="#cycle-1-1">Cycle 1</a></h4>
<h5 id="design-4"><a class="header" href="#design-4">Design</a></h5>
-<p>At first, we wanted to obtain the sequence of both 20ipaD and control flag-tag so that we could amplify them via PCR reaction. The 20ipaD is one of the single-VH domain antibodies (VHHs) capable of recognizing distinct epitopes within the antigen IpaD of pathogen Shigella. In this way, we hoped that by fusing 20ipaD and control flag-tag into the <em>Lactococcus lactis</em> expression vector pNZ8148, we would achieve the surface display and expression of 20ipaD on <em>Lactococcus lactis</em>. </p>
+<p>At first, we wanted to obtain the sequence of both 20ipaD and control flag-tag so that we could amplify them via PCR reaction. The 20ipaD is one of the single-VH domain antibodies (VHHs) capable of recognizing distinct epitopes within the antigen IpaD of pathogen Shigella. In this way, we hoped that by fusing 20ipaD and control flag-tag into the <em>Lactococcus lactis</em> expression vector pNZ8148, we would achieve the surface display and expression of 20ipaD on <em>Lactococcus lactis</em>.</p>
<h5 id="build-2"><a class="header" href="#build-2">Build</a></h5>
-<p>To obtain the sequence of 20ipaD, we constructed the plasmid with the 20ipaD sequence surrounded by two different restriction sites of enzymes BamHI and SacI. In this way, through the restrictive digestion of <em>Bam</em>HI and <em>Sac</em>I, ideally the sequence of 20ipaD would be obtained. The similar construction was also applied with the sequence of control flag-tag, where the enzymes used for restrictive digestion were changed to be NcoI and HindIII. </p>
-<h5 id="test-2"><a class="header" href="#test-2">Test</a></h5>
-<p>After successfully received the synthesized plasmid sequence for 20ipaD and control flag-tag, we conducted the digestion of BamHI and SacI for the obtain of 20ipaD sequence, and the digestion of <em>Nco</em>I and <em>Hind</em>III for the obtain of control flag-tag sequence. Gel electrophorese was applied to confirm the size of the sequence. Control flag-tag sequence was successfully obtained. However, according to the gel picture, the band of 20ipaD showed a very different size from that in theory. </p>
-<h5 id="learn-2"><a class="header" href="#learn-2">Learn</a></h5>
-<p>We checked the source of error and found that the designed sequence of 20ipaD has been inserted into the pUC19 vector when being synthesized by the company. Unfortunately, pUC19 vector also contained a restriction site for BamHI itself, thus leading to a different enzymatic digestion than what we have expected before. </p>
+<p>To obtain the sequence of 20ipaD, we constructed the plasmid with the 20ipaD sequence surrounded by two different restriction sites of enzymes BamHI and SacI. In this way, through the restrictive digestion of <em>Bam</em>HI and <em>Sac</em>I, ideally the sequence of 20ipaD would be obtained. The similar construction was also applied with the sequence of control flag-tag, where the enzymes used for restrictive digestion were changed to be NcoI and HindIII.</p>
+<h5 id="test-1"><a class="header" href="#test-1">Test</a></h5>
+<p>After successfully received the synthesized plasmid sequence for 20ipaD and control flag-tag, we conducted the digestion of BamHI and SacI for the obtain of 20ipaD sequence, and the digestion of <em>Nco</em>I and <em>Hind</em>III for the obtain of control flag-tag sequence. Gel electrophorese was applied to confirm the size of the sequence. Control flag-tag sequence was successfully obtained. However, according to the gel picture, the band of 20ipaD showed a very different size from that in theory.</p>
+<h5 id="learn-1"><a class="header" href="#learn-1">Learn</a></h5>
+<p>We checked the source of error and found that the designed sequence of 20ipaD has been inserted into the pUC19 vector when being synthesized by the company. Unfortunately, pUC19 vector also contained a restriction site for BamHI itself, thus leading to a different enzymatic digestion than what we have expected before.</p>
<h4 id="cycle-2-1"><a class="header" href="#cycle-2-1">Cycle 2</a></h4>
<h5 id="design-5"><a class="header" href="#design-5">Design</a></h5>
-<p>Since pUC19 vector also contained a restriction site for BamHI itself, which would lead to unspecific enzymatic digestion and the failure of getting 20ipaD sequence, we redesigned the experimental steps in order to overcome such a problem. </p>
+<p>Since pUC19 vector also contained a restriction site for BamHI itself, which would lead to unspecific enzymatic digestion and the failure of getting 20ipaD sequence, we redesigned the experimental steps in order to overcome such a problem.</p>
<h5 id="build-3"><a class="header" href="#build-3">Build</a></h5>
-<p>In this try, we would do the PCR amplification of 20ipaD sequence to insert it directly into the pNZ8148 vector first. This would circumvent the enzymatic digestion of pUC19 vector by BamHI that had the insertion of 20ipaD. </p>
-<h5 id="learn-3"><a class="header" href="#learn-3">Learn</a></h5>
-<p>From this process we learnt that when the synthesized plasmid went wrong from our expectations, apart from directly asking the company to redo the synthesis, we could also alter the steps of ligation via PCR reaction to solve the problem. </p>
+<p>In this try, we would do the PCR amplification of 20ipaD sequence to insert it directly into the pNZ8148 vector first. This would circumvent the enzymatic digestion of pUC19 vector by BamHI that had the insertion of 20ipaD.</p>
+<h5 id="learn-2"><a class="header" href="#learn-2">Learn</a></h5>
+<p>From this process we learnt that when the synthesized plasmid went wrong from our expectations, apart from directly asking the company to redo the synthesis, we could also alter the steps of ligation via PCR reaction to solve the problem.</p>
<h4 id="cycle-3-1"><a class="header" href="#cycle-3-1">Cycle 3</a></h4>
<h5 id="design-6"><a class="header" href="#design-6">Design</a></h5>
<p>We wanted to insert the engineered pNZ8148 vector with 20ipaD into the strain <em>Lactococcus lactis</em> NZ9000. According to literature review, electroporation is the commonly used technique to insert vectors into <em>Lactococcus lactis</em>.</p>
<h5 id="build-4"><a class="header" href="#build-4">Build</a></h5>
<p>When the OD600 of <em>Lactococcus lactis</em> reached 0.3, the bacteria would be subjected to electroporation. The bacteria would be washed with liquid detergent I containing 0.5mol∙L-1 sucrose and 10% glycerol for the insertion of 0.2 μg vector. The pulse of electroporation was delivered by a Gene-Pulser (Scientz) at 25μF and 2.5kV, while the electroporation cuvette (0.2cm in size) was connected in parallel to a 400-Ω resistor (the parameters were searched online and were consulted from technician at Scientz). According to multiple researches done previously, the transformation efficiency would be the highest is the recovery time is 1.5h after electroporation.</p>
-<h5 id="test-3"><a class="header" href="#test-3">Test</a></h5>
-<p>The process of electroporation was not successful because we failed to insert the vector into <em>Lactococcus lactis</em>. </p>
-<h5 id="learn-4"><a class="header" href="#learn-4">Learn</a></h5>
-<p>We suspect that the making of electrocompetent cells might be the source of failure. After checking with the team advisor, we found that the type of glycerol used was intended for protein purification, which could cause problems for the electrocompetent cell. </p>
+<h5 id="test-2"><a class="header" href="#test-2">Test</a></h5>
+<p>The process of electroporation was not successful because we failed to insert the vector into <em>Lactococcus lactis</em>.</p>
+<h5 id="learn-3"><a class="header" href="#learn-3">Learn</a></h5>
+<p>We suspect that the making of electrocompetent cells might be the source of failure. After checking with the team advisor, we found that the type of glycerol used was intended for protein purification, which could cause problems for the electrocompetent cell.</p>
<h4 id="cycle-4-1"><a class="header" href="#cycle-4-1">Cycle 4</a></h4>
<h5 id="design-7"><a class="header" href="#design-7">Design</a></h5>
<p>To further increase efficiency, after doing more literature reviews we added the pretreatment of <em>Lactococcus lactis</em> with lithium acetate (LiAc) and/or dithiothreitol (DTT). We also substituted the type of glycerol used based on the previous error analysis.</p>
<h5 id="build-5"><a class="header" href="#build-5">Build</a></h5>
-<p>According to the newly found protocol, the Lactococcus lactis was firstly suspended at room temperature for 30 min in 8ml of 100mM LiAc, 10mM DTT, 0.6M sucrose, and 10mM Tris-HCl (pH=7.5). Following the treatment, <em>Lactococcus lactis</em> was pelleted and was resuspended in 1.5ml microcentrifuge tube, and was then washed as previously described. Afterwards, electroporation was conducted as previously described. </p>
+<p>According to the newly found protocol, the <em>Lactococcus lactis</em> was firstly suspended at room temperature for 30 min in 8ml of 100mM LiAc, 10mM DTT, 0.6M sucrose, and 10mM Tris-HCl (pH=7.5). Following the treatment, <em>Lactococcus lactis</em> was pelleted and was resuspended in 1.5ml microcentrifuge tube, and was then washed as previously described. Afterwards, electroporation was conducted as previously described.</p>
<h3 id="escherichia-coli"><a class="header" href="#escherichia-coli"><em>Escherichia coli</em></a></h3>
<p><img src="https://static.igem.wiki/teams/4161/wiki/e-eng-cyc.png" alt="E.coli Engineering Cycle" /></p>
<h4 id="cycle-1-2"><a class="header" href="#cycle-1-2">Cycle 1</a></h4>
<h5 id="design-8"><a class="header" href="#design-8">Design</a></h5>
-<p>Initially, we planned to try three different nanobodies (20ipaD, JPS-G3, and JMK-H2) agianst the <em>Shigella</em> antigen ipaD from a research paper <sup class="footnote-reference"><a href="#Barta,2017">1</a></sup>. We also wanted to try two different surface display systems, beta domain of the E.<em>coli</em> outer membrane protein intimin <sup class="footnote-reference"><a href="#Salema,2013">2</a></sup> and the E.<em>coli</em> curli fiber protein, <em>csg</em>B <sup class="footnote-reference"><a href="#Gelfat,2021">3</a></sup>. Our target probiotic is E. <em>coli</em> Nissle 1917 <sup class="footnote-reference"><a href="#Gelfat,2021">3</a></sup>. By inserting the target nanobody sequence behind intimin or <em>csg</em>B, reconstructing the plasmid pET30a and transforming the plasmid into E.<em>coli</em> Nissle 1917, we expect the protein to be displayed on the surface of E.<em>coli</em>, so that it can capture the pathogen via antigen-antibody binding. </p>
+<p>Initially, we planned to try three different nanobodies (20ipaD, JPS-G3, and JMK-H2) agianst the <em>Shigella</em> antigen ipaD from a research paper <sup class="footnote-reference"><a href="#Barta,2017">1</a></sup>. We also wanted to try two different surface display systems, beta domain of the E.<em>coli</em> outer membrane protein intimin <sup class="footnote-reference"><a href="#Salema,2013">3</a></sup> and the E.<em>coli</em> curli fiber protein, <em>csg</em>B <sup class="footnote-reference"><a href="#Gelfat,2021">4</a></sup>. Our target probiotic is E. <em>coli</em> Nissle 1917 <sup class="footnote-reference"><a href="#Gelfat,2021">4</a></sup>. By inserting the target nanobody sequence behind intimin or <em>csg</em>B, reconstructing the plasmid pET30a and transforming the plasmid into E.<em>coli</em> Nissle 1917, we expect the protein to be displayed on the surface of E.<em>coli</em>, so that it can capture the pathogen via antigen-antibody binding.</p>
<h5 id="build--test"><a class="header" href="#build--test">Build & Test</a></h5>
<p>We designed the following sequences to make the recombinant protein.</p>
<ul>
@@ -178,40 +180,47 @@
<p>ipaD-3xHA</p>
</li>
</ul>
-<p>However, due to limitations in budget & time for gene synthesis, we only have JPS-G3-3xFLAG and ipaD-3xHA (inserted into pUC19 plasmids). By plasmid extraction, double digestion (<em>Bam</em>HI & <em>Xho</em>I) and PCR, we successfully obtained the sequences and verified the accuracy by Sanger sequencing, but we don't have csgB or intimin for surface display. </p>
-<h5 id="learn-5"><a class="header" href="#learn-5">Learn</a></h5>
+<p>However, due to limitations in budget & time for gene synthesis, we only have JPS-G3-3xFLAG and ipaD-3xHA (inserted into pUC19 plasmids). By plasmid extraction, double digestion (<em>Bam</em>HI & <em>Xho</em>I) and PCR, we successfully obtained the sequences and verified the accuracy by Sanger sequencing, but we don't have csgB or intimin for surface display.</p>
+<h5 id="learn-4"><a class="header" href="#learn-4">Learn</a></h5>
<p>Complex sequences including potential harmful genes may impact synthesis efficiency.</p>
<h4 id="cycle-2-2"><a class="header" href="#cycle-2-2">Cycle 2</a></h4>
<h5 id="design-9"><a class="header" href="#design-9">Design</a></h5>
-<p>Alternatively, we chose the curli fiber <em>csg</em>A <sup class="footnote-reference"><a href="#Gelfat et. al., 2021">4</a></sup> sequence for surface display. </p>
+<p>Alternatively, we chose the curli fiber <em>csg</em>A <sup class="footnote-reference"><a href="#Gelfat et. al., 2021">5</a></sup> sequence for surface display.</p>
<h5 id="build--test-1"><a class="header" href="#build--test-1">Build & Test</a></h5>
<p>We designed the following sequences:</p>
<ul>
<li>
-<p>csgA-JPS-G3-3xFLAG </p>
+<p>csgA-JPS-G3-3xFLAG</p>
</li>
<li>
<p>csgA-ipaD-3xHA (displaying the antigen on the surface of E.<em>coli</em> BL21 to mimic <em>Shigella flexneri</em>, so that the effectiveness can be evaluated)</p>
</li>
</ul>
-<p><em>csg</em>A gene is obtained from the E.<em>coli</em> strains (pGEX-4T-1-csgA-shMT) provided by the XJLTU iGEM team via PCR. To connect different parts, we plan to use overlapping PCR. </p>
+<p><em>csg</em>A gene is obtained from the E.<em>coli</em> strains (pGEX-4T-1-csgA-shMT) provided by the XJLTU iGEM team via PCR. To connect different parts, we plan to use overlapping PCR.</p>
<h2 id="reference"><a class="header" href="#reference">Reference</a></h2>
-<div class="footnote-definition" id="Barta,2017"><sup class="footnote-definition-label">1</sup>
-<p>Barta, M., Shearer, J., Arizmendi, O., Tremblay, J., Mehzabeen, N., Zheng, Q., . . . Picking, W. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. <em>Journal of Biological Chemistry</em>, 292, jbc.M117.802231. <a href="doi:10.1074/jbc.M117.802231">doi:10.1074/jbc.M117.802231</a></p>
+<div class="footnote-definition" id="Salema,2013"><sup class="footnote-definition-label">3</sup>
+<p>Salema, V., MarÃn, E., MartÃnez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., Teira, X., Gutierrez, C., Bodelón, G., & Fernández, L. Ã. (2013). Selection of Single Domain Antibodies from Immune Libraries Displayed on the Surface of <em>E. coli</em> Cells with Two β-Domains of Opposite Topologies. <em>PLoS ONE</em>, 8(9), e75126. <a href="https://doi.org/10.1371/journal.pone.0075126">https://doi.org/10.1371/journal.pone.0075126</a></p>
</div>
-<div class="footnote-definition" id="Salema,2013"><sup class="footnote-definition-label">2</sup>
-<p>Salema, V., MarÃn, E., MartÃnez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., Teira, X., Gutierrez, C., Bodelón, G., & Fernández, L. Ã. (2013). Selection of Single Domain Antibodies from Immune Libraries Displayed on the Surface of E. coli Cells with Two β-Domains of Opposite Topologies. <em>PLoS ONE</em>, 8(9), e75126. <a href="https://doi.org/10.1371/journal.pone.0075126">https://doi.org/10.1371/journal.pone.0075126</a></p>
+<div class="footnote-definition" id="Gelfat,2021"><sup class="footnote-definition-label">4</sup>
+<p>Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic <em>E. coli</em> Nissle 1917 (p. 2021.06.18.448998). <em>bioRxiv</em>. <a href="https://doi.org/10.1101/2021.06.18.448998">https://doi.org/10.1101/2021.06.18.448998</a></p>
+</div>
+<div class="footnote-definition" id="Barta,2017"><sup class="footnote-definition-label">1</sup>
+<p>Barta, M. L., Shearer, J. P., Arizmendi, O., Tremblay, J. M., Mehzabeen, N., Zheng, Q., Battaile, K. P., Lovell, S., Tzipori, S., Picking, W. D., Shoemaker, C. B., & Picking, W. L. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem, 292(40), 16677-16687. <a href="https://doi.org/10.1074/jbc.M117.802231">https://doi.org/10.1074/jbc.M117.802231</a></p>
</div>
-<div class="footnote-definition" id="Gelfat,2021"><sup class="footnote-definition-label">3</sup>
-<p>Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). <em>bioRxiv</em>. <a href="https://doi.org/10.1101/2021.06.18.448998">https://doi.org/10.1101/2021.06.18.448998</a></p>
+<div class="footnote-definition" id="Sierocki,2021"><sup class="footnote-definition-label">2</sup>
+<p>Sierocki, R., Jneid, B., Orsini Delgado, M. L., Plaisance, M., Maillere, B., Nozach, H., & Simon, S. (2021). An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLoS Negl Trop Dis, 15(3), e0009231. <a href="https://doi.org/10.1371/journal.pntd.0009231">https://doi.org/10.1371/journal.pntd.0009231</a></p>
</div>
-<p>Barta, M. L., Shearer, J. P., Arizmendi, O., Tremblay, J. M., Mehzabeen, N., Zheng, Q., Battaile, K. P., Lovell, S., Tzipori, S., Picking, W. D., Shoemaker, C. B., & Picking, W. L. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem, 292(40), 16677-16687. https://doi.org/10.1074/jbc.M117.802231</p>
-<p>Sierocki, R., Jneid, B., Orsini Delgado, M. L., Plaisance, M., Maillere, B., Nozach, H., & Simon, S. (2021). An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLoS Negl Trop Dis, 15(3), e0009231. https://doi.org/10.1371/journal.pntd.0009231 </p>
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+<h1 id="introduction"><a class="header" href="#introduction">Introduction</a></h1>
+<p>The probiotics market in China is expected to reach a size of USD 13,527.100 million by 2025, growing at a CAGR of 8.81 percent. In 2019, the market was valued at US8,149.466 million <sup class="footnote-reference"><a href="#1">1</a></sup>. Previous research findings has emphasized on the significance of gut microbiome on human health, and this has opened up the marketing of probiotics. Taking advantage of the booming market and the maturation of bioengineering technology, our project aims to guard our guts through bacteria-bacteria interaction, a method that is an alternative to antibiotics. Some probiotic product utilizing bacteria-bacteria cell interaction has already gone through clinical trials and entered the market, such as Lactobacillus reuteri DSM17648 that treats H.pylori infection <sup class="footnote-reference"><a href="#2">2</a></sup>. Therefore, it is possible for our product to secure a place in the probiotic market.</p>
+<p>The terminal of our designed product is a drug used in people. We understand that animal model testings as well as clinical trials are often involved in the process of drug development. What we have reached so far is only a prototype tested in vitro. After the completion of the in vitro testing we will proceed to in vivo models. To improve our plan we interviewed Jisheng Lin from Sinovac Biotech company, to collected feedbacks and suggestions about how to turn our products into commercial ones as well as cautions on putting our products in a real world situation. Here we provide considerations from various aspects of accessing our products into market and our solutions so far.</p>
+<h2 id="safety"><a class="header" href="#safety">Safety</a></h2>
+<p>"Safety is always the first concern," as suggested by Mr. Lin, "even it doesn't work well, at least does no harm." Based on Mr. Lin's suggestions as well as our previous thoughts, several sources of safety concerns are listed as follows: First, the plasmid we used for selection contains a bacterial ampicillin resistance gene. though not expressed in yeast due to different promoter and codon structures, potential horizontal gene transfers still leave risks of spread antibiotic resistent genes to other prokaryotes in the intestine. Second, though our vectors cell linage yeast strain EBY100 has been well studied, the genomic background of our engineered yeast is unknown. Our engineering process may alter the growth and metabolic characteristics. Efforts should be given to test if engineered yeast could harm human bodies. Besides, human intestine is a complicated microenvironment comprises of a microbiota yet not fully understood. It is also important to clarify how long does our engineered yeast can survive in human body, whether it gains competitive advantages over native gut microorganisms, and how it alter the structure of gut microbiome. Third, similar to antibody therapies, allergy may be a question to some people. Therefore, an approach should be developed to pre-test patients' irritability. Fourth, as a commercial product, a standard of quality control during each step of the engineering or the drug production is also needed.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/entre-image.jpg" alt="Entre_image" /></p>
+<h2 id="effectiveness"><a class="header" href="#effectiveness">Effectiveness</a></h2>
+<p>Effectiveness demonstrates the values of our products. We have shown qualitatively the expression of the antibodies and the binding between the antigen and the antibodies. For a real world application, we need to establish standard to access and quantify these values. Moreover, the success in the simplified in vitro assay does not guarantee the effectiveness of the drug to work in a real scenario. Considering the real world application that our products function in human GI tracts, it requires the engineered yeast be able to settle down, proliferate, and bind to <em>Shigella</em> spike proteins. Hence, the growth curve about the engineered yeast in human intestines should also be tested. More importantly, the performance of the drug should also be assessed. Potential questions include whether there is dosage-dependent protection effect, how to assess these effects if they exist, and whether this product focuses on therapy or is precaution oriented.</p>
+<h2 id="economics"><a class="header" href="#economics">Economics</a></h2>
+<p>The third aspect related to the economics about our products. Apart from the reagents and consumable usage, stabilities, including plasmid stability and the stability of the phenotype expressions, are important factor influence the cost of production. A passaging lineage stably expression the recombinant antibodies greatly reduce the cost of continuously re-engineering the yeast to harvest antibody expression. Efforts should be devoted to focus on increasing the stability antibody expression during passages.</p>
+<h2 id="future"><a class="header" href="#future">Future</a></h2>
+<p>We should also seek for further development of our products in the future, such as increasing the valency of our product so that it can target multiple pathogens at the same time.</p>
+<h2 id="our-solution"><a class="header" href="#our-solution">Our Solution</a></h2>
+<p>As many goals are still far from being achieved, here we proposed our future plan altogether with what we have reached. We used two different approaches to remove the influence of ampicillin resistance gene. In the first approach, we designed a PCR-fusion that jumps the whole ampicillin resistant gene and the bacterial replication origin. The resting plasmid contains around 3200bp including the TRP1 gene that is a suitable size for PCR amplification and enables the selection of transformant yeast cells. The alternative approach used CRISPR-Cas9 to integrate the whole "promoter-Aga2-20ipaD" cassette into yeast genome. The latter also increases phenotype stability as no plasmid is needed to maintain the phenotype. For expression level assessment, we have already established a system employed ELISA to quantify the expression. However, one drawback of this approach is that it does not differentiate surface displayed antibodies from the antibodies no correctly presented on surface. An improved design uses biotins to labeled all surface proteins followed by avidin affinity binding to isolate these proteins from the protein repertoire. Isolated surface protein can be then analyzed via ELISA. To improve expression level, we have listed a set of developed constitutive yeast promoters as candidates. However, we also realized that promoter engineering processes may be required in the future. For the effectiveness test, we have designed a cell invasion test in vitro. Engineered yeast cells together with <em>Shigella</em> will be applied to Vero cell cultures. Effectiveness will be measured by proportion of cells being infected.</p>
+<p>To remove the influence of cell lines on the result of invasion test, we plan to substitute the Vero cell lines to epithelial cells in the future. After the completion of in vitro assay, further in vivo assay may be applied.</p>
+<h1 id="conclusion"><a class="header" href="#conclusion">Conclusion</a></h1>
+<p>We realized that what we have built is only a prototype of a <em>Shigella</em> infection precaution drug. There is still a long way to go for optimizing the drug in vitro as well as testing the drug in vivo. However, via a series of design processes, we have developed plans to turn it into real world application.</p>
+<div class="footnote-definition" id="1"><sup class="footnote-definition-label">1</sup>
+<p>China Probiotics Market Size, Share, Opportunities, COVID-19 Impact, And Trends By Ingredient (Bacteria, Yeast), By Form (Liquid, Dry), By Application (Functional Food And Beverages, Dietary Supplements, Animal Feed), And By End-User (Human, Animal) - Forecasts From 2020 To 2025. (2020). <a href="https://www.knowledge-sourcing.com/report/china-probiotics-market#:~:text=China%20probiotics%20market%20is%20estimated,intestinal%20tracts%2C%20and%20bowel%20function">https://www.knowledge-sourcing.com/report/china-probiotics-market#:~:text=China%20probiotics%20market%20is%20estimated,intestinal%20tracts%2C%20and%20bowel%20function</a></p>
+</div>
+<div class="footnote-definition" id="2"><sup class="footnote-definition-label">2</sup>
+<p>Significant Reduction in Helicobacter pylori Load in Humans with Non-viable Lactobacillus reuteri DSM17648: A Pilot Study. (2015). <a href="https://pubmed.ncbi.nlm.nih.gov/25481036/">https://pubmed.ncbi.nlm.nih.gov/25481036/</a></p>
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-<h1 id="experiment"><a class="header" href="#experiment">Experiment</a></h1>
-<h2 id="introduction"><a class="header" href="#introduction">Introduction</a></h2>
-<p>This page will give a detailed record about the experiment process,
-including the lab notes and protocols.</p>
-<h2 id="experiment-1"><a class="header" href="#experiment-1">Experiment</a></h2>
-<h3 id="yeast"><a class="header" href="#yeast">Yeast</a></h3>
-<h4 id="lab-notes"><a class="header" href="#lab-notes">Lab Notes</a></h4>
-<h4 id="protocols"><a class="header" href="#protocols">Protocols</a></h4>
-<h3 id="lactococcus-lactis"><a class="header" href="#lactococcus-lactis"><em>Lactococcus lactis</em></a></h3>
+<div class="h1-bg">
+ <h1 class>Experiments</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/wetlab5-for-bg.png" />
+</div>
+<h2 id="yeast"><a class="header" href="#yeast">Yeast</a></h2>
+<h3 id="experiment-overview"><a class="header" href="#experiment-overview">Experiment Overview</a></h3>
+<p><strong>Phases</strong>: 1. Stock vectors preparation and vectors storage; 2. Stock gene preparation and amplification; 3. Gene cloning, plasmid construction, storage, and verification; 4. Yeast transformation, protein display, and detection</p>
+<p><strong>Phase I:</strong> Stock vectors preparation and vectors storage
+By the end of this phase, we would get:
+One tube of pYD1 vector stock solution
+One glycerol stock containing <em>E. coli</em> DH5α that were transformed with pYD1 vectors</p>
+<p><strong>Phase II</strong>: Gene cloning, plasmid construction, storage, and verification
+By the end of this step, we would get:
+One tube of pY20ipaD recombinant stock solution (not pure)
+One glycerol stock containing <em>E. coli</em> DH5α that were transformed with pYD1 vectors</p>
+<p><strong>Phase IV</strong>: Yeast transformation, protein display, and detection
+By the end of this phase, we would get:
+Glycerol stock of yeast that were transformed with recombinant plasmids
+Induced yeasts (display the nanobody on the surface)</p>
+<h3 id="lab-notes"><a class="header" href="#lab-notes">Lab Notes</a></h3>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/saccharomyces-cerevisiae-lab-notebook.pdf">Yeast Lab Notes</a></p>
+<h3 id="protocols"><a class="header" href="#protocols">Protocols</a></h3>
+<p>"One-step Method Competent Cell Preparation Kit" from Beyotime was used for this experiment. The protocol follows the manual of the product<sup class="footnote-reference"><a href="#1">1</a></sup>.</p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/e-coli-competent-cell-transformation.pdf">E.coli_competent_cell_transformation</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/plasmid-extraction.pdf">Plasmid_Extraction</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/genetic-cloning-enzyme-digestion-ligation.pdf">Genetic_cloning_Enzyme_digestion_ligation</a></p>
+<p>"DNA Agarose Gel Recycle Kit" from Beyotime was used for this experiment. The protocol follows the manual of the product.<sup class="footnote-reference"><a href="#2">2</a></sup></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/gel-purification.pdf">Gel_Purification.pdf</a></p>
+<p>"Frozen-EZ Yeast Transformation II Kit" from Zymo was used for this experiment. The protocol follows the manual of the product.<sup class="footnote-reference"><a href="#3">3</a></sup></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/yeast-induction.pdf">Yeast_Induction.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/florescence-activated-cell-sorting.pdf">Fluorescence_Activated_Cell_Sorting.pdf</a></p>
+<p>"FLAG Tag Immuno-precipitation Kit (Immunomagnetic Beads Method)" from Beyotime was used for this experiment. The protocol follows the manual of the product<sup class="footnote-reference"><a href="#4">4</a></sup>.</p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/protein-purification.pdf">Protein_Purification.pdf</a></p>
+<p>“TIANprep Mini Plasmid kit†was used for this experiment. The protocol follows the manual of the product <sup class="footnote-reference"><a href="#5">5</a></sup>.</p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/plasmid-extraction.pdf">Plasmid_Extraction.pdf</a></p>
+<h2 id="escherichia-coli"><a class="header" href="#escherichia-coli"><em>Escherichia coli</em></a></h2>
+<h3 id="experiment-overview-1"><a class="header" href="#experiment-overview-1">Experiment Overview</a></h3>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/group-e-workflow.pdf">Group E Workflow</a></p>
+<p><strong>Group E.<em>coli</em> Experimental Procedures</strong></p>
+<p><strong>1. Cloning</strong></p>
+<p><strong>2. Recombinant Protein Expression</strong></p>
+<p><strong>2.1 Express the Protein in E.<em>coli</em> DE3 Cytoplasm</strong></p>
+<p>3 different VHHs (JPS-G3, JMK-H2, 20ipaD) and 1 antigen (ipaD) are expressed separately in E.<em>coli</em> DE3 for protein purification. As is shown in the diagram below (<strong>Figure 1</strong>), the DNA sequences of the proteins are bind to different detection tags (VHHs - FLAG-tag, antigen - HA-tag) and inserted into pET41a plasmids for bacterial transformation and protein purification. The pET41a plasmid contains a T7 promoter and a T7 terminator for high-level protein expression in E. <em>coli</em> DE3, and a GST tag with a Tb (thrombin) site for protein purification. After transformation, the exogenous proteins will be expressed by the bacteria.</p>
+<p><strong>Fig.1 | Schematic Representation of the Protein Expression & Purification Process</strong></p>
+<p><strong>2.2 Protein Purification and Affinity Test</strong></p>
+<p>Next, we use the GST tag to purify the recombinant protein. The target proteins will be extracted via GSH-GST interaction, and the remaining GST tag will be cut by thrombin. Then, we can get the purified recombinant proteins (target protein + detection tag).</p>
+<p>Lastly, co-IP (immuno-precipitation) followed by Western analysis will be used to test the affinity between VHHs and the antigen. As is shown in the figure below (<strong>Figure 2</strong>), by adding anti-FLAG antibodies and anti-HA antibodies to the samples, we can pull down the recombinant proteins with corresponding tags. If adding either anti-FLAG antibodies or anti-HA antibodies leads to a positive result in 'FLAG-VHH + HA-ipaD', we can say that there is high affinity between the expressed VHHs and the antigen.</p>
+<p><strong>Fig.2 | Expected Western Blot Results of the co-IP Experiment</strong></p>
+<p><strong>3. Surface Display</strong></p>
+<p><strong>3.1 Surface Display via csgA</strong>
+CsgA, or major curlin subunit, is a component of biofilm. The design was a modified version of the PATCH system from Neel Joshi lab. It is composed of a temperature-controlled promoter, Csg synthetic operon, and the VHH targeting Type III secretion system. The design is predicted to be beneficial in a therapeutic context because biofilm formation effectively inhibits the invasion of shigella into epithelial cells.</p>
+<p><strong>3.2 Surface Display via intimin</strong></p>
+<p><strong>3.3 Detecting E.<em>coli</em> surface display</strong></p>
+<p><strong>Congo red binding assay</strong><br />
+We use a quantitative congo-red binding assay to detect the expression of curli fibers. Congo red is a dye that binds to the hydroxyl group of polypeptide chains in amyloid through hydrogen bonds. A control group with no curli expression and a group with curli expression are cultured under the same condition. The 490nm absorbance of both groups are measured to quantify the amount of congo red not in binding with curli fiber <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6898321/">(1)</a><a href="https://pubs.acs.org/doi/full/10.1021/acsbiomaterials.6b00437">(2)</a>.
+<strong>Whole cell filtration ELISA</strong><br />
+To detect the expression of curli fibers on the cell surface, we perform whole-cell ELISA. Whole-cell ELISA requires the cells to be seeded to the bottoms of the wells, providing conditions to detect proteins in whole cells <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6898321/">(3)</a><a href="https://www.lsbio.com/products/elisakits/cellbased">(4)</a>.</p>
+<p><strong>3.4 Detecting the Binding Affinity Between E.<em>coli</em> Expressing VHHs and the antigen</strong></p>
+<p><strong>Aggregation Assay using OD600 measurements <a href="https://doi.org/10.1016/j.cell.2018.06.041">(5)</a></strong><br />
+Ag (antigen)-only E.<em>coli</em>, Nb (nanobody, i.e., VHHs)-only E.<em>coli</em> and the mixture of the two are cultured separately in LB liquid medium for 24 hours. OD600 of their supernatant are measured immediately/after 24 hours to see whether there is significant difference between the Ag-only group, Nb-only group, and mixture group. A significant low OD600 in the mixture group indicates that the E.<em>coli</em> expressing VHHs and antigens bind to each other, form assembly, and sink.</p>
+<p><strong>Observing the Morphologies using Confocal Microscopy <a href="https://doi.org/10.1016/j.cell.2018.06.041">(5)</a></strong><br />
+GFP and m<em>Cherry</em> genes were expressed respectively in Ag-only E.<em>coli</em> and Nb-only E.<em>coli</em>. When observing the morphology via a confocal microscope, we should see that most neighbors of a certain bacterium should have opposite colors.</p>
<h4 id="lab-notes-1"><a class="header" href="#lab-notes-1">Lab Notes</a></h4>
-<h4 id="protocols-1"><a class="header" href="#protocols-1">Protocols</a></h4>
-<h3 id="escherichia-coli"><a class="header" href="#escherichia-coli"><em>Escherichia coli</em></a></h3>
-<h4 id="lab-notes-2"><a class="header" href="#lab-notes-2">Lab Notes</a></h4>
-<p>Please see attached.</p>
<p><a href="https://static.igem.wiki/teams/4161/wiki/igem-e-labnotes.pdf">E.<em>coli</em> Lab Notes</a></p>
-<h4 id="protocols-2"><a class="header" href="#protocols-2">Protocols</a></h4>
-<p>Please see attached.</p>
+<h4 id="protocols-1"><a class="header" href="#protocols-1">Protocols</a></h4>
<p><a href="https://static.igem.wiki/teams/4161/wiki/igem-e-protocols.pdf">E.<em>coli</em> Protocols</a></p>
+<h2 id="lactococcus-lactis"><a class="header" href="#lactococcus-lactis"><em>Lactococcus lactis</em></a></h2>
+<h3 id="experiment-overview-2"><a class="header" href="#experiment-overview-2">Experiment Overview</a></h3>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/workflow-of-l-lactis-team.png" alt="L_Workflow" /></p>
+<h3 id="lab-notes-2"><a class="header" href="#lab-notes-2">Lab Notes</a></h3>
+<p>Because of financial and logistical reasons, wet lab experiments of group L were halted. We therefore can only present the experimental procedures and protocols designed by our members.</p>
+<h3 id="protocols-2"><a class="header" href="#protocols-2">Protocols</a></h3>
+<p>Group L intends to display 20ipaD, a nanobody against Shigella, onto L.lactis. The plasmid construction is performed in E.<em>coli</em> and then transformed into L.lactis.</p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/electroporation-protocol-for-lactococcus-lactis.pdf">Electroporation_protocol_for_Lactococcus_lactis.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/gel-extraction-protocol.pdf">gel_extraction_protocol.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/plasmid-extraction-of-l-lactis-gram-positive-bacteria.pdf">Plasmid_extraction_of_L.lactis__Gram_positive_bacteria_.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/protocol-for-activating-and-preparing-glycerol-stock.pdf">Protocol_for_activating_and_preparing_glycerol_stock.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/protocol-for-extracting-dna-from-lactococcus-lactis-nz9000.pdf">Protocol_for_extracting_DNA_from_Lactococcus_Lactis_NZ9000.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/protocol-for-ligation.pdf">Protocol_for_ligation.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/protocol-for-medium-making.pdf">Protocol_for_medium_making.pdf</a></p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/protocol-for-restriction-enzyme-digestion.pdf">Protocol_for_restriction_enzyme_digestion.pdf</a>
+plasmid extraction and gel purification are the same as Group Y.</p>
+<p><a href="https://static.igem.wiki/teams/4161/wiki/solarbio-protocol-of-dna-extraction.pdf">Solarbio_protocol_of_DNA_extraction.pdf</a></p>
+<div class="footnote-definition" id="1"><sup class="footnote-definition-label">1</sup>
+<p>Beyotime One-step Method Competent Cell Preparation Kit. <a href="https://www.beyotime.com/product/D0301.htm">https://www.beyotime.com/product/D0301.htm</a></p>
+</div>
+<div class="footnote-definition" id="2"><sup class="footnote-definition-label">2</sup>
+<p>Beyotime DNA Agarose Gel Recycle Kit. <a href="https://www.beyotime.com/product/D0056.htm">https://www.beyotime.com/product/D0056.htm</a></p>
+</div>
+<div class="footnote-definition" id="3"><sup class="footnote-definition-label">3</sup>
+<p>Zymo Frozen-EZ_Yeast_Transformation_II_Kit. <a href="https://files.zymoresearch.com/protocols/_t2001_frozen-ez_yeast_transformation_ii.pdf">https://files.zymoresearch.com/protocols/_t2001_frozen-ez_yeast_transformation_ii.pdf</a></p>
+</div>
+<div class="footnote-definition" id="4"><sup class="footnote-definition-label">4</sup>
+<p>Beyotime FLAG Tag Immuno-precipitation Kit (Immunomagnetic Beads Method). <a href="https://m.beyotime.com/Manual/P2181%20Flag%E6%A0%87%E7%AD%BE%E8%9B%8B%E7%99%BD%E5%85%8D%E7%96%AB%E6%B2%89%E6%B7%80%E8%AF%95%E5%89%82%E7%9B%92(%E7%A3%81%E7%8F%A0%E6%B3%95).pdf">https://m.beyotime.com/Manual/P2181%20Flag%E6%A0%87%E7%AD%BE%E8%9B%8B%E7%99%BD%E5%85%8D%E7%96%AB%E6%B2%89%E6%B7%80%E8%AF%95%E5%89%82%E7%9B%92(%E7%A3%81%E7%8F%A0%E6%B3%95).pdf</a></p>
+</div>
+<div class="footnote-definition" id="5"><sup class="footnote-definition-label">5</sup>
+<p>TIANprep Mini Plasmid kit. <a href="https://en.tiangen.com/download/manual.html?one=34&two=1085&three=1086&id=4307">https://en.tiangen.com/download/manual.html?one=34&two=1085&three=1086&id=4307</a></p>
+</div>
</main>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
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+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
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diff --git a/public/human-practices.html b/public/human-practices.html
index c393bda7aa909e25e6f1f82293169c1afd648fba..19f682e73c6fd1bd224be5bc15657759691a6a4a 100644
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@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
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@@ -99,432 +99,33 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="human-practice"><a class="header" href="#human-practice">Human Practice</a></h1>
-<h2 id="interview-with-prof-cao"><a class="header" href="#interview-with-prof-cao">Interview with Prof Cao</a></h2>
-<p>We interviewed Huansheng Cao,
-Assistant professor of Environmental Science at Duke Kunshan University
-for suggestions on our initial lab plans.</p>
-<p>In the interview, team members Yuxin Wang and Chang Shen presented the main design,
-bacterial surface display, to consult Prof Cao on its feasibility.
-After confirming the rich research foundations of our plan,
-he encouraged us to add computational elements to our lab design.</p>
-<p>As a scientist working in computational biology and bioinformatics,
-he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody
-and the antigen unit.
-As a well-trained biologist, he also suggested
-fitting our design to more than one model organisms,
-which shows integration in our drug design.</p>
-<p>The interview was full of enthusiasm, so we were able to come across many other topics.
-We discussed the trends in bioinformatics and biotechnology,
-including bacteria-based bioelectricity,
-and the relationship between human longevity and gut microbiota.</p>
-<p>This interview was both encouraging and informative,
-and contributed greatly to the first stage of human practice.</p>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/prof-cao-interview1.jpg" alt="photo" /></p>
-<h2 id="2022-college-student-innovation-and-entrepreneurship-training-program"><a class="header" href="#2022-college-student-innovation-and-entrepreneurship-training-program">2022 College Student Innovation and Entrepreneurship Training Program</a></h2>
-<p>We participated in 2022's College Student Innovation and Entrepreneurship Training
-Program—a national training program for college students on innovation and entrepreneurship.
-It encourages students to participate in scientific research, technological development,
-and entrepreneurship.</p>
-<p>During the final pitch,
-Lisa Wu and Lingrui Lai made the presentation about our project of Shigella treatment
-using the concept of of synthetic biology.
-Lingrui went through the basic concept of shigella and synthetic biology,
-then,
-the current challenges that we are facing for shigella treatment
-and our suggestions.<br />
-Lisa introduced the methodology involved and techniques used in our project.
-At the end they stressed the significance of our project.</p>
-<p>Judgers include Kai Huang (Division Chair of Natural and Applied Sciences of DKU),
-Joohyun Lee (Assistant professor of biology of DKU),
-Anastasia Tsigkou (Associate Professor of Biology of DKU),
-Ming-Chun Huang (Associate professor of data and computational science of DKU),
-Liqi Ren (Associate Director for Innovation and Entrepreneurship).</p>
-<p>After the presentation,
-Prof. Lee and Dr. Tsigkou presented valuable questions and suggestions.</p>
-<p>Prof. Lee recognized the difficulty of antibody therapy and
-informed us of the clear restrictions of FDI approval.
-We assured him that our project nanobodies are thoroughly researched,
-and that we will continue to modify the project to enhance biosafety.
-Dr. Tsigkou asked us about the binding affinity test and false positive.
-This is a question that did not come to us then, so we answered that
-the detection is conduct through fluorescence microscopy.</p>
-<p>After discussion with our PI, Prof. Linfeng Huang,
-we decide that we will use the pull down method
-in the detection of binding affinity.
-We will conduct the experiment by pulling down on
-both sides of the nanobody-antigen complex.
-For false positives, DKU iGEM member Lingrui Lai suggested isotype testing.</p>
-<h2 id="interview-with-prof-floyd"><a class="header" href="#interview-with-prof-floyd">Interview with Prof Floyd</a></h2>
-<p>After we successfully predicted the 3d structure of fusion protein-antibody
-complex by using Robetta and Alphafold2, the focus shift to how the fusion
-protein will influence the binding (docking) between antibody and antigen. We
-plan to get some insights about this from computer modeling before the wet lab
-begins.</p>
-<p>We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University
-for suggestions on our protein docking simulation.</p>
-<p>At the beginning, team leader Lisa Wu introduced the synthetic biology part of
-our project. Modeling team leader Zhenyu Xu introduced the progress of protein
-structure prediction and the need for protein docking simulation.</p>
-<p>As a scientist working in modern medicine, Prof. Floyd pointed us to some
-useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These
-software are powerful at predicting the docking scenario and are used by many
-researchers, with many online teaching resources accessible.</p>
-<p>To improve the speed of computer modeling, Prof. Floyd emphasized the
-preprocessing of protein structures. Namely, the antigen structure. He
-suggested us delete the floating molecules outside the binding sites and keep
-those inside, since we only care about the binding scenario. He also pointed
-that virtual screening could help if we want to do more mutations to the
-binding sites. Concerning the fusion protein-antibody complex models, since
-they are the optimal prediction given by Robetta and Alphafold2, we assume
-these models do not need preprocessing anymore.</p>
-<p>For docking, he suggested us try rigid docking first, and then flexible docking
-if we want to get closer to reality.</p>
-<h2 id="journal-club"><a class="header" href="#journal-club">Journal Club</a></h2>
-<p>In order to have better educational effect and promote our project , we
-organized the Journal Club activity in the Duke Kunshan community.</p>
-<p>The first Journal Club was held on April 30th, 2022. At the very beginning of
-the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us
-and introduced in detail what systems biology is and the basic methods of
-studying systems biology. This journal club event mainly focused on COVID-19
-and then developed into three sub-topics including the antigen test for
-SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray
-presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the
-iGEM team, around 10 freshman students with various backgrounds participated in
-the sharing and raised many inspiring questions.</p>
-<h2 id="interview-with-dr-neel-joshi"><a class="header" href="#interview-with-dr-neel-joshi">Interview with Dr. Neel Joshi</a></h2>
-<h3 id="introduction"><a class="header" href="#introduction">Introduction</a></h3>
-<p>Dr. Neel Joshi is an expert in bioengineering
-with tracks in human disease and new therapies.
-In his 2019 and 2021 literature,
-he and his team described genetically engineering E. coli Nissle 1917
-to treat some gastrointestinal diseases like bowel inflammation,
-which provide essential references for our project.
-To further understand the logics and advantages of this bioengineered model,
-we invited Dr. Joshi for an interview.</p>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/dr-joshi-interview1.png" alt="Dr. Joshi interview photo 1" /></p>
-<h3 id="interview-content"><a class="header" href="#interview-content">Interview Content</a></h3>
-<p><strong>Q:</strong>
-What stimulated you and your team to develop
-the surface-displaced single domain antibodies?
-What practical problems do you think this model can solve?</p>
-<p><strong>A:</strong>
-Although the nanobodies have great potentials in treating gastrointestinal diseases,
-it is somewhat hard to deliver those nanobodies directly to the digestive track.
-Therefore,
-the probiotics can serve as a scaffold to make the delivery of nanobodies easy.</p>
-<p><strong>Q:</strong>
-But why did you choose to display the nanobodies on the surface?
-Why not directly make the bacteria synthesize nanobodies and release them?</p>
-<p><strong>A:</strong>
-The surface display resolution has the property of multi-valency.
-By displaying the nanobodies on the surface,
-we would have the potential to space the binding domains together
-to bind to a pathogen surface.
-It could increase binding affinity and decrease the dissociation constant.
-It can also diffusion into different directions and increase the local concentration.</p>
-<p><strong>Q:</strong>
-What about the method of drug delivery?
-That is to say,
-how do you decide to send the engineered probiotics to human gastrointestinal track?
-And could you explain why you use that delivery method?</p>
-<p><strong>A:</strong>
-We only proposed an approach of micro biological therapy.
-But to deliver the bacteria,
-I think it can be freeze-dried to produce a freeze-dried product.
-Because a large portion of the geographical locations
-that suffered from these gut problems are the poor areas,
-and those areas do not have the condition
-to store the bacteria that require a very low temperature.
-The freeze-dried products do not require that strict storage conditions,
-so they are more available in those areas.</p>
-<p><strong>Q:</strong>
-Why pBbB8k plasmid backbone with kanamycin selection marker?
-(what's the difference between pUC19,
-which is our choice,
-and pBbB8K?)</p>
-<p><strong>A:</strong>
-pBbB8k is a rather arbitrary choice,
-we simply chose it
-because it was used due to antibiotics incompatibility in the previous experiment.
-When doing in vivo studies,
-we engineered plasmids from the original E. coli Nissle genome,
-the pMUT plasmids.
-These plasmids are more stable than the pBbB8K.
-For pUC19,
-I don’t see problems with the expression of pUC19 plasmid.
-However,
-you do need to consider if your antibiotic resistant marker
-in the plasmid is compatible with the shigella testing.
-If shigella is killed due to the antibiotic selecting E. coli,
-it can be a problem.</p>
-<p><strong>Q:</strong>
-What are the setbacks of
-the Probiotic-associated therapeutic curli hybrids (PATCH) system?</p>
-<p><strong>A:</strong>
-The first is safety concerns of curli fibers.
-It has been known that curli fibers induce various types of diseases,
-including neurological diseases,
-etc.
-The other is inherit disadvantages for E. coli to produce curli fibers in vivo.
-However,
-we have been able to shown effective production of curli fiber in vivo
-by measuring the amount of curli fibers coming from the fecal samples.</p>
-<p><strong>Q:</strong>
-What if the E. coli went out of control and grow infinitely in the gut,
-disrupting the original gastrointestinal microorganism environment?</p>
-<p><strong>A:</strong>
-This is a very popular question when it comes to distributing microbes to gut.
-Actually,
-we could use some of the auxotrophic strains to limit the growth of the bacteria.
-And I think there are many “switchesâ€
-that can turn on the suicide program of those bacteria.
-But in this case,
-I think E. coli Nissle 1917 is a very safe bacteria,
-it has already been identified as a harmless bacterium,
-so there should be less safety issues of this strain.</p>
-<h3 id="qa-section"><a class="header" href="#qa-section">Q&A Section</a></h3>
-<p><strong>Q:</strong>
-Is it possible to apply magnetic triggers to shigella infection
-and cooperate this into the PATCH system?</p>
-<p><strong>A:</strong>
-Magnetic triggers are mostly applied in cancer treatment.
-This is because in cancer,
-you know the spot of the disease.
-In bacterial infection it’s hard to locate.</p>
-<p><strong>Q:</strong>
-In Barta et al.,
-the authors described the different indexes of the nanobodies,
-including binding domains and neutralization effects.
-What is your rationale when choosing the nanobodies?</p>
-<p><strong>A:</strong>
-It really depends on how you generate the nanobodies.
-When different parts of the pathogen are used in Alpaca immunizations,
-the nanobodies will vary.
-When displaying the nanobodies,
-some work and others don’t.
-We assume this is because of folding problems,
-but we did not figure out the exact reason.</p>
-<p><strong>Q:</strong>
-What do you think about sequence optimization in silica?
-Do you have experience working with this?
-Do you have any suggestions?</p>
-<p><strong>A:</strong>
-I would suggest generating different mutations in the sequence
-and do some docking analysis.
-Then generate the mutations and do wet labs.</p>
-<p><strong>Q:</strong>
-Our project aims to tackle the antibiotic resistance problem worldwide.
-Would the PATCH system generate drug resistance issues?</p>
-<p><strong>A:</strong>
-This is possible.
-For example,
-a mutation in the binding domain of the antigen might cause binding problems.
-However,
-I would say the selective pressure by the nanobody is smaller
-compared to that of the antibiotic.
-This is because antibiotic kills the pathogen,
-while PATCH only binds to the pathogen,
-keeping it from invasive activities.</p>
-<p><strong>Q:</strong>
-We are worried
-that the proteins in the GI tract environment would coat the surface of the probiotic,
-which would cause dysfunction of the nanobodies.
-How did your team encounter this problem?</p>
-<p><strong>A:</strong>
-The animal model was effective,
-which was sufficient to show
-that the GI tract environment did not inhibit the binding activity.
-The curli production is continuous in vivo,
-which provides adequate chance for the binding to occur.
-However,
-the proteases in the GI tract is something to consider.</p>
-<h3 id="summary-and-reflection"><a class="header" href="#summary-and-reflection">Summary and Reflection</a></h3>
-<p>Dr. Joshi provided lots of perspectives from a brand-new aspect,
-which were extra inspirable for the whole team.
-First,
-Dr. Joshi elaborated on the practical problems
-that this model could potentially resolve.
-That the probiotic expression system could
-make the delivery of nanobodies easier expanded our understanding of
-the model as the delivery problem does not only exist in the step of bacteria delivery,
-it starts from the delivery of the essential nanobodies.</p>
-<p>Next,
-the freeze-dry delivery approach gives
-a less stricter storage condition of this drug,
-making it more available in poor areas,
-which corresponds with our assumed delivery method.
-As for the safety problem that the public is most interested in,
-Dr. Joshi proposed to use some molecular switches
-to eliminate those bacteria in addition to using safe strains like Nissle,
-giving important clue and indication for our project design.</p>
-<p>In the Q&A section,
-questions regarding drug localization,
-drug resistance,
-choice of nanobodies were mentioned by team members.
-Dr. Joshi gave many valuable advices depending on the questions.
-Overall,
-the interview was successful,
-and we were able to arm ourselves with adequate knowledge for the wet lab.</p>
-<h2 id="club-expo"><a class="header" href="#club-expo">Club Expo</a></h2>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/club-expo1.jpg" alt="Club expo figure 1" /></p>
-<p>We participated in 2022 online DKU club expo,
-introducing IGEM club to international students.
-Our club is meant to share knowledge and techniques of biosynthesis
-and to seek for potential team members of DKU IGEM team next year.
-The relevant club activities are conducted in the form of student presentation
-and speeches given by guest speakers.
-The IGEM team composition has also been introduced to
-DKU students from class of 2026.
-We divided IGEM teamwork into 4 parts,
-biological experiments,
-modelling,
-wiki design and human practice.</p>
-<p>For the offline club expo,
-we also made a small presentation to spread common knowledge about probiotics
-and provided our advice for consuming commercial probiotic products.
-Our central idea is that the aim of commercial probiotic products
-should be limited to minor gut discomforts or hoping to improve general health,
-and long-term consumption is not suggested by doctors we consulted.
-Also, we introduced some potential harms of consuming probiotics,
-trying to give them <!-- todo: what is them -->
-a full image of the commonly advertised probiotic products.
-We brought some experimental equipment,
-such as microcentrifuge tubes and plates,
-to introduce some basic experimental skills.
-Students who attended the club expo got basic knowledge of
-how to streak in an agar plate
-and how to use micropipette and centrifuge machines.
-Besides providing basic knowledge and doing the offline presentation,
-we prepared some interesting questions related to Biology and gut microbiomes
-for college students from all majors.
-They were designed to enlarge their knowledge about gut microbiomes
-and make biology interesting.
-The questions include "how H. pylori were proved to be able to cause ulcers,"
-"pick out the probiotics from several names of microorganisms,"
-"estimate the number of microorganisms in their stomach,"
-and so on.</p>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/club-expo2.jpg" alt="Club expo figure 2" /></p>
-<h2 id="gi-tract--probiotics-brochure"><a class="header" href="#gi-tract--probiotics-brochure">GI tract & Probiotics Brochure</a></h2>
-<h3 id="gi-tract"><a class="header" href="#gi-tract">GI Tract</a></h3>
-<p>The human GI (Gastrointestinal) tract consists of stomach (pH = 2),
-small intestine (pH = 4-5),
-and large intestine (pH = 7),
-which comprises 200 m^2 of surface area in total (<strong>Figure 1</strong>).
-It is responsible for the digestion of food and absorption of nutrients.</p>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/the-gi-tract.jpg" alt="Figure_1" /> </p>
-<p><strong>Figure 1</strong> | The GI tract. <sup class="footnote-reference"><a href="#Peate">1</a></sup></p>
-<h3 id="gi-microbiome"><a class="header" href="#gi-microbiome">GI Microbiome</a></h3>
-<p>A normal functioning human body contains the visible human organs,
-such as the heart,
-lung,
-brain etc.
-containing 10^-14 cells (~23000 genes),
-and the invisible microbiome,
-which is a group of up to 10^-14 million microbes (~9 million genes)
-that live in your body.
-These bacteria help with digestion,
-destroys harmful bacteria,
-and helps control your immune system.
-The interaction between the host (human) and its microbiota is complex;
-thus,
-knowing the human microbiome helps with the development of
-biomarkers for predicting predisposition to diseases,
-designing targeted therapies,
-personalized drug therapies and probiotics.</p>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/oversight-microbial-populations.png" alt="Figure_2" /></p>
-<p><strong>Figure 2</strong> | Oversight of major microbial populations
-in the body sites sampled by human microbiome projects. <sup class="footnote-reference"><a href="#Brock">2</a></sup></p>
-<p>The GI microbiota contains 10^13 to 10^14 microbial cells.
-Microbes in gut affect early development,
-health,
-and predisposition to disease.
-The microbial colonization of gut begins at birth.
-As is shown in <strong>Figure 2</strong>,
-from sampling data of the human microbiome project,
-in the GI tract,
-the species <em>Bacteroidetes</em> and <em>Firmicutes</em> have the highest abundance,
-followed by <em>Proteobacteria</em>,
-<em>Tenericutes</em>,
-and others.
-The microbial population in different areas of the GI tract are influenced by
-diet and the physical conditions in the area.
-In the stomach and small intestine,
-the low pH level prevents the growth and colonization of many microbials;
-however,
-<em>Firmicutes</em>,
-<em>Bacteroidetes</em>,
-and <em>Actinobacteria</em> are commonly found in the gastric fluid,
-while <em>Firmicutes</em> and <em>Proteobacteria</em> are common in the mucus layer of the stomach.
-Some pathogens,
-such as <em>Helicobacter pylori</em>,
-are also discovered in the gastric mucosa.</p>
-<p><img src="https://static.igem.wiki/teams/4161/wiki/microenvironments-large-intestine.png" alt="Figure_3" /></p>
-<p><strong>Figure 3</strong> | Different microenvironments in the large intestine. <sup class="footnote-reference"><a href="#Brock">2</a></sup></p>
-<p>The microbiome in the large intestine generally serves as
-an in vivo fermentation vessel,
-with the microbiota using nutrients derived from the digestion of food
-(<strong>Figure 3</strong>).
-The essential biochemical and metabolic contributions of
-intestinal microorganisms contain different types of vitamins (e.g.,
-thiamine,
-riboflavin,
-pyridoxine,
-B12,
-K,
-etc.),
-amino acids (e.g.,
-asparagine,
-glutamate,
-methionine,
-etc.),
-gases (e.g.,
-CO2,
-CH4,
-H2),
-odor,
-organic acids,
-glycosidase reactions,
-and steroid metabolism.
-As a result,
-the pathological changes in the GI tract microbiome may lead to deficiencies in
-important metabolic reactions (e.g.,
-lack of vitamin B12 may lead to pernicious anemia
-– the red blood cells cannot function well).</p>
-<h3 id="gi-microbiome-antibiotics-and-probiotics"><a class="header" href="#gi-microbiome-antibiotics-and-probiotics">GI Microbiome, Antibiotics, and Probiotics</a></h3>
-<p>Currently,
-physicians usually recommend using antibiotics when treating GI tract bacterial infections.
-However,
-since antibiotics usually also kill the beneficial microbiota,
-it increases the risk of developing IBD (inflammatory bowel disease) after treatment.
-IBD is characterized of chronic inflammation of the GI tract,
-which may result in irreversible damage.
-In addition,
-some antibiotics can cause ADR (adverse drug reaction) and allergies.
-Therefore,
-the development of alternative treatment methods,
-such as the use of probiotics,
-have attracted much attention.
-Unlike antibiotics,
-probiotics do not kill all the bacteria in an unbolted way.
-They help inhibit the growth of pathogens
-and preserve the healthy microbiota via competitive exclusion,
-anti-adherence,
-etc.
-Recently,
-engineered probiotics have also become a hot topic for new drug development.</p>
-<h3 id="reference"><a class="header" href="#reference">Reference</a></h3>
-<div class="footnote-definition" id="Brock"><sup class="footnote-definition-label">2</sup>
-<p>Brock, T. D., Madigan, M. T., Martinko, J. M., & Parker, J. (2003). Brock biology of microorganisms. Upper Saddle River (NJ): Prentice-Hall, 2003.</p>
-</div>
-<div class="footnote-definition" id="Peate"><sup class="footnote-definition-label">1</sup>
-<p>Peate, I. (2018). Anatomy and physiology, 9. The gastrointestinal system. British Journal of Healthcare Assistants, 12(3), 110–114. <a href="https://doi.org/10.12968/bjha.2018.12.3.110">https://doi.org/10.12968/bjha.2018.12.3.110</a></p>
-</div>
+<h1 id="integrated-human-practice"><a class="header" href="#integrated-human-practice">Integrated Human Practice</a></h1>
+<p>Antibiotic resistance is a problem in its scale and subtlety.
+Shigella infection has its significance in antibiotic resistance because of its identity as one of the most antibiotic resistant bacterias recognized by CDC. In our integrated human practice, we followed the procedure of research-design-engagement-modification. </p>
+<h2 id="recognizing-the-problem-and-designing-the-approach"><a class="header" href="#recognizing-the-problem-and-designing-the-approach">Recognizing the problem and designing the approach</a></h2>
+<p>The subtlety of antibiotic resistance did not come to mind until some of the team members took the microbiology class at DKU:
+From the amazing lectures given by Dr. Linfeng Huang, we realized that the race against bacterial infection is largely dependent on discoveries of newly synthesized drugs. People modify the drug molecule by perhaps a small sidechain, changing the chemical property but perhaps not changing the chemical property. This can lead to significant advances because it can possibly alter the pathogen's ability to recognize the drug, therefore no longer maintain its resistance. </p>
+<p>Antibiotics are thus labeled as the best weapon. It is almost always the solution to infections. It can be bought at ordinary pharmacies, and are consumed at a scale larger than ever. From talking with the people around us, we realized that the lack of knowledge of antibiotic resistance exists as possibly a larger threat than the pathogen itself. </p>
+<p>We ask ourselves: What if one day, we have exhausted all the combinations of chemicals? What if we lose the race because we have strengthened antibiotic resistance to the point of no return?</p>
+<p>And clearly this has been considered. The field of immunology has become more heated than ever before. What if we could deploit the weapon that is the gift of the creation-our own immune systems?</p>
+<p>We looked into nanobody therapy, because it is easy to perform in our lab, and effective nanobodies for Shigella T3SS has been revealed by previous studies.</p>
+<h2 id="engaging-stakeholders"><a class="header" href="#engaging-stakeholders">Engaging stakeholders</a></h2>
+<p>We further consulted experts in this area, including Dr. Neel Joshi from Northwestern University, whose lab had worked on nanobody therapy and bacterial surface display. He answered our questions about the choice of probiotics and gave us more information on the multi-valency potential of the surface display method. He also reminded us that areas with high shigella infection rates and mortality are usally underdeveloped areas, thus we should consider the delivery method to be economic friendly and easy to maintain. In the interview with Dr. Lin from SINOVAC, he suggested that our final design should consider safety, effectiveness and economics. <a href="entrepreneurship.html">See entrepreneurship for more details.</a> To engage with the general public in our design, we distributed a questionaire and received over 500 responses on what people know about antibiotic resistance and shigella infection, and identified potential barriers of drug distribution to the general public. <a href="https://static.igem.wiki/teams/4161/wiki/general-public-questionaire-report.pdf">See our report here.</a></p>
+<h2 id="modification"><a class="header" href="#modification">Modification</a></h2>
+<p>In aspect of our design, we adopted the PATCH system by Dr. Neel Joshi, for better multivalency performance. We also changed our design logic: our drug is more vaccine orientated than the conventional drug designs. The drug should be ideal for prevention of regional spread of shigella infection, acting as a blocking agent for further transmission. The delivery method is in freeze-dried powder, delivered in economic-friendly microcapsules. For the advice from Dr. Lin, we made multiple modifications that would promote the safety and effectiveness of our design. <a href="entrepreneurship.html">See entrepreneurship for more details.</a> As for the general public response, we found one major problem, which is that a significant amount of people see E.<em>coli</em> as the main causative agent for dysentery syndrome. We assessed that this may cause major problems if we reveal our approach as probiotic-nanobody therapy, in specific, yeast and E.<em>coli</em> Nissle 1917 can be subject to public opinions including skepticism. Therefore, we attempted educational approaches to give more information on probiotics at both DKU and local high schools.</p>
+<h2 id="conclusion"><a class="header" href="#conclusion">Conclusion</a></h2>
+<p>Our integrated human practices influenced our experimental design, and the overall logic of our project. We are able to engage with our stakeholders and the general public, acheiving satisfying outcomes. Engagement is the key to creating a project design with actual social impact, and we will carry this spirit on as we progress further into our project and future careers.</p>
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+ <img src="https://static.igem.wiki/teams/4161/wiki/wet-lab-for-bg.png" />
+</div>
<h2 id="infection-precaution"><a class="header" href="#infection-precaution">Infection Precaution</a></h2>
<p>The end-products of our project are small tablets or capsules that contain dry
powders of probiotics that express anti-Shigella antibodies on their surface.
@@ -111,13 +114,13 @@ unsanitary water in high diarrhea incidence areas. In consideration of the
prevalent transmission pathways of Shigella, we also suggest people whose
family members have developed Shigella infections and children in school with
diarrhea cases take our tablets to prevent person-to-person transmission, which
-is the major form of Shigella spreading (Kotloff et al., 2018).</p>
+is the major form of Shigella spreading <sup class="footnote-reference"><a href="#Kotloff,2018">1</a></sup>.</p>
<h2 id="infection-therapy"><a class="header" href="#infection-therapy">Infection Therapy</a></h2>
<p>Due to intracellular pathogen nature of Shigella, the effect of antibodies
reduces as pathogens evade into the cells. The ability of reprogramming the
infected cells to form protrusion adjacent cells allows Shigella to spread
within intestine epithelial cells, reducing the chance of exposing to body
-internal environment (Sansonetti et al., 1994). This special characteristic
+internal environment <sup class="footnote-reference"><a href="#Sansonetti,1994">2</a></sup>. This special characteristic
implies antibody may not be a one-size-fits-all solution for different stages
of infection. We call for the combination of clinical phases of antibiotics
treatment with our tablets together.</p>
@@ -141,15 +144,24 @@ need to be performed to prevent possible anaphylaxis. Besides, considering the
pathogenesis and transmission pathway of Shigella, our products may not be a
one-size-fits all solution for all infection stages but focuses more on the
prevention of infection.</p>
-<ol>
-<li>Kotloff, K. L., Riddle, M. S., Platts-Mills, J. A., Pavlinac, P., & Zaidi, A. K. M. (2018). Shigellosis. The Lancet, 391(10122), 801-812. https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8 </li>
-<li>Sansonetti, P. J., Mounier, J., Prévost, M. C., & Mège, R.-M. (1994). Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell, 76(5), 829-839. https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1 </li>
-</ol>
+<h2 id="references"><a class="header" href="#references">References</a></h2>
+<div class="footnote-definition" id="Kotloff,2018"><sup class="footnote-definition-label">1</sup>
+<p>Kotloff, K. L., Riddle, M. S., Platts-Mills, J. A., Pavlinac, P., & Zaidi, A. K. M. (2018). Shigellosis. The Lancet, 391(10122), 801-812. <a href="https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8">https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8</a></p>
+</div>
+<div class="footnote-definition" id="Sansonetti,1994"><sup class="footnote-definition-label">2</sup>
+<p>Sansonetti, P. J., Mounier, J., Prévost, M. C., & Mège, R.-M. (1994). Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell, 76(5), 829-839. <a href="https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1">https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1</a></p>
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+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
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Creative Commons Attribution 4.0 International license
diff --git a/public/improve.html b/public/improve.html
index c989c63b2083d1a165a992c8e2197c21f33c78d9..6f2d061240be616235f3afcfc4dd530d946f0a36 100644
--- a/public/improve.html
+++ b/public/improve.html
@@ -39,7 +39,7 @@
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+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item expanded "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item expanded "><a href="improve.html" class="active">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
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@@ -99,11 +99,21 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
+<h2 id="part-improvement"><a class="header" href="#part-improvement">Part improvement</a></h2>
+<p>Our part <a href="http://parts.igem.org/Part:BBa_K4161301">BBa_K4161301</a> is an improvement of part <a href="http://parts.igem.org/Part:BBa_K416000">BBa_K416000</a> from iGEM10_NYU (2010).</p>
+<p>In 2010, iGEM10_NYU designed the part “BBa_K416000†which was the CDS of Aga2 protein for yeast surface display. The part was achieved by deleting the stop codon of the Aga2 CDS region from vector pCTCON2 so that the element can be fused with other fragments to express fusion proteins.</p>
+<p>On the basis of this part, we designed the integrated expression module “BBa_K4161301â€. This part integrated the yeast surface protein Aga2, GAL1 promotor, nanobody 20ipaD, and 3xFLAG tag sequences, which make it a complete expression module that is controllable. The addition of GAL1 promotor ensures the whole surface display part would only be induced by galactose and denied the leaky expression. The nanobody segment provides the real function for the whole module so that it can bind to its corresponding antigen to inhibit pathogens like Shigella. Additionally, the 3xFLAG tag eases the detection of the expression of this module.</p>
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+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/inclusivity.html b/public/inclusivity.html
index 6aeefb7fad97dadf9f7b80e5b6f2e9399a9bd19c..2e4ef9b700bbf712984b2dcb2a5c732f3da2a6bd 100644
--- a/public/inclusivity.html
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@@ -39,7 +39,7 @@
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@@ -104,6 +104,12 @@
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index 42da6ee467411d6f360bbc60402e5ab0339de03b..065496f3c772dcaceb068770ef05899841b37377 100644
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@@ -39,7 +39,7 @@
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+<img alt="G"" src="https://static.igem.wiki/teams/4161/wiki/logo-transparent.png" class="w-16" />ut<img alt="G"" src="https://static.igem.wiki/teams/4161/wiki/logo-transparent.png" class="w-16" />uard</h1>
+<div id="promotion_video" class="flex justify-center">
+<iframe title="DKU: GutGuard (2022) - Project Promotion [English]" width="560" height="315" src="https://video.igem.org/videos/embed/c28db71c-27b0-4945-863c-3aed20c3bfde" frameborder="0" allowfullscreen="" sandbox="allow-same-origin allow-scripts allow-popups" class="py-40"></iframe>
</div>
-<article class="grid grid-flow-col grid-cols-2 gap-20 pb-40">
+<article class="grid grid-flow-col grid-cols-2 gap-20 py-40">
<div>
<p>Shigella, as one of the most antibiotic resistant pathogens,
poses a great threat to food safety especially in developing areas.</p>
@@ -114,10 +119,11 @@ poses a great threat to food safety especially in developing areas.</p>
<p>Side effects include degration of GI tract microbiome,
and the emergence of more antibiotic resistant strains.</p>
</div>
-<img alt="logo" src="https://static.igem.wiki/teams/4161/wiki/logo-transparent.png" class="w-full" />
+<img alt="Figure 1" src="https://static.igem.wiki/teams/4161/wiki/hmpg1-1-main.png" class="w-full" />
+<img alt="Figure 1 legend", src="https://static.igem.wiki/teams/4161/wiki/hmpg1-1-legend.png", width = "50", height = "46"/>
</article>
-<article class="grid grid-flow-col grid-cols-2 gap-20 pb-40">
-<img alt="logo" src="https://static.igem.wiki/teams/4161/wiki/logo-transparent.png" class="w-full" />
+<article class="grid grid-flow-col grid-cols-2 gap-20 py-40">
+<img alt="Figure 2" src="https://static.igem.wiki/teams/4161/wiki/hmpg-2.png" class="w-full" />
<div>
<p>We are in an endless race against pathogens.</p>
<p>Antibiotics are our weapons. Mutations are their strategies to survival.</p>
@@ -126,20 +132,20 @@ and the emergence of more antibiotic resistant strains.</p>
<p>It is different from antibiotics and can be more effective when triggering the host immune system.</p>
</div>
</article>
-<article class="grid grid-flow-col grid-cols-2 gap-20 pb-40">
+<article class="grid grid-flow-col grid-cols-2 gap-20 py-40">
<div>
<p>However, conventional antibodies have a high cost because of the complicated synthesis procedure.</p>
<p>It can also be vulnerable to proteosomes in the GI tract.</p>
</div>
-<img alt="logo" src="https://static.igem.wiki/teams/4161/wiki/logo-transparent.png" class="w-full" />
+<img alt="Figure 3" src="https://static.igem.wiki/teams/4161/wiki/hmpg-3.png" class="w-full" />
</article>
-<article class="grid grid-flow-col grid-cols-2 gap-20 pb-40">
-<img alt="logo" src="https://static.igem.wiki/teams/4161/wiki/logo-transparent.png" class="w-full" />
+<article class="grid grid-flow-col grid-cols-2 gap-20 py-40">
+<img alt="Figure 4" src="https://static.igem.wiki/teams/4161/wiki/hmpg-4.png" class="w-full" />
<div>
<p>Thus we propose a novel method to display nanobodies on the surface of probiotics.</p>
<p>It exploits the natural pathogen inhibition effects of the probiotics.</p>
<p>It also explores possibilities of antibody therapy mass production.</p>
-<p>Click on the left menu to learn more about the details.</p>
+<p>Click on the left menu to learn more.</p>
</div>
</article>
@@ -147,6 +153,12 @@ and the emergence of more antibiotic resistant strains.</p>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/measurement.html b/public/measurement.html
index c8fcf24016c755d28be7e3a7155219801e6b69ee..4006b6c6914068e952f3fe54fe94db0ce8e137e7 100644
--- a/public/measurement.html
+++ b/public/measurement.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
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+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item expanded "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item expanded "><a href="measurement.html" class="active">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -104,6 +104,12 @@
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/model.html b/public/model.html
index 51b3bb35e44a012b38811735e73dc39ca709d7cf..950cca8ba2c4c0a6e052299260be4f1b86015076 100644
--- a/public/model.html
+++ b/public/model.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item expanded "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item expanded "><a href="model.html" class="active">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item expanded "><a href="model.html" class="active">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -99,12 +99,15 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="model"><a class="header" href="#model">Model</a></h1>
+<div class="h1-bg">
+ <h1 class>Model</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/model-bg.png" />
+</div>
<p>Models are powerful tools in terms of imagining reasonable future scenarios. Also,
assumptions and results from the model push us to reflect on the present situation
and make adjustments to our existing plans and experiments, which might also develop
our final goal into a more realistic version.</p>
-<p>There are 2 modeling sections in our project:</p>
+<p>There are 3 modeling sections in our project:</p>
<ul>
<li>
<p><strong>Visualization</strong><br />
@@ -117,9 +120,16 @@ This section mainly describes the efficiency of protein expression, and tries to
predict the scenario after a patient
takes the drug.</p>
</li>
+<li>
+<p><strong>Hardware</strong><br />
+This section shows the 3D model of the micro-capsule where Yeast cells are sealed in.
+The micro-capsule is made of shellac, and the pH-dependent solubility that
+prefers a mild basic environment makes shellac perfect for
+releasing probiotics in intestines.</p>
+</li>
</ul>
-<h1 id="visualization"><a class="header" href="#visualization">Visualization</a></h1>
-<h2 id="overview"><a class="header" href="#overview">Overview:</a></h2>
+<h2 id="visualization"><a class="header" href="#visualization">Visualization</a></h2>
+<h3 id="overview"><a class="header" href="#overview">Overview:</a></h3>
<p>We used online softwares to help us visualize the 3D protein structures and
modeled
their docking
@@ -128,7 +138,7 @@ and then we evaluated their stability by using some common parameters. This
section
aims to visually display the protein structure synthesized in this project and
provide ideas or directions for future experiments or experimental teams</p>
-<h3 id="part-1-general-pattern"><a class="header" href="#part-1-general-pattern">Part 1: General pattern</a></h3>
+<h4 id="part-1-general-pattern"><a class="header" href="#part-1-general-pattern">Part 1: General pattern</a></h4>
<p>Our team designed DNA sequences for fusion protein-nanobody complex
ourselves<!-- todo: from what -->
and these newly designed protein's 3D structures are unknown.
@@ -137,7 +147,7 @@ which,
in our case,
would be the nanobody's docking on the membrane and its binding to the antigen.</p>
<!-- todo: review -->
-<h4 id="protein-structure-prediction"><a class="header" href="#protein-structure-prediction">Protein structure prediction</a></h4>
+<p><em><strong>Protein structure prediction</strong></em></p>
<p>Based on the amino acid sequence of the protein, various algorithms can predict
the
protein's 3D structure. These algorithms use machine learning to learn from
@@ -185,7 +195,7 @@ automatically produces
the model with highest score.</p>
<p>We view these pdb files in PyMOL<sup class="footnote-reference"><a href="#PyMOL">6</a></sup>, a powerful tool for 3D structure
visualization.</p>
-<h4 id="protein-structure-evaluation"><a class="header" href="#protein-structure-evaluation">Protein structure evaluation</a></h4>
+<p><em><strong>Protein structure evaluation</strong></em></p>
<p>Assessment of these resultant structures from Robetta and Alphafold2 is needed
for
deciding which structure is more credible and can be used in future anlysis.
@@ -225,14 +235,14 @@ be higher than 80% for a good model. <sup class="footnote-reference"><a href="#S
<li>Overall quality factor:<br />
An overall score for the model provided by SAVES server<sup class="footnote-reference"><a href="#SAVES">7</a></sup>, ranging from 0
to 100.
-It should be higher than 80 for a good model.</li>
+It should be higher than 80 for a good model.<sup class="footnote-reference"><a href="#Standard">10</a></sup></li>
<li>Z-score:<br />
Indicate whether the z-score of the input structure is within the range of
scores typically
found for native proteins of similar size<sup class="footnote-reference"><a href="#ProSA">8</a></sup>.</li>
</ol>
<p>All the structures shown later are the highest scoring structures.</p>
-<h4 id="protein-structure-alignment"><a class="header" href="#protein-structure-alignment">Protein structure alignment</a></h4>
+<p><em><strong>Protein structure alignment</strong></em></p>
<p>After the evaluation of models we got from Robetta<sup class="footnote-reference"><a href="#Robetta">1</a></sup> and AlphaFold Colab
notebook<sup class="footnote-reference"><a href="#AlphaFoldPh">3</a></sup>, we can compare the antibody structure in the model with
its original
@@ -242,12 +252,12 @@ is very low,
we regard two structures similar, which means the nanobody in our
fusion-nanobody complex
will theoretically function well.</p>
-<h3 id="part-2-yeast-20ipad-visualization"><a class="header" href="#part-2-yeast-20ipad-visualization">Part 2: Yeast-20ipaD visualization</a></h3>
+<h4 id="part-2-yeast-20ipad-visualization"><a class="header" href="#part-2-yeast-20ipad-visualization">Part 2: Yeast-20ipaD visualization</a></h4>
<p>We have successfully expressed the fusion protein-nanobody complex, which is
Yeast-20ipaD.
Here is the highest-scoring structure of Yeast-20ipaD (<strong>Figure 1</strong>).</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/fig1-yeast-20ipad.png"
-width="500"/></p>
+/></p>
<p><strong>Figure 1</strong> | 3D structure of Yeast-20ipaD complex</p>
<p>Ramachandran plot of the above structure showed that
85.1% of residues are in the most favorite regions,
@@ -268,7 +278,7 @@ The calculated average energy over 40 residues is always under 0. Overall, the
above structure
can be regarded as a good model of Yeast-20ipaD.</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/fig2-alignment.png"
-width="500"/></p>
+/></p>
<p><strong>Figure 2</strong> | Alignment of 20ipaD between itself in complex and it's original
structure.</p>
<p>The alignment between 20ipaD in the complex
@@ -276,48 +286,48 @@ and 20ipaD's original structure shows that our complex can
have good effect theoretically (<strong>Figure 2</strong>). The RMSD value is tested to
be 0.807, which means the complex have little influence on the
structure of 20ipaD.</p>
-<h3 id="part-3-docking-modeling"><a class="header" href="#part-3-docking-modeling">Part 3: Docking modeling</a></h3>
+<h4 id="part-3-docking-modeling"><a class="header" href="#part-3-docking-modeling">Part 3: Docking modeling</a></h4>
<p>Interaction imformation (binding sites) of 20ipaD and ipaD
is found in the paper: <em><strong>Single-Domain Antibodies Pinpoint Potential Targets
within Shigella
Invasion Plasmid Antigen D
-of the Needle Tip Complex for Inhibition of Type III Secretion</strong></em> <sup class="footnote-reference"><a href="#Binding">10</a></sup>.
+of the Needle Tip Complex for Inhibition of Type III Secretion</strong></em> <sup class="footnote-reference"><a href="#Binding">11</a></sup>.
Since the alignment shows that the 20ipaD
in complex is almost the same with it's
original structure, we can default the binding sites unchanged. Below is the
binding sites between 20ipaD and ipaD (<strong>Figure 3</strong>).</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/fig3-binding-positions.png"
-width="500"/></p>
+/></p>
<p><strong>Figure 3</strong> | Binding sites between 20ipaD and Ipad</p>
-<p>We provided the interaction information for online server HADDOCK <sup class="footnote-reference"><a href="#HADDOCK">11</a></sup> to
+<p>We provided the interaction information for online server HADDOCK <sup class="footnote-reference"><a href="#HADDOCK">12</a></sup> to
simulate the docking between the complex and ipaD.
Below is the docking structure
(<strong>Figure 4</strong>).</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/fig-4-docking-result.png"
-width="500"/></p>
-<p><strong>Figure 4</strong> | Docking between 20ipaD (in complex)
+/></p>
+<p><strong>Figure 4</strong> | Docking between 20ipaD (in complex)
and IpaD</p>
-<p>Ramachandran plot of the above structure showed that
-85.0% of residues are in the most favorite regions,
-and 12.7% are in the allowed regions; 1.2% of the residues are in the generously allowed regions
-and 1.0% in the disallowed regions.
-The Atomic-Z-score RMS is tested to be 1.441, which is relatively close to 1.
+<p>Ramachandran plot of the above structure showed that
+85.0% of residues are in the most favorite regions,
+and 12.7% are in the allowed regions; 1.2% of the residues are in the generously allowed regions
+and 1.0% in the disallowed regions.
+The Atomic-Z-score RMS is tested to be 1.441, which is relatively close to 1.
The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 87.61%.
The overall quality factor is 85.53, which is acceptable.
-ProSA calculated Z-score is -7.16, which falls in the range of scores typically found for
-experimentally determined (X-ray, NMR) structure for native proteins of similar size in
+ProSA calculated Z-score is -7.16, which falls in the range of scores typically found for
+experimentally determined (X-ray, NMR) structure for native proteins of similar size in
PDB database.
The calculated average energy over 40 residues is always under 0.
Overall, the above structure indicates that 20ipaD can bind with IpaD well theoretically.</p>
-<p>Below is the alignment between our docking result and the original docking
-between 20ipaD and IpaD.
-RMSD is 0.36, which is very small and acceptable. </p>
+<p>Below is the alignment between our docking result and the original docking
+between 20ipaD and IpaD.
+RMSD is 0.36, which is very small and acceptable.</p>
<p><img src="https://static.igem.wiki/teams/4161/wiki/fig-5-alignment-of-docking-and-original.png"
-width="500"/></p>
+/></p>
<p><strong>Figure 5</strong> | Alignment between Yeast-20ipaD-IpaD and 20ipaD-IpaD.</p>
-<p>All the above shows that our Yeast-20ipaD complex could theoretically work well
+<p>All the above shows that our Yeast-20ipaD complex could theoretically work well
when binding with IpaD.</p>
-<h3 id="part-4-other-combinations-of-probiotic-nanobody-complex"><a class="header" href="#part-4-other-combinations-of-probiotic-nanobody-complex">Part 4: Other combinations of probiotic-nanobody complex</a></h3>
+<h4 id="part-4-other-combinations-of-probiotic-nanobody-complex"><a class="header" href="#part-4-other-combinations-of-probiotic-nanobody-complex">Part 4: Other combinations of probiotic-nanobody complex</a></h4>
<p>In this section, we would like to show other possible combinations of fusion
protein-nanobody
complex that might theoretically function well. To do this, we modeled their 3D
@@ -325,6 +335,62 @@ structures
and their docking scenarios, and analyzed them. This could be helpful for
future experiment
and future teams.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/table-1-for-part-4-of-model.png"
+/></p>
+<p><strong>Table 1</strong> | Evaluation of other combinations of probiotic-nanobody complex</p>
+<p>The <em>E. coli</em> Intimin protein complex has good results in 4 out of 5 quantitative parameters,
+making it a great model.
+First, its Ramachandran plot reveals a good distribution in favored regions.
+83% of its residues are in the core regions, 14.7% are in the allowed regions, 1.3%
+are
+in the general regions and 0.9% in the disallowed regions.
+Second, the % amino acids having scored 0.2 in 3D/1D profile is 85.91%,
+higher than the standard 80%. Its atomic model is therefore
+fairly compatible with its amino acid sequence. Third, its overall quality factor,
+that accounts for the error value of individual residue, is at 92,
+surpassing the 80 score cut-off.
+Its Z-score is also within the range of scores found for native proteins
+of similar size. The main downside to this model is that Z-score is not around one,showing
+that
+it has greater average magnitude of the volume irregularities in the structure.</p>
+<p>The <em>E. coli</em> CsgA protein complex is a good model that
+fulfills 4 out of 5 quantitative parameters. Like Intimin, CsgA’s Ramachandran plot
+displays a good distribution in favored regions: 83.5% of
+residues are in the core regions, 12.7% are in the allowed regions, 2.0% are in
+the general regions and 1.8%
+in the disallowed regions. The % amino acids having scored 0.2 in 3D/1D profile
+is 84.27%, higher than the
+standard 80% but not nearly as high as Intimin. Its overall quality factor is
+91,exceeding the 80 score
+cut-off. The Z-score is within the range of scores found for native proteins of
+similar size, and like Intimin,
+the CsgA model’s Z-score is not around one.</p>
+<p>The Lacto tag 1 protein complex is a good model that fulfills 4 out of 5
+quantitative parameters. CsgA’s
+Ramachandran plot displays a well enough distribution in favored regions: 83.1%
+of residues are in the core regions,
+15.2% are in the allowed regions, 1.5% are in the general regions and 0.2% in
+the disallowed regions.
+The % of amino acids having scored 0.2 in 3D/1D profile is 79.97%, close enough
+to the standard 80% but
+comparatively low against Intimin and CsgA. Its overall quality factor is 92, surpassing
+the 80 score cut-off.
+The Z-score is within the range of scores found for native proteins of similar
+size, and similar to Intimin and CsGA,
+the CsgA model’s Z-score is not around one.</p>
+<p>Overall, all three protein docking jobs show satisfactory results and
+could be helpful for
+future experiments and future teams. In light of these promising findings,
+we encourage future
+researchers to test these models in the lab, with the <em>E. coli</em> Intimin model
+that performed the
+best among the three.</p>
+<h3 id="summary"><a class="header" href="#summary">Summary</a></h3>
+<p>To conclude, we have developed the best 3D model for Yeast-20ipaD
+and the docking structure between Yeast-20ipaD and IpaD. They are well analyzed
+and are decided to have good effect theoretically.
+Moreover, we modeled other 3 possible combinations of fusion protein and nanobody,
+which might serve as a guidance for future experiment design.</p>
<div class="footnote-definition" id="Robetta"><sup class="footnote-definition-label">1</sup>
<p>Robetta <a href="https://robetta.bakerlab.org">https://robetta.bakerlab.org</a></p>
</div>
@@ -334,17 +400,17 @@ and future teams.</p>
</div>
<div class="footnote-definition" id="AlphaFoldPh"><sup class="footnote-definition-label">3</sup>
<p>AlphaFold(Phenix Version)
-<https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf
+<<a href="https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf">https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf</a>
old2/AlphaFold2.ipynb></p>
</div>
<div class="footnote-definition" id="ColabFold"><sup class="footnote-definition-label">4</sup>
<p>ColabFold
-<https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol
+<<a href="https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol">https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol</a>
d2.ipynb></p>
</div>
<div class="footnote-definition" id="AlphaFold2Colab"><sup class="footnote-definition-label">5</sup>
<p>AlphaFold2
-<https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks
+<<a href="https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks">https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks</a>
/AlphaFold.ipynb></p>
</div>
<div class="footnote-definition" id="PyMOL"><sup class="footnote-definition-label">6</sup>
@@ -359,39 +425,213 @@ d2.ipynb></p>
<div class="footnote-definition" id="Z-scoreRMS"><sup class="footnote-definition-label">9</sup>
<p>Deviations from standard atomic volumes as a quality measure for
protein crystal structures
-<https://pubmed.ncbi.nlm.nih.gov/8950272/#:~:text=Deviations%20of%20the%20atomic
-%20volumes%20from%20the%20standard,magnitude%20of%20the%20volume%20irregularitie
-s%20in%20the%20structure.></p>
+<a href="https://pubmed.ncbi.nlm.nih.gov/8950272/">https://pubmed.ncbi.nlm.nih.gov/8950272/</a></p>
</div>
-<div class="footnote-definition" id="HADDOCK"><sup class="footnote-definition-label">11</sup>
+<div class="footnote-definition" id="HADDOCK"><sup class="footnote-definition-label">12</sup>
<p>HADDOCK online server <a href="https://wenmr.science.uu.nl/haddock2.4/">https://wenmr.science.uu.nl/haddock2.4/</a></p>
</div>
-<div class="footnote-definition" id="Binding"><sup class="footnote-definition-label">10</sup>
+<div class="footnote-definition" id="Binding"><sup class="footnote-definition-label">11</sup>
<p>Single-Domain Antibodies Pinpoint Potential Targets within Shigella
Invasion Plasmid Antigen D
of the Needle Tip Complex for Inhibition of Type III Secretion.
DOI: 10.1074/jbc.M117.802231
<a href="https://pubmed.ncbi.nlm.nih.gov/28842484/">https://pubmed.ncbi.nlm.nih.gov/28842484/</a></p>
</div>
-<h1 id="description-and-prediction-of-drug-efficacy"><a class="header" href="#description-and-prediction-of-drug-efficacy">Description and Prediction of drug efficacy</a></h1>
-<h2 id="overview-1"><a class="header" href="#overview-1">Overview:</a></h2>
+<div class="footnote-definition" id="Standard"><sup class="footnote-definition-label">10</sup>
+<p>Homology modeling and virtual screening approaches to identify potent inhibitors of VEB-1 β-lactamase.
+DOI: 10.1186/1742-4682-10-22
+<a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668210/">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668210/</a></p>
+</div>
+<h2 id="description-and-prediction-of-drug-efficacy"><a class="header" href="#description-and-prediction-of-drug-efficacy">Description and Prediction of drug efficacy</a></h2>
+<h3 id="overview-1"><a class="header" href="#overview-1">Overview</a></h3>
<p>Wet lab results showed that we have successfully expressed 20ipaD on the surface
of Yeast. Our goal is to describe
efficiency of expression and predict the scenario after the drug is released in the
patient's jejunal.</p>
-<h3 id="part-1-protein-expression-efficiency"><a class="header" href="#part-1-protein-expression-efficiency">Part 1: Protein expression efficiency</a></h3>
+<h4 id="part-1-protein-expression-efficiency"><a class="header" href="#part-1-protein-expression-efficiency">Part 1: Protein expression efficiency</a></h4>
<p>To describe how efficient is Yeast concerning the expression of 20ipaD, we manually
calculated the efficiency by counting the number of Yeast cells that expressed
-20ipaD and the total number of Yeast cells (<strong>Figure 1</strong>).</p>
-<img src="https://static.igem.wiki/teams/4161/wiki/fig1-efficiency-expression.png" width="800"/>
+20ipaD and the total number of Yeast cells (<strong>Figure 1</strong>).Through separated assessments conducted by two individuals, we found that our model has a 31.25% expression rate with a STD of ± 0.75.</p>
+<img src="https://static.igem.wiki/teams/4161/wiki/fig1-efficiency-expression.png"/>
<p><strong>Figure 1</strong> | Fluorescent cells for Yeast cells that obviously expressed 20ipaD.
Dark cells for no or very little expression</p>
-<h3 id="part-2-prediction-of-post-medication-scenario"><a class="header" href="#part-2-prediction-of-post-medication-scenario">Part 2: Prediction of post-medication scenario</a></h3>
+<h4 id="part-2-prediction-of-post-medication-scenario"><a class="header" href="#part-2-prediction-of-post-medication-scenario">Part 2: Prediction of post-medication scenario</a></h4>
+<p>In this section, we want to predict post-medication scenario by using math modeling.
+In detail, we want to see how will the number of floating Shigella change
+after the drug release,
+this will be depending on natural growth of Shigella, the binding efficiency of
+20ipaD and IpaD, the concentration of Yeast cells,
+and the survival rate of Yeast cells.</p>
+<p>Yeast cells are sealed in micro-capsules made of shellac before
+being delivered into bodies.
+The pH-dependent solubility that prefers a mild basic environment makes shellac
+perfect for releasing probiotics in jejunal.</p>
+<p>There are several important assumptions for this model:</p>
+<ul>
+<li>Each floating Yeast cell carries one 20ipaD;</li>
+<li>Each floating Shigella cell carries one IpaD;</li>
+<li>Growth of Shigella cultured in BHI (Brian Heart Infusion) medium is similar with
+the growth of Shigella in human's jejunal;</li>
+<li>Each 20ipad binds with one IpaD once;</li>
+<li>Died Yeast cell cannot display 20ipaD and cannot bind with IpaD;</li>
+<li>Yeast growth is not considered here since a healthy immune system does not
+allow overgrowth of the yeast, and the growth of the yeast is very slow in neutral;
+or even slightly alkaline conditions<sup class="footnote-reference"><a href="#Yeast_growth">13</a></sup>.</li>
+</ul>
+<p>Based on these assumptions, the following two equations describe the change in
+number of shigella and Yeast:
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:2.1149em;vertical-align:-0.686em;"></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.4289em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord mathnormal">t</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord"><span class="mord mathnormal">L</span><span class="msupsub"><span class="vlist-t"><span class="vlist-r"><span class="vlist" style="height:0.7519em;"><span style="top:-3.063em;margin-right:0.05em;"><span class="pstrut" style="height:2.7em;"></span><span class="sizing reset-size6 size3 mtight"><span class="mord mtight"><span class="mord mtight">′</span></span></span></span></span></span></span></span></span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:2.113em;vertical-align:-0.686em;"></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.427em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord mathnormal">t</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal" style="margin-right:0.05278em;">β</span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span><span class="mord mathnormal" style="margin-right:0.02778em;">D</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span></span>
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:2.113em;vertical-align:-0.686em;"></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.427em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord mathnormal">t</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal" style="margin-right:0.02778em;">D</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal" style="margin-right:0.05556em;">γ</span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span><span class="mord mathnormal" style="margin-right:0.02778em;">D</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span></span>
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1.0019em;vertical-align:-0.25em;"></span><span class="mord"><span class="mord mathnormal">L</span><span class="msupsub"><span class="vlist-t"><span class="vlist-r"><span class="vlist" style="height:0.7519em;"><span style="top:-3.063em;margin-right:0.05em;"><span class="pstrut" style="height:2.7em;"></span><span class="sizing reset-size6 size3 mtight"><span class="mord mtight"><span class="mord mtight">′</span></span></span></span></span></span></span></span></span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span>: the log count of the number of shigella in jejunal at time <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6151em;"></span><span class="mord mathnormal">t</span></span></span></span> after drug release;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span>: the log count of the number of shigella in jejunal at time <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6151em;"></span><span class="mord mathnormal">t</span></span></span></span> before drug release;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.8889em;vertical-align:-0.1944em;"></span><span class="mord mathnormal" style="margin-right:0.05278em;">β</span></span></span></span>: the binding efficiency between 20ipaD and IpaD;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal" style="margin-right:0.02778em;">D</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span>: the log count of number of Yeast in jejunal at time <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6151em;"></span><span class="mord mathnormal">t</span></span></span></span> after drug release;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.625em;vertical-align:-0.1944em;"></span><span class="mord mathnormal" style="margin-right:0.05556em;">γ</span></span></span></span>:survival rate of Yeast in jejunal</p>
+<p><strong>Detail:</strong><br />
+The natural growth of shigella in jejunal can be described in the form of Gompertz equation<sup class="footnote-reference"><a href="#Shigella_natural">14</a></sup>:
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:0.7667em;vertical-align:-0.0833em;"></span><span class="mord mathnormal">A</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">+</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal" style="margin-right:0.07153em;">C</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">[</span><span class="mord">−</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">(</span><span class="mord">−</span><span class="mord mathnormal" style="margin-right:0.05017em;">B</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span><span class="mclose">))]</span></span></span></span></span>
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span>: the log count of the number of shigella in jejunal at time t before drug release;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal">A</span></span></span></span>: the asymptotic log count as <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6151em;"></span><span class="mord mathnormal">t</span></span></span></span> decreases indefinitely;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.07153em;">C</span></span></span></span>: the asymptotic amount of growth (log number) that occurs as <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6151em;"></span><span class="mord mathnormal">t</span></span></span></span> increases indefinitely;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span>: the time at which the absolute growth rate is maximum;<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.05017em;">B</span></span></span></span>: the relative growth rate at <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span></p>
+<p>Parameters <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal">A</span></span></span></span>, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.07153em;">C</span></span></span></span>, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span>,and <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.05017em;">B</span></span></span></span> depend on the environmental conditions: temperature <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.13889em;">T</span></span></span></span>, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.8778em;vertical-align:-0.1944em;"></span><span class="mord mathnormal">p</span><span class="mord mathnormal" style="margin-right:0.08125em;">H</span></span></span></span>, and sodium chloride concentration <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.4306em;"></span><span class="mord mathnormal">c</span></span></span></span>. <br />
+In our case,
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.13889em;">T</span></span></span></span> is defaulted to 37 degrees;
+the <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.8778em;vertical-align:-0.1944em;"></span><span class="mord mathnormal">p</span><span class="mord mathnormal" style="margin-right:0.08125em;">H</span></span></span></span> is about 6.9 in jejunal and about 7.2 in ileal<sup class="footnote-reference"><a href="#pH">15</a></sup>;
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.4306em;"></span><span class="mord mathnormal">c</span></span></span></span> in jejunal is about 112<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal">m</span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span><sup class="footnote-reference"><a href="#NaCl">16</a></sup>.</p>
+<p>Translate the concentration into the form of percentage:<br />
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:2.2519em;vertical-align:-0.8804em;"></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.1076em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord">100</span><span class="mord mathnormal">m</span><span class="mord mathnormal" style="margin-right:0.01968em;">l</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal" style="margin-right:0.03588em;">xg</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.3714em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord">58.44</span><span class="mord mathnormal" style="margin-right:0.03588em;">g</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord">1</span><span class="mord mathnormal">m</span><span class="mord mathnormal">o</span><span class="mord mathnormal" style="margin-right:0.01968em;">l</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.8804em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.3714em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord">1</span><span class="mord mathnormal">L</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord">1000</span><span class="mord mathnormal">m</span><span class="mord mathnormal" style="margin-right:0.01968em;">l</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord">0.012</span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span></span>
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.4306em;"></span><span class="mord mathnormal">x</span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:0.6444em;"></span><span class="mord">0.65</span></span></span></span></span>
+So, the concentration of sodium chloride is about 0.65% in jejunal.</p>
+<p>Gompertz equation parameters and calculated growth curve values for Shigella can
+be found in the paper: <em><strong>Effect of Sodium Chloride, pH and Temperature on Growth
+of Shigella flexneri</strong></em><sup class="footnote-reference"><a href="#Shigella_natural">14</a></sup>.
+Parameters in our situation do not perfectly fit the calculated ones, but they
+do fall in a certain range:</p>
+<ul>
+<li>
+<p>Lower limit:<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.13889em;">T</span></span></span></span>=37 degrees, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.8778em;vertical-align:-0.1944em;"></span><span class="mord mathnormal">p</span><span class="mord mathnormal" style="margin-right:0.08125em;">H</span></span></span></span>=6.5, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.4306em;"></span><span class="mord mathnormal">c</span></span></span></span>=0.5%<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal">A</span></span></span></span>=4.53, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.05017em;">B</span></span></span></span>=0.493, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.07153em;">C</span></span></span></span>=4.47, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span>=3.68
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:0.7278em;vertical-align:-0.0833em;"></span><span class="mord">4.53</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">+</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">4.47</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">[</span><span class="mord">−</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">(</span><span class="mord">−</span><span class="mord">0.493</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">3.68</span><span class="mclose">))]</span></span></span></span></span>
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:2.113em;vertical-align:-0.686em;"></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.427em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord mathnormal">t</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">2.20</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">[</span><span class="mord">−</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">(</span><span class="mord">−</span><span class="mord">0.493</span><span class="mopen">(</span><span class="mord mathnormal">x</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">3.68</span><span class="mclose">))</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">0.493</span><span class="mopen">(</span><span class="mord mathnormal">x</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">3.68</span><span class="mclose">)]</span></span></span></span></span></p>
+</li>
+<li>
+<p>Higher limit:<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.13889em;">T</span></span></span></span>=37 degrees, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.8778em;vertical-align:-0.1944em;"></span><span class="mord mathnormal">p</span><span class="mord mathnormal" style="margin-right:0.08125em;">H</span></span></span></span>=7.5, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.4306em;"></span><span class="mord mathnormal">c</span></span></span></span>=0.5%<br />
+<span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal">A</span></span></span></span>=4.26, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.05017em;">B</span></span></span></span>=0.435, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.07153em;">C</span></span></span></span>=5.41, <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.10903em;">M</span></span></span></span>=4.54
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:0.7278em;vertical-align:-0.0833em;"></span><span class="mord">4.26</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">+</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">5.41</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">[</span><span class="mord">−</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">(</span><span class="mord">−</span><span class="mord">0.435</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">4.54</span><span class="mclose">))]</span></span></span></span></span>
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:2.113em;vertical-align:-0.686em;"></span><span class="mord"><span class="mopen nulldelimiter"></span><span class="mfrac"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:1.427em;"><span style="top:-2.314em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">d</span><span class="mord mathnormal">t</span></span></span><span style="top:-3.23em;"><span class="pstrut" style="height:3em;"></span><span class="frac-line" style="border-bottom-width:0.04em;"></span></span><span style="top:-3.677em;"><span class="pstrut" style="height:3em;"></span><span class="mord"><span class="mord mathnormal">L</span><span class="mopen">(</span><span class="mord mathnormal">t</span><span class="mclose">)</span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.686em;"><span></span></span></span></span></span><span class="mclose nulldelimiter"></span></span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">2.35</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">[</span><span class="mord">−</span><span class="mord mathnormal">e</span><span class="mord mathnormal">x</span><span class="mord mathnormal">p</span><span class="mopen">(</span><span class="mord">−</span><span class="mord">0.435</span><span class="mopen">(</span><span class="mord mathnormal">x</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">4.54</span><span class="mclose">))</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">0.435</span><span class="mopen">(</span><span class="mord mathnormal">x</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">−</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord">4.54</span><span class="mclose">)]</span></span></span></span></span></p>
+</li>
+</ul>
+<p>Since our situation is in this range, so we can have an upper limit and lower limit
+for the growth scenario of Shigella (<strong>Figure 2</strong>).</p>
+<img src="https://static.igem.wiki/teams/4161/wiki/fig-model-part2-growth-of-shigella.png"/>
+<p><strong>Figure 2</strong> | Upper limit and lower limit for Shigella's natural growth in jejunal.
+The x axis indicates the time with unit of hour; the y axis indicates the
+log count of number of Shigella.</p>
+<p>The survival rate of Yeast cells in jejunal varies with time (<strong>Figure 3</strong>) <sup class="footnote-reference"><a href="#pH">15</a></sup>.</p>
+<img src="https://static.igem.wiki/teams/4161/wiki/fig-model-part-2-yeast-survival-rate.png"/>
+<p><strong>Figure 3</strong> | Survival rate of Yeast cells in jejunal with time of digestion.</p>
+<p>The survival rate is highest at t=2h, when 30.8%
+of intake Yeast cells are viable. Then, the viability decreases with time, finally 13%
+of intake Yeast cells are viable at 5h.</p>
+<h4 id="part-3-medication-guidance"><a class="header" href="#part-3-medication-guidance">Part 3: Medication guidance</a></h4>
+<p>Our drug is designed to 'kill' the Shigella before it invades
+the surface of jejunal, or more realistically, to decrease the concentration of
+floating Shigella so that a mass invasion could be avoided or stopped as soon as possible.
+Based on the information from wet-lab and math modeling, we would like to give
+a possible conclusion or a medication guidance for the patients and the managers
+of the healthcare system, so that our vision could be realized.</p>
+<p>For a single micro-capsule, assume it contains at least 10 billion CFU (colony-forming unit) <sup class="footnote-reference"><a href="#CFU">17</a></sup>,
+then it contains at least 10 billion live Yeast cells. Since the expression rate is about 31.25%,
+there would be at least 3 billion live Yeast cells that expressed at least one
+20ipaD on each of their surfaces. After the capsule reaches jejunal, it will dissolve and start to release
+Yeast cells. After 2 hours, there will be about 0.9 billion
+Yeast cells (30.8%
+of the intake)
+that are viable to display 20ipaD and bind with IpaD.</p>
+<p>For Shigella, since the upper limit and lower limit of natural growth are found,
+we can calculate the maximum population density in the following form:
+<span class="katex-display"><span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:1em;vertical-align:-0.25em;"></span><span class="mord mathnormal">De</span><span class="mord mathnormal">n</span><span class="mord mathnormal">s</span><span class="mord mathnormal">i</span><span class="mord mathnormal">t</span><span class="mord"><span class="mord mathnormal" style="margin-right:0.03588em;">y</span><span class="msupsub"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:0.1514em;"><span style="top:-2.55em;margin-left:-0.0359em;margin-right:0.05em;"><span class="pstrut" style="height:2.7em;"></span><span class="sizing reset-size6 size3 mtight"><span class="mord mtight"><span class="mord mathnormal mtight">ma</span><span class="mord mathnormal mtight">x</span></span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.15em;"><span></span></span></span></span></span></span><span class="mopen">(</span><span class="mord mathnormal" style="margin-right:0.01968em;">l</span><span class="mord mathnormal">o</span><span class="mord"><span class="mord mathnormal" style="margin-right:0.03588em;">g</span><span class="msupsub"><span class="vlist-t vlist-t2"><span class="vlist-r"><span class="vlist" style="height:0.3011em;"><span style="top:-2.55em;margin-left:-0.0359em;margin-right:0.05em;"><span class="pstrut" style="height:2.7em;"></span><span class="sizing reset-size6 size3 mtight"><span class="mord mtight"><span class="mord mtight">10</span></span></span></span></span><span class="vlist-s">​</span></span><span class="vlist-r"><span class="vlist" style="height:0.15em;"><span></span></span></span></span></span></span><span class="mord mathnormal">c</span><span class="mord mathnormal" style="margin-right:0.10764em;">f</span><span class="mord mathnormal">u</span><span class="mord">/</span><span class="mord mathnormal">m</span><span class="mord mathnormal" style="margin-right:0.01968em;">l</span><span class="mclose">)</span><span class="mspace" style="margin-right:0.2778em;"></span><span class="mrel">=</span><span class="mspace" style="margin-right:0.2778em;"></span></span><span class="base"><span class="strut" style="height:0.7667em;vertical-align:-0.0833em;"></span><span class="mord mathnormal">A</span><span class="mspace" style="margin-right:0.2222em;"></span><span class="mbin">+</span><span class="mspace" style="margin-right:0.2222em;"></span></span><span class="base"><span class="strut" style="height:0.6833em;"></span><span class="mord mathnormal" style="margin-right:0.07153em;">C</span></span></span></span></span></p>
+<p>So the uppper limit of the max density at <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.6151em;"></span><span class="mord mathnormal">t</span></span></span></span>=5h will be about 5 billion Shigella, and
+the lower limit will be about 1 billion Shigella.</p>
+<p>Therefore, it is proper to take 5-6 capsules every 5 hours after the patient start to have symptoms,
+and distribute 1-5 capsules every 5 hours to the people who might develop symptoms due to
+living togethor or common life styles.</p>
+<h3 id="summary--future-plan"><a class="header" href="#summary--future-plan">Summary & Future plan</a></h3>
+<p>To conclude, we have described the 20ipaD expression efficiency of Yeast cell through wet-lab results
+and predicted the post-medication scenario through math modeling.
+The expression efficiency is found to be about 31.25%± 0.75,
+and the upper limit and lower limit of natural growth of Shigella
+could help us to define a range for Shigella to grow naturally in jejunal.
+By assuming each capsule contains 10 billion CFU,
+we are able to give a medication guidance for symptomatic patient to take 5-6 capsules per 5 hours
+and for potential patients to take 1-5 capsules per 5 hours.</p>
+<p>In the future, more work can be devoted to deciding the binding efficiency <span class="katex"><span class="katex-html" aria-hidden="true"><span class="base"><span class="strut" style="height:0.8889em;vertical-align:-0.1944em;"></span><span class="mord mathnormal" style="margin-right:0.05278em;">β</span></span></span></span> between Yeast-20ipaD and IpaD,
+and how much CFU is needed and realistic can a single capsule contain. These work can help us
+better understand the change of number of Shigella after medication,
+so that a more precise medication guidance is available.</p>
+<div class="footnote-definition" id="Yeast_growth"><sup class="footnote-definition-label">13</sup>
+<p>Investigation of the Best Saccharomyces cerevisiae Growth Condition. Electron Physician. DOI: 10.19082/3592 <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5308499/">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5308499/</a></p>
+</div>
+<div class="footnote-definition" id="Shigella_natural"><sup class="footnote-definition-label">14</sup>
+<p>Effect of Sodium Chloride, pH and Temperature on Growth of Shigella flexneri. Journal of Food Protection. DOI:10.4315/0362-028x-52.5.356 <a href="https://pubmed.ncbi.nlm.nih.gov/31003269/">https://pubmed.ncbi.nlm.nih.gov/31003269/</a></p>
+</div>
+<div class="footnote-definition" id="pH"><sup class="footnote-definition-label">15</sup>
+<p>Effect of a New Probiotic Saccharomyces cerevisiae Strain on Survival of <em>Escherichia Coli</em> O157:H7 in a Dynamic Gastrointestinal Model. Applied and Environmental Microbiology. DOI:10.1128/AEM.02130-10 <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3028742/">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3028742/</a></p>
+</div>
+<div class="footnote-definition" id="NaCl"><sup class="footnote-definition-label">16</sup>
+<p>The mechanisms of sodium absorption in the human small intestine. The Journal of Clinical Investigation. DOI:10.1172/JCI105781 <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC297237/">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC297237/</a></p>
+</div>
+<div class="footnote-definition" id="CFU"><sup class="footnote-definition-label">17</sup>
+<p>Choosing the Best Probiotic: How Many CFUs is Enough?<a href="https://deerland.com/chew/choosing-best-probiotic-many-cfus-enough/">https://deerland.com/chew/choosing-best-probiotic-many-cfus-enough/</a></p>
+</div>
+<h2 id="hardware"><a class="header" href="#hardware">Hardware</a></h2>
+<p>Probiotics will be sealed in microcapsules(<strong>Figure 1</strong>) made of shellac
+before being delivered into bodies. The pH-dependent solubility that prefers
+a mild basic environment makes shellac perfect for releasing probiotics in intestines.</p>
+<img src="https://static.igem.wiki/teams/4161/wiki/hardware.png" />
+<p><strong>Figure 1</strong> | 3D model of the microcapsule</p>
+<p>Microcapsule is a microscope-scale capsulation format.
+The probiotics were wrapped by materials that can ensure the reservation,
+activation, release, and environmental-resistance of the probiotics.
+It would be presented as powder.
+“Microencapsulation is a technology that serves as a tool to protect the
+sensitive and expensive nutrients (Meyers et al., 1998), by providing them with
+a protective wall,
+which allows them to get released at a particular site, at a particular time,
+and under particular conditions." <sup class="footnote-reference"><a href="#Microencapsulation">18</a></sup>
+To summarize, the technology of
+microencapsulation is to ensure the safe delivery of sensitive compound.</p>
+<p>Shellac is a natural polymer that is generally recognized as a safe (GRAS) material.
+It is insoluble in neutral and acidic aqueous solution but dissolves at alkaline condition
+<sup class="footnote-reference"><a href="#pH_shellac">19</a></sup>.
+So, shellac is proper for the controlled release of Yeast cells in the intestine.</p>
+<p>Research has shown that the microcapsules with the addition of shellac
+"contributed to better probiotic survivals after freeze drying, simulated digestion,heating and ambient storage,
+and whey protein isolate (WPI) addition had a synergistic effect."<sup class="footnote-reference"><a href="#Shellac">20</a></sup></p>
+<div class="footnote-definition" id="Microencapsulation"><sup class="footnote-definition-label">18</sup>
+<p>Microencapsulation: An overview on concepts, methods, properties and applications in foods. Food Frontiers. <a href="https://doi.org/10.1002/fft2.94">https://doi.org/10.1002/fft2.94</a></p>
+</div>
+<div class="footnote-definition" id="Shellac"><sup class="footnote-definition-label">20</sup>
+<p>Microencapsulation of probiotic lactobacilli with shellac as moisture barrier and to allow controlled release. Journal of the Science of Food and Agriculture. <a href="https://doi.org/10.1002/jsfa.10685">https://doi.org/10.1002/jsfa.10685</a></p>
+</div>
+<div class="footnote-definition" id="pH_shellac"><sup class="footnote-definition-label">19</sup>
+<p>Comparison of spray drying, freeze drying and convective hot air drying for the production of a probiotic orange powder. J Funct Foods <a href="https://doi.org/10.1016/j.jff.2015.06.001">https://doi.org/10.1016/j.jff.2015.06.001</a></p>
+</div>
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index 6639106a33bc513264b0014ed7cfdf40d5cf2b1f..1deab572193efd5e1110c4dd4983fcfb666f679f 100644
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@@ -104,6 +104,12 @@
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+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/part-collection.html b/public/part-collection.html
index 08b9f7c6043e1d81606196433b6c148800fed7ec..f22e270c3a806dcc9393698ab4eb1bc8b422cfb5 100644
--- a/public/part-collection.html
+++ b/public/part-collection.html
@@ -39,7 +39,7 @@
<body>
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@@ -99,14 +99,18 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="parts"><a class="header" href="#parts">Parts</a></h1>
+<div class="h1-bg">
+ <h1 class>Parts</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/wetlab6-for-bg.png" />
+</div>
+<h2 id="yeast-group-y-parts"><a class="header" href="#yeast-group-y-parts">Yeast (Group Y) Parts</a></h2>
<p>All genetic parts of group Y can be divided into 3 categories, including single
element, key composite segment, and vector.</p>
-<h2 id="single-element"><a class="header" href="#single-element">Single element</a></h2>
+<h3 id="group-y-single-elements"><a class="header" href="#group-y-single-elements">Group Y single elements</a></h3>
<p>The single elements refer to every functional unit of our key genetic parts,
like promoter, linker, important polypeptide, etc. A total of seven single
elements were documented.</p>
-<div class="table-wrapper"><table><thead><tr><th>Part Code</th><th>Part name</th><th>Website</th></tr></thead><tbody>
+<div class="table-wrapper"><table><thead><tr><th>Part Code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
<tr><td>BBa_K4161501</td><td>T7 Promoter</td><td><a href="http://parts.igem.org/Part:BBa_K4161501">http://parts.igem.org/Part:BBa_K4161501</a></td></tr>
<tr><td>BBa_K4161502</td><td>GAL1 Promoter</td><td><a href="http://parts.igem.org/Part:BBa_K4161502">http://parts.igem.org/Part:BBa_K4161502</a></td></tr>
<tr><td>BBa_K4161503</td><td>Aga2</td><td><a href="http://parts.igem.org/Part:BBa_K4161503">http://parts.igem.org/Part:BBa_K4161503</a></td></tr>
@@ -116,32 +120,97 @@ elements were documented.</p>
<tr><td>BBa_K4161507</td><td>HA</td><td><a href="http://parts.igem.org/Part:BBa_K4161507">http://parts.igem.org/Part:BBa_K4161507</a></td></tr>
</tbody></table>
</div>
-<h2 id="key-composite-segment"><a class="header" href="#key-composite-segment">Key composite segment</a></h2>
+<h3 id="group-y-key-composite-segments"><a class="header" href="#group-y-key-composite-segments">Group Y key composite segments</a></h3>
<p>The key composite segments are clusters of multiple single elements, they make
up the key expression modules or functional units of the genetic model. Two key
composite segments were documented.</p>
-<p>| Part Code | Part name |
-Website |
-|--------------|--------------------------------------------------------------|-
-----------------------------------------|
-| BBa_K4161301 | Single Domain Antibody 20ipaD Conjugated Aga2 Express Module |
-<a href="http://parts.igem.org/Part:BBa_K4161301">http://parts.igem.org/Part:BBa_K4161301</a> |
-| BBa_K4161508 | Composite part |
-<a href="http://parts.igem.org/Part:BBa_K4161508">http://parts.igem.org/Part:BBa_K4161508</a> |</p>
-<h2 id="vector"><a class="header" href="#vector">Vector</a></h2>
+<div class="table-wrapper"><table><thead><tr><th>Part Code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161301</td><td>Single Domain Antibody 20ipaD Conjugated Aga2 Express Module</td><td><a href="http://parts.igem.org/Part:BBa_K4161301">http://parts.igem.org/Part:BBa_K4161301</a></td></tr>
+<tr><td>BBa_K4161508</td><td>488aa recombinant protein, Aga2 + ipaD</td><td><a href="http://parts.igem.org/Part:BBa_K4161508">http://parts.igem.org/Part:BBa_K4161508</a></td></tr>
+</tbody></table>
+</div>
+<h3 id="group-y-vector"><a class="header" href="#group-y-vector">Group Y vector</a></h3>
<p>Most of our genetic designs were based on the yeast surface display vector
pYD1, which is also documented.</p>
-<p>| Part Code | Part name |
-Website |
-|--------------|--------------------------------------------------------------|-
-----------------------------------------|
-| BBa_K4161302 | pYD1 plasmid |
-<a href="http://parts.igem.org/Part:BBa_K4161302">http://parts.igem.org/Part:BBa_K4161302</a> |</p>
-
+<div class="table-wrapper"><table><thead><tr><th>Part Code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161302</td><td>pYD1 plasmid</td><td><a href="http://parts.igem.org/Part:BBa_K4161302">http://parts.igem.org/Part:BBa_K4161302</a></td></tr>
+</tbody></table>
+</div>
+<h2 id="ecoli-nissle-1917-group-e-parts"><a class="header" href="#ecoli-nissle-1917-group-e-parts">E.coli Nissle 1917 (Group E) Parts</a></h2>
+<h3 id="group-e-single-elements"><a class="header" href="#group-e-single-elements">Group E single elements</a></h3>
+<p>Single elements of Group E include nanobodies,
+curli protein (csg) operon fragments,
+linkers, tags, signal peptides,
+promoters and terminators. A total of 15 parts were documented.</p>
+<div class="table-wrapper"><table><thead><tr><th>Part code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161001</td><td>20IpaD</td><td><a href="http://parts.igem.org/Part:BBa_K4161001">http://parts.igem.org/Part:BBa_K4161001</a></td></tr>
+<tr><td>BBa_K4161002</td><td>JMK-H2</td><td><a href="http://parts.igem.org/Part:BBa_K4161002">http://parts.igem.org/Part:BBa_K4161002</a></td></tr>
+<tr><td>BBa_K4161010</td><td>csgA</td><td><a href="http://parts.igem.org/Part:BBa_K4161010">http://parts.igem.org/Part:BBa_K4161010</a></td></tr>
+<tr><td>BBa_K4161011</td><td>csgB</td><td><a href="http://parts.igem.org/Part:BBa_K4161011">http://parts.igem.org/Part:BBa_K4161011</a></td></tr>
+<tr><td>BBa_K4161012</td><td>csgC</td><td><a href="http://parts.igem.org/Part:BBa_K4161012">http://parts.igem.org/Part:BBa_K4161012</a></td></tr>
+<tr><td>BBa_K4161013</td><td>csgE</td><td><a href="http://parts.igem.org/Part:BBa_K4161013">http://parts.igem.org/Part:BBa_K4161013</a></td></tr>
+<tr><td>BBa_K4161014</td><td>csgF</td><td><a href="http://parts.igem.org/Part:BBa_K4161014">http://parts.igem.org/Part:BBa_K4161014</a></td></tr>
+<tr><td>BBa_K4161015</td><td>csgG</td><td><a href="http://parts.igem.org/Part:BBa_K4161015">http://parts.igem.org/Part:BBa_K4161015</a></td></tr>
+<tr><td>BBa_K4161016</td><td>riboJ</td><td><a href="http://parts.igem.org/Part:BBa_K4161016">http://parts.igem.org/Part:BBa_K4161016</a></td></tr>
+<tr><td>BBa_K4161017</td><td>Neae: the intimin fragment for surface display</td><td><a href="http://parts.igem.org/Part:BBa_K4161017">http://parts.igem.org/Part:BBa_K4161017</a></td></tr>
+<tr><td>BBa_K4161018</td><td>pTlpA promotor C7 variant</td><td><a href="http://parts.igem.org/Part:BBa_K4161018">http://parts.igem.org/Part:BBa_K4161018</a></td></tr>
+<tr><td>BBa_K4161019</td><td>FE-36 linker</td><td><a href="http://parts.igem.org/Part:BBa_K4161019">http://parts.igem.org/Part:BBa_K4161019</a></td></tr>
+<tr><td>BBa_K4161020</td><td>JPS-G3</td><td><a href="http://parts.igem.org/Part:BBa_K4161020">http://parts.igem.org/Part:BBa_K4161020</a></td></tr>
+<tr><td>BBa_K4161021</td><td>3xFlag</td><td><a href="http://parts.igem.org/Part:BBa_K4161021">http://parts.igem.org/Part:BBa_K4161021</a></td></tr>
+<tr><td>BBa_K4161022</td><td>thr terminator</td><td><a href="http://parts.igem.org/Part:BBa_K4161022">http://parts.igem.org/Part:BBa_K4161022</a></td></tr>
+</tbody></table>
+</div>
+<h3 id="group-e-composite-segments"><a class="header" href="#group-e-composite-segments">Group E composite segments</a></h3>
+<p>Group E's composite parts are designed to express surface protein-nanobody fusion proteins. A total of 4 composite parts are documented.</p>
+<div class="table-wrapper"><table><thead><tr><th>Part code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161003</td><td>csg-JMK-H2, Csg surface display system on <em>E. coli</em> Nissle 1917</td><td><a href="http://parts.igem.org/Part:BBa_K4161003">http://parts.igem.org/Part:BBa_K4161003</a></td></tr>
+<tr><td>BBa_K4161004</td><td>intimin-20IpaD, Nanobody surface display system based on intimin</td><td><a href="http://parts.igem.org/Part:BBa_K4161004">http://parts.igem.org/Part:BBa_K4161004</a></td></tr>
+<tr><td>BBa_K4161023</td><td>csgA-JPS-G3-3xFLAG, Csg surface display system on <em>E. coli</em> Nissle 1917</td><td><a href="http://parts.igem.org/Part:BBa_K4161023">http://parts.igem.org/Part:BBa_K4161023</a></td></tr>
+<tr><td>BBa_K4161100</td><td>Csg surface display system on <em>E. coli</em> Nissle 1917</td><td><a href="http://parts.igem.org/Part:BBa_K4161100">http://parts.igem.org/Part:BBa_K4161100</a></td></tr>
+</tbody></table>
+</div>
+<h3 id="group-e-vectors"><a class="header" href="#group-e-vectors">Group E vectors</a></h3>
+<p>Vectors pET30a and pUC19 are used for recombinant plasmid construction and protein expression.</p>
+<div class="table-wrapper"><table><thead><tr><th>Part code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161024</td><td>pET30a, empty vector</td><td><a href="http://parts.igem.org/Part:BBa_K4161024">http://parts.igem.org/Part:BBa_K4161024</a></td></tr>
+<tr><td>BBa_K4161025</td><td>pUC19, empty vector</td><td><a href="http://parts.igem.org/Part:BBa_K4161025">http://parts.igem.org/Part:BBa_K4161025</a></td></tr>
+</tbody></table>
+</div>
+<h2 id="llactis-nz9000-parts"><a class="header" href="#llactis-nz9000-parts">L.lactis NZ9000 parts</a></h2>
+<h3 id="group-l-single-elements"><a class="header" href="#group-l-single-elements">Group L single elements</a></h3>
+<p>Single parts in Group L includes the following elements:
+Group L parts</p>
+<div class="table-wrapper"><table><thead><tr><th>Part code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161600</td><td>Usp45 nisin promoter</td><td><a href="http://parts.igem.org/Part:BBa_K4161600">http://parts.igem.org/Part:BBa_K4161600</a></td></tr>
+<tr><td>BBa_K4161603</td><td>AcmA3b</td><td><a href="http://parts.igem.org/Part:BBa_K4161603">http://parts.igem.org/Part:BBa_K4161603</a></td></tr>
+<tr><td>BBa_K4161602</td><td>20ipaD</td><td><a href="http://parts.igem.org/Part:BBa_K4161602">http://parts.igem.org/Part:BBa_K4161602</a></td></tr>
+<tr><td>BBa_K4161604</td><td>signalling peptide in <em>L.lactis</em></td><td><a href="http://parts.igem.org/Part:BBa_K4161604">http://parts.igem.org/Part:BBa_K4161604</a></td></tr>
+<tr><td>BBa_K4161605</td><td>Flag-tag</td><td><a href="http://parts.igem.org/Part:BBa_K4161605">http://parts.igem.org/Part:BBa_K4161605</a></td></tr>
+</tbody></table>
+</div>
+<h3 id="composite-elemnent"><a class="header" href="#composite-elemnent">Composite elemnent</a></h3>
+<p>The composite element of Group L includes Usp45-signaling peptide in L.lactis-Flagtag-20ipaD-AcmA3b.</p>
+<div class="table-wrapper"><table><thead><tr><th>Part code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161600</td><td>Usp45-signaling peptide in L.lactis-20ipaD-AcmA3b</td><td><a href="http://parts.igem.org/Part:BBa_K4161997">http://parts.igem.org/Part:BBa_K4161997</a></td></tr>
+</tbody></table>
+</div>
+<h3 id="group-l-vector"><a class="header" href="#group-l-vector">Group L vector</a></h3>
+<h3 id="composite-elemnent-1"><a class="header" href="#composite-elemnent-1">Composite elemnent</a></h3>
+<p>The plasmid backbone of Group L is pNZ8148, a plasmid suitable for L.lactis.</p>
+<div class="table-wrapper"><table><thead><tr><th>Part code</th><th>Part name</th><th>Link</th></tr></thead><tbody>
+<tr><td>BBa_K4161601</td><td>pNZ8148</td><td><a href="http://parts.igem.org/Part:BBa_K4161601">http://parts.igem.org/Part:BBa_K4161601</a></td></tr>
+</tbody></table>
+</div>
</main>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/partnership.html b/public/partnership.html
index 444f1907fcf533f16e2df4fb63c4b7ce9eea2cca..cfe5d4f4d3905aa44f8513eb3e209481fe52e65f 100644
--- a/public/partnership.html
+++ b/public/partnership.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item expanded "><a href="partnership.html" class="active">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item expanded "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item expanded "><a href="partnership.html" class="active">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -99,15 +99,19 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
+<div class="h1-bg">
+ <h1 class>Partnership</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/fig-collaboration-xjtlu-2.jpg" />
+</div>
<h2 id="meeting-with-xjltu"><a class="header" href="#meeting-with-xjltu">Meeting with XJLTU</a></h2>
<h3 id="xjltus-project"><a class="header" href="#xjltus-project">XJLTU's Project</a></h3>
<p>They plan to develop a biofilter core
to replace current industry filter cores for heavy metal wastewater.
-Specifically, they plan to engineer E. coli to express csgA protein at high levels
+Specifically, they plan to engineer <em>E. coli</em> to express csgA protein at high levels
and immobilize the bacteria into a filter.
In that way, the heavy metal ions in the wastewater can be captured by csgA protein
-that is expressed by E. coli located in the filter.</p>
-<h3 id="questions--advice-from-xjltu"><a class="header" href="#questions--advice-from-xjltu">Questions & Advice From XJLTU:</a></h3>
+that is expressed by <em>E. coli</em> located in the filter.</p>
+<h3 id="questions--advice-from-xjltu"><a class="header" href="#questions--advice-from-xjltu">Questions & Advice From XJLTU</a></h3>
<ol>
<li>
<p>They would like to know how we will interact with and educate the public.<br />
@@ -123,7 +127,7 @@ it's about how and why we choose each part of the plasmid for surface display.<b
A: We applied three microorganisms
and the whole team was divided into three groups,
each responsible for E. coli,
-Yeast cell and Lactococcus lactis.
+Yeast cell and <em>Lactococcus</em> lactis.
All groups applied a strategy
which conjugates the targeted nanobody with a surface protein that is to be expressed,
transported and located to the extracellular space.
@@ -132,12 +136,12 @@ and each nanobody is marked with at least one protein tag for their identificati
We also provided links to igem parts so they can check it directly.</p>
</li>
</ol>
-<h3 id="questions--advice-from-dku"><a class="header" href="#questions--advice-from-dku">Questions & Advice From DKU:</a></h3>
+<h3 id="questions--advice-from-dku"><a class="header" href="#questions--advice-from-dku">Questions & Advice From DKU</a></h3>
<ol>
<li>
-<p>Will the biofilter be blocked due to E. coli proliferation?<br />
+<p>Will the biofilter be blocked due to <em>E. coli</em> proliferation?<br />
A: The microorganisms are immobilized in filters,
-and the filtration condition may not allow E. coli to grow at such a speed.</p>
+and the filtration condition may not allow <em>E. coli</em> to grow at such a speed.</p>
</li>
<li>
<p>The csgA protein's ability to absorb heavy metal ions under different conditions
@@ -147,7 +151,7 @@ then adjust the pH and check the remaining concentration of metal ions in time,
so we can acquire a proper pH for the protein to capture heavy metal ions.</p>
</li>
</ol>
-<h3 id="discussion-topics"><a class="header" href="#discussion-topics">Discussion Topics:</a></h3>
+<h3 id="discussion-topics"><a class="header" href="#discussion-topics">Discussion Topics</a></h3>
<ul>
<li>Model for bacteria growth<br />
The XJLTU team developed a model for predicting bacteria growth,
@@ -164,7 +168,7 @@ As a result, this approach remains to be a concern.</li>
<li>Detection and measurement of displayed csg protein.<br />
The XJLTU team controlled the expression level by adjusting inducer concentration
and estimated the expression by calculating theoretically.</li>
-<li>The condition of csg and heavy metal ions after the death of E. coli cells<br />
+<li>The condition of csg and heavy metal ions after the death of <em>E. coli</em> cells<br />
We consider that the heavy metal ions will remain captured,
as protein itself has a great affinity to the heavy metal ions.
But, it remains to be seen
@@ -175,6 +179,12 @@ whether the released protein will leak out from the filter.</li>
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/plant.html b/public/plant.html
index 9b1b46d3cc0e4556d57edff5d556d83fc0ce73ec..6613cd93f565a51778e0f30f334418872e02e2f5 100644
--- a/public/plant.html
+++ b/public/plant.html
@@ -39,7 +39,7 @@
<body>
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index 1a0dc69de4d14c5b855cd8436259270092b5e0fb..87fe1e106db07b248823754581b118b6580be991 100644
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+<h2 id="overview"><a class="header" href="#overview">Overview</a></h2>
+<p>The novel drug we proposed was to anchor nanobodies on the surface of probiotics, including yeast, Lactococcus, and E. coli, which were then delivered to the gut through a shellac-membraned capsule to combat against pathogens like Shigella. Multiple objectives have been achieved to prove our product.</p>
+<h2 id="construction-of-recombinant-plasmids-for-yeast-surface-display"><a class="header" href="#construction-of-recombinant-plasmids-for-yeast-surface-display">Construction of recombinant plasmids for yeast surface display</a></h2>
+<p>In order to enable yeast to express surface protein conjugated with target proteins, we cloned the nanobody gene sequence and the antigen gene sequences into the vectors. The vector pYD1 is a yeast surface display unit where the surface-sealed protein Aga2 was controlled by GAL1 promoter. Using XhoI and ApaI, the nanobody gene 20ipaD and the antigen gene ipaD was cloned into the corresponding restriction sites. The gene segment of 20ipaD was ~500bp, while that of ipaD was ~1000bp. The PCR results that amplify an originally ~400bp fragment of empty vector supported the success in plasmid construction (Figure 1, Figure 2). Sequencing data of the region further confirmed the construction of correct plasmids (Figure 3).</p>
+<h2 id="construction-of-engineered-yeasts-that-display-nanobodies-and-capable-for-use"><a class="header" href="#construction-of-engineered-yeasts-that-display-nanobodies-and-capable-for-use">Construction of engineered yeasts that display nanobodies and capable for use</a></h2>
+<p>Using the plasmids constructed in the previous steps, baker's yeast EBY100 was transformed. Considering the TRP1 maker in the plasmid, the yeast was selected on the SCDAA medium where tryptophan was absent. Colonies appeared after incubation, indicating the success of engineered probiotic construction (Figure 4). The yeasts that were transformed with recombinant plasmids were now able to display the nanobodies on their surface.</p>
+<p>Then, the yeasts were induced by galactose, which can promote the transcriptional activity of GAL1 promoter. After 24h induction, a portion of the cells were shown to display the anticipated proteins on their surface by immunofluorescent microscopic imaging (Figure 5).</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig-1.png" alt="y-fig-1" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig-2.png" alt="y-fig-2" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig3.png" alt="y-fig3" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig4.png" alt="y-fig4" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig5.png" alt="y-fig5" /></p>
+<h2 id="summary-and-conclusion"><a class="header" href="#summary-and-conclusion">Summary and conclusion</a></h2>
+<p>As a drug of a novel strategy to target the pathogen, our engineered probiotics should combat the pathogenic Shigella by displaying nanobodies on surfaces to efficiently get over the antibiotic resistance problem. To prove the feasibility and efficiency of this proposed drug, evidence from different aspects should be taken into consideration. First, the most solid and important evidence should be the entity of the imagined product. In wet lab, we have shown the success construction of nanobody-displaying yeasts, proving the possibility and authenticity of producing such engineered probiotics. Second, whether the probiotic works to inhibit pathogen would be another important evidence to prove the efficiency of this drug. We also shown the success of pathogen-mimicking yeasts construction and proposed the binding affinity assay that could prove the inhibition feature of the engineered probiotics. Third, evidence for optimization possibility is required to prove the improvement potential of the drug. For the collection of evidence from this aspect, multiple expression enhancement elements refitting and mutation-screening binding affinity enhancement were designed to get the optimized combination of expression abundancy and binding affinity. Last but not least, a solid storage and delivery method should be risen as evidence proving the practicability and productization ability. The shellac-based microcapsulation plus tablet/capsule wrapping theoretically achieved the room temperature storage and intestine-target release of engineered probiotics, thus proving the reliability of low-cost production and storage of the whole drug and the target specificity of the efficient component.</p>
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diff --git a/public/results.html b/public/results.html
index bef21162183dad85a90a691beb56762a9553039f..83b18a9bf207aacba03673d44636e48765709998 100644
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-<h1 id="results"><a class="header" href="#results">Results</a></h1>
+<div class="h1-bg">
+ <h1 class>Results</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/wetlab8-for-bg.png" />
+</div>
<h2 id="introduction"><a class="header" href="#introduction">Introduction</a></h2>
<p>This page will give a detailed record about the experiment results, future plans & project achievements.</p>
<h2 id="experiment-results"><a class="header" href="#experiment-results">Experiment Results</a></h2>
<h3 id="yeast"><a class="header" href="#yeast">Yeast</a></h3>
+<h4 id="summary-of-lab-design"><a class="header" href="#summary-of-lab-design">Summary of Lab Design</a></h4>
+<p>In order to decorate the yeast surface with nanobodies against the pathogen, we designed the vector which contains the nanobody gene behind a membrane-sealed protein. The overall experiment design could be divided into 3 phases. In phase I, the expected vector that could potentially express our designed module would be constructed and stored. In phase II, the expression vector would be transformed into yeast and detected for its expression abundance and location. In phase III, the binding affinity and inhibitory efficiency on pathogen would be tested. Due to the limitation of materials and time under the background of local pandemic situation, the experiments only accomplished Phase I & II.</p>
+<h4 id="genes-of-nanobody-and-pathogen-were-harvested"><a class="header" href="#genes-of-nanobody-and-pathogen-were-harvested">Genes of nanobody and pathogen were harvested</a></h4>
+<p>The DNA sequence of nanobody 20ipaD and antigen ipaD were obtained from Sangon in the form of pUC19 plasmid insertions, which were stored inside E. coli. The storage bacteria were amplified, and plasmids containing sequences of interest were extracted with Plasmid mini-prep kit from TIangen. Those plasmids were digested by XhoI and ApaI, and the sequences of interest were recycled by agarose gel recycle kit from Beyotime (<strong>Fig1</strong>).</p>
+<h4 id="recombinant-plasmids-were-constructed"><a class="header" href="#recombinant-plasmids-were-constructed">Recombinant plasmids were constructed</a></h4>
+<p>The purified ipaD and 20ipaD DNA segments mentioned in the previous section, along with the pYD1 vector digested by XhoI & ApaI, were ligated, and transformed into DH5α cells that were selected by ampicillin. Colony direct PCR was applied to inspect the plasmid condition of the colonies formed. pYD1-forward and pyd1-reverse primers were used to show the size of Aga2-Protein, thus verifying the sequence between the primer pairs (<strong>Table 1</strong>). The size of pYD1-ipaD plasmid primer box should be about 1500bp, while the size of pYD1-20ipaD should be about 1000bp. As shown in <strong>Fig2 a</strong>, sample “2-3â€, “2-5†meet the requirement for pYD1-ipaD, so the bacteria in those colonies contain the recombinant plasmid pYD1-ipaD. Additionally, all samples in lane 1~10 met the requirement for pYD1-ipaD, which indicates the bacteria in those colonies contain pYD1-20ipad recombinant plasmids (<strong>Fig2 b</strong>). Those colonies were amplified, and the plasmids were extracted. Sequencing data further supported the successful construction of the recombinant plasmids (<strong>Fig3</strong>).</p>
+<h4 id="recombinant-plasmids-were-transformed-into-yeast-eby100"><a class="header" href="#recombinant-plasmids-were-transformed-into-yeast-eby100">Recombinant plasmids were transformed into yeast EBY100</a></h4>
+<p>We performed yeast transformation using constructed pYD1-ipaD and pYD1-20ipaD plasmids. Yeast competent cells were prepared by Frozen-EZ Yeast transformation II kit (Zymo Research, T2001). The yeasts were successfully transformed by chemical method using carrier DNA and PEG/LiAc. The plasmids and competent cells were thawed on ice. 10μL of Carrier DNA and 2μg of plasmid was added into 100μL of competent cells. Then 500μL of PEF/LiAc solution was added. The tube was inverted 6-8 times and incubated at 30°C with an inversion at 10-minute interval. Then, 20μL of DMSO was added to increase the transformation efficiency. Then, the tube was incubated under 42°C with an inversion of 5-minute interval. The cells were centrifuged at 12000rpm for 5 seconds and incubated with YPD medium for 1 hour at 30°C. After incubation, the cells were pelleted and resuspend by 100μL of 0.9% NaCl, 50μL of which were spread onto SDCAA medium, and another 50μL of cells onto YPD medium. The plates were incubated at 30°C for 2 days.</p>
+<p>The result of the plates was positive (<strong>Fig4</strong>). SDCAA plates, which are the selective plates lack of tryptophan, has demonstrated fewer colony growth compared to YPD plates, indicating successful transformation. Single colonies were taken and incubated at 30°C in SDCAA liquid medium for amplification.</p>
+<h4 id="nanobody-and-antigen-were-expressed-and-displayed-on-yeast-surface"><a class="header" href="#nanobody-and-antigen-were-expressed-and-displayed-on-yeast-surface">Nanobody and antigen were expressed and displayed on yeast surface</a></h4>
+<p>The yeasts that were transformed with pYD1-ipaD, pYD1-20ipaD, and pYD1 were amplified in SDCAA liquid medium for 36h. The cells were harvested by centrifuge at 5000xg for 5 minutes and diluted in SGCAA liquid containing the induction agent galactose to obtain an OD600=0.5. Four milliliters of each diluted cells were transferred into new culture tubes and induced at 21°C for 24h. An additional prep of EBY100 cells without plasmids were also diluted to OD600=0.5 and induced in SGCAA for 24h.</p>
+<p>The induced cells were harvested and washed with PBS. The yeasts containing pYD1-ipaD were inoculated with rabbit anti-HA tag antibodies, while the yeasts containing pYD1-20ipaD, pYD1, or no plasmids were inoculated with rabbit anti-FLAG tag antibodies and BSA. After washed with PBS, the cells were inoculated with FITC-conjugated goat anti-rabbit immunoglobin antibodies and BSA without light. The cells were washed twice with PBS before imaged under UV-light. As <strong>Fig5</strong> shows, the yeasts containing pYD1-ipaD and pYD1-20ipaD emitted green fluorescence, whereas the yeasts containing empty plasmids, or no plasmids did not. This fluorescence pattern proved the yeasts indeed expressed and displayed the nanobody and the antigen on their surfaces, which announced the success of engineering.</p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig-1.png" alt="y-fig-1" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig-2.png" alt="y-fig-2" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig3.png" alt="y-fig3" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig4.png" alt="y-fig4" /></p>
+<p><img src="https://static.igem.wiki/teams/4161/wiki/y-fig5.png" alt="y-fig5" /></p>
<h3 id="lactococcus-lactis"><a class="header" href="#lactococcus-lactis"><em>Lactococcus lactis</em></a></h3>
<h3 id="escherichia-coli"><a class="header" href="#escherichia-coli"><em>Escherichia coli</em></a></h3>
<h4 id="summary-of-experiment-design"><a class="header" href="#summary-of-experiment-design">Summary of Experiment Design</a></h4>
-<p>We plan to display the nanobody JPS-G3 agianst the <em>Shigella</em> antigen ipaD on the surface of E.<em>coli</em> Nissle 1917 via the curli fiber protein <em>csg</em>A <sup class="footnote-reference"><a href="#Gelfat,2021">1</a></sup>. We expect the engineered E.<em>coli</em> Nissle 1917 to be capable of capturing the pathogen <em>Shigella flexneri</em> via antigen-antibody specific binding. Please check the detailed experiment design at 'design' part.</p>
+<p>We plan to display the nanobody JPS-G3 agianst the <em>Shigella</em> antigen ipaD on the surface of E.<em>coli</em> Nissle 1917 via the curli fiber protein <em>csg</em>A <sup class="footnote-reference"><a href="#Gelfat,2021">1</a></sup>. We expect the engineered E.<em>coli</em> Nissle 1917 to be capable of capturing the pathogen <em>Shigella flexneri</em> via antigen-antibody specific binding.</p>
<h4 id="plasmid-extraction"><a class="header" href="#plasmid-extraction">Plasmid Extraction</a></h4>
<p>pUC19-JPS-G3-3xHA and pUC19-ipaD-3xHA were extracted using the TIANGEN plasmid extraction kit.</p>
<h4 id="target-sequence-amplification"><a class="header" href="#target-sequence-amplification">Target Sequence Amplification</a></h4>
@@ -119,14 +139,14 @@
<tr><td>JPS-G3_FW</td><td>CGCGGATCCGGAAGTACACAAGTACAGCTAG</td><td><em>Bam</em>HI</td></tr>
<tr><td>JPS-G3_RV</td><td>CGCGGATCCGGAAGTACACAAGTACAGCTAG</td><td><em>Xho</em>I</td></tr>
</tbody></table>
-</div><img src="https://static.igem.wiki/teams/4161/wiki/e-labnote-8-31-1.png" width="500"/>
+</div><img src="https://static.igem.wiki/teams/4161/wiki/e-labnote-8-31-1.png"/>
<p><strong>Figure 1</strong> | Gel Electrophoresis Result for Target Sequence Amplification</p>
<h4 id="molecular-cloning-for-cytoplasmic-protein-expression"><a class="header" href="#molecular-cloning-for-cytoplasmic-protein-expression">Molecular Cloning for Cytoplasmic Protein Expression</a></h4>
<p>In order to construct the recombinant plasmids pET30a-ipaD-3xHA and pET30a-JPS-G3-3xFLAG, the PCR products obtained from the last step were digested by endonucleases <em>Bam</em>HI and <em>Xho</em>I to create sticky ends. Meanwhile, the pET30a plasmids were transformed into E.<em>coli</em> DH5a competent cells for propagation. After transformation and overnight culture, the extracted plasmids were also digested with endonucleases <em>Bam</em>HI and <em>Xho</em>I to create sticky ends. Afterwards, the digested plasmids and target sequences were ligated and transformed into E.<em>coli</em> DH5a competent cells (<strong>Figure 2</strong>).</p>
-<img src="https://static.igem.wiki/teams/4161/wiki/e-labnote-9-13-2.jpg" width="500"/>
+<img src="https://static.igem.wiki/teams/4161/wiki/e-labnote-9-13-2.jpg"/>
<p><strong>Figure 2</strong> | Plates for pET30a-ipaD-3xHA (i-1 & i-2) and pET30a-JPS-G3-3xFLAG (J-1 & J-2).</p>
<p>Single colonies were picked from the plates and the inserted sequence were verified by colony PCR (<strong>Figure 3</strong>) and Sanger sequencing.</p>
-<img src="https://static.igem.wiki/teams/4161/wiki/e-labnote-9-14-1.png" width="500"/>
+<img src="https://static.igem.wiki/teams/4161/wiki/e-labnote-9-14-1.png"/>
<p><strong>Figure 3</strong> | Gel Electrophoresis Result for Colony PCR</p>
<h4 id="overlap-extension-pcr"><a class="header" href="#overlap-extension-pcr">Overlap Extension PCR</a></h4>
<p>In order to construct the recombinant DNA sequences csgA-JPS-G3-3xFLAG and csgA-ipaD-3xHA, the following overlap extension PCR primers are used (<strong>Table 2</strong>).</p>
@@ -182,13 +202,19 @@
</ul>
<h2 id="reference"><a class="header" href="#reference">Reference</a></h2>
<div class="footnote-definition" id="Gelfat,2021"><sup class="footnote-definition-label">1</sup>
-<p>Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). <em>bioRxiv</em>. <a href="https://doi.org/10.1101/2021.06.18.448998">https://doi.org/10.1101/2021.06.18.448998</a></p>
+<p>Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic <em>E. coli</em> Nissle 1917 (p. 2021.06.18.448998). <em>bioRxiv</em>. <a href="https://doi.org/10.1101/2021.06.18.448998">https://doi.org/10.1101/2021.06.18.448998</a></p>
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@@ -99,7 +99,10 @@
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-<h1 id="safety"><a class="header" href="#safety">Safety</a></h1>
+<div class="h1-bg">
+ <h1 class>Safety</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/wetlab4-for-bg.png" />
+</div>
<h2 id="introduction"><a class="header" href="#introduction">Introduction</a></h2>
<p>The Duke Kunshan University (DKU) iGEM team sets safety as an integral part of
science. It includes protection for sensitive groups and the environment. For
@@ -117,7 +120,7 @@ disposal of hazardous substances. Also, experiments were first presented in
detail by our two supervisors to eliminate biosafety concerns.</p>
<h2 id="microorganisms-review"><a class="header" href="#microorganisms-review">Microorganisms review</a></h2>
<p>Protein expression for diagnostic tests was performed in non-pathogenic
-Escherichia coli strains (E.coli Nissle 1917), Lactococcus Lactis NZ9000 and
+Escherichia coli strains (E.coli Nissle 1917), <em>Lactococcus lactis</em> NZ9000 and
yeast (EBY100). These gene carriers are probiotic or at least harmless. They do
not possess serious illnesses or lead to other problems to people or the
environment. In addition, they are in whitelist, belonging to BSL-1 organisms.</p>
@@ -168,6 +171,12 @@ fluid before and after conducting wetlabs.</p>
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Shigella, as one of the most antibiotic resistant pathogens, poses a great threat to food safety especially in developing areas. 10 million will be subject to mortalities caused by shigella infection by 2050. Distribution of antibiotics is the main treatment as of today. It is costly and time consuming. Side effects include degration of GI tract microbiome, and the emergence of more antibiotic resistant strains. We are in an endless race against pathogens. Antibiotics are our weapons. Mutations are their strategies to survival. Now, DKU iGEM team has proposed an alternative to jump out of this race and possibly, go far beyond. Antibody therapy is a popular topic in therapeutics. It is different from antibiotics and can be more effective when triggering the host immune system. However, conventional antibodies have a high cost because of the complicated synthesis procedure. It can also be vulnerable to proteosomes in the GI tract. Thus we propose a novel method to display nanobodies on the surface of probiotics. It exploits the natural pathogen inhibition effects of the probiotics. It also explores possibilities of antibody therapy mass production. Click on the left menu to learn more about the details.","breadcrumbs":"Home","id":"0","title":"Home"},"1":{"body":"","breadcrumbs":"Team » Team","id":"1","title":"Team"},"10":{"body":"Jiani Chen Yang Yu","breadcrumbs":"Team » Team » Advisor","id":"10","title":"Advisor"},"100":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161301 | Single Domain Antibody 20ipaD Conjugated Aga2 Express Module | http://parts.igem.org/Part:BBa_K4161301 | | BBa_K4161508 | Composite part | http://parts.igem.org/Part:BBa_K4161508 |","breadcrumbs":"Parts » Part Collection » Key composite segment","id":"100","title":"Key composite segment"},"101":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161302 | pYD1 plasmid | http://parts.igem.org/Part:BBa_K4161302 |","breadcrumbs":"Parts » Part Collection » Vector","id":"101","title":"Vector"},"102":{"body":"","breadcrumbs":"Parts » Improve","id":"102","title":"Parts"},"103":{"body":"","breadcrumbs":"Safety » Safety","id":"103","title":"Safety"},"104":{"body":"The Duke Kunshan University (DKU) iGEM team sets safety as an integral part of science. It includes protection for sensitive groups and the environment. For this reason, safety was considered from two perspectives—inside and outside the laboratory. For more detailed information, please check our safety form.","breadcrumbs":"Safety » Introduction","id":"104","title":"Introduction"},"105":{"body":"All laboratories of universities in China must be accredited by the Office under the Ministry of Environment following the standard. This year, the project was conducted in the BSL-1 laboratory. Team members wore lab coats and gloves during experiments. Experiments related to bacteria were performed in the biosafety cabinet and near butane burners. Before laboratory started, the team received safety training including how to use equipment properly, following laboratorial hygiene rules and proper disposal of hazardous substances. Also, experiments were first presented in detail by our two supervisors to eliminate biosafety concerns.","breadcrumbs":"Safety » Lab Safety","id":"105","title":"Lab Safety"},"106":{"body":"Protein expression for diagnostic tests was performed in non-pathogenic Escherichia coli strains (E.coli Nissle 1917), Lactococcus Lactis NZ9000 and yeast (EBY100). These gene carriers are probiotic or at least harmless. They do not possess serious illnesses or lead to other problems to people or the environment. In addition, they are in whitelist, belonging to BSL-1 organisms.","breadcrumbs":"Safety » Microorganisms review","id":"106","title":"Microorganisms review"},"107":{"body":"The engineered probiotics were designed to express 20ipad nanobody on their surface by transforming recombinant plasmids with optimized genes. Thus, they can combine with the antigen on the surface of Shigella. Since Shigella is one of the BSL-2 organisms, we decide to express our targeted antigen in probiotics that we used to express the antibody. We optimized the DNA sequences which code the antigen by using machine-learning software. Using yeast as an example, amino acids are essential for the growth of yeast. Amino acids are absorbed by human bodies in the small intestine. There is a competitive absorption of amino acids between intestinal epithelial cells and yeast. This prevents the overgrowth of yeast cells, preventing the destruction of bacterial flora structure. Using yeast as gene carriers limits the leak of antibiotics resistance genes, compared with using bacteria as carriers. In addition, galactose was used to induce the expression of the antibody and antigen. Since we used antibiotics resistance genes, we also pay attention to the potential risks of the leak of antibiotics resistance genes during wetlab process. Discarded liquids and plates that contain antibiotics were placed in specific vessels and then autoclaved.","breadcrumbs":"Safety » Experiments","id":"107","title":"Experiments"},"108":{"body":"Part of planned experiments had to be done by using harmful reagents or procedures. All team members follow the rules under the guideline provided by our lab manager and assistants during experiment safety training. UV light was used to sterilize the biosafety cabinets and equipment inside the cabinets. Safety measures were taken to avoid people`s direct exposure to UV light. Gel imaging system was used for visualizing agarose gel, combined with standard laboratory procedures with blue light transilluminator. Antibiotics were used to select transformants. They can be harmful to sensitive groups. Situations of allergy of team members were collected. Antibiotics were well stored and Handled with proper safety measures according to disposal protocols. Other hazardous chemicals , such as Tris-HCl and methyl alcohol were stored and relevant procedures were conducted in chemical ventilation cabinets. Liquid waste was handled with appropriate safety measures.","breadcrumbs":"Safety » Harmful reagents and procedures","id":"108","title":"Harmful reagents and procedures"},"109":{"body":"Team members followed all the government and university guidelines based on the pandemic situation of Covid-19 in China. For April and May, team`s meetings were online because of school closure and in-person activities were allowed after deblocking. Covid-19 tests were performed regularly and all team members got vaccinated. When wetlabs began, team members` attendance was recorded. The usage of lab equipment was registered. All working surfaces were cleaned with disinfectant fluid before and after conducting wetlabs.","breadcrumbs":"Safety » Covid-19 associated safety measures","id":"109","title":"Covid-19 associated safety measures"},"11":{"body":"Lingfeng Huang","breadcrumbs":"Team » Team » Principal Investigator","id":"11","title":"Principal Investigator"},"110":{"body":"","breadcrumbs":"Human Practices » Human Practice","id":"110","title":"Human Practice"},"111":{"body":"We interviewed Huansheng Cao, Assistant professor of Environmental Science at Duke Kunshan University for suggestions on our initial lab plans. In the interview, team members Yuxin Wang and Chang Shen presented the main design, bacterial surface display, to consult Prof Cao on its feasibility. After confirming the rich research foundations of our plan, he encouraged us to add computational elements to our lab design. As a scientist working in computational biology and bioinformatics, he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody and the antigen unit. As a well-trained biologist, he also suggested fitting our design to more than one model organisms, which shows integration in our drug design. The interview was full of enthusiasm, so we were able to come across many other topics. We discussed the trends in bioinformatics and biotechnology, including bacteria-based bioelectricity, and the relationship between human longevity and gut microbiota. This interview was both encouraging and informative, and contributed greatly to the first stage of human practice. photo","breadcrumbs":"Human Practices » Interview with Prof Cao","id":"111","title":"Interview with Prof Cao"},"112":{"body":"We participated in 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. It encourages students to participate in scientific research, technological development, and entrepreneurship. During the final pitch, Lisa Wu and Lingrui Lai made the presentation about our project of Shigella treatment using the concept of of synthetic biology. Lingrui went through the basic concept of shigella and synthetic biology, then, the current challenges that we are facing for shigella treatment and our suggestions. Lisa introduced the methodology involved and techniques used in our project. At the end they stressed the significance of our project. Judgers include Kai Huang (Division Chair of Natural and Applied Sciences of DKU), Joohyun Lee (Assistant professor of biology of DKU), Anastasia Tsigkou (Associate Professor of Biology of DKU), Ming-Chun Huang (Associate professor of data and computational science of DKU), Liqi Ren (Associate Director for Innovation and Entrepreneurship). After the presentation, Prof. Lee and Dr. Tsigkou presented valuable questions and suggestions. Prof. Lee recognized the difficulty of antibody therapy and informed us of the clear restrictions of FDI approval. We assured him that our project nanobodies are thoroughly researched, and that we will continue to modify the project to enhance biosafety. Dr. Tsigkou asked us about the binding affinity test and false positive. This is a question that did not come to us then, so we answered that the detection is conduct through fluorescence microscopy. After discussion with our PI, Prof. Linfeng Huang, we decide that we will use the pull down method in the detection of binding affinity. We will conduct the experiment by pulling down on both sides of the nanobody-antigen complex. For false positives, DKU iGEM member Lingrui Lai suggested isotype testing.","breadcrumbs":"Human Practices » 2022 College Student Innovation and Entrepreneurship Training Program","id":"112","title":"2022 College Student Innovation and Entrepreneurship Training Program"},"113":{"body":"After we successfully predicted the 3d structure of fusion protein-antibody complex by using Robetta and Alphafold2, the focus shift to how the fusion protein will influence the binding (docking) between antibody and antigen. We plan to get some insights about this from computer modeling before the wet lab begins. We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University for suggestions on our protein docking simulation. At the beginning, team leader Lisa Wu introduced the synthetic biology part of our project. Modeling team leader Zhenyu Xu introduced the progress of protein structure prediction and the need for protein docking simulation. As a scientist working in modern medicine, Prof. Floyd pointed us to some useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These software are powerful at predicting the docking scenario and are used by many researchers, with many online teaching resources accessible. To improve the speed of computer modeling, Prof. Floyd emphasized the preprocessing of protein structures. Namely, the antigen structure. He suggested us delete the floating molecules outside the binding sites and keep those inside, since we only care about the binding scenario. He also pointed that virtual screening could help if we want to do more mutations to the binding sites. Concerning the fusion protein-antibody complex models, since they are the optimal prediction given by Robetta and Alphafold2, we assume these models do not need preprocessing anymore. For docking, he suggested us try rigid docking first, and then flexible docking if we want to get closer to reality.","breadcrumbs":"Human Practices » Interview with Prof Floyd","id":"113","title":"Interview with Prof Floyd"},"114":{"body":"In order to have better educational effect and promote our project , we organized the Journal Club activity in the Duke Kunshan community. The first Journal Club was held on April 30th, 2022. At the very beginning of the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us and introduced in detail what systems biology is and the basic methods of studying systems biology. This journal club event mainly focused on COVID-19 and then developed into three sub-topics including the antigen test for SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the iGEM team, around 10 freshman students with various backgrounds participated in the sharing and raised many inspiring questions.","breadcrumbs":"Human Practices » Journal Club","id":"114","title":"Journal Club"},"115":{"body":"","breadcrumbs":"Human Practices » Interview with Dr. Neel Joshi","id":"115","title":"Interview with Dr. Neel Joshi"},"116":{"body":"Dr. Neel Joshi is an expert in bioengineering with tracks in human disease and new therapies. In his 2019 and 2021 literature, he and his team described genetically engineering E. coli Nissle 1917 to treat some gastrointestinal diseases like bowel inflammation, which provide essential references for our project. To further understand the logics and advantages of this bioengineered model, we invited Dr. Joshi for an interview. Dr. Joshi interview photo 1","breadcrumbs":"Human Practices » Introduction","id":"116","title":"Introduction"},"117":{"body":"Q: What stimulated you and your team to develop the surface-displaced single domain antibodies? What practical problems do you think this model can solve? A: Although the nanobodies have great potentials in treating gastrointestinal diseases, it is somewhat hard to deliver those nanobodies directly to the digestive track. Therefore, the probiotics can serve as a scaffold to make the delivery of nanobodies easy. Q: But why did you choose to display the nanobodies on the surface? Why not directly make the bacteria synthesize nanobodies and release them? A: The surface display resolution has the property of multi-valency. By displaying the nanobodies on the surface, we would have the potential to space the binding domains together to bind to a pathogen surface. It could increase binding affinity and decrease the dissociation constant. It can also diffusion into different directions and increase the local concentration. Q: What about the method of drug delivery? That is to say, how do you decide to send the engineered probiotics to human gastrointestinal track? And could you explain why you use that delivery method? A: We only proposed an approach of micro biological therapy. But to deliver the bacteria, I think it can be freeze-dried to produce a freeze-dried product. Because a large portion of the geographical locations that suffered from these gut problems are the poor areas, and those areas do not have the condition to store the bacteria that require a very low temperature. The freeze-dried products do not require that strict storage conditions, so they are more available in those areas. Q: Why pBbB8k plasmid backbone with kanamycin selection marker? (what's the difference between pUC19, which is our choice, and pBbB8K?) A: pBbB8k is a rather arbitrary choice, we simply chose it because it was used due to antibiotics incompatibility in the previous experiment. When doing in vivo studies, we engineered plasmids from the original E. coli Nissle genome, the pMUT plasmids. These plasmids are more stable than the pBbB8K. For pUC19, I don’t see problems with the expression of pUC19 plasmid. However, you do need to consider if your antibiotic resistant marker in the plasmid is compatible with the shigella testing. If shigella is killed due to the antibiotic selecting E. coli, it can be a problem. Q: What are the setbacks of the Probiotic-associated therapeutic curli hybrids (PATCH) system? A: The first is safety concerns of curli fibers. It has been known that curli fibers induce various types of diseases, including neurological diseases, etc. The other is inherit disadvantages for E. coli to produce curli fibers in vivo. However, we have been able to shown effective production of curli fiber in vivo by measuring the amount of curli fibers coming from the fecal samples. Q: What if the E. coli went out of control and grow infinitely in the gut, disrupting the original gastrointestinal microorganism environment? A: This is a very popular question when it comes to distributing microbes to gut. Actually, we could use some of the auxotrophic strains to limit the growth of the bacteria. And I think there are many “switches†that can turn on the suicide program of those bacteria. But in this case, I think E. coli Nissle 1917 is a very safe bacteria, it has already been identified as a harmless bacterium, so there should be less safety issues of this strain.","breadcrumbs":"Human Practices » Interview Content","id":"117","title":"Interview Content"},"118":{"body":"Q: Is it possible to apply magnetic triggers to shigella infection and cooperate this into the PATCH system? A: Magnetic triggers are mostly applied in cancer treatment. This is because in cancer, you know the spot of the disease. In bacterial infection it’s hard to locate. Q: In Barta et al., the authors described the different indexes of the nanobodies, including binding domains and neutralization effects. What is your rationale when choosing the nanobodies? A: It really depends on how you generate the nanobodies. When different parts of the pathogen are used in Alpaca immunizations, the nanobodies will vary. When displaying the nanobodies, some work and others don’t. We assume this is because of folding problems, but we did not figure out the exact reason. Q: What do you think about sequence optimization in silica? Do you have experience working with this? Do you have any suggestions? A: I would suggest generating different mutations in the sequence and do some docking analysis. Then generate the mutations and do wet labs. Q: Our project aims to tackle the antibiotic resistance problem worldwide. Would the PATCH system generate drug resistance issues? A: This is possible. For example, a mutation in the binding domain of the antigen might cause binding problems. However, I would say the selective pressure by the nanobody is smaller compared to that of the antibiotic. This is because antibiotic kills the pathogen, while PATCH only binds to the pathogen, keeping it from invasive activities. Q: We are worried that the proteins in the GI tract environment would coat the surface of the probiotic, which would cause dysfunction of the nanobodies. How did your team encounter this problem? A: The animal model was effective, which was sufficient to show that the GI tract environment did not inhibit the binding activity. The curli production is continuous in vivo, which provides adequate chance for the binding to occur. However, the proteases in the GI tract is something to consider.","breadcrumbs":"Human Practices » Q&A Section","id":"118","title":"Q&A Section"},"119":{"body":"Dr. Joshi provided lots of perspectives from a brand-new aspect, which were extra inspirable for the whole team. First, Dr. Joshi elaborated on the practical problems that this model could potentially resolve. That the probiotic expression system could make the delivery of nanobodies easier expanded our understanding of the model as the delivery problem does not only exist in the step of bacteria delivery, it starts from the delivery of the essential nanobodies. Next, the freeze-dry delivery approach gives a less stricter storage condition of this drug, making it more available in poor areas, which corresponds with our assumed delivery method. As for the safety problem that the public is most interested in, Dr. Joshi proposed to use some molecular switches to eliminate those bacteria in addition to using safe strains like Nissle, giving important clue and indication for our project design. In the Q&A section, questions regarding drug localization, drug resistance, choice of nanobodies were mentioned by team members. Dr. Joshi gave many valuable advices depending on the questions. Overall, the interview was successful, and we were able to arm ourselves with adequate knowledge for the wet lab.","breadcrumbs":"Human Practices » Summary and Reflection","id":"119","title":"Summary and Reflection"},"12":{"body":"","breadcrumbs":"Team » Team » The whole team","id":"12","title":"The whole team"},"120":{"body":"Club expo figure 1 We participated in 2022 online DKU club expo, introducing IGEM club to international students. Our club is meant to share knowledge and techniques of biosynthesis and to seek for potential team members of DKU IGEM team next year. The relevant club activities are conducted in the form of student presentation and speeches given by guest speakers. The IGEM team composition has also been introduced to DKU students from class of 2026. We divided IGEM teamwork into 4 parts, biological experiments, modelling, wiki design and human practice. For the offline club expo, we also made a small presentation to spread common knowledge about probiotics and provided our advice for consuming commercial probiotic products. Our central idea is that the aim of commercial probiotic products should be limited to minor gut discomforts or hoping to improve general health, and long-term consumption is not suggested by doctors we consulted. Also, we introduced some potential harms of consuming probiotics, trying to give them a full image of the commonly advertised probiotic products. We brought some experimental equipment, such as microcentrifuge tubes and plates, to introduce some basic experimental skills. Students who attended the club expo got basic knowledge of how to streak in an agar plate and how to use micropipette and centrifuge machines. Besides providing basic knowledge and doing the offline presentation, we prepared some interesting questions related to Biology and gut microbiomes for college students from all majors. They were designed to enlarge their knowledge about gut microbiomes and make biology interesting. The questions include \"how H. pylori were proved to be able to cause ulcers,\" \"pick out the probiotics from several names of microorganisms,\" \"estimate the number of microorganisms in their stomach,\" and so on. Club expo figure 2","breadcrumbs":"Human Practices » Club Expo","id":"120","title":"Club Expo"},"121":{"body":"","breadcrumbs":"Human Practices » GI tract & Probiotics Brochure","id":"121","title":"GI tract & Probiotics Brochure"},"122":{"body":"The human GI (Gastrointestinal) tract consists of stomach (pH = 2), small intestine (pH = 4-5), and large intestine (pH = 7), which comprises 200 m^2 of surface area in total ( Figure 1 ). It is responsible for the digestion of food and absorption of nutrients. Figure_1 Figure 1 | The GI tract. [1]","breadcrumbs":"Human Practices » GI Tract","id":"122","title":"GI Tract"},"123":{"body":"A normal functioning human body contains the visible human organs, such as the heart, lung, brain etc. containing 10^-14 cells (~23000 genes), and the invisible microbiome, which is a group of up to 10^-14 million microbes (~9 million genes) that live in your body. These bacteria help with digestion, destroys harmful bacteria, and helps control your immune system. The interaction between the host (human) and its microbiota is complex; thus, knowing the human microbiome helps with the development of biomarkers for predicting predisposition to diseases, designing targeted therapies, personalized drug therapies and probiotics. Figure_2 Figure 2 | Oversight of major microbial populations in the body sites sampled by human microbiome projects. [2] The GI microbiota contains 10^13 to 10^14 microbial cells. Microbes in gut affect early development, health, and predisposition to disease. The microbial colonization of gut begins at birth. As is shown in Figure 2 , from sampling data of the human microbiome project, in the GI tract, the species Bacteroidetes and Firmicutes have the highest abundance, followed by Proteobacteria , Tenericutes , and others. The microbial population in different areas of the GI tract are influenced by diet and the physical conditions in the area. In the stomach and small intestine, the low pH level prevents the growth and colonization of many microbials; however, Firmicutes , Bacteroidetes , and Actinobacteria are commonly found in the gastric fluid, while Firmicutes and Proteobacteria are common in the mucus layer of the stomach. Some pathogens, such as Helicobacter pylori , are also discovered in the gastric mucosa. Figure_3 Figure 3 | Different microenvironments in the large intestine. [2] The microbiome in the large intestine generally serves as an in vivo fermentation vessel, with the microbiota using nutrients derived from the digestion of food ( Figure 3 ). The essential biochemical and metabolic contributions of intestinal microorganisms contain different types of vitamins (e.g., thiamine, riboflavin, pyridoxine, B12, K, etc.), amino acids (e.g., asparagine, glutamate, methionine, etc.), gases (e.g., CO2, CH4, H2), odor, organic acids, glycosidase reactions, and steroid metabolism. As a result, the pathological changes in the GI tract microbiome may lead to deficiencies in important metabolic reactions (e.g., lack of vitamin B12 may lead to pernicious anemia – the red blood cells cannot function well).","breadcrumbs":"Human Practices » GI Microbiome","id":"123","title":"GI Microbiome"},"124":{"body":"Currently, physicians usually recommend using antibiotics when treating GI tract bacterial infections. However, since antibiotics usually also kill the beneficial microbiota, it increases the risk of developing IBD (inflammatory bowel disease) after treatment. IBD is characterized of chronic inflammation of the GI tract, which may result in irreversible damage. In addition, some antibiotics can cause ADR (adverse drug reaction) and allergies. Therefore, the development of alternative treatment methods, such as the use of probiotics, have attracted much attention. Unlike antibiotics, probiotics do not kill all the bacteria in an unbolted way. They help inhibit the growth of pathogens and preserve the healthy microbiota via competitive exclusion, anti-adherence, etc. Recently, engineered probiotics have also become a hot topic for new drug development.","breadcrumbs":"Human Practices » GI Microbiome, Antibiotics, and Probiotics","id":"124","title":"GI Microbiome, Antibiotics, and Probiotics"},"125":{"body":"Brock, T. D., Madigan, M. T., Martinko, J. M., & Parker, J. (2003). Brock biology of microorganisms. Upper Saddle River (NJ): Prentice-Hall, 2003. Peate, I. (2018). Anatomy and physiology, 9. The gastrointestinal system. British Journal of Healthcare Assistants, 12(3), 110–114. https://doi.org/10.12968/bjha.2018.12.3.110","breadcrumbs":"Human Practices » Reference","id":"125","title":"Reference"},"126":{"body":"photo Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo In GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo In probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Education","id":"126","title":"Education"},"127":{"body":"photo Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo In GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo In probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Education » Education","id":"127","title":"Education"},"128":{"body":"","breadcrumbs":"Awards » Entrepreneurship","id":"128","title":"Awards"},"129":{"body":"","breadcrumbs":"Awards » Hardware","id":"129","title":"Awards"},"13":{"body":"","breadcrumbs":"Team » Attributions » Attributions","id":"13","title":"Attributions"},"130":{"body":"","breadcrumbs":"Awards » Inclusivity","id":"130","title":"Awards"},"131":{"body":"","breadcrumbs":"Awards » Measurement","id":"131","title":"Awards"},"132":{"body":"Models are powerful tools in terms of imagining reasonable future scenarios. Also, assumptions and results from the model push us to reflect on the present situation and make adjustments to our existing plans and experiments, which might also develop our final goal into a more realistic version. There are 2 modeling sections in our project: Visualization This section mainly shows the structure of proteins and their docking results, and also tries to provide guides for future experiment design. Description and Prediction of durg efficacy This section mainly describes the efficiency of protein expression, and tries to predict the scenario after a patient takes the drug.","breadcrumbs":"Awards » Model » Model","id":"132","title":"Model"},"133":{"body":"","breadcrumbs":"Awards » Model » Visualization","id":"133","title":"Visualization"},"134":{"body":"We used online softwares to help us visualize the 3D protein structures and modeled their docking scenarios, and then we evaluated their stability by using some common parameters. This section aims to visually display the protein structure synthesized in this project and provide ideas or directions for future experiments or experimental teams","breadcrumbs":"Awards » Model » Overview:","id":"134","title":"Overview:"},"135":{"body":"Our team designed DNA sequences for fusion protein-nanobody complex ourselves and these newly designed protein's 3D structures are unknown. A protein's 3D structure determines its functionality, which, in our case, would be the nanobody's docking on the membrane and its binding to the antigen. Protein structure prediction Based on the amino acid sequence of the protein, various algorithms can predict the protein's 3D structure. These algorithms use machine learning to learn from databases of known amino acid sequences and structures. It would intuitively indicate whether the designs are feasible by checking their structures. Prediction service We use Robetta and AlphaFold to predict the structure of the proteins we designed. Robetta [1] is an online public service to predict protein structure. It is based on the algorithms of Rosetta from the Rosetta Commons. Robetta is a protein structure prediction server developed by the Baker lab at the University of Washington. At it's core is the Rosetta macromolecular modeling suite developed by the Rosetta Commons, a multi-institutional collaborative research and software development group. Robetta's primary service is to predict the 3-dimensional structure of a protein given the amino acid sequence. AlphaFold [2] is a prediction software that can structure the 3D model of a protein based on its amino acid sequence, using a combination of bioinformatics and physical approaches. We run models on AlphaFold (Phenix version) [3] Colab notebook and it will automatically give the highest-scoring model. This Colab notebook is derived from ColabFold [4] and the DeepMind AlphaFold2 Colab [5] Robetta [1] and AlphaFold Colab notebook [3] both accept single-letter code amino acid sequences and generate Protein Database (PDB) files, which contains information about the protein's structure. Robetta produces 5 models of different configuration with same score for each sequence. Alphafold automatically produces the model with highest score. We view these pdb files in PyMOL [6] , a powerful tool for 3D structure visualization. Protein structure evaluation Assessment of these resultant structures from Robetta and Alphafold2 is needed for deciding which structure is more credible and can be used in future anlysis. There are several parameters to consider: ramachandran plot, overall G-factors, atomic Z-score RMS, percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, overall quality factor, and Z-score. We use online server SAVES v6.0 [7] and ProSA [8] for the validation. Parameters Ramachandran plot: Ramachandran plot shows the theoretical conformation of amino acid residues and is mainly used to evaluate the model quality after homologous modeling. It considers whether the conformation of amino acids is reasonable. Based on an analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions. [7] Atomic Z-score RMS: Z-score root mean square deviation (Z-score RMS) measures the \"average magnitude of the volume irregularities in the structure.\" [9] Z-score RMS for a good model should be around 1.0. Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile: Indicate whether the atomic model is compatible with its amino acid sequence. It should be higher than 80% for a good model. [7] Overall quality factor: An overall score for the model provided by SAVES server [7] , ranging from 0 to 100. It should be higher than 80 for a good model. Z-score: Indicate whether the z-score of the input structure is within the range of scores typically found for native proteins of similar size [8] . All the structures shown later are the highest scoring structures. Protein structure alignment After the evaluation of models we got from Robetta [1] and AlphaFold Colab notebook [3] , we can compare the antibody structure in the model with its original structure by using PyMOL [6] alignment. If RMSD (root mean square deviation) value is very low, we regard two structures similar, which means the nanobody in our fusion-nanobody complex will theoretically function well.","breadcrumbs":"Awards » Model » Part 1: General pattern","id":"135","title":"Part 1: General pattern"},"136":{"body":"We have successfully expressed the fusion protein-nanobody complex, which is Yeast-20ipaD. Here is the highest-scoring structure of Yeast-20ipaD ( Figure 1 ). Figure 1 | 3D structure of Yeast-20ipaD complex Ramachandran plot of the above structure showed that 85.1% of residues are in the most favorite regions, and 11.9% are in the allowed regions; 1.9% of the residues are in the generously allowed regions and 1.1% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.536, which is a little bit out of range. A very good model would have a value close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 92.39%. The overall quality factor is 82.89, which is acceptable. ProSA calculated Z-score is -8.7, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure can be regarded as a good model of Yeast-20ipaD. Figure 2 | Alignment of 20ipaD between itself in complex and it's original structure. The alignment between 20ipaD in the complex and 20ipaD's original structure shows that our complex can have good effect theoretically ( Figure 2 ). The RMSD value is tested to be 0.807, which means the complex have little influence on the structure of 20ipaD.","breadcrumbs":"Awards » Model » Part 2: Yeast-20ipaD visualization","id":"136","title":"Part 2: Yeast-20ipaD visualization"},"137":{"body":"Interaction imformation (binding sites) of 20ipaD and ipaD is found in the paper: Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion [10] . Since the alignment shows that the 20ipaD in complex is almost the same with it's original structure, we can default the binding sites unchanged. Below is the binding sites between 20ipaD and ipaD ( Figure 3 ). Figure 3 | Binding sites between 20ipaD and Ipad We provided the interaction information for online server HADDOCK [11] to simulate the docking between the complex and ipaD. Below is the docking structure ( Figure 4 ). Figure 4 | Docking between 20ipaD (in complex) and IpaD Ramachandran plot of the above structure showed that 85.0% of residues are in the most favorite regions, and 12.7% are in the allowed regions; 1.2% of the residues are in the generously allowed regions and 1.0% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.441, which is relatively close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 87.61%. The overall quality factor is 85.53, which is acceptable. ProSA calculated Z-score is -7.16, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure indicates that 20ipaD can bind with IpaD well theoretically. Below is the alignment between our docking result and the original docking between 20ipaD and IpaD. RMSD is 0.36, which is very small and acceptable. Figure 5 | Alignment between Yeast-20ipaD-IpaD and 20ipaD-IpaD. All the above shows that our Yeast-20ipaD complex could theoretically work well when binding with IpaD.","breadcrumbs":"Awards » Model » Part 3: Docking modeling","id":"137","title":"Part 3: Docking modeling"},"138":{"body":"In this section, we would like to show other possible combinations of fusion protein-nanobody complex that might theoretically function well. To do this, we modeled their 3D structures and their docking scenarios, and analyzed them. This could be helpful for future experiment and future teams. Robetta https://robetta.bakerlab.org AlphaFold https://www.nature.com/articles/s41586-021-03819-2 AlphaFold(Phenix Version) <https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf old2/AlphaFold2.ipynb> ColabFold <https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol d2.ipynb> AlphaFold2 <https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks /AlphaFold.ipynb> PyMOL https://pymol.org/2/ SAVES https://saves.mbi.ucla.edu/ Prosa https://prosa.services.came.sbg.ac.at/prosa.php Deviations from standard atomic volumes as a quality measure for protein crystal structures <https://pubmed.ncbi.nlm.nih.gov/8950272/#:~:text=Deviations%20of%20the%20atomic %20volumes%20from%20the%20standard,magnitude%20of%20the%20volume%20irregularitie s%20in%20the%20structure.> HADDOCK online server https://wenmr.science.uu.nl/haddock2.4/ Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion. DOI: 10.1074/jbc.M117.802231 https://pubmed.ncbi.nlm.nih.gov/28842484/","breadcrumbs":"Awards » Model » Part 4: Other combinations of probiotic-nanobody complex","id":"138","title":"Part 4: Other combinations of probiotic-nanobody complex"},"139":{"body":"","breadcrumbs":"Awards » Model » Description and Prediction of drug efficacy","id":"139","title":"Description and Prediction of drug efficacy"},"14":{"body":"","breadcrumbs":"Team » Attributions » Biology team","id":"14","title":"Biology team"},"140":{"body":"Wet lab results showed that we have successfully expressed 20ipaD on the surface of Yeast. Our goal is to describe efficiency of expression and predict the scenario after the drug is released in the patient's jejunal.","breadcrumbs":"Awards » Model » Overview:","id":"140","title":"Overview:"},"141":{"body":"To describe how efficient is Yeast concerning the expression of 20ipaD, we manually calculated the efficiency by counting the number of Yeast cells that expressed 20ipaD and the total number of Yeast cells ( Figure 1 ). Figure 1 | Fluorescent cells for Yeast cells that obviously expressed 20ipaD. Dark cells for no or very little expression","breadcrumbs":"Awards » Model » Part 1: Protein expression efficiency","id":"141","title":"Part 1: Protein expression efficiency"},"142":{"body":"","breadcrumbs":"Awards » Model » Part 2: Prediction of post-medication scenario","id":"142","title":"Part 2: Prediction of post-medication scenario"},"143":{"body":"","breadcrumbs":"Awards » Plant","id":"143","title":"Awards"},"144":{"body":"","breadcrumbs":"Awards » Software","id":"144","title":"Awards"},"145":{"body":"","breadcrumbs":"Awards » Sustainable » Sustainable Development Goals (SDGs)","id":"145","title":"Sustainable Development Goals (SDGs)"},"146":{"body":"Scientific research has always had far-reaching significance in our study and daily routine, and even in the development of the whole society. Scientific research can comprehend us a better understanding of the nature and properties of matter. Analyzing the research objects elaboratively can accelerate the development of human knowledge accumulation. Our project follows a shared blueprint for peace and prosperity for people and the planet whose heart is the 17 sustainable development goals (UN, 2022). We respond to the urgent call for action by all countries that end poverty and other deprivations, improve health and education, reduce inequality, and spur economic growth (UN, 2022). This year, our team aims to provide a biological method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . Our method can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity while having stronger pathogen inhibition compared to traditional probiotic treatment (Langdon et al., 2016). Project “GutGuard†is mainly based on Goals 3, 9, 17","breadcrumbs":"Awards » Sustainable » Introduction","id":"146","title":"Introduction"},"147":{"body":"Ensure healthy lives and promoting well-being for all persons with disabilities We prospect our team’s project can make our local community and even the world conscious of the prominence of life and health, especially the gut problem. The gut problem may cause a person to struggle to absorb nutrients and regulate blood sugar. Additionally, weight loss or gain may be caused by bacteria overgrowth or lack of nutrients. The current therapeutics is antibiotics and the potential problem with the usage of antibiotics is that taking antibiotics too often or for the wrong reasons can change bacteria so much that antibiotics do not work against them (Cronan, 2019). Moreover, long-term use of antibiotics in late adulthood may be a risk factor for all-cause and cardiovascular mortality (Heianza, 2020). As the current therapies of antibiotics promote Shigella to develop antibiotic resistance, we are inspired by this problem and focus on shigella’s drug. Reducing antibiotic resistance and minimizing the side effects including the degradation of GI tract microbiome diversity can be achieved compared to the traditional probiotic treatment (Langdon et al., 2016). We mainly worked toward contributing to target 3.5 (Strength the prevention and treatment of substance abuse, including narcotic drug abuse and harmful use of alcohol) (UN, 2022).","breadcrumbs":"Awards » Sustainable » Goal 3| Good health and well-being","id":"147","title":"Goal 3| Good health and well-being"},"148":{"body":"Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation We are capable to lead a new approach and ideologically telling certain product developers to dare to innovate and not to stick to antibiotics to create drugs. To contribute to the goal, we aimed at target 9.5 (Enhance scientific research, upgrade the technological capabilities of industrial sectors in all countries, in particular developing countries, including, by 2030, encouraging innovation and substantially increasing the number of research and development workers per 1 million people and public and private research and development spending) (UN, 2022). We proposed a novel scientific solution to an existing global problem. We mainly focused on a novel method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . While meeting the goal, our laboratory team did various ways (using three different cells for trial: E. coli, Yeast and Lactococcus lactis) to achieve and increase the possibility of success. Additionally, our team collaborates with other iGEM teams from developing countries to contribute to scientific advancement there.","breadcrumbs":"Awards » Sustainable » Goal 9| Industry, Innovation and Infrastructure","id":"148","title":"Goal 9| Industry, Innovation and Infrastructure"},"149":{"body":"Strengthen the means of implementation and revitalize the global partnership for sustainable development We, as a team, share and hold the view of win-win cooperation. We know that iGEM is not just a competition, but a platform for mutual communication and cooperation. We welcome various teams coming from different backgrounds and help to create solutions to the question. Our team strictly followed target 17.16 (Enhance the global partnership for sustainable development, complemented by multi-stakeholder partnerships that mobilize and share knowledge, expertise, technology, and financial resources, to support the achievement of the sustainable development goals in all countries, in particular developing countries.) (UN, 2022). Our team played an active part in collaborating with other iGEM teams (LZU and XJLTU) to gain insights into local society and comprehend more knowledge. This kind of collaboration enriched us and ensured the sharing of knowledge and raising of awareness on both sides.","breadcrumbs":"Awards » Sustainable » Goal 17| Partnerships for the goals","id":"149","title":"Goal 17| Partnerships for the goals"},"15":{"body":"Biology Team leader. In charge of wet lab organization and human practice organizations. Designed the overall topic and approach of the problem to tackle with synthetic biology design. Designer of E.coli csgA surface display and lab experiments of the E. coli group.","breadcrumbs":"Team » Attributions » Yixuan Wu (Lisa)","id":"15","title":"Yixuan Wu (Lisa)"},"150":{"body":"To sum up, we address and fulfill sustainable development goals 3, 9, and 17 . While meeting the goal of displaying nanobodies on the surface of the probiotics to battle antibiotic-resistant pathogens, we can also contribute to improved healthcare globally in the sustainable development aspect. It can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity. The inhibition of the pathogen will be stronger compared to traditional probiotic treatment. Our methods are easy to use and can be improved for further applications.","breadcrumbs":"Awards » Sustainable » Conclusion","id":"150","title":"Conclusion"},"151":{"body":"United Nations. (2022). The 17 goals | sustainable development. United Nations. https://sdgs.un.org/goals United Nations. (2022). #ENVISION2030: 17 goals to transform the world for persons with disabilities enable. United Nations. https://www.un.org/development/desa/disabilities/envision2030.html Langdon, A., Crook, N., & Dantas, G. (2016, April 13). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome medicine. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831151/ Cronan, K. M. (Ed.). (2019, July). The danger of antibiotic overuse (for parents) - nemours kidshealth. KidsHealth. Retrieved September 28, 2022, from https://kidshealth.org/en/parents/antibiotic-overuse.html Heianza, Y., Ma, W., Li, X., Cao, Y., Chan, A. T., Rimm, E. B., Hu, F. B., Rexrode, K. M., Manson, J. A. E., & Qi, L. (2020). Duration and life-stage of antibiotic use and risks of all-cause and cause-specific mortality. Circulation Research, 126(3), 364–373. https://doi.org/10.1161/circresaha.119.315279","breadcrumbs":"Awards » Sustainable » References","id":"151","title":"References"},"152":{"body":"Attribution 4.0 International (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/ ======================================================================= Creative Commons Corporation (\"Creative Commons\") is not a law firm and does not provide legal services or legal advice. Distribution of Creative Commons public licenses does not create a lawyer-client or other relationship. Creative Commons makes its licenses and related information available on an \"as-is\" basis. Creative Commons gives no warranties regarding its licenses, any material licensed under their terms and conditions, or any related information. Creative Commons disclaims all liability for damages resulting from their use to the fullest extent possible. 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Except for the limited purpose of indicating that material is shared under a Creative Commons public license or as otherwise permitted by the Creative Commons policies published at creativecommons.org/policies, Creative Commons does not authorize the use of the trademark \"Creative Commons\" or any other trademark or logo of Creative Commons without its prior written consent including, without limitation, in connection with any unauthorized modifications to any of its public licenses or any other arrangements, understandings, or agreements concerning use of licensed material. For the avoidance of doubt, this paragraph does not form part of the public licenses. Creative Commons may be contacted at creativecommons.org.","breadcrumbs":"LICENSE","id":"152","title":"LICENSE"},"16":{"body":"Co-established the project topic. In charge of lab design and wet lab for the yeast group. Also assisted in Wiki writing and expert interview.","breadcrumbs":"Team » Attributions » Yuxin Wang","id":"16","title":"Yuxin Wang"},"17":{"body":"In charge of background research, E. coli group lab design, wet labs & wiki writing. Hosted journal clubs and science lectures for human practice.","breadcrumbs":"Team » Attributions » Yunyi Ru","id":"17","title":"Yunyi Ru"},"18":{"body":"Designed lactococcus lab procedures and in charge of lactococcus and yeast lab experiments. Conducted expert interviews for human practice.","breadcrumbs":"Team » Attributions » Zhujun Yao","id":"18","title":"Zhujun Yao"},"19":{"body":"Proposed the project topic, participated in plasmid design and workflow design of E.coli group, participated in wet labs and background research. Helped conduct collaboration with XJLTU as a part of human practice.","breadcrumbs":"Team » Attributions » Chang Shen","id":"19","title":"Chang Shen"},"2":{"body":"Yixuan Wu (Lisa) Yixuan Liu Sihan Wang Zhujun Yao Lingrui Lai Yuxin Wang Jingyun Jin Chang Shen Yunyi Ru Renwei Gao Qizhou Jiang","breadcrumbs":"Team » Biology","id":"2","title":"Biology"},"20":{"body":"Responsible for wet lab design and experiment for yeast group. Contribute to Human Practice with Conference of China iGEMer Community.","breadcrumbs":"Team » Attributions » Lingrui Lai","id":"20","title":"Lingrui Lai"},"21":{"body":"Helped conduct human practices and wetlabs for the yeast group. Designed the safety and education wiki and organized local high school activities education.","breadcrumbs":"Team » Attributions » Qizhou Jiang","id":"21","title":"Qizhou Jiang"},"22":{"body":"Helped with background research, designed lab detection protocols for the lactococcus group, conducted wetlab experiments, helped with human practice organization including journal club organization and wiki writing.","breadcrumbs":"Team » Attributions » Sihan Wang","id":"22","title":"Sihan Wang"},"23":{"body":"Organized and chaired the iGEM2022 Journal Club Seminar ever since 2021. Actively participate in human practice part including designing and popularizing events in local collegiate school. Help conduct wet labs.","breadcrumbs":"Team » Attributions » Yixuan Liu","id":"23","title":"Yixuan Liu"},"24":{"body":"Fund manager of the team, in charge of labware purchasing, helped with background research and survey distribution as a part of human practice.","breadcrumbs":"Team » Attributions » Renwei Gao","id":"24","title":"Renwei Gao"},"25":{"body":"Helped design survey as a part of human practice, helped with E. coli wet lab experiments.","breadcrumbs":"Team » Attributions » Jingyun Jin","id":"25","title":"Jingyun Jin"},"26":{"body":"","breadcrumbs":"Team » Attributions » Modeling team","id":"26","title":"Modeling team"},"27":{"body":"Organized protein structure and docking modeling. Helped conduct human practice. Shot and edited the promotion video. Wiki writing.","breadcrumbs":"Team » Attributions » Zhenyu Xu","id":"27","title":"Zhenyu Xu"},"28":{"body":"Main Wiki developer and technical support. Built the Wiki infrastructure. Set up and maintains the GitLab repository for team communication and Wiki editing. Introduced Git and GitLab to the team and helped the team adopt to the workflow on GitLab. Helped with protein modeling using RoseTTAFold, Robetta, and PyMOL.","breadcrumbs":"Team » Attributions » Sichang He (Steven)","id":"28","title":"Sichang He (Steven)"},"29":{"body":"Conceptualized cell surface display technology project during preliminary brainstorming and provided proof of concept through review of related literature. Wrote the project abstract and refined general methodology framework. Built protein models for candidate microbes via Alphafold and Haddock and evaluated fidelity of each model via quantiative metrics. Modelled growth of chosen microbe model computationally.","breadcrumbs":"Team » Attributions » Jasmine Santos","id":"29","title":"Jasmine Santos"},"3":{"body":"Sichang He (Steven) Jasmine Santos Yuxiang He Zhenyu Xu","breadcrumbs":"Team » Modeling","id":"3","title":"Modeling"},"30":{"body":"Built a 3D model for the drug delivery system.","breadcrumbs":"Team » Attributions » Yuxiang He","id":"30","title":"Yuxiang He"},"31":{"body":"","breadcrumbs":"Team » Attributions » Advising support","id":"31","title":"Advising support"},"32":{"body":"Overall project advising, principal investigator.","breadcrumbs":"Team » Attributions » Linfeng Huang","id":"32","title":"Linfeng Huang"},"33":{"body":"Oversee wet lab experiments and overall project advising.","breadcrumbs":"Team » Attributions » Jiani Chen","id":"33","title":"Jiani Chen"},"34":{"body":"Oversee wet lab experiments, helped optimize lab protocols and troubleshooting.","breadcrumbs":"Team » Attributions » Yang Yu","id":"34","title":"Yang Yu"},"35":{"body":"Thanks to the generous funding support of Duke Kunshan University Natural Science Divisions, Wang-Cai Biochemistry Lab, Synear Food Molecular Biology Lab, DKU Innovation and Entrepreneurship Initiative, and Marcia B. France, DKU Dean of Undergraduate Studies. Thanks to free licenses provided by SnapGene.","breadcrumbs":"Team » Attributions » Funding support","id":"35","title":"Funding support"},"36":{"body":"Thanks to Dr. Floyd Beckford and Dr. Huansheng Cao at Duke Kunshan University, Dr. Neel Joshi from Northwestern University, and Dr. Jisheng Lin at Sinovac Biotech CO.,LTD. for providing effective advice on our project design and development.","breadcrumbs":"Team » Attributions » Communications support","id":"36","title":"Communications support"},"37":{"body":"We collaborated with LZU, another iGEM team focusing on probiotics, on education. We found that there are many misleading claims about probiotics and their effects in the market, so we planned to conduct science promotion in local areas to improve people's understanding of probiotics. We chose a local international university to give a lecture on science popularization, and more than 300 middle and high school students and teachers attended.","breadcrumbs":"Team » Collaborations » Collaborations","id":"37","title":"Collaborations"},"38":{"body":"","breadcrumbs":"Project » Communication","id":"38","title":"Communication"},"39":{"body":"We had science communications during different stages of our project. We designed these communications to have different manner, audience and scope, aiming at informing, educating, raising awareness of the topic of Gastrointestinal health, and increasing the sense of wonder about fighting against antibiotic resistance.","breadcrumbs":"Project » Overview","id":"39","title":"Overview"},"4":{"body":"Jiani Chen Yang Yu","breadcrumbs":"Team » Advisor","id":"4","title":"Advisor"},"40":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Socially-Oriented Questionnaire","id":"40","title":"Socially-Oriented Questionnaire"},"41":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus. In addition, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating.","breadcrumbs":"Project » On-Campus Communication","id":"41","title":"On-Campus Communication"},"42":{"body":"In order to carry out science communications on a larger scale, we participated the 9th CCiC Conference (Conference of China iGEMer Community), which is a national summit independently initiated by Chinese iGEM teams, aiming to provide a platform for iGEM teams to share resources and promote mutual learning and communication. We made poster and presented at the conference, answering questions from the audience and judges. After the conference, we collaborated with team LZU on science popularization about probiotics.","breadcrumbs":"Project » CCiC: iGEM community in China","id":"42","title":"CCiC: iGEM community in China"},"43":{"body":"In the later stage of the experiment, in order to better promote the knowledge of synthetic biology and gastrointestinal health in the local area, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers.We distributed science manuals to everyone in the audience and introduced the GI tract, dysentery, probiotic therapy, and antibiotic resistance.","breadcrumbs":"Project » Local School Education","id":"43","title":"Local School Education"},"44":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the communication and cooperation with other Chinese IGEM teams enabled us to learn more knowledge, and also to understand the current issues of synthetic biology in China that deserve attention. The science popularization and education in local schools also gave us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Project » Summary","id":"44","title":"Summary"},"45":{"body":"","breadcrumbs":"Project » Communication » Communication","id":"45","title":"Communication"},"46":{"body":"We had science communications during different stages of our project. We designed these communications to have different manner, audience and scope, aiming at informing, educating, raising awareness of the topic of Gastrointestinal health, and increasing the sense of wonder about fighting against antibiotic resistance.","breadcrumbs":"Project » Communication » Overview","id":"46","title":"Overview"},"47":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Communication » Socially-Oriented Questionnaire","id":"47","title":"Socially-Oriented Questionnaire"},"48":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus. In addition, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating.","breadcrumbs":"Project » Communication » On-Campus Communication","id":"48","title":"On-Campus Communication"},"49":{"body":"In order to carry out science communications on a larger scale, we participated the 9th CCiC Conference (Conference of China iGEMer Community), which is a national summit independently initiated by Chinese iGEM teams, aiming to provide a platform for iGEM teams to share resources and promote mutual learning and communication. We made poster and presented at the conference, answering questions from the audience and judges. After the conference, we collaborated with team LZU on science popularization about probiotics.","breadcrumbs":"Project » Communication » CCiC: iGEM community in China","id":"49","title":"CCiC: iGEM community in China"},"5":{"body":"Lingfeng Huang","breadcrumbs":"Team » Principal Investigator","id":"5","title":"Principal Investigator"},"50":{"body":"In the later stage of the experiment, in order to better promote the knowledge of synthetic biology and gastrointestinal health in the local area, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers.We distributed science manuals to everyone in the audience and introduced the GI tract, dysentery, probiotic therapy, and antibiotic resistance.","breadcrumbs":"Project » Communication » Local School Education","id":"50","title":"Local School Education"},"51":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the communication and cooperation with other Chinese IGEM teams enabled us to learn more knowledge, and also to understand the current issues of synthetic biology in China that deserve attention. The science popularization and education in local schools also gave us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Project » Communication » Summary","id":"51","title":"Summary"},"52":{"body":"We designed cell surface display platforms for probiotics including yeast, E. coli Nissle 1917, and L. lactis . To be specific, the yeast Aga2 surface display platform for nanobodies were developed, We also designed a novel way to detect protein surface expression by using flow cytometry. Another contribution is protein modeling protocol. We designed an integrated protocol involving the usage of PyMol, RobeTTA, and Alphafold2. Through literature review, we were able to determine multiple parameters that measure the accuracy of the protein model, and conducted evaluation on our protein design.","breadcrumbs":"Project » Contribution » Contribution","id":"52","title":"Contribution"},"53":{"body":"Cell surface display platforms can be utilized to cater to many protein engineering and therapeutic drug design purposes. In our case, the therapeutic effect and the nanobody localization on the cellular membrane of yeast yields future possibilities for iGEM teams to utilize this surface display platform based on the yeast Aga2 protein, specifically for therapeutic designs, but possible to be utilized to express other proteins as well.","breadcrumbs":"Project » Contribution » Cell surface display platforms","id":"53","title":"Cell surface display platforms"},"54":{"body":"Online programs are helpful for visualizing and analyzing the structure of different proteins and their docking scenarios. We use Robetta and Alphafold2 to model the structures of our protein, and used HADDOCK to visualize the docking structure. Evaluation focuses on different parameters: Ramachandran plot, Overall G-factors, Atomic Z-score RMS, Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, Overall quality factor, and Z-score. These parameters determine whether a certain structure is stable.","breadcrumbs":"Project » Contribution » Integrated protein modeling protocol","id":"54","title":"Integrated protein modeling protocol"},"55":{"body":"The Shigella species is listed as one of the eight dangerous drug resistant bacteria [1] , with associated mortalities projected to rise to 10 million globally by 2050. The use of conventional antibiotics aggravates the multidrug resistance of most Shigella strains. Besides aiding in the selection of resistant pathogens, antibiotics reduce intestinal species diversity and population, and disrupt the defensive, metabolic, and trophic functions of interdependent microbes [2] . Engineered probiotics with cell surface display systems are promising in tackling this problem due to a weaker selective pressure and specific binding proteins that are less likely to disrupt the host gut microbiome. Through literature review, E. coli Nissle 1917, yeast and L. lactis are chosen for expression because their probiotic nature present no known harm to the GI tract and the convenience in lab culturing. Centers for Disease Control and Prevention. (2019). 2019 AR Threats Report. https://www.cdc.gov/drugresistance/biggest-threats.html Francino, M. P. (2016, January 1). Antibiotics and the human gut microbiome: Dysbioses and accumulation of resistances. Frontiers. Retrieved March 28, 2022, from https://www.frontiersin.org/articles/10.3389/fmicb.2015.01543/full","breadcrumbs":"Project » Description » Project Description","id":"55","title":"Project Description"},"56":{"body":"","breadcrumbs":"Project » Engineering » Engineering Cycle","id":"56","title":"Engineering Cycle"},"57":{"body":"This page will give a detailed explanation about the engineering cycle. To make yeast capable of displaying the target nanobody 20ipaD on the cell surface, 20ipaD gene was inserted behind the yeast membrane-sealed protein Aga 2; therefore, Aga 2 would bring the nanobody to the cell surface. The recombinant plasmid pYD1-20ipaD was successfully built, which was supported by PCR amplification data and sequencing data. Apart from yeast, Lactococcus lactis and Escherichia coli were also chosen as probiotics for surface displace of nanobodies at the beginning, where 20ipaD/JPS-G3 and control 3xFLAG tags were inserted into pNZ8148 (L. lactis) and pET30a (E. coli) for expression respectively. However, due to failure in transformation and plasmid construction, only yeast was selected as the final product.","breadcrumbs":"Project » Engineering » Introduction","id":"57","title":"Introduction"},"58":{"body":"","breadcrumbs":"Project » Engineering » Engineering Cycle","id":"58","title":"Engineering Cycle"},"59":{"body":"Cycle 1 Design We located a single-domain antibody (VHH) named 20ipaD from the database, whose binding ability with the needle tip protein ipaD of Shigella type III secretion system has be testified (Barta et al., 2017; Sierocki et al., 2021). Peptide sequences of 20ipaD from Barta et al (2017). Codon optimization was performed to get DNA sequences. Two flank sequences containing XhoI and ApaI cutting sites as well as C-terminal Flag-tag were added to the ipaD DNA sequence. Build Designed 20ipaD sequences were chemically de novo synthesized and sent in pUC19. XhoI and ApaI double-digestion enabled us to ligate the 20ipaD DNA sequence into pYD1, a plasmid allowing the surface display of the gene it carries in yeast. The ligation of 20ipaD into pYD1 generates a DNA sequencing coding a recombinant protein of 20ipaD and Aga2, a yeast extracellular membrane protein. pYD1 also contained a replication origin recognized by bacteria and an ampicillin resistance gene. After plasmid ligation, recombinant plasmids were transferred into E. coli to get a clone via ampicillin selection. Cloned plasmids were then transferred into yeast cells. Yeast cells containing the plasmid were selected by tryptophane-deficient medium. Expression of the recombinant protein was induced by add galactose. Test After transformation of recombinant plasmid into E. coli and single colony collection, we perform enzyme digestion and gel electrophoresis to check if the ligation and transformation is successful. For expression assay, we incubated induced yeast cells with anti-flag-tag primary antibody. After incubating with FITC conjugated secondary antibody, cells were examined under florescence microscopy and flow cytometry. Learn Recombinant proteins were observed to express on the cell surfaces on a portion of the cell population. We therefore planned to further testify the effectiveness of our recombinant protein. Though previous modeling through Rosetta suggested that the recombinant Aga2 region as well as the linkers sequences do not undermine the correct folding of the VHH part, we still sought for a experimental support as well as a way to quantify the binding affinity. Cycle 2 Design In this cycle, we aimed to test binding affinity between the recombinant nanobody and the ipaD epitopes. ipaD were retrieved from NCBI database. Codon optimization was also performed to collect the DNA sequence. Similar to 20ipaD, flank regions were inserted into ipaD except the substitution of Flag-tag to HA-tag. Build Synthesized ipaD sequences were got from the same company. Using the same method, we expressed ipaD recombinant protein of the yeast surface. Test Learn Cycle 3 Design In this cycle, we aims to improve the expression level of the recombinant protein. Energy flows within the yeast cells would be controlled to concentrate more on protein production rather than other metabolic activities. We started by looking for a strong and continuously expressed promoter to drive the expression of 20ipaD recombinant protein. At the same time, we also tried to reduce other cellular activities. Cycle 4 Design In this cycle, we aims to improve the binding affinity of the recombinant protein with the antigen epitope. We would perform error prone PCRs to introduce mutations into 20ipaD sequences. Concentrations of the nucleotide analogs would be controlled so that only point mutants would be produced. All mutants would be screened to identify binding affinity improvements. To reduce the workload of screening, we would perform a modeling prescreen. In the prescreen, we would predict how single amino acid change influence the binding affinity between 20ipaD and ipaD.","breadcrumbs":"Project » Engineering » Yeast","id":"59","title":"Yeast"},"6":{"body":"","breadcrumbs":"Team » The whole team","id":"6","title":"The whole team"},"60":{"body":"Cycle 1 Design At first, we wanted to obtain the sequence of both 20ipaD and control flag-tag so that we could amplify them via PCR reaction. The 20ipaD is one of the single-VH domain antibodies (VHHs) capable of recognizing distinct epitopes within the antigen IpaD of pathogen Shigella. In this way, we hoped that by fusing 20ipaD and control flag-tag into the Lactococcus lactis expression vector pNZ8148, we would achieve the surface display and expression of 20ipaD on Lactococcus lactis . Build To obtain the sequence of 20ipaD, we constructed the plasmid with the 20ipaD sequence surrounded by two different restriction sites of enzymes BamHI and SacI. In this way, through the restrictive digestion of Bam HI and Sac I, ideally the sequence of 20ipaD would be obtained. The similar construction was also applied with the sequence of control flag-tag, where the enzymes used for restrictive digestion were changed to be NcoI and HindIII. Test After successfully received the synthesized plasmid sequence for 20ipaD and control flag-tag, we conducted the digestion of BamHI and SacI for the obtain of 20ipaD sequence, and the digestion of Nco I and Hind III for the obtain of control flag-tag sequence. Gel electrophorese was applied to confirm the size of the sequence. Control flag-tag sequence was successfully obtained. However, according to the gel picture, the band of 20ipaD showed a very different size from that in theory. Learn We checked the source of error and found that the designed sequence of 20ipaD has been inserted into the pUC19 vector when being synthesized by the company. Unfortunately, pUC19 vector also contained a restriction site for BamHI itself, thus leading to a different enzymatic digestion than what we have expected before. Cycle 2 Design Since pUC19 vector also contained a restriction site for BamHI itself, which would lead to unspecific enzymatic digestion and the failure of getting 20ipaD sequence, we redesigned the experimental steps in order to overcome such a problem. Build In this try, we would do the PCR amplification of 20ipaD sequence to insert it directly into the pNZ8148 vector first. This would circumvent the enzymatic digestion of pUC19 vector by BamHI that had the insertion of 20ipaD. Learn From this process we learnt that when the synthesized plasmid went wrong from our expectations, apart from directly asking the company to redo the synthesis, we could also alter the steps of ligation via PCR reaction to solve the problem. Cycle 3 Design We wanted to insert the engineered pNZ8148 vector with 20ipaD into the strain Lactococcus lactis NZ9000. According to literature review, electroporation is the commonly used technique to insert vectors into Lactococcus lactis . Build When the OD600 of Lactococcus lactis reached 0.3, the bacteria would be subjected to electroporation. The bacteria would be washed with liquid detergent I containing 0.5mol∙L-1 sucrose and 10% glycerol for the insertion of 0.2 μg vector. The pulse of electroporation was delivered by a Gene-Pulser (Scientz) at 25μF and 2.5kV, while the electroporation cuvette (0.2cm in size) was connected in parallel to a 400-Ω resistor (the parameters were searched online and were consulted from technician at Scientz). According to multiple researches done previously, the transformation efficiency would be the highest is the recovery time is 1.5h after electroporation. Test The process of electroporation was not successful because we failed to insert the vector into Lactococcus lactis . Learn We suspect that the making of electrocompetent cells might be the source of failure. After checking with the team advisor, we found that the type of glycerol used was intended for protein purification, which could cause problems for the electrocompetent cell. Cycle 4 Design To further increase efficiency, after doing more literature reviews we added the pretreatment of Lactococcus lactis with lithium acetate (LiAc) and/or dithiothreitol (DTT). We also substituted the type of glycerol used based on the previous error analysis. Build According to the newly found protocol, the Lactococcus lactis was firstly suspended at room temperature for 30 min in 8ml of 100mM LiAc, 10mM DTT, 0.6M sucrose, and 10mM Tris-HCl (pH=7.5). Following the treatment, Lactococcus lactis was pelleted and was resuspended in 1.5ml microcentrifuge tube, and was then washed as previously described. Afterwards, electroporation was conducted as previously described.","breadcrumbs":"Project » Engineering » Lactococcus lactis","id":"60","title":"Lactococcus lactis"},"61":{"body":"E. coli Engineering Cycle Cycle 1 Design Initially, we planned to try three different nanobodies (20ipaD, JPS-G3, and JMK-H2) agianst the Shigella antigen ipaD from a research paper [1] . We also wanted to try two different surface display systems, beta domain of the E. coli outer membrane protein intimin [2] and the E. coli curli fiber protein, csg B [3] . Our target probiotic is E. coli Nissle 1917 [3] . By inserting the target nanobody sequence behind intimin or csg B, reconstructing the plasmid pET30a and transforming the plasmid into E. coli Nissle 1917, we expect the protein to be displayed on the surface of E. coli , so that it can capture the pathogen via antigen-antibody binding. Build & Test We designed the following sequences to make the recombinant protein. intimin-20ipaD-3xFLAG csgB-JMK-H2-3xFLAG JPS-G3-3xFLAG ipaD-3xHA However, due to limitations in budget & time for gene synthesis, we only have JPS-G3-3xFLAG and ipaD-3xHA (inserted into pUC19 plasmids). By plasmid extraction, double digestion ( Bam HI & Xho I) and PCR, we successfully obtained the sequences and verified the accuracy by Sanger sequencing, but we don't have csgB or intimin for surface display. Learn Complex sequences including potential harmful genes may impact synthesis efficiency. Cycle 2 Design Alternatively, we chose the curli fiber csg A [4] sequence for surface display. Build & Test We designed the following sequences: csgA-JPS-G3-3xFLAG csgA-ipaD-3xHA (displaying the antigen on the surface of E. coli BL21 to mimic Shigella flexneri , so that the effectiveness can be evaluated) csg A gene is obtained from the E. coli strains (pGEX-4T-1-csgA-shMT) provided by the XJLTU iGEM team via PCR. To connect different parts, we plan to use overlapping PCR.","breadcrumbs":"Project » Engineering » Escherichia coli","id":"61","title":"Escherichia coli"},"62":{"body":"Barta, M., Shearer, J., Arizmendi, O., Tremblay, J., Mehzabeen, N., Zheng, Q., . . . Picking, W. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. Journal of Biological Chemistry , 292, jbc.M117.802231. doi:10.1074/jbc.M117.802231 Salema, V., MarÃn, E., MartÃnez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., Teira, X., Gutierrez, C., Bodelón, G., & Fernández, L. Ã. (2013). Selection of Single Domain Antibodies from Immune Libraries Displayed on the Surface of E. coli Cells with Two β-Domains of Opposite Topologies. PLoS ONE , 8(9), e75126. https://doi.org/10.1371/journal.pone.0075126 Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998 Barta, M. L., Shearer, J. P., Arizmendi, O., Tremblay, J. M., Mehzabeen, N., Zheng, Q., Battaile, K. P., Lovell, S., Tzipori, S., Picking, W. D., Shoemaker, C. B., & Picking, W. L. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem, 292(40), 16677-16687. https://doi.org/10.1074/jbc.M117.802231 Sierocki, R., Jneid, B., Orsini Delgado, M. L., Plaisance, M., Maillere, B., Nozach, H., & Simon, S. (2021). An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLoS Negl Trop Dis, 15(3), e0009231. https://doi.org/10.1371/journal.pntd.0009231","breadcrumbs":"Project » Engineering » Reference","id":"62","title":"Reference"},"63":{"body":"","breadcrumbs":"Project » Experiments » Experiment","id":"63","title":"Experiment"},"64":{"body":"This page will give a detailed record about the experiment process, including the lab notes and protocols.","breadcrumbs":"Project » Experiments » Introduction","id":"64","title":"Introduction"},"65":{"body":"","breadcrumbs":"Project » Experiments » Experiment","id":"65","title":"Experiment"},"66":{"body":"Lab Notes Protocols","breadcrumbs":"Project » Experiments » Yeast","id":"66","title":"Yeast"},"67":{"body":"Lab Notes Protocols","breadcrumbs":"Project » Experiments » Lactococcus lactis","id":"67","title":"Lactococcus lactis"},"68":{"body":"Lab Notes Please see attached. E. coli Lab Notes Protocols Please see attached. E. coli Protocols","breadcrumbs":"Project » Experiments » Escherichia coli","id":"68","title":"Escherichia coli"},"69":{"body":"","breadcrumbs":"Project » Notebook","id":"69","title":"Project"},"7":{"body":"","breadcrumbs":"Team » Team » Team","id":"7","title":"Team"},"70":{"body":"","breadcrumbs":"Project » Implementation » Implementation","id":"70","title":"Implementation"},"71":{"body":"The end-products of our project are small tablets or capsules that contain dry powders of probiotics that express anti-Shigella antibodies on their surface. Our products serve the dual roles of Shigella infection precaution as well as disease therapy. The abilities of room temperature storage provide our tablets with cost reduction for storage and transportation. Tablets should be taken when facing potential exposure to Shigella infection sources, such as drinking unsanitary water in high diarrhea incidence areas. In consideration of the prevalent transmission pathways of Shigella, we also suggest people whose family members have developed Shigella infections and children in school with diarrhea cases take our tablets to prevent person-to-person transmission, which is the major form of Shigella spreading (Kotloff et al., 2018).","breadcrumbs":"Project » Implementation » Infection Precaution","id":"71","title":"Infection Precaution"},"72":{"body":"Due to intracellular pathogen nature of Shigella, the effect of antibodies reduces as pathogens evade into the cells. The ability of reprogramming the infected cells to form protrusion adjacent cells allows Shigella to spread within intestine epithelial cells, reducing the chance of exposing to body internal environment (Sansonetti et al., 1994). This special characteristic implies antibody may not be a one-size-fits-all solution for different stages of infection. We call for the combination of clinical phases of antibiotics treatment with our tablets together.","breadcrumbs":"Project » Implementation » Infection Therapy","id":"72","title":"Infection Therapy"},"73":{"body":"Along with the high household transmission rates, Shigella also display high secondary infection rates. Therefore, we suggest families with members developing Shigella to take our pills for a time period to provide continuously protection apart from keep good hygiene conditions. In the meanwhile, patients who have developed Shigella infection before should also take our tablets when facing a second exposure.","breadcrumbs":"Project » Implementation » Prognosis and Secondary infection","id":"73","title":"Prognosis and Secondary infection"},"74":{"body":"People who exposed to potential Shigella infection source, especially in a household environment. Children in school with Shigella cases reported. People with antibiotic allergy that cannot use clinical antibiotic treatment. Government that aims to provide low cost solution for Shigella incidence in low- and middle- income, less developed region.","breadcrumbs":"Project » Implementation » End Users","id":"74","title":"End Users"},"75":{"body":"Our product contains exogenous antibody proteins. Therefore, allergy test may need to be performed to prevent possible anaphylaxis. Besides, considering the pathogenesis and transmission pathway of Shigella, our products may not be a one-size-fits all solution for all infection stages but focuses more on the prevention of infection. Kotloff, K. L., Riddle, M. S., Platts-Mills, J. A., Pavlinac, P., & Zaidi, A. K. M. (2018). Shigellosis. The Lancet, 391(10122), 801-812. https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8 Sansonetti, P. J., Mounier, J., Prévost, M. C., & Mège, R.-M. (1994). Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell, 76(5), 829-839. https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1","breadcrumbs":"Project » Implementation » Caveats","id":"75","title":"Caveats"},"76":{"body":"","breadcrumbs":"Project » Partnership » Meeting with XJLTU","id":"76","title":"Meeting with XJLTU"},"77":{"body":"They plan to develop a biofilter core to replace current industry filter cores for heavy metal wastewater. Specifically, they plan to engineer E. coli to express csgA protein at high levels and immobilize the bacteria into a filter. In that way, the heavy metal ions in the wastewater can be captured by csgA protein that is expressed by E. coli located in the filter.","breadcrumbs":"Project » Partnership » XJLTU's Project","id":"77","title":"XJLTU's Project"},"78":{"body":"They would like to know how we will interact with and educate the public. A: We have made questionnaires to evaluate their knowledge related to antibiotics, probiotics, and microorganisms. We are also planning to make some handouts and deliver a lecture about it in a high school. They were interested in the specific design of our plasmids. Specifically, it's about how and why we choose each part of the plasmid for surface display. A: We applied three microorganisms and the whole team was divided into three groups, each responsible for E. coli, Yeast cell and Lactococcus lactis. All groups applied a strategy which conjugates the targeted nanobody with a surface protein that is to be expressed, transported and located to the extracellular space. The surface protein and the targeted nanobody were connected with a linker sequence, and each nanobody is marked with at least one protein tag for their identification. We also provided links to igem parts so they can check it directly.","breadcrumbs":"Project » Partnership » Questions & Advice From XJLTU:","id":"78","title":"Questions & Advice From XJLTU:"},"79":{"body":"Will the biofilter be blocked due to E. coli proliferation? A: The microorganisms are immobilized in filters, and the filtration condition may not allow E. coli to grow at such a speed. The csgA protein's ability to absorb heavy metal ions under different conditions (like pH) can be tested through experiments. For example, we can put csg protein into a certain amount of wastewater, then adjust the pH and check the remaining concentration of metal ions in time, so we can acquire a proper pH for the protein to capture heavy metal ions.","breadcrumbs":"Project » Partnership » Questions & Advice From DKU:","id":"79","title":"Questions & Advice From DKU:"},"8":{"body":"Yixuan Wu (Lisa) Yixuan Liu Sihan Wang Zhujun Yao Lingrui Lai Yuxin Wang Jingyun Jin Chang Shen Yunyi Ru Renwei Gao Qizhou Jiang","breadcrumbs":"Team » Team » Biology","id":"8","title":"Biology"},"80":{"body":"Model for bacteria growth The XJLTU team developed a model for predicting bacteria growth, and it may also be applied to our situation by adjusting some of the parameters. Quantified expression of csg through controlling IPTG concentration The XJLTU team intended to control the expression of csg protein by adjusting the amount of IPTG inducer, which can also be a helpful approach for our team to check the relationship between the cell-cell adhesion affinity and the number of expressed nanobodies. However, as we also applied the TlpA promotor, it may influence the actual expression to a great extent and cause a big difference from the theoretical calculation. As a result, this approach remains to be a concern. Detection and measurement of displayed csg protein. The XJLTU team controlled the expression level by adjusting inducer concentration and estimated the expression by calculating theoretically. The condition of csg and heavy metal ions after the death of E. coli cells We consider that the heavy metal ions will remain captured, as protein itself has a great affinity to the heavy metal ions. But, it remains to be seen whether the released protein will leak out from the filter.","breadcrumbs":"Project » Partnership » Discussion Topics:","id":"80","title":"Discussion Topics:"},"81":{"body":"","breadcrumbs":"Project » Proof of Concept","id":"81","title":"Project"},"82":{"body":"","breadcrumbs":"Project » Results » Results","id":"82","title":"Results"},"83":{"body":"This page will give a detailed record about the experiment results, future plans & project achievements.","breadcrumbs":"Project » Results » Introduction","id":"83","title":"Introduction"},"84":{"body":"","breadcrumbs":"Project » Results » Experiment Results","id":"84","title":"Experiment Results"},"85":{"body":"","breadcrumbs":"Project » Results » Yeast","id":"85","title":"Yeast"},"86":{"body":"","breadcrumbs":"Project » Results » Lactococcus lactis","id":"86","title":"Lactococcus lactis"},"87":{"body":"Summary of Experiment Design We plan to display the nanobody JPS-G3 agianst the Shigella antigen ipaD on the surface of E. coli Nissle 1917 via the curli fiber protein csg A [1] . We expect the engineered E. coli Nissle 1917 to be capable of capturing the pathogen Shigella flexneri via antigen-antibody specific binding. Please check the detailed experiment design at 'design' part. Plasmid Extraction pUC19-JPS-G3-3xHA and pUC19-ipaD-3xHA were extracted using the TIANGEN plasmid extraction kit. Target Sequence Amplification Using following primers ( Table 1 ), the JPS-G3-3xHA and ipaD-3xHA sequences were successfully amplified, and the results were verified by gel electrophoresis ( Figure 1 ). PCR products were purified for further manipulation. Table 1 | PCR Primers Used Name Sequence (5' -> 3') Endonuclease Site ipaD_FW CGCGGATCCATGAATATTACAACTC Bam HI ipaD_RV GGCCTCGAGTCAAGCGTAG Xho I JPS-G3_FW CGCGGATCCGGAAGTACACAAGTACAGCTAG Bam HI JPS-G3_RV CGCGGATCCGGAAGTACACAAGTACAGCTAG Xho I Figure 1 | Gel Electrophoresis Result for Target Sequence Amplification Molecular Cloning for Cytoplasmic Protein Expression In order to construct the recombinant plasmids pET30a-ipaD-3xHA and pET30a-JPS-G3-3xFLAG, the PCR products obtained from the last step were digested by endonucleases Bam HI and Xho I to create sticky ends. Meanwhile, the pET30a plasmids were transformed into E. coli DH5a competent cells for propagation. After transformation and overnight culture, the extracted plasmids were also digested with endonucleases Bam HI and Xho I to create sticky ends. Afterwards, the digested plasmids and target sequences were ligated and transformed into E. coli DH5a competent cells ( Figure 2 ). Figure 2 | Plates for pET30a-ipaD-3xHA (i-1 & i-2) and pET30a-JPS-G3-3xFLAG (J-1 & J-2). Single colonies were picked from the plates and the inserted sequence were verified by colony PCR ( Figure 3 ) and Sanger sequencing. Figure 3 | Gel Electrophoresis Result for Colony PCR Overlap Extension PCR In order to construct the recombinant DNA sequences csgA-JPS-G3-3xFLAG and csgA-ipaD-3xHA, the following overlap extension PCR primers are used ( Table 2 ). Table 2 | Overlap Extension PCR Primers Name Sequence (5' -> 3') Endonuclease Site OvF_csgA-shMT CCGCGTGGATCCATGAAACTTTTAAAAGTAG Bam HI OvR1_csgA-shMT TAGCTGTACTTGTGTACTTCCCCGCTGCCGCCGTACTGATGA / OvR2_csgA-shMT TAGTCAGAGTTGTAATATTCATCCGCTGCCGCCGTACTGATGA / OvF_JPS-G3 CATCAGTACGGCGGCAGCGGGGAAGTACACAAGTACAGCTAGC / OvR_JPS-G3 GAATCTCGAGTTATTTGTCGTCGTCATCC Xho I OvF_ipaD CATCAGTACGGCGGCAGCGGATGAATATTACAACTCTGACTAAT / OvR_ipaD GGCCTCGAGTCAAGCGTAGTCAGGTAC Xho I However, due to time limitation, this part has not been successfully implemented.","breadcrumbs":"Project » Results » Escherichia coli","id":"87","title":"Escherichia coli"},"88":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改)","breadcrumbs":"Project » Results » Project Achievements & Analysis Summary","id":"88","title":"Project Achievements & Analysis Summary"},"89":{"body":"Constructed the recombinant xxx plasmid, and transformed it into xxx strain. Expressed xxx protein. Effectiveness tested by xxx.","breadcrumbs":"Project » Results » Successes","id":"89","title":"Successes"},"9":{"body":"Sichang He (Steven) Jasmine Santos Yuxiang He Zhenyu Xu","breadcrumbs":"Team » Team » Modeling","id":"9","title":"Modeling"},"90":{"body":"Failed to construct and transform the recombinant plasmids in E. coli and L. lactis .","breadcrumbs":"Project » Results » Failures","id":"90","title":"Failures"},"91":{"body":"","breadcrumbs":"Project » Results » Inspirations","id":"91","title":"Inspirations"},"92":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改) Express proteins in well-studied probiotic strains. Insert nanobody sequences after other promoters that can ensure proper expression in vivo . Conduct hemolysis experiments to see the effectiveness of killing Shigella flexneri . Conduct in vivo experiments to test the therapeutic effects in rodent GI system.","breadcrumbs":"Project » Results » Future Plans","id":"92","title":"Future Plans"},"93":{"body":"Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998","breadcrumbs":"Project » Results » Reference","id":"93","title":"Reference"},"94":{"body":"All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Parts","id":"94","title":"Parts"},"95":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. Part Code Part name Website BBa_K4161501 T7 Promoter http://parts.igem.org/Part:BBa_K4161501 BBa_K4161502 GAL1 Promoter http://parts.igem.org/Part:BBa_K4161502 BBa_K4161503 Aga2 http://parts.igem.org/Part:BBa_K4161503 BBa_K4161504 G4S http://parts.igem.org/Part:BBa_K4161504 BBa_K4161505 T7, Xpress http://parts.igem.org/Part:BBa_K4161505 BBa_K4161506 ipaD http://parts.igem.org/Part:BBa_K4161506 BBa_K4161507 HA http://parts.igem.org/Part:BBa_K4161507","breadcrumbs":"Parts » Single element","id":"95","title":"Single element"},"96":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161301 | Single Domain Antibody 20ipaD Conjugated Aga2 Express Module | http://parts.igem.org/Part:BBa_K4161301 | | BBa_K4161508 | Composite part | http://parts.igem.org/Part:BBa_K4161508 |","breadcrumbs":"Parts » Key composite segment","id":"96","title":"Key composite segment"},"97":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161302 | pYD1 plasmid | http://parts.igem.org/Part:BBa_K4161302 |","breadcrumbs":"Parts » Vector","id":"97","title":"Vector"},"98":{"body":"All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Part Collection » Parts","id":"98","title":"Parts"},"99":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. 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Shigella, as one of the most antibiotic resistant pathogens, poses a great threat to food safety especially in developing areas. 10 million will be subject to mortalities caused by shigella infection by 2050. Distribution of antibiotics is the main treatment as of today. It is costly and time consuming. Side effects include degration of GI tract microbiome, and the emergence of more antibiotic resistant strains. We are in an endless race against pathogens. Antibiotics are our weapons. Mutations are their strategies to survival. Now, DKU iGEM team has proposed an alternative to jump out of this race and possibly, go far beyond. Antibody therapy is a popular topic in therapeutics. It is different from antibiotics and can be more effective when triggering the host immune system. However, conventional antibodies have a high cost because of the complicated synthesis procedure. It can also be vulnerable to proteosomes in the GI tract. Thus we propose a novel method to display nanobodies on the surface of probiotics. It exploits the natural pathogen inhibition effects of the probiotics. It also explores possibilities of antibody therapy mass production. Click on the left menu to learn more.","breadcrumbs":"Home","id":"0","title":"Home"},"1":{"body":"Team Yixuan Wu (Lisa) UG Class of 2024 Biology Yixuan Liu UG Class of 2024 Biology Sihan Wang UG Class of 2023 Biology Zhujun Yao UG Class of 2024 Biology Lingrui Lai UG Class of 2023 Biology Yuxin Wang UG Class of 2025 Jingyun Jin UG Class of 2024 Biology Chang Shen UG Class of 2025 Yunyi Ru UG Class of 2023 Biology Renwei Gao UG Class of 2023 Biology Qizhou Jiang UG Class of 2025","breadcrumbs":"Team » Biology","id":"1","title":"Biology"},"10":{"body":"","breadcrumbs":"Team » Team » The whole team","id":"10","title":"The whole team"},"100":{"body":"Failed to construct and transform the recombinant plasmids in E. coli and L. lactis .","breadcrumbs":"Project » Results » Failures","id":"100","title":"Failures"},"101":{"body":"","breadcrumbs":"Project » Results » Inspirations","id":"101","title":"Inspirations"},"102":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改) Express proteins in well-studied probiotic strains. Insert nanobody sequences after other promoters that can ensure proper expression in vivo . Conduct hemolysis experiments to see the effectiveness of killing Shigella flexneri . Conduct in vivo experiments to test the therapeutic effects in rodent GI system.","breadcrumbs":"Project » Results » Future Plans","id":"102","title":"Future Plans"},"103":{"body":"Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998","breadcrumbs":"Project » Results » Reference","id":"103","title":"Reference"},"104":{"body":"Model Models are powerful tools in terms of imagining reasonable future scenarios. Also, assumptions and results from the model push us to reflect on the present situation and make adjustments to our existing plans and experiments, which might also develop our final goal into a more realistic version. There are 3 modeling sections in our project: Visualization This section mainly shows the structure of proteins and their docking results, and also tries to provide guides for future experiment design. Description and Prediction of durg efficacy This section mainly describes the efficiency of protein expression, and tries to predict the scenario after a patient takes the drug. Hardware This section shows the 3D model of the micro-capsule where Yeast cells are sealed in. The micro-capsule is made of shellac, and the pH-dependent solubility that prefers a mild basic environment makes shellac perfect for releasing probiotics in intestines.","breadcrumbs":"Model » Visualization","id":"104","title":"Visualization"},"105":{"body":"We used online softwares to help us visualize the 3D protein structures and modeled their docking scenarios, and then we evaluated their stability by using some common parameters. This section aims to visually display the protein structure synthesized in this project and provide ideas or directions for future experiments or experimental teams Part 1: General pattern Our team designed DNA sequences for fusion protein-nanobody complex ourselves and these newly designed protein's 3D structures are unknown. A protein's 3D structure determines its functionality, which, in our case, would be the nanobody's docking on the membrane and its binding to the antigen. Protein structure prediction Based on the amino acid sequence of the protein, various algorithms can predict the protein's 3D structure. These algorithms use machine learning to learn from databases of known amino acid sequences and structures. It would intuitively indicate whether the designs are feasible by checking their structures. Prediction service We use Robetta and AlphaFold to predict the structure of the proteins we designed. Robetta [1] is an online public service to predict protein structure. It is based on the algorithms of Rosetta from the Rosetta Commons. Robetta is a protein structure prediction server developed by the Baker lab at the University of Washington. At it's core is the Rosetta macromolecular modeling suite developed by the Rosetta Commons, a multi-institutional collaborative research and software development group. Robetta's primary service is to predict the 3-dimensional structure of a protein given the amino acid sequence. AlphaFold [2] is a prediction software that can structure the 3D model of a protein based on its amino acid sequence, using a combination of bioinformatics and physical approaches. We run models on AlphaFold (Phenix version) [3] Colab notebook and it will automatically give the highest-scoring model. This Colab notebook is derived from ColabFold [4] and the DeepMind AlphaFold2 Colab [5] Robetta [1] and AlphaFold Colab notebook [3] both accept single-letter code amino acid sequences and generate Protein Database (PDB) files, which contains information about the protein's structure. Robetta produces 5 models of different configuration with same score for each sequence. Alphafold automatically produces the model with highest score. We view these pdb files in PyMOL [6] , a powerful tool for 3D structure visualization. Protein structure evaluation Assessment of these resultant structures from Robetta and Alphafold2 is needed for deciding which structure is more credible and can be used in future anlysis. There are several parameters to consider: ramachandran plot, overall G-factors, atomic Z-score RMS, percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, overall quality factor, and Z-score. We use online server SAVES v6.0 [7] and ProSA [8] for the validation. Parameters Ramachandran plot: Ramachandran plot shows the theoretical conformation of amino acid residues and is mainly used to evaluate the model quality after homologous modeling. It considers whether the conformation of amino acids is reasonable. Based on an analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions. [7] Atomic Z-score RMS: Z-score root mean square deviation (Z-score RMS) measures the \"average magnitude of the volume irregularities in the structure.\" [9] Z-score RMS for a good model should be around 1.0. Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile: Indicate whether the atomic model is compatible with its amino acid sequence. It should be higher than 80% for a good model. [7] Overall quality factor: An overall score for the model provided by SAVES server [7] , ranging from 0 to 100. It should be higher than 80 for a good model. [10] Z-score: Indicate whether the z-score of the input structure is within the range of scores typically found for native proteins of similar size [8] . All the structures shown later are the highest scoring structures. Protein structure alignment After the evaluation of models we got from Robetta [1] and AlphaFold Colab notebook [3] , we can compare the antibody structure in the model with its original structure by using PyMOL [6] alignment. If RMSD (root mean square deviation) value is very low, we regard two structures similar, which means the nanobody in our fusion-nanobody complex will theoretically function well. Part 2: Yeast-20ipaD visualization We have successfully expressed the fusion protein-nanobody complex, which is Yeast-20ipaD. Here is the highest-scoring structure of Yeast-20ipaD ( Figure 1 ). Figure 1 | 3D structure of Yeast-20ipaD complex Ramachandran plot of the above structure showed that 85.1% of residues are in the most favorite regions, and 11.9% are in the allowed regions; 1.9% of the residues are in the generously allowed regions and 1.1% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.536, which is a little bit out of range. A very good model would have a value close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 92.39%. The overall quality factor is 82.89, which is acceptable. ProSA calculated Z-score is -8.7, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure can be regarded as a good model of Yeast-20ipaD. Figure 2 | Alignment of 20ipaD between itself in complex and it's original structure. The alignment between 20ipaD in the complex and 20ipaD's original structure shows that our complex can have good effect theoretically ( Figure 2 ). The RMSD value is tested to be 0.807, which means the complex have little influence on the structure of 20ipaD. Part 3: Docking modeling Interaction imformation (binding sites) of 20ipaD and ipaD is found in the paper: Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion [11] . Since the alignment shows that the 20ipaD in complex is almost the same with it's original structure, we can default the binding sites unchanged. Below is the binding sites between 20ipaD and ipaD ( Figure 3 ). Figure 3 | Binding sites between 20ipaD and Ipad We provided the interaction information for online server HADDOCK [12] to simulate the docking between the complex and ipaD. Below is the docking structure ( Figure 4 ). Figure 4 | Docking between 20ipaD (in complex) and IpaD Ramachandran plot of the above structure showed that 85.0% of residues are in the most favorite regions, and 12.7% are in the allowed regions; 1.2% of the residues are in the generously allowed regions and 1.0% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.441, which is relatively close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 87.61%. The overall quality factor is 85.53, which is acceptable. ProSA calculated Z-score is -7.16, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure indicates that 20ipaD can bind with IpaD well theoretically. Below is the alignment between our docking result and the original docking between 20ipaD and IpaD. RMSD is 0.36, which is very small and acceptable. Figure 5 | Alignment between Yeast-20ipaD-IpaD and 20ipaD-IpaD. All the above shows that our Yeast-20ipaD complex could theoretically work well when binding with IpaD. Part 4: Other combinations of probiotic-nanobody complex In this section, we would like to show other possible combinations of fusion protein-nanobody complex that might theoretically function well. To do this, we modeled their 3D structures and their docking scenarios, and analyzed them. This could be helpful for future experiment and future teams. Table 1 | Evaluation of other combinations of probiotic-nanobody complex The E. coli Intimin protein complex has good results in 4 out of 5 quantitative parameters, making it a great model. First, its Ramachandran plot reveals a good distribution in favored regions. 83% of its residues are in the core regions, 14.7% are in the allowed regions, 1.3% are in the general regions and 0.9% in the disallowed regions. Second, the % amino acids having scored 0.2 in 3D/1D profile is 85.91%, higher than the standard 80%. Its atomic model is therefore fairly compatible with its amino acid sequence. Third, its overall quality factor, that accounts for the error value of individual residue, is at 92, surpassing the 80 score cut-off. Its Z-score is also within the range of scores found for native proteins of similar size. The main downside to this model is that Z-score is not around one,showing that it has greater average magnitude of the volume irregularities in the structure. The E. coli CsgA protein complex is a good model that fulfills 4 out of 5 quantitative parameters. Like Intimin, CsgA’s Ramachandran plot displays a good distribution in favored regions: 83.5% of residues are in the core regions, 12.7% are in the allowed regions, 2.0% are in the general regions and 1.8% in the disallowed regions. The % amino acids having scored 0.2 in 3D/1D profile is 84.27%, higher than the standard 80% but not nearly as high as Intimin. Its overall quality factor is 91,exceeding the 80 score cut-off. The Z-score is within the range of scores found for native proteins of similar size, and like Intimin, the CsgA model’s Z-score is not around one. The Lacto tag 1 protein complex is a good model that fulfills 4 out of 5 quantitative parameters. CsgA’s Ramachandran plot displays a well enough distribution in favored regions: 83.1% of residues are in the core regions, 15.2% are in the allowed regions, 1.5% are in the general regions and 0.2% in the disallowed regions. The % of amino acids having scored 0.2 in 3D/1D profile is 79.97%, close enough to the standard 80% but comparatively low against Intimin and CsgA. Its overall quality factor is 92, surpassing the 80 score cut-off. The Z-score is within the range of scores found for native proteins of similar size, and similar to Intimin and CsGA, the CsgA model’s Z-score is not around one. Overall, all three protein docking jobs show satisfactory results and could be helpful for future experiments and future teams. In light of these promising findings, we encourage future researchers to test these models in the lab, with the E. coli Intimin model that performed the best among the three.","breadcrumbs":"Model » Overview:","id":"105","title":"Overview:"},"106":{"body":"To conclude, we have developed the best 3D model for Yeast-20ipaD and the docking structure between Yeast-20ipaD and IpaD. They are well analyzed and are decided to have good effect theoretically. Moreover, we modeled other 3 possible combinations of fusion protein and nanobody, which might serve as a guidance for future experiment design. Robetta https://robetta.bakerlab.org AlphaFold https://www.nature.com/articles/s41586-021-03819-2 AlphaFold(Phenix Version) < https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf old2/AlphaFold2.ipynb> ColabFold < https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol d2.ipynb> AlphaFold2 < https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks /AlphaFold.ipynb> PyMOL https://pymol.org/2/ SAVES https://saves.mbi.ucla.edu/ Prosa https://prosa.services.came.sbg.ac.at/prosa.php Deviations from standard atomic volumes as a quality measure for protein crystal structures https://pubmed.ncbi.nlm.nih.gov/8950272/ HADDOCK online server https://wenmr.science.uu.nl/haddock2.4/ Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion. DOI: 10.1074/jbc.M117.802231 https://pubmed.ncbi.nlm.nih.gov/28842484/ Homology modeling and virtual screening approaches to identify potent inhibitors of VEB-1 β-lactamase. DOI: 10.1186/1742-4682-10-22 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668210/","breadcrumbs":"Model » Summary","id":"106","title":"Summary"},"107":{"body":"","breadcrumbs":"Model » Description and Prediction of drug efficacy","id":"107","title":"Description and Prediction of drug efficacy"},"108":{"body":"Wet lab results showed that we have successfully expressed 20ipaD on the surface of Yeast. Our goal is to describe efficiency of expression and predict the scenario after the drug is released in the patient's jejunal. Part 1: Protein expression efficiency To describe how efficient is Yeast concerning the expression of 20ipaD, we manually calculated the efficiency by counting the number of Yeast cells that expressed 20ipaD and the total number of Yeast cells ( Figure 1 ).Through separated assessments conducted by two individuals, we found that our model has a 31.25% expression rate with a STD of ± 0.75. Figure 1 | Fluorescent cells for Yeast cells that obviously expressed 20ipaD. Dark cells for no or very little expression Part 2: Prediction of post-medication scenario In this section, we want to predict post-medication scenario by using math modeling. In detail, we want to see how will the number of floating Shigella change after the drug release, this will be depending on natural growth of Shigella, the binding efficiency of 20ipaD and IpaD, the concentration of Yeast cells, and the survival rate of Yeast cells. Yeast cells are sealed in micro-capsules made of shellac before being delivered into bodies. The pH-dependent solubility that prefers a mild basic environment makes shellac perfect for releasing probiotics in jejunal. There are several important assumptions for this model: Each floating Yeast cell carries one 20ipaD; Each floating Shigella cell carries one IpaD; Growth of Shigella cultured in BHI (Brian Heart Infusion) medium is similar with the growth of Shigella in human's jejunal; Each 20ipad binds with one IpaD once; Died Yeast cell cannot display 20ipaD and cannot bind with IpaD; Yeast growth is not considered here since a healthy immune system does not allow overgrowth of the yeast, and the growth of the yeast is very slow in neutral; or even slightly alkaline conditions [13] . Based on these assumptions, the following two equations describe the change in number of shigella and Yeast: dtdL′(t)​=dtdL(t)​−βL(t)D(t) dtD(t)​=γL(t)D(t) L′(t): the log count of the number of shigella in jejunal at time t after drug release; L(t): the log count of the number of shigella in jejunal at time t before drug release; β: the binding efficiency between 20ipaD and IpaD; D(t): the log count of number of Yeast in jejunal at time t after drug release; γ:survival rate of Yeast in jejunal Detail: The natural growth of shigella in jejunal can be described in the form of Gompertz equation [14] : L(t)=A+Cexp[−exp(−B(t−M))] L(t): the log count of the number of shigella in jejunal at time t before drug release; A: the asymptotic log count as t decreases indefinitely; C: the asymptotic amount of growth (log number) that occurs as t increases indefinitely; M: the time at which the absolute growth rate is maximum; B: the relative growth rate at M Parameters A, C, M,and B depend on the environmental conditions: temperature T, pH, and sodium chloride concentration c. In our case, T is defaulted to 37 degrees; the pH is about 6.9 in jejunal and about 7.2 in ileal [15] ; c in jejunal is about 112mM [16] . Translate the concentration into the form of percentage: 100mlxg​58.44g1mol​1L1000ml​=0.012M x=0.65 So, the concentration of sodium chloride is about 0.65% in jejunal. Gompertz equation parameters and calculated growth curve values for Shigella can be found in the paper: Effect of Sodium Chloride, pH and Temperature on Growth of Shigella flexneri [14] . Parameters in our situation do not perfectly fit the calculated ones, but they do fall in a certain range: Lower limit: T=37 degrees, pH=6.5, c=0.5% A=4.53, B=0.493, C=4.47, M=3.68 L(t)=4.53+4.47exp[−exp(−0.493(t−3.68))] dtL(t)​=2.20exp[−exp(−0.493(x−3.68))−0.493(x−3.68)] Higher limit: T=37 degrees, pH=7.5, c=0.5% A=4.26, B=0.435, C=5.41, M=4.54 L(t)=4.26+5.41exp[−exp(−0.435(t−4.54))] dtL(t)​=2.35exp[−exp(−0.435(x−4.54))−0.435(x−4.54)] Since our situation is in this range, so we can have an upper limit and lower limit for the growth scenario of Shigella ( Figure 2 ). Figure 2 | Upper limit and lower limit for Shigella's natural growth in jejunal. The x axis indicates the time with unit of hour; the y axis indicates the log count of number of Shigella. The survival rate of Yeast cells in jejunal varies with time ( Figure 3 ) [15] . Figure 3 | Survival rate of Yeast cells in jejunal with time of digestion. The survival rate is highest at t=2h, when 30.8% of intake Yeast cells are viable. Then, the viability decreases with time, finally 13% of intake Yeast cells are viable at 5h. Part 3: Medication guidance Our drug is designed to 'kill' the Shigella before it invades the surface of jejunal, or more realistically, to decrease the concentration of floating Shigella so that a mass invasion could be avoided or stopped as soon as possible. Based on the information from wet-lab and math modeling, we would like to give a possible conclusion or a medication guidance for the patients and the managers of the healthcare system, so that our vision could be realized. For a single micro-capsule, assume it contains at least 10 billion CFU (colony-forming unit) [17] , then it contains at least 10 billion live Yeast cells. Since the expression rate is about 31.25%, there would be at least 3 billion live Yeast cells that expressed at least one 20ipaD on each of their surfaces. After the capsule reaches jejunal, it will dissolve and start to release Yeast cells. After 2 hours, there will be about 0.9 billion Yeast cells (30.8% of the intake) that are viable to display 20ipaD and bind with IpaD. For Shigella, since the upper limit and lower limit of natural growth are found, we can calculate the maximum population density in the following form: Densitymax​(log10​cfu/ml)=A+C So the uppper limit of the max density at t=5h will be about 5 billion Shigella, and the lower limit will be about 1 billion Shigella. Therefore, it is proper to take 5-6 capsules every 5 hours after the patient start to have symptoms, and distribute 1-5 capsules every 5 hours to the people who might develop symptoms due to living togethor or common life styles.","breadcrumbs":"Model » Overview","id":"108","title":"Overview"},"109":{"body":"To conclude, we have described the 20ipaD expression efficiency of Yeast cell through wet-lab results and predicted the post-medication scenario through math modeling. The expression efficiency is found to be about 31.25%± 0.75, and the upper limit and lower limit of natural growth of Shigella could help us to define a range for Shigella to grow naturally in jejunal. By assuming each capsule contains 10 billion CFU, we are able to give a medication guidance for symptomatic patient to take 5-6 capsules per 5 hours and for potential patients to take 1-5 capsules per 5 hours. In the future, more work can be devoted to deciding the binding efficiency β between Yeast-20ipaD and IpaD, and how much CFU is needed and realistic can a single capsule contain. These work can help us better understand the change of number of Shigella after medication, so that a more precise medication guidance is available. Investigation of the Best Saccharomyces cerevisiae Growth Condition. Electron Physician. DOI: 10.19082/3592 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5308499/ Effect of Sodium Chloride, pH and Temperature on Growth of Shigella flexneri. Journal of Food Protection. DOI:10.4315/0362-028x-52.5.356 https://pubmed.ncbi.nlm.nih.gov/31003269/ Effect of a New Probiotic Saccharomyces cerevisiae Strain on Survival of Escherichia Coli O157:H7 in a Dynamic Gastrointestinal Model. Applied and Environmental Microbiology. DOI:10.1128/AEM.02130-10 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3028742/ The mechanisms of sodium absorption in the human small intestine. The Journal of Clinical Investigation. DOI:10.1172/JCI105781 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC297237/ Choosing the Best Probiotic: How Many CFUs is Enough? https://deerland.com/chew/choosing-best-probiotic-many-cfus-enough/","breadcrumbs":"Model » Summary & Future plan","id":"109","title":"Summary & Future plan"},"11":{"body":"Attributions","breadcrumbs":"Team » Attributions » Biology team","id":"11","title":"Biology team"},"110":{"body":"Probiotics will be sealed in microcapsules( Figure 1 ) made of shellac before being delivered into bodies. The pH-dependent solubility that prefers a mild basic environment makes shellac perfect for releasing probiotics in intestines. Figure 1 | 3D model of the microcapsule Microcapsule is a microscope-scale capsulation format. The probiotics were wrapped by materials that can ensure the reservation, activation, release, and environmental-resistance of the probiotics. It would be presented as powder. “Microencapsulation is a technology that serves as a tool to protect the sensitive and expensive nutrients (Meyers et al., 1998), by providing them with a protective wall, which allows them to get released at a particular site, at a particular time, and under particular conditions.\" [18] To summarize, the technology of microencapsulation is to ensure the safe delivery of sensitive compound. Shellac is a natural polymer that is generally recognized as a safe (GRAS) material. It is insoluble in neutral and acidic aqueous solution but dissolves at alkaline condition [19] . So, shellac is proper for the controlled release of Yeast cells in the intestine. Research has shown that the microcapsules with the addition of shellac \"contributed to better probiotic survivals after freeze drying, simulated digestion,heating and ambient storage, and whey protein isolate (WPI) addition had a synergistic effect.\" [20] Microencapsulation: An overview on concepts, methods, properties and applications in foods. Food Frontiers. https://doi.org/10.1002/fft2.94 Microencapsulation of probiotic lactobacilli with shellac as moisture barrier and to allow controlled release. Journal of the Science of Food and Agriculture. https://doi.org/10.1002/jsfa.10685 Comparison of spray drying, freeze drying and convective hot air drying for the production of a probiotic orange powder. J Funct Foods https://doi.org/10.1016/j.jff.2015.06.001","breadcrumbs":"Model » Hardware","id":"110","title":"Hardware"},"111":{"body":"Parts All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Yeast (Group Y) Parts","id":"111","title":"Yeast (Group Y) Parts"},"112":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. Part Code Part name Link BBa_K4161501 T7 Promoter http://parts.igem.org/Part:BBa_K4161501 BBa_K4161502 GAL1 Promoter http://parts.igem.org/Part:BBa_K4161502 BBa_K4161503 Aga2 http://parts.igem.org/Part:BBa_K4161503 BBa_K4161504 G4S http://parts.igem.org/Part:BBa_K4161504 BBa_K4161505 T7, Xpress http://parts.igem.org/Part:BBa_K4161505 BBa_K4161506 ipaD http://parts.igem.org/Part:BBa_K4161506 BBa_K4161507 HA http://parts.igem.org/Part:BBa_K4161507","breadcrumbs":"Parts » Group Y single elements","id":"112","title":"Group Y single elements"},"113":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. Part Code Part name Link BBa_K4161301 Single Domain Antibody 20ipaD Conjugated Aga2 Express Module http://parts.igem.org/Part:BBa_K4161301 BBa_K4161508 488aa recombinant protein, Aga2 + ipaD http://parts.igem.org/Part:BBa_K4161508","breadcrumbs":"Parts » Group Y key composite segments","id":"113","title":"Group Y key composite segments"},"114":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. Part Code Part name Link BBa_K4161302 pYD1 plasmid http://parts.igem.org/Part:BBa_K4161302","breadcrumbs":"Parts » Group Y vector","id":"114","title":"Group Y vector"},"115":{"body":"","breadcrumbs":"Parts » E.coli Nissle 1917 (Group E) Parts","id":"115","title":"E.coli Nissle 1917 (Group E) Parts"},"116":{"body":"Single elements of Group E include nanobodies, curli protein (csg) operon fragments, linkers, tags, signal peptides, promoters and terminators. A total of 15 parts were documented. Part code Part name Link BBa_K4161001 20IpaD http://parts.igem.org/Part:BBa_K4161001 BBa_K4161002 JMK-H2 http://parts.igem.org/Part:BBa_K4161002 BBa_K4161010 csgA http://parts.igem.org/Part:BBa_K4161010 BBa_K4161011 csgB http://parts.igem.org/Part:BBa_K4161011 BBa_K4161012 csgC http://parts.igem.org/Part:BBa_K4161012 BBa_K4161013 csgE http://parts.igem.org/Part:BBa_K4161013 BBa_K4161014 csgF http://parts.igem.org/Part:BBa_K4161014 BBa_K4161015 csgG http://parts.igem.org/Part:BBa_K4161015 BBa_K4161016 riboJ http://parts.igem.org/Part:BBa_K4161016 BBa_K4161017 Neae: the intimin fragment for surface display http://parts.igem.org/Part:BBa_K4161017 BBa_K4161018 pTlpA promotor C7 variant http://parts.igem.org/Part:BBa_K4161018 BBa_K4161019 FE-36 linker http://parts.igem.org/Part:BBa_K4161019 BBa_K4161020 JPS-G3 http://parts.igem.org/Part:BBa_K4161020 BBa_K4161021 3xFlag http://parts.igem.org/Part:BBa_K4161021 BBa_K4161022 thr terminator http://parts.igem.org/Part:BBa_K4161022","breadcrumbs":"Parts » Group E single elements","id":"116","title":"Group E single elements"},"117":{"body":"Group E's composite parts are designed to express surface protein-nanobody fusion proteins. A total of 4 composite parts are documented. Part code Part name Link BBa_K4161003 csg-JMK-H2, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161003 BBa_K4161004 intimin-20IpaD, Nanobody surface display system based on intimin http://parts.igem.org/Part:BBa_K4161004 BBa_K4161023 csgA-JPS-G3-3xFLAG, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161023 BBa_K4161100 Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161100","breadcrumbs":"Parts » Group E composite segments","id":"117","title":"Group E composite segments"},"118":{"body":"Vectors pET30a and pUC19 are used for recombinant plasmid construction and protein expression. Part code Part name Link BBa_K4161024 pET30a, empty vector http://parts.igem.org/Part:BBa_K4161024 BBa_K4161025 pUC19, empty vector http://parts.igem.org/Part:BBa_K4161025","breadcrumbs":"Parts » Group E vectors","id":"118","title":"Group E vectors"},"119":{"body":"","breadcrumbs":"Parts » L.lactis NZ9000 parts","id":"119","title":"L.lactis NZ9000 parts"},"12":{"body":"Biology Team leader. In charge of wet lab organization, human practice organizations and wiki construction. Designed the overall topic and approach of the problem to tackle with synthetic biology design. Designer of E.coli csgA surface display and lab experiments of the E. coli group.","breadcrumbs":"Team » Attributions » Yixuan Wu (Lisa)","id":"12","title":"Yixuan Wu (Lisa)"},"120":{"body":"Single parts in Group L includes the following elements: Group L parts Part code Part name Link BBa_K4161600 Usp45 nisin promoter http://parts.igem.org/Part:BBa_K4161600 BBa_K4161603 AcmA3b http://parts.igem.org/Part:BBa_K4161603 BBa_K4161602 20ipaD http://parts.igem.org/Part:BBa_K4161602 BBa_K4161604 signalling peptide in L.lactis http://parts.igem.org/Part:BBa_K4161604 BBa_K4161605 Flag-tag http://parts.igem.org/Part:BBa_K4161605","breadcrumbs":"Parts » Group L single elements","id":"120","title":"Group L single elements"},"121":{"body":"The composite element of Group L includes Usp45-signaling peptide in L.lactis-Flagtag-20ipaD-AcmA3b. Part code Part name Link BBa_K4161600 Usp45-signaling peptide in L.lactis-20ipaD-AcmA3b http://parts.igem.org/Part:BBa_K4161997","breadcrumbs":"Parts » Composite elemnent","id":"121","title":"Composite elemnent"},"122":{"body":"","breadcrumbs":"Parts » Group L vector","id":"122","title":"Group L vector"},"123":{"body":"The plasmid backbone of Group L is pNZ8148, a plasmid suitable for L.lactis. Part code Part name Link BBa_K4161601 pNZ8148 http://parts.igem.org/Part:BBa_K4161601","breadcrumbs":"Parts » Composite elemnent","id":"123","title":"Composite elemnent"},"124":{"body":"Parts All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Part Collection » Yeast (Group Y) Parts","id":"124","title":"Yeast (Group Y) Parts"},"125":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. Part Code Part name Link BBa_K4161501 T7 Promoter http://parts.igem.org/Part:BBa_K4161501 BBa_K4161502 GAL1 Promoter http://parts.igem.org/Part:BBa_K4161502 BBa_K4161503 Aga2 http://parts.igem.org/Part:BBa_K4161503 BBa_K4161504 G4S http://parts.igem.org/Part:BBa_K4161504 BBa_K4161505 T7, Xpress http://parts.igem.org/Part:BBa_K4161505 BBa_K4161506 ipaD http://parts.igem.org/Part:BBa_K4161506 BBa_K4161507 HA http://parts.igem.org/Part:BBa_K4161507","breadcrumbs":"Parts » Part Collection » Group Y single elements","id":"125","title":"Group Y single elements"},"126":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. Part Code Part name Link BBa_K4161301 Single Domain Antibody 20ipaD Conjugated Aga2 Express Module http://parts.igem.org/Part:BBa_K4161301 BBa_K4161508 488aa recombinant protein, Aga2 + ipaD http://parts.igem.org/Part:BBa_K4161508","breadcrumbs":"Parts » Part Collection » Group Y key composite segments","id":"126","title":"Group Y key composite segments"},"127":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. Part Code Part name Link BBa_K4161302 pYD1 plasmid http://parts.igem.org/Part:BBa_K4161302","breadcrumbs":"Parts » Part Collection » Group Y vector","id":"127","title":"Group Y vector"},"128":{"body":"","breadcrumbs":"Parts » Part Collection » E.coli Nissle 1917 (Group E) Parts","id":"128","title":"E.coli Nissle 1917 (Group E) Parts"},"129":{"body":"Single elements of Group E include nanobodies, curli protein (csg) operon fragments, linkers, tags, signal peptides, promoters and terminators. A total of 15 parts were documented. Part code Part name Link BBa_K4161001 20IpaD http://parts.igem.org/Part:BBa_K4161001 BBa_K4161002 JMK-H2 http://parts.igem.org/Part:BBa_K4161002 BBa_K4161010 csgA http://parts.igem.org/Part:BBa_K4161010 BBa_K4161011 csgB http://parts.igem.org/Part:BBa_K4161011 BBa_K4161012 csgC http://parts.igem.org/Part:BBa_K4161012 BBa_K4161013 csgE http://parts.igem.org/Part:BBa_K4161013 BBa_K4161014 csgF http://parts.igem.org/Part:BBa_K4161014 BBa_K4161015 csgG http://parts.igem.org/Part:BBa_K4161015 BBa_K4161016 riboJ http://parts.igem.org/Part:BBa_K4161016 BBa_K4161017 Neae: the intimin fragment for surface display http://parts.igem.org/Part:BBa_K4161017 BBa_K4161018 pTlpA promotor C7 variant http://parts.igem.org/Part:BBa_K4161018 BBa_K4161019 FE-36 linker http://parts.igem.org/Part:BBa_K4161019 BBa_K4161020 JPS-G3 http://parts.igem.org/Part:BBa_K4161020 BBa_K4161021 3xFlag http://parts.igem.org/Part:BBa_K4161021 BBa_K4161022 thr terminator http://parts.igem.org/Part:BBa_K4161022","breadcrumbs":"Parts » Part Collection » Group E single elements","id":"129","title":"Group E single elements"},"13":{"body":"Co-established the project topic. In charge of lab design and wet lab for the yeast group. Also assisted in Wiki writing and expert interview.","breadcrumbs":"Team » Attributions » Yuxin Wang","id":"13","title":"Yuxin Wang"},"130":{"body":"Group E's composite parts are designed to express surface protein-nanobody fusion proteins. A total of 4 composite parts are documented. Part code Part name Link BBa_K4161003 csg-JMK-H2, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161003 BBa_K4161004 intimin-20IpaD, Nanobody surface display system based on intimin http://parts.igem.org/Part:BBa_K4161004 BBa_K4161023 csgA-JPS-G3-3xFLAG, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161023 BBa_K4161100 Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161100","breadcrumbs":"Parts » Part Collection » Group E composite segments","id":"130","title":"Group E composite segments"},"131":{"body":"Vectors pET30a and pUC19 are used for recombinant plasmid construction and protein expression. Part code Part name Link BBa_K4161024 pET30a, empty vector http://parts.igem.org/Part:BBa_K4161024 BBa_K4161025 pUC19, empty vector http://parts.igem.org/Part:BBa_K4161025","breadcrumbs":"Parts » Part Collection » Group E vectors","id":"131","title":"Group E vectors"},"132":{"body":"","breadcrumbs":"Parts » Part Collection » L.lactis NZ9000 parts","id":"132","title":"L.lactis NZ9000 parts"},"133":{"body":"Single parts in Group L includes the following elements: Group L parts Part code Part name Link BBa_K4161600 Usp45 nisin promoter http://parts.igem.org/Part:BBa_K4161600 BBa_K4161603 AcmA3b http://parts.igem.org/Part:BBa_K4161603 BBa_K4161602 20ipaD http://parts.igem.org/Part:BBa_K4161602 BBa_K4161604 signalling peptide in L.lactis http://parts.igem.org/Part:BBa_K4161604 BBa_K4161605 Flag-tag http://parts.igem.org/Part:BBa_K4161605","breadcrumbs":"Parts » Part Collection » Group L single elements","id":"133","title":"Group L single elements"},"134":{"body":"The composite element of Group L includes Usp45-signaling peptide in L.lactis-Flagtag-20ipaD-AcmA3b. Part code Part name Link BBa_K4161600 Usp45-signaling peptide in L.lactis-20ipaD-AcmA3b http://parts.igem.org/Part:BBa_K4161997","breadcrumbs":"Parts » Part Collection » Composite elemnent","id":"134","title":"Composite elemnent"},"135":{"body":"","breadcrumbs":"Parts » Part Collection » Group L vector","id":"135","title":"Group L vector"},"136":{"body":"The plasmid backbone of Group L is pNZ8148, a plasmid suitable for L.lactis. Part code Part name Link BBa_K4161601 pNZ8148 http://parts.igem.org/Part:BBa_K4161601","breadcrumbs":"Parts » Part Collection » Composite elemnent","id":"136","title":"Composite elemnent"},"137":{"body":"Our part BBa_K4161301 is an improvement of part BBa_K416000 from iGEM10_NYU (2010). In 2010, iGEM10_NYU designed the part “BBa_K416000†which was the CDS of Aga2 protein for yeast surface display. The part was achieved by deleting the stop codon of the Aga2 CDS region from vector pCTCON2 so that the element can be fused with other fragments to express fusion proteins. On the basis of this part, we designed the integrated expression module “BBa_K4161301â€. This part integrated the yeast surface protein Aga2, GAL1 promotor, nanobody 20ipaD, and 3xFLAG tag sequences, which make it a complete expression module that is controllable. The addition of GAL1 promotor ensures the whole surface display part would only be induced by galactose and denied the leaky expression. The nanobody segment provides the real function for the whole module so that it can bind to its corresponding antigen to inhibit pathogens like Shigella. Additionally, the 3xFLAG tag eases the detection of the expression of this module.","breadcrumbs":"Parts » Improve » Part improvement","id":"137","title":"Part improvement"},"138":{"body":"Safety The Duke Kunshan University (DKU) iGEM team sets safety as an integral part of science. It includes protection for sensitive groups and the environment. For this reason, safety was considered from two perspectives—inside and outside the laboratory. For more detailed information, please check our safety form.","breadcrumbs":"Safety » Introduction","id":"138","title":"Introduction"},"139":{"body":"All laboratories of universities in China must be accredited by the Office under the Ministry of Environment following the standard. This year, the project was conducted in the BSL-1 laboratory. Team members wore lab coats and gloves during experiments. Experiments related to bacteria were performed in the biosafety cabinet and near butane burners. Before laboratory started, the team received safety training including how to use equipment properly, following laboratorial hygiene rules and proper disposal of hazardous substances. Also, experiments were first presented in detail by our two supervisors to eliminate biosafety concerns.","breadcrumbs":"Safety » Lab Safety","id":"139","title":"Lab Safety"},"14":{"body":"In charge of background research, E. coli group lab design, wet labs & wiki writing. Hosted journal clubs and science lectures for human practice.","breadcrumbs":"Team » Attributions » Yunyi Ru","id":"14","title":"Yunyi Ru"},"140":{"body":"Protein expression for diagnostic tests was performed in non-pathogenic Escherichia coli strains (E.coli Nissle 1917), Lactococcus lactis NZ9000 and yeast (EBY100). These gene carriers are probiotic or at least harmless. They do not possess serious illnesses or lead to other problems to people or the environment. In addition, they are in whitelist, belonging to BSL-1 organisms.","breadcrumbs":"Safety » Microorganisms review","id":"140","title":"Microorganisms review"},"141":{"body":"The engineered probiotics were designed to express 20ipad nanobody on their surface by transforming recombinant plasmids with optimized genes. Thus, they can combine with the antigen on the surface of Shigella. Since Shigella is one of the BSL-2 organisms, we decide to express our targeted antigen in probiotics that we used to express the antibody. We optimized the DNA sequences which code the antigen by using machine-learning software. Using yeast as an example, amino acids are essential for the growth of yeast. Amino acids are absorbed by human bodies in the small intestine. There is a competitive absorption of amino acids between intestinal epithelial cells and yeast. This prevents the overgrowth of yeast cells, preventing the destruction of bacterial flora structure. Using yeast as gene carriers limits the leak of antibiotics resistance genes, compared with using bacteria as carriers. In addition, galactose was used to induce the expression of the antibody and antigen. Since we used antibiotics resistance genes, we also pay attention to the potential risks of the leak of antibiotics resistance genes during wetlab process. Discarded liquids and plates that contain antibiotics were placed in specific vessels and then autoclaved.","breadcrumbs":"Safety » Experiments","id":"141","title":"Experiments"},"142":{"body":"Part of planned experiments had to be done by using harmful reagents or procedures. All team members follow the rules under the guideline provided by our lab manager and assistants during experiment safety training. UV light was used to sterilize the biosafety cabinets and equipment inside the cabinets. Safety measures were taken to avoid people`s direct exposure to UV light. Gel imaging system was used for visualizing agarose gel, combined with standard laboratory procedures with blue light transilluminator. Antibiotics were used to select transformants. They can be harmful to sensitive groups. Situations of allergy of team members were collected. Antibiotics were well stored and Handled with proper safety measures according to disposal protocols. Other hazardous chemicals , such as Tris-HCl and methyl alcohol were stored and relevant procedures were conducted in chemical ventilation cabinets. Liquid waste was handled with appropriate safety measures.","breadcrumbs":"Safety » Harmful reagents and procedures","id":"142","title":"Harmful reagents and procedures"},"143":{"body":"Team members followed all the government and university guidelines based on the pandemic situation of Covid-19 in China. For April and May, team`s meetings were online because of school closure and in-person activities were allowed after deblocking. Covid-19 tests were performed regularly and all team members got vaccinated. When wetlabs began, team members` attendance was recorded. The usage of lab equipment was registered. All working surfaces were cleaned with disinfectant fluid before and after conducting wetlabs.","breadcrumbs":"Safety » Covid-19 associated safety measures","id":"143","title":"Covid-19 associated safety measures"},"144":{"body":"Antibiotic resistance is a problem in its scale and subtlety. Shigella infection has its significance in antibiotic resistance because of its identity as one of the most antibiotic resistant bacterias recognized by CDC. In our integrated human practice, we followed the procedure of research-design-engagement-modification.","breadcrumbs":"Human Practices » Integrated Human Practice","id":"144","title":"Integrated Human Practice"},"145":{"body":"The subtlety of antibiotic resistance did not come to mind until some of the team members took the microbiology class at DKU: From the amazing lectures given by Dr. Linfeng Huang, we realized that the race against bacterial infection is largely dependent on discoveries of newly synthesized drugs. People modify the drug molecule by perhaps a small sidechain, changing the chemical property but perhaps not changing the chemical property. This can lead to significant advances because it can possibly alter the pathogen's ability to recognize the drug, therefore no longer maintain its resistance. Antibiotics are thus labeled as the best weapon. It is almost always the solution to infections. It can be bought at ordinary pharmacies, and are consumed at a scale larger than ever. From talking with the people around us, we realized that the lack of knowledge of antibiotic resistance exists as possibly a larger threat than the pathogen itself. We ask ourselves: What if one day, we have exhausted all the combinations of chemicals? What if we lose the race because we have strengthened antibiotic resistance to the point of no return? And clearly this has been considered. The field of immunology has become more heated than ever before. What if we could deploit the weapon that is the gift of the creation-our own immune systems? We looked into nanobody therapy, because it is easy to perform in our lab, and effective nanobodies for Shigella T3SS has been revealed by previous studies.","breadcrumbs":"Human Practices » Recognizing the problem and designing the approach","id":"145","title":"Recognizing the problem and designing the approach"},"146":{"body":"We further consulted experts in this area, including Dr. Neel Joshi from Northwestern University, whose lab had worked on nanobody therapy and bacterial surface display. He answered our questions about the choice of probiotics and gave us more information on the multi-valency potential of the surface display method. He also reminded us that areas with high shigella infection rates and mortality are usally underdeveloped areas, thus we should consider the delivery method to be economic friendly and easy to maintain. In the interview with Dr. Lin from SINOVAC, he suggested that our final design should consider safety, effectiveness and economics. See entrepreneurship for more details. To engage with the general public in our design, we distributed a questionaire and received over 500 responses on what people know about antibiotic resistance and shigella infection, and identified potential barriers of drug distribution to the general public. See our report here.","breadcrumbs":"Human Practices » Engaging stakeholders","id":"146","title":"Engaging stakeholders"},"147":{"body":"In aspect of our design, we adopted the PATCH system by Dr. Neel Joshi, for better multivalency performance. We also changed our design logic: our drug is more vaccine orientated than the conventional drug designs. The drug should be ideal for prevention of regional spread of shigella infection, acting as a blocking agent for further transmission. The delivery method is in freeze-dried powder, delivered in economic-friendly microcapsules. For the advice from Dr. Lin, we made multiple modifications that would promote the safety and effectiveness of our design. See entrepreneurship for more details. As for the general public response, we found one major problem, which is that a significant amount of people see E. coli as the main causative agent for dysentery syndrome. We assessed that this may cause major problems if we reveal our approach as probiotic-nanobody therapy, in specific, yeast and E. coli Nissle 1917 can be subject to public opinions including skepticism. Therefore, we attempted educational approaches to give more information on probiotics at both DKU and local high schools.","breadcrumbs":"Human Practices » Modification","id":"147","title":"Modification"},"148":{"body":"Our integrated human practices influenced our experimental design, and the overall logic of our project. We are able to engage with our stakeholders and the general public, acheiving satisfying outcomes. Engagement is the key to creating a project design with actual social impact, and we will carry this spirit on as we progress further into our project and future careers.","breadcrumbs":"Human Practices » Conclusion","id":"148","title":"Conclusion"},"149":{"body":"Education Overview: We conduct popular science education both on and off campus. On campus, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating. We also cohosted a Biology Seminar Series, inviting Prof. Dong Hyun Jo, from Seoul National University College of Medicine to give a talk on therapeutic revolution for the DKU community. Off campus, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers about our project and synthetic biology. Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo For GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo For probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Off campus education","id":"149","title":"Off campus education"},"15":{"body":"Designed Lactococcus lab procedures and in charge of Lactococcus and yeast lab experiments. Conducted expert interviews for human practice.","breadcrumbs":"Team » Attributions » Zhujun Yao","id":"15","title":"Zhujun Yao"},"150":{"body":"Wang-Cai Biology Seminar Series Wang-Cai Talk In this Wang-Cai biology seminar series, the DKU iGEM team was honored to co-host the speech delivered by Prof. Dong Hyun Jo from Seoul National University College of Medicine. The talk was titled “Therapeutic Revolution: Application of Novel Technologiesâ€, where Dr Jo introduced the brief history and therapeutic development for one specific type of cancer, retinoblastoma. Dr Jo is the assistant professor of Seoul National University College of Medicine in Republic of Korea. He had his medical degree at Seoul National University in 2007. In 2012, Dr Jo received residency at the Department of Ophthalmology, Seoul National University Hospital, and in 2016, he received his PhD at Seoul National University. Dr Jo’s research interest focuses on 3 aspects. The first is the development of novel therapeutic approaches against retinal diseases. The second is the molecular mechanisms of physiological and pathological angiogenesis in the retina and associated organs, the third is translational research on retinoblastoma. At the end of the talk. Dr. Jo shared his career pathway as both a physician and a researcher. The devotion he made to the clinical therapy of retinoblastoma and the improvement of the health of his patients made him feel that biomedical sciences are not limited to theoretical knowledge, but rather quite practical and can benefit the whole population. The experience and thoughts expressed by Dr. Jo greatly inspired us, which allow us to have more understanding of graduate choices and future career plans. Journal club In order to have better educational effect and promote our project , we organized the Journal Club activity in the Duke Kunshan community. The first Journal Club was held on April 30th, 2022. At the very beginning of the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us and introduced in detail what systems biology is and the basic methods of studying systems biology. This journal club event mainly focused on COVID-19 and then developed into three sub-topics including the antigen test for SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the iGEM team, around 10 freshman students with various backgrounds participated in the sharing and raised many inspiring questions.","breadcrumbs":"Awards » On campus education","id":"150","title":"On campus education"},"151":{"body":"We have devoted in several education activities. On-campus education allows us to better transfer knowledge about synthetic biology and shigella treatment to our students, as well as gather fresh blood for the next year's team. The science popularization and education in local school also gives us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Awards » Summary","id":"151","title":"Summary"},"152":{"body":"Education Overview: We conduct popular science education both on and off campus. On campus, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating. We also cohosted a Biology Seminar Series, inviting Prof. Dong Hyun Jo, from Seoul National University College of Medicine to give a talk on therapeutic revolution for the DKU community. Off campus, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers about our project and synthetic biology. Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo For GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo For probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Education » Off campus education","id":"152","title":"Off campus education"},"153":{"body":"Wang-Cai Biology Seminar Series Wang-Cai Talk In this Wang-Cai biology seminar series, the DKU iGEM team was honored to co-host the speech delivered by Prof. Dong Hyun Jo from Seoul National University College of Medicine. The talk was titled “Therapeutic Revolution: Application of Novel Technologiesâ€, where Dr Jo introduced the brief history and therapeutic development for one specific type of cancer, retinoblastoma. Dr Jo is the assistant professor of Seoul National University College of Medicine in Republic of Korea. He had his medical degree at Seoul National University in 2007. In 2012, Dr Jo received residency at the Department of Ophthalmology, Seoul National University Hospital, and in 2016, he received his PhD at Seoul National University. Dr Jo’s research interest focuses on 3 aspects. The first is the development of novel therapeutic approaches against retinal diseases. The second is the molecular mechanisms of physiological and pathological angiogenesis in the retina and associated organs, the third is translational research on retinoblastoma. At the end of the talk. Dr. Jo shared his career pathway as both a physician and a researcher. The devotion he made to the clinical therapy of retinoblastoma and the improvement of the health of his patients made him feel that biomedical sciences are not limited to theoretical knowledge, but rather quite practical and can benefit the whole population. The experience and thoughts expressed by Dr. Jo greatly inspired us, which allow us to have more understanding of graduate choices and future career plans. Journal club In order to have better educational effect and promote our project , we organized the Journal Club activity in the Duke Kunshan community. The first Journal Club was held on April 30th, 2022. At the very beginning of the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us and introduced in detail what systems biology is and the basic methods of studying systems biology. This journal club event mainly focused on COVID-19 and then developed into three sub-topics including the antigen test for SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the iGEM team, around 10 freshman students with various backgrounds participated in the sharing and raised many inspiring questions.","breadcrumbs":"Awards » Education » On campus education","id":"153","title":"On campus education"},"154":{"body":"We have devoted in several education activities. On-campus education allows us to better transfer knowledge about synthetic biology and shigella treatment to our students, as well as gather fresh blood for the next year's team. The science popularization and education in local school also gives us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Awards » Education » Summary","id":"154","title":"Summary"},"155":{"body":"The probiotics market in China is expected to reach a size of USD 13,527.100 million by 2025, growing at a CAGR of 8.81 percent. In 2019, the market was valued at US8,149.466 million [1] . Previous research findings has emphasized on the significance of gut microbiome on human health, and this has opened up the marketing of probiotics. Taking advantage of the booming market and the maturation of bioengineering technology, our project aims to guard our guts through bacteria-bacteria interaction, a method that is an alternative to antibiotics. Some probiotic product utilizing bacteria-bacteria cell interaction has already gone through clinical trials and entered the market, such as Lactobacillus reuteri DSM17648 that treats H.pylori infection [2] . Therefore, it is possible for our product to secure a place in the probiotic market. The terminal of our designed product is a drug used in people. We understand that animal model testings as well as clinical trials are often involved in the process of drug development. What we have reached so far is only a prototype tested in vitro. After the completion of the in vitro testing we will proceed to in vivo models. To improve our plan we interviewed Jisheng Lin from Sinovac Biotech company, to collected feedbacks and suggestions about how to turn our products into commercial ones as well as cautions on putting our products in a real world situation. Here we provide considerations from various aspects of accessing our products into market and our solutions so far.","breadcrumbs":"Awards » Entrepreneurship » Introduction","id":"155","title":"Introduction"},"156":{"body":"\"Safety is always the first concern,\" as suggested by Mr. Lin, \"even it doesn't work well, at least does no harm.\" Based on Mr. Lin's suggestions as well as our previous thoughts, several sources of safety concerns are listed as follows: First, the plasmid we used for selection contains a bacterial ampicillin resistance gene. though not expressed in yeast due to different promoter and codon structures, potential horizontal gene transfers still leave risks of spread antibiotic resistent genes to other prokaryotes in the intestine. Second, though our vectors cell linage yeast strain EBY100 has been well studied, the genomic background of our engineered yeast is unknown. Our engineering process may alter the growth and metabolic characteristics. Efforts should be given to test if engineered yeast could harm human bodies. Besides, human intestine is a complicated microenvironment comprises of a microbiota yet not fully understood. It is also important to clarify how long does our engineered yeast can survive in human body, whether it gains competitive advantages over native gut microorganisms, and how it alter the structure of gut microbiome. Third, similar to antibody therapies, allergy may be a question to some people. Therefore, an approach should be developed to pre-test patients' irritability. Fourth, as a commercial product, a standard of quality control during each step of the engineering or the drug production is also needed. Entre_image","breadcrumbs":"Awards » Entrepreneurship » Safety","id":"156","title":"Safety"},"157":{"body":"Effectiveness demonstrates the values of our products. We have shown qualitatively the expression of the antibodies and the binding between the antigen and the antibodies. For a real world application, we need to establish standard to access and quantify these values. Moreover, the success in the simplified in vitro assay does not guarantee the effectiveness of the drug to work in a real scenario. Considering the real world application that our products function in human GI tracts, it requires the engineered yeast be able to settle down, proliferate, and bind to Shigella spike proteins. Hence, the growth curve about the engineered yeast in human intestines should also be tested. More importantly, the performance of the drug should also be assessed. Potential questions include whether there is dosage-dependent protection effect, how to assess these effects if they exist, and whether this product focuses on therapy or is precaution oriented.","breadcrumbs":"Awards » Entrepreneurship » Effectiveness","id":"157","title":"Effectiveness"},"158":{"body":"The third aspect related to the economics about our products. Apart from the reagents and consumable usage, stabilities, including plasmid stability and the stability of the phenotype expressions, are important factor influence the cost of production. A passaging lineage stably expression the recombinant antibodies greatly reduce the cost of continuously re-engineering the yeast to harvest antibody expression. Efforts should be devoted to focus on increasing the stability antibody expression during passages.","breadcrumbs":"Awards » Entrepreneurship » Economics","id":"158","title":"Economics"},"159":{"body":"We should also seek for further development of our products in the future, such as increasing the valency of our product so that it can target multiple pathogens at the same time.","breadcrumbs":"Awards » Entrepreneurship » Future","id":"159","title":"Future"},"16":{"body":"Proposed the project topic, participated in plasmid design and workflow design of E.coli group, participated in wet labs and background research. Helped conduct collaboration with XJLTU as a part of human practice.","breadcrumbs":"Team » Attributions » Chang Shen","id":"16","title":"Chang Shen"},"160":{"body":"As many goals are still far from being achieved, here we proposed our future plan altogether with what we have reached. We used two different approaches to remove the influence of ampicillin resistance gene. In the first approach, we designed a PCR-fusion that jumps the whole ampicillin resistant gene and the bacterial replication origin. The resting plasmid contains around 3200bp including the TRP1 gene that is a suitable size for PCR amplification and enables the selection of transformant yeast cells. The alternative approach used CRISPR-Cas9 to integrate the whole \"promoter-Aga2-20ipaD\" cassette into yeast genome. The latter also increases phenotype stability as no plasmid is needed to maintain the phenotype. For expression level assessment, we have already established a system employed ELISA to quantify the expression. However, one drawback of this approach is that it does not differentiate surface displayed antibodies from the antibodies no correctly presented on surface. An improved design uses biotins to labeled all surface proteins followed by avidin affinity binding to isolate these proteins from the protein repertoire. Isolated surface protein can be then analyzed via ELISA. To improve expression level, we have listed a set of developed constitutive yeast promoters as candidates. However, we also realized that promoter engineering processes may be required in the future. For the effectiveness test, we have designed a cell invasion test in vitro. Engineered yeast cells together with Shigella will be applied to Vero cell cultures. Effectiveness will be measured by proportion of cells being infected. To remove the influence of cell lines on the result of invasion test, we plan to substitute the Vero cell lines to epithelial cells in the future. After the completion of in vitro assay, further in vivo assay may be applied.","breadcrumbs":"Awards » Entrepreneurship » Our Solution","id":"160","title":"Our Solution"},"161":{"body":"We realized that what we have built is only a prototype of a Shigella infection precaution drug. There is still a long way to go for optimizing the drug in vitro as well as testing the drug in vivo. However, via a series of design processes, we have developed plans to turn it into real world application. China Probiotics Market Size, Share, Opportunities, COVID-19 Impact, And Trends By Ingredient (Bacteria, Yeast), By Form (Liquid, Dry), By Application (Functional Food And Beverages, Dietary Supplements, Animal Feed), And By End-User (Human, Animal) - Forecasts From 2020 To 2025. (2020). https://www.knowledge-sourcing.com/report/china-probiotics-market#:~:text=China%20probiotics%20market%20is%20estimated,intestinal%20tracts%2C%20and%20bowel%20function Significant Reduction in Helicobacter pylori Load in Humans with Non-viable Lactobacillus reuteri DSM17648: A Pilot Study. (2015). https://pubmed.ncbi.nlm.nih.gov/25481036/","breadcrumbs":"Awards » Entrepreneurship » Conclusion","id":"161","title":"Conclusion"},"162":{"body":"","breadcrumbs":"Awards » Inclusivity","id":"162","title":"Awards"},"163":{"body":"","breadcrumbs":"Awards » Measurement","id":"163","title":"Awards"},"164":{"body":"","breadcrumbs":"Awards » Plant","id":"164","title":"Awards"},"165":{"body":"","breadcrumbs":"Awards » Software","id":"165","title":"Awards"},"166":{"body":"","breadcrumbs":"Awards » Sustainable » Sustainable Development Goals (SDGs)","id":"166","title":"Sustainable Development Goals (SDGs)"},"167":{"body":"Scientific research has always had far-reaching significance in our study and daily routine, and even in the development of the whole society. Scientific research can comprehend us a better understanding of the nature and properties of matter. Analyzing the research objects elaboratively can accelerate the development of human knowledge accumulation. Our project follows a shared blueprint for peace and prosperity for people and the planet whose heart is the 17 sustainable development goals (UN, 2022). We respond to the urgent call for action by all countries that end poverty and other deprivations, improve health and education, reduce inequality, and spur economic growth (UN, 2022). This year, our team aims to provide a biological method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . Our method can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity while having stronger pathogen inhibition compared to traditional probiotic treatment (Langdon et al., 2016). Project “GutGuard†is mainly based on Goals 3, 9, 17","breadcrumbs":"Awards » Sustainable » Introduction","id":"167","title":"Introduction"},"168":{"body":"Ensure healthy lives and promoting well-being for all persons with disabilities We prospect our team’s project can make our local community and even the world conscious of the prominence of life and health, especially the gut problem. The gut problem may cause a person to struggle to absorb nutrients and regulate blood sugar. Additionally, weight loss or gain may be caused by bacteria overgrowth or lack of nutrients. The current therapeutics is antibiotics and the potential problem with the usage of antibiotics is that taking antibiotics too often or for the wrong reasons can change bacteria so much that antibiotics do not work against them (Cronan, 2019). Moreover, long-term use of antibiotics in late adulthood may be a risk factor for all-cause and cardiovascular mortality (Heianza, 2020). As the current therapies of antibiotics promote Shigella to develop antibiotic resistance, we are inspired by this problem and focus on shigella’s drug. Reducing antibiotic resistance and minimizing the side effects including the degradation of GI tract microbiome diversity can be achieved compared to the traditional probiotic treatment (Langdon et al., 2016). We mainly worked toward contributing to target 3.5 (Strength the prevention and treatment of substance abuse, including narcotic drug abuse and harmful use of alcohol) (UN, 2022).","breadcrumbs":"Awards » Sustainable » Goal 3| Good health and well-being","id":"168","title":"Goal 3| Good health and well-being"},"169":{"body":"Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation We are capable to lead a new approach and ideologically telling certain product developers to dare to innovate and not to stick to antibiotics to create drugs. To contribute to the goal, we aimed at target 9.5 (Enhance scientific research, upgrade the technological capabilities of industrial sectors in all countries, in particular developing countries, including, by 2030, encouraging innovation and substantially increasing the number of research and development workers per 1 million people and public and private research and development spending) (UN, 2022). We proposed a novel scientific solution to an existing global problem. We mainly focused on a novel method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . While meeting the goal, our laboratory team did various ways (using three different cells for trial: E. coli, Yeast and Lactococcus lactis ) to achieve and increase the possibility of success. Additionally, our team collaborates with other iGEM teams from developing countries to contribute to scientific advancement there.","breadcrumbs":"Awards » Sustainable » Goal 9| Industry, Innovation and Infrastructure","id":"169","title":"Goal 9| Industry, Innovation and Infrastructure"},"17":{"body":"Responsible for wet lab design and experiment for yeast group. Contribute to Human Practice with Conference of China iGEMer Community.","breadcrumbs":"Team » Attributions » Lingrui Lai","id":"17","title":"Lingrui Lai"},"170":{"body":"Strengthen the means of implementation and revitalize the global partnership for sustainable development We, as a team, share and hold the view of win-win cooperation. We know that iGEM is not just a competition, but a platform for mutual communication and cooperation. We welcome various teams coming from different backgrounds and help to create solutions to the question. Our team strictly followed target 17.16 (Enhance the global partnership for sustainable development, complemented by multi-stakeholder partnerships that mobilize and share knowledge, expertise, technology, and financial resources, to support the achievement of the sustainable development goals in all countries, in particular developing countries.) (UN, 2022). Our team played an active part in collaborating with other iGEM teams (LZU and XJLTU) to gain insights into local society and comprehend more knowledge. This kind of collaboration enriched us and ensured the sharing of knowledge and raising of awareness on both sides.","breadcrumbs":"Awards » Sustainable » Goal 17| Partnerships for the goals","id":"170","title":"Goal 17| Partnerships for the goals"},"171":{"body":"To sum up, we address and fulfill sustainable development goals 3, 9, and 17 . While meeting the goal of displaying nanobodies on the surface of the probiotics to battle antibiotic-resistant pathogens, we can also contribute to improved healthcare globally in the sustainable development aspect. It can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity. The inhibition of the pathogen will be stronger compared to traditional probiotic treatment. Our methods are easy to use and can be improved for further applications.","breadcrumbs":"Awards » Sustainable » Conclusion","id":"171","title":"Conclusion"},"172":{"body":"United Nations. (2022). The 17 goals | sustainable development. United Nations. https://sdgs.un.org/goals United Nations. (2022). #ENVISION2030: 17 goals to transform the world for persons with disabilities enable. United Nations. https://www.un.org/development/desa/disabilities/envision2030.html Langdon, A., Crook, N., & Dantas, G. (2016, April 13). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome medicine. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831151/ Cronan, K. M. (Ed.). (2019, July). The danger of antibiotic overuse (for parents) - nemours kidshealth. KidsHealth. Retrieved September 28, 2022, from https://kidshealth.org/en/parents/antibiotic-overuse.html Heianza, Y., Ma, W., Li, X., Cao, Y., Chan, A. T., Rimm, E. B., Hu, F. B., Rexrode, K. M., Manson, J. A. E., & Qi, L. (2020). Duration and life-stage of antibiotic use and risks of all-cause and cause-specific mortality. Circulation Research, 126(3), 364–373. https://doi.org/10.1161/circresaha.119.315279","breadcrumbs":"Awards » Sustainable » References","id":"172","title":"References"},"173":{"body":"Attribution 4.0 International (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/ ======================================================================= Creative Commons Corporation (\"Creative Commons\") is not a law firm and does not provide legal services or legal advice. Distribution of Creative Commons public licenses does not create a lawyer-client or other relationship. Creative Commons makes its licenses and related information available on an \"as-is\" basis. Creative Commons gives no warranties regarding its licenses, any material licensed under their terms and conditions, or any related information. Creative Commons disclaims all liability for damages resulting from their use to the fullest extent possible. 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Except for the limited purpose of indicating that material is shared under a Creative Commons public license or as otherwise permitted by the Creative Commons policies published at creativecommons.org/policies, Creative Commons does not authorize the use of the trademark \"Creative Commons\" or any other trademark or logo of Creative Commons without its prior written consent including, without limitation, in connection with any unauthorized modifications to any of its public licenses or any other arrangements, understandings, or agreements concerning use of licensed material. For the avoidance of doubt, this paragraph does not form part of the public licenses. Creative Commons may be contacted at creativecommons.org.","breadcrumbs":"LICENSE","id":"173","title":"LICENSE"},"18":{"body":"Helped conduct human practices and wetlabs for the yeast group. Designed the safety and education wiki and organized local high school activities education.","breadcrumbs":"Team » Attributions » Qizhou Jiang","id":"18","title":"Qizhou Jiang"},"19":{"body":"Helped with background research, designed lab detection protocols for the lactococcus group, conducted wetlab experiments, helped with human practice organization including journal club organization and wiki writing.","breadcrumbs":"Team » Attributions » Sihan Wang","id":"19","title":"Sihan Wang"},"2":{"body":"Sichang He (Steven) UG Class of 2024 Data Science Jasmine Santos UG Class of 2024 Biology Yuxiang He UG Class of 2025 Zhenyu Xu UG Class of 2024 Physics","breadcrumbs":"Team » Modeling","id":"2","title":"Modeling"},"20":{"body":"Organized and chaired the iGEM2022 Journal Club Seminar ever since 2021. Actively participate in human practice part including designing and popularizing events in local collegiate school. Help conduct wet labs.","breadcrumbs":"Team » Attributions » Yixuan Liu","id":"20","title":"Yixuan Liu"},"21":{"body":"Fund manager of the team, in charge of labware purchasing, helped with background research and survey distribution as a part of human practice.","breadcrumbs":"Team » Attributions » Renwei Gao","id":"21","title":"Renwei Gao"},"22":{"body":"Helped design survey as a part of human practice, helped with E. coli wet lab experiments.","breadcrumbs":"Team » Attributions » Jingyun Jin","id":"22","title":"Jingyun Jin"},"23":{"body":"","breadcrumbs":"Team » Attributions » Modeling team","id":"23","title":"Modeling team"},"24":{"body":"Organized protein structure and docking modeling. Helped conduct human practice. Shot and edited the promotion video. Wiki writing.","breadcrumbs":"Team » Attributions » Zhenyu Xu","id":"24","title":"Zhenyu Xu"},"25":{"body":"Main Wiki developer and technical support. Built the Wiki infrastructure. Set up and maintains the GitLab repository for team communication and Wiki editing. Introduced Git and GitLab to the team and helped the team adopt to the workflow on GitLab. Helped with protein modeling using RoseTTAFold, Robetta, and PyMOL.","breadcrumbs":"Team » Attributions » Sichang He (Steven)","id":"25","title":"Sichang He (Steven)"},"26":{"body":"Conceptualized cell surface display technology project during preliminary brainstorming and provided proof of concept through review of related literature. Wrote the project abstract and refined general methodology framework. Built protein models for candidate microbes via Alphafold and Haddock and evaluated fidelity of each model via quantiative metrics. Modelled growth of chosen microbe model computationally.","breadcrumbs":"Team » Attributions » Jasmine Santos","id":"26","title":"Jasmine Santos"},"27":{"body":"Built a 3D model for the drug delivery system.","breadcrumbs":"Team » Attributions » Yuxiang He","id":"27","title":"Yuxiang He"},"28":{"body":"","breadcrumbs":"Team » Attributions » Advising support","id":"28","title":"Advising support"},"29":{"body":"Overall project advising, principal investigator.","breadcrumbs":"Team » Attributions » Linfeng Huang","id":"29","title":"Linfeng Huang"},"3":{"body":"Jiani Chen UG Class of 2023 Biology Yang Yu UG Class of 2023 Biology","breadcrumbs":"Team » Advisor","id":"3","title":"Advisor"},"30":{"body":"Oversee wet lab experiments and overall project advising.","breadcrumbs":"Team » Attributions » Jiani Chen","id":"30","title":"Jiani Chen"},"31":{"body":"Oversee wet lab experiments, helped optimize lab protocols and troubleshooting.","breadcrumbs":"Team » Attributions » Yang Yu","id":"31","title":"Yang Yu"},"32":{"body":"Thanks to the generous funding support of Duke Kunshan University Natural Science Divisions, Wang-Cai Biochemistry Lab, Synear Food Molecular Biology Lab, DKU Innovation and Entrepreneurship Initiative, and Marcia B. France, DKU Dean of Undergraduate Studies. Thanks to free licenses provided by SnapGene.","breadcrumbs":"Team » Attributions » Funding support","id":"32","title":"Funding support"},"33":{"body":"Thanks to Dr. Floyd Beckford and Dr. Huansheng Cao at Duke Kunshan University, Dr. Neel Joshi from Northwestern University, and Dr. Jisheng Lin at Sinovac Biotech CO.,LTD. for providing effective advice on our project design and development.","breadcrumbs":"Team » Attributions » Communications support","id":"33","title":"Communications support"},"34":{"body":"Collaborations Duke-DKU iGEM History Duke Kunshan University (DKU) is our sister school in Kunshan, China. Like Duke, DKU set out to provide a transformative and innovative education to students around the world. In addition, students are given the opportunity to study abroad in both semesters, further cementing our status as sister schools. Since taking its inaugural class of undergraduate students in 2018, DKU only had its very first iGEM team. Duke, on the other hand, has competed in the competition ever since 2006. Thus, when we learned about their interest in iGEM, we were beyond happy and excited to build a strong partnership between our teams. Our Partnership Since DKU iGEM only started in 2021, we continued to look to Duke iGEM for support and guidance. This year, we are still able to meet on the Duke campus and give each other suggestions. We shared the trouble shooting processes of our wet labs and reached mutual agreement to construct a PCR trouble shooting guide for future iGEM teams to use. dku-duke-group0","breadcrumbs":"Team » Collaborations » Collaboration with Duke iGEM","id":"34","title":"Collaboration with Duke iGEM"},"35":{"body":"CCiC certificate In order to carry out science communications on a larger scale, we participated the 9th CCiC Conference (Conference of China iGEMer Community), which is a national summit independently initiated by Chinese iGEM teams, aiming to provide a platform for iGEM teams to share resources and promote mutual learning and communication. We made poster and presented at the conference, answering questions from the audience and judges. After the conference, we collaborated with team LZU on science popularization about probiotics. CCiC photo","breadcrumbs":"Team » Collaborations » CCiC Meetup","id":"35","title":"CCiC Meetup"},"36":{"body":"Communications We had science communications during different stages of our project. Firstly, we designed a socially-oriented questionnaire to find out how much the public knows about shigella. Then,throughout expert interviews, we managed to gain insights of our project feasibility and possible future directions. Finally, we participated in on-campus communication to let more people know about shigella and surface display technology.","breadcrumbs":"Project » Overview","id":"36","title":"Overview"},"37":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Socially-Oriented Questionnaire","id":"37","title":"Socially-Oriented Questionnaire"},"38":{"body":"We interviewed Huansheng Cao, Assistant professor of Environmental Science at Duke Kunshan University for suggestions on our initial lab plans. In the interview, team members Yuxin Wang and Chang Shen presented the main design, bacterial surface display, to consult Prof Cao on its feasibility. After confirming the rich research foundations of our plan, he encouraged us to add computational elements to our lab design. As a scientist working in computational biology and bioinformatics, he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody and the antigen unit. As a well-trained biologist, he also suggested fitting our design to more than one model organisms, which shows integration in our drug design. The interview was full of enthusiasm, so we were able to come across many other topics. We discussed the trends in bioinformatics and biotechnology, including bacteria-based bioelectricity, and the relationship between human longevity and gut microbiota. This interview was both encouraging and informative, and contributed greatly to the first stage of human practice.","breadcrumbs":"Project » Interview with Prof. Cao","id":"38","title":"Interview with Prof. Cao"},"39":{"body":"After we successfully predicted the 3d structure of fusion protein-antibody complex by using Robetta and Alphafold2, the focus shift to how the fusion protein will influence the binding (docking) between antibody and antigen. We plan to get some insights about this from computer modeling before the wet lab begins. We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University for suggestions on our protein docking simulation. At the beginning, team leader Lisa Wu introduced the synthetic biology part of our project. Modeling team leader Zhenyu Xu introduced the progress of protein structure prediction and the need for protein docking simulation. As a scientist working in modern medicine, Prof. Floyd pointed us to some useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These software are powerful at predicting the docking scenario and are used by many researchers, with many online teaching resources accessible. To improve the speed of computer modeling, Prof. Floyd emphasized the preprocessing of protein structures. Namely, the antigen structure. He suggested us delete the floating molecules outside the binding sites and keep those inside, since we only care about the binding scenario. He also pointed that virtual screening could help if we want to do more mutations to the binding sites. Concerning the fusion protein-antibody complex models, since they are the optimal prediction given by Robetta and Alphafold2, we assume these models do not need preprocessing anymore. For docking, he suggested us try rigid docking first, and then flexible docking if we want to get closer to reality.","breadcrumbs":"Project » Interview with Prof. Beckford","id":"39","title":"Interview with Prof. Beckford"},"4":{"body":"Lingfeng Huang, Ph.D. Associate Professor of Biology, Duke Kunshan University","breadcrumbs":"Team » Principal Investigator","id":"4","title":"Principal Investigator"},"40":{"body":"Introduction Dr. Neel Joshi is an expert in bioengineering with tracks in human disease and new therapies. In his 2019 and 2021 literature, he and his team described genetically engineering E. coli Nissle 1917 to treat some gastrointestinal diseases like bowel inflammation, which provide essential references for our project. To further understand the logics and advantages of this bioengineered model, we invited Dr. Joshi for an interview. Dr. Joshi interview photo 1 Interview Content Q: What stimulated you and your team to develop the surface-displaced single domain antibodies? What practical problems do you think this model can solve? A: Although the nanobodies have great potentials in treating gastrointestinal diseases, it is somewhat hard to deliver those nanobodies directly to the digestive track. Therefore, the probiotics can serve as a scaffold to make the delivery of nanobodies easy. Q: But why did you choose to display the nanobodies on the surface? Why not directly make the bacteria synthesize nanobodies and release them? A: The surface display resolution has the property of multi-valency. By displaying the nanobodies on the surface, we would have the potential to space the binding domains together to bind to a pathogen surface. It could increase binding affinity and decrease the dissociation constant. It can also diffusion into different directions and increase the local concentration. Q: What about the method of drug delivery? That is to say, how do you decide to send the engineered probiotics to human gastrointestinal track? And could you explain why you use that delivery method? A: We only proposed an approach of micro biological therapy. But to deliver the bacteria, I think it can be freeze-dried to produce a freeze-dried product. Because a large portion of the geographical locations that suffered from these gut problems are the poor areas, and those areas do not have the condition to store the bacteria that require a very low temperature. The freeze-dried products do not require that strict storage conditions, so they are more available in those areas. Q: Why pBbB8k plasmid backbone with kanamycin selection marker? (what's the difference between pUC19, which is our choice, and pBbB8K?) A: pBbB8k is a rather arbitrary choice, we simply chose it because it was used due to antibiotics incompatibility in the previous experiment. When doing in vivo studies, we engineered plasmids from the original E. coli Nissle genome, the pMUT plasmids. These plasmids are more stable than the pBbB8K. For pUC19, I don’t see problems with the expression of pUC19 plasmid. However, you do need to consider if your antibiotic resistant marker in the plasmid is compatible with the shigella testing. If shigella is killed due to the antibiotic selecting E. coli, it can be a problem. Q: What are the setbacks of the Probiotic-associated therapeutic curli hybrids (PATCH) system? A: The first is safety concerns of curli fibers. It has been known that curli fibers induce various types of diseases, including neurological diseases, etc. The other is inherit disadvantages for E. coli to produce curli fibers in vivo. However, we have been able to shown effective production of curli fiber in vivo by measuring the amount of curli fibers coming from the fecal samples. Q: What if the E. coli went out of control and grow infinitely in the gut, disrupting the original gastrointestinal microorganism environment? A: This is a very popular question when it comes to distributing microbes to gut. Actually, we could use some of the auxotrophic strains to limit the growth of the bacteria. And I think there are many “switches†that can turn on the suicide program of those bacteria. But in this case, I think E. coli Nissle 1917 is a very safe bacteria, it has already been identified as a harmless bacterium, so there should be less safety issues of this strain. Q&A Section Q: Is it possible to apply magnetic triggers to shigella infection and cooperate this into the PATCH system? A: Magnetic triggers are mostly applied in cancer treatment. This is because in cancer, you know the spot of the disease. In bacterial infection it’s hard to locate. Q: In Barta et al., the authors described the different indexes of the nanobodies, including binding domains and neutralization effects. What is your rationale when choosing the nanobodies? A: It really depends on how you generate the nanobodies. When different parts of the pathogen are used in Alpaca immunizations, the nanobodies will vary. When displaying the nanobodies, some work and others don’t. We assume this is because of folding problems, but we did not figure out the exact reason. Q: What do you think about sequence optimization in silica? Do you have experience working with this? Do you have any suggestions? A: I would suggest generating different mutations in the sequence and do some docking analysis. Then generate the mutations and do wet labs. Q: Our project aims to tackle the antibiotic resistance problem worldwide. Would the PATCH system generate drug resistance issues? A: This is possible. For example, a mutation in the binding domain of the antigen might cause binding problems. However, I would say the selective pressure by the nanobody is smaller compared to that of the antibiotic. This is because antibiotic kills the pathogen, while PATCH only binds to the pathogen, keeping it from invasive activities. Q: We are worried that the proteins in the GI tract environment would coat the surface of the probiotic, which would cause dysfunction of the nanobodies. How did your team encounter this problem? A: The animal model was effective, which was sufficient to show that the GI tract environment did not inhibit the binding activity. The curli production is continuous in vivo, which provides adequate chance for the binding to occur. However, the proteases in the GI tract is something to consider. Summary and Reflection Dr. Joshi provided lots of perspectives from a brand-new aspect, which were extra inspirable for the whole team. First, Dr. Joshi elaborated on the practical problems that this model could potentially resolve. That the probiotic expression system could make the delivery of nanobodies easier expanded our understanding of the model as the delivery problem does not only exist in the step of bacteria delivery, it starts from the delivery of the essential nanobodies. Next, the freeze-dry delivery approach gives a less stricter storage condition of this drug, making it more available in poor areas, which corresponds with our assumed delivery method. As for the safety problem that the public is most interested in, Dr. Joshi proposed to use some molecular switches to eliminate those bacteria in addition to using safe strains like Nissle, giving important clue and indication for our project design. In the Q&A section, questions regarding drug localization, drug resistance, choice of nanobodies were mentioned by team members. Dr. Joshi gave many valuable advices depending on the questions. Overall, the interview was successful, and we were able to arm ourselves with adequate knowledge for the wet lab.","breadcrumbs":"Project » Interview with Dr. Neel Joshi","id":"40","title":"Interview with Dr. Neel Joshi"},"41":{"body":"See Entrepreneurship.","breadcrumbs":"Project » Interview with SINOVAC","id":"41","title":"Interview with SINOVAC"},"42":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus.","breadcrumbs":"Project » On-Campus Communication","id":"42","title":"On-Campus Communication"},"43":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the expert interviews enabled us to reflect on the feasibility and future directions of our lab design. These science communication helped us be more clear about the direction of the experiment and the significance of this project.","breadcrumbs":"Project » Summary","id":"43","title":"Summary"},"44":{"body":"Communications We had science communications during different stages of our project. Firstly, we designed a socially-oriented questionnaire to find out how much the public knows about shigella. Then,throughout expert interviews, we managed to gain insights of our project feasibility and possible future directions. Finally, we participated in on-campus communication to let more people know about shigella and surface display technology.","breadcrumbs":"Project » Communication » Overview","id":"44","title":"Overview"},"45":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Communication » Socially-Oriented Questionnaire","id":"45","title":"Socially-Oriented Questionnaire"},"46":{"body":"We interviewed Huansheng Cao, Assistant professor of Environmental Science at Duke Kunshan University for suggestions on our initial lab plans. In the interview, team members Yuxin Wang and Chang Shen presented the main design, bacterial surface display, to consult Prof Cao on its feasibility. After confirming the rich research foundations of our plan, he encouraged us to add computational elements to our lab design. As a scientist working in computational biology and bioinformatics, he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody and the antigen unit. As a well-trained biologist, he also suggested fitting our design to more than one model organisms, which shows integration in our drug design. The interview was full of enthusiasm, so we were able to come across many other topics. We discussed the trends in bioinformatics and biotechnology, including bacteria-based bioelectricity, and the relationship between human longevity and gut microbiota. This interview was both encouraging and informative, and contributed greatly to the first stage of human practice.","breadcrumbs":"Project » Communication » Interview with Prof. Cao","id":"46","title":"Interview with Prof. Cao"},"47":{"body":"After we successfully predicted the 3d structure of fusion protein-antibody complex by using Robetta and Alphafold2, the focus shift to how the fusion protein will influence the binding (docking) between antibody and antigen. We plan to get some insights about this from computer modeling before the wet lab begins. We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University for suggestions on our protein docking simulation. At the beginning, team leader Lisa Wu introduced the synthetic biology part of our project. Modeling team leader Zhenyu Xu introduced the progress of protein structure prediction and the need for protein docking simulation. As a scientist working in modern medicine, Prof. Floyd pointed us to some useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These software are powerful at predicting the docking scenario and are used by many researchers, with many online teaching resources accessible. To improve the speed of computer modeling, Prof. Floyd emphasized the preprocessing of protein structures. Namely, the antigen structure. He suggested us delete the floating molecules outside the binding sites and keep those inside, since we only care about the binding scenario. He also pointed that virtual screening could help if we want to do more mutations to the binding sites. Concerning the fusion protein-antibody complex models, since they are the optimal prediction given by Robetta and Alphafold2, we assume these models do not need preprocessing anymore. For docking, he suggested us try rigid docking first, and then flexible docking if we want to get closer to reality.","breadcrumbs":"Project » Communication » Interview with Prof. Beckford","id":"47","title":"Interview with Prof. Beckford"},"48":{"body":"Introduction Dr. Neel Joshi is an expert in bioengineering with tracks in human disease and new therapies. In his 2019 and 2021 literature, he and his team described genetically engineering E. coli Nissle 1917 to treat some gastrointestinal diseases like bowel inflammation, which provide essential references for our project. To further understand the logics and advantages of this bioengineered model, we invited Dr. Joshi for an interview. Dr. Joshi interview photo 1 Interview Content Q: What stimulated you and your team to develop the surface-displaced single domain antibodies? What practical problems do you think this model can solve? A: Although the nanobodies have great potentials in treating gastrointestinal diseases, it is somewhat hard to deliver those nanobodies directly to the digestive track. Therefore, the probiotics can serve as a scaffold to make the delivery of nanobodies easy. Q: But why did you choose to display the nanobodies on the surface? Why not directly make the bacteria synthesize nanobodies and release them? A: The surface display resolution has the property of multi-valency. By displaying the nanobodies on the surface, we would have the potential to space the binding domains together to bind to a pathogen surface. It could increase binding affinity and decrease the dissociation constant. It can also diffusion into different directions and increase the local concentration. Q: What about the method of drug delivery? That is to say, how do you decide to send the engineered probiotics to human gastrointestinal track? And could you explain why you use that delivery method? A: We only proposed an approach of micro biological therapy. But to deliver the bacteria, I think it can be freeze-dried to produce a freeze-dried product. Because a large portion of the geographical locations that suffered from these gut problems are the poor areas, and those areas do not have the condition to store the bacteria that require a very low temperature. The freeze-dried products do not require that strict storage conditions, so they are more available in those areas. Q: Why pBbB8k plasmid backbone with kanamycin selection marker? (what's the difference between pUC19, which is our choice, and pBbB8K?) A: pBbB8k is a rather arbitrary choice, we simply chose it because it was used due to antibiotics incompatibility in the previous experiment. When doing in vivo studies, we engineered plasmids from the original E. coli Nissle genome, the pMUT plasmids. These plasmids are more stable than the pBbB8K. For pUC19, I don’t see problems with the expression of pUC19 plasmid. However, you do need to consider if your antibiotic resistant marker in the plasmid is compatible with the shigella testing. If shigella is killed due to the antibiotic selecting E. coli, it can be a problem. Q: What are the setbacks of the Probiotic-associated therapeutic curli hybrids (PATCH) system? A: The first is safety concerns of curli fibers. It has been known that curli fibers induce various types of diseases, including neurological diseases, etc. The other is inherit disadvantages for E. coli to produce curli fibers in vivo. However, we have been able to shown effective production of curli fiber in vivo by measuring the amount of curli fibers coming from the fecal samples. Q: What if the E. coli went out of control and grow infinitely in the gut, disrupting the original gastrointestinal microorganism environment? A: This is a very popular question when it comes to distributing microbes to gut. Actually, we could use some of the auxotrophic strains to limit the growth of the bacteria. And I think there are many “switches†that can turn on the suicide program of those bacteria. But in this case, I think E. coli Nissle 1917 is a very safe bacteria, it has already been identified as a harmless bacterium, so there should be less safety issues of this strain. Q&A Section Q: Is it possible to apply magnetic triggers to shigella infection and cooperate this into the PATCH system? A: Magnetic triggers are mostly applied in cancer treatment. This is because in cancer, you know the spot of the disease. In bacterial infection it’s hard to locate. Q: In Barta et al., the authors described the different indexes of the nanobodies, including binding domains and neutralization effects. What is your rationale when choosing the nanobodies? A: It really depends on how you generate the nanobodies. When different parts of the pathogen are used in Alpaca immunizations, the nanobodies will vary. When displaying the nanobodies, some work and others don’t. We assume this is because of folding problems, but we did not figure out the exact reason. Q: What do you think about sequence optimization in silica? Do you have experience working with this? Do you have any suggestions? A: I would suggest generating different mutations in the sequence and do some docking analysis. Then generate the mutations and do wet labs. Q: Our project aims to tackle the antibiotic resistance problem worldwide. Would the PATCH system generate drug resistance issues? A: This is possible. For example, a mutation in the binding domain of the antigen might cause binding problems. However, I would say the selective pressure by the nanobody is smaller compared to that of the antibiotic. This is because antibiotic kills the pathogen, while PATCH only binds to the pathogen, keeping it from invasive activities. Q: We are worried that the proteins in the GI tract environment would coat the surface of the probiotic, which would cause dysfunction of the nanobodies. How did your team encounter this problem? A: The animal model was effective, which was sufficient to show that the GI tract environment did not inhibit the binding activity. The curli production is continuous in vivo, which provides adequate chance for the binding to occur. However, the proteases in the GI tract is something to consider. Summary and Reflection Dr. Joshi provided lots of perspectives from a brand-new aspect, which were extra inspirable for the whole team. First, Dr. Joshi elaborated on the practical problems that this model could potentially resolve. That the probiotic expression system could make the delivery of nanobodies easier expanded our understanding of the model as the delivery problem does not only exist in the step of bacteria delivery, it starts from the delivery of the essential nanobodies. Next, the freeze-dry delivery approach gives a less stricter storage condition of this drug, making it more available in poor areas, which corresponds with our assumed delivery method. As for the safety problem that the public is most interested in, Dr. Joshi proposed to use some molecular switches to eliminate those bacteria in addition to using safe strains like Nissle, giving important clue and indication for our project design. In the Q&A section, questions regarding drug localization, drug resistance, choice of nanobodies were mentioned by team members. Dr. Joshi gave many valuable advices depending on the questions. Overall, the interview was successful, and we were able to arm ourselves with adequate knowledge for the wet lab.","breadcrumbs":"Project » Communication » Interview with Dr. Neel Joshi","id":"48","title":"Interview with Dr. Neel Joshi"},"49":{"body":"See Entrepreneurship.","breadcrumbs":"Project » Communication » Interview with SINOVAC","id":"49","title":"Interview with SINOVAC"},"5":{"body":"","breadcrumbs":"Team » The whole team","id":"5","title":"The whole team"},"50":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus.","breadcrumbs":"Project » Communication » On-Campus Communication","id":"50","title":"On-Campus Communication"},"51":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the expert interviews enabled us to reflect on the feasibility and future directions of our lab design. These science communication helped us be more clear about the direction of the experiment and the significance of this project.","breadcrumbs":"Project » Communication » Summary","id":"51","title":"Summary"},"52":{"body":"Contribution We designed cell surface display platforms for probiotics including yeast, E. coli Nissle 1917, and L. lactis . To be specific, the yeast Aga2 surface display platform for nanobodies were developed, We also designed a novel way to detect protein surface expression by using flow cytometry. Another contribution is protein modeling protocol. We designed an integrated protocol involving the usage of PyMol, RobeTTA, and Alphafold2. Through literature review, we were able to determine multiple parameters that measure the accuracy of the protein model, and conducted evaluation on our protein design. We also contributed to previous parts by designing our parts with imporvement based on past iGEM teams. Cell surface display platforms can be utilized to cater to many protein engineering and therapeutic drug design purposes. In our case, the therapeutic effect and the nanobody localization on the cellular membrane of yeast yields future possibilities for iGEM teams to utilize this surface display platform based on the yeast Aga2 protein, specifically for therapeutic designs, but possible to be utilized to express other proteins as well.","breadcrumbs":"Project » Contribution » Cell surface display platforms","id":"52","title":"Cell surface display platforms"},"53":{"body":"Online programs are helpful for visualizing and analyzing the structure of different proteins and their docking scenarios. We use Robetta and Alphafold2 to model the structures of our protein, and used HADDOCK to visualize the docking structure. Evaluation focuses on different parameters: Ramachandran plot, Overall G-factors, Atomic Z-score RMS, Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, Overall quality factor, and Z-score. These parameters determine whether a certain structure is stable. More details please see our Modeling Page","breadcrumbs":"Project » Contribution » Integrated protein modeling protocol","id":"53","title":"Integrated protein modeling protocol"},"54":{"body":"See Improvement","breadcrumbs":"Project » Contribution » Improvement of parts","id":"54","title":"Improvement of parts"},"55":{"body":"Project Description The Shigella species is listed as one of the eight dangerous drug resistant bacteria [1] , with associated mortalities projected to rise to 10 million globally by 2050, if not properly addressed [2] . In the United States alone, over 77,000 antibiotic resistant cases were reported annually and 90% of overall Shigella cases were found to be resistant to the first choice medication ciprofloxacin [3] . Shigella, as a highly infective, enteroinvasive and occasionally toxin-releasing [4] [5] bacterial genus, may cause severe infection and bacterial dysentery in the colorectal mucosa even with as low a dose as 10 - 100 organisms [6] . Shigella-related infections thereby spread rapidly, particularly in low-resource populations [7] and among vulnerable groups including children in care facilities, the homeless, and returned travelers [8] [9] [10] [5] . The use of conventional antibiotics aggravates the multidrug resistance of most Shigella strains. Besides aiding in the selection of resistant pathogens, antibiotics reduce intestinal species diversity and population, and disrupt the defensive, metabolic, and trophic functions of interdependent microbes [11] . Although antibiotics are able to prevent and treat infections, antibiotic exposure to the intestinal microbiota can lead to loss of colonization resistance, rendering the host more susceptible to future invasion [12] [13] . Engineered probiotics with cell surface display systems are an especially promising alternative that improve Shigella eradication rates without heavy reliance on antibiotics. Single VH domain (VHH) antibodies displayed on the probiotic surface reduce virulent activity of Shigella [14] through probiotic-pathogen binding while minimizing toxicity to non-targets [15] [16] . Specifically, these antibodies recognize and target epitopes within the tip complex that is conserved across all pathogens that utilize type III secretion system (T3SS) to translocate effector proteins into the host cells [15] . Innovations in VHH-ipaD binding not only offer a solution that preserves the potency of antibiotics and microbial composition of the gut microbiome, but also illuminates targeted approaches to treat related T3SS bacteria like Salmonella and enterohemorrhagic E. coli, and other novel opportunities for passive immunization [17] . Engineered probiotics with cell surface display systems are an especially promising alternative that improve Shigella eradication rates without heavy reliance on antibiotics. Single VH domain (VHH) antibodies displayed on the probiotic surface reduce virulent activity of Shigella [14] through probiotic-pathogen binding while minimizing toxicity to non-targets [15] [16] . Specifically, these antibodies recognize and target epitopes within the tip complex that is conserved across all pathogens that utilize type III secretion system (T3SS) to translocate effector proteins into the host cells [15] . Innovations in VHH-ipaD binding not only offer a solution that preserves the potency of antibiotics and microbial composition of the gut microbiome, but also illuminates targeted approaches to treat related T3SS bacteria like Salmonella and enterohemorrhagic E. coli, and other novel opportunities for passive immunization [17] .","breadcrumbs":"Project » Description » Background","id":"55","title":"Background"},"56":{"body":"","breadcrumbs":"Project » Description » Design","id":"56","title":"Design"},"57":{"body":"Y_Design Idea of probiotics Saccharomyces cerevisiae, or baker’s yeast, is widely used in food industry and scientific research. Its facultative anaerobic feature enables it to make fluffy bread [18] . Also, its variable metabolism pathways make it a good agent for alcohol fermentation and wine production [19] . Last but not least, the already-annotated genome makes it an excellent model organism for molecular biology research [20] . With all these features, yeasts have been considered to be safe by Food and Drug Administration for a long time. Apart from our treatment strategy, this probiotic has been engineered as new conceptual drugs for other diseases treatment, such as vaginal infections, diarrhea, and irritable bowel syndrome (IBS) [21] [22] . Compared to other prokaryotic probiotics, the eukaryotic yeast could support more complex protein folding, which is favorable for the generation of antibodies of interest. Moreover, previous works have successfully developed a mature Aga proteins yeast surface display system, which have been put in practical use in vaccine selection and sorting [23] [24] . This established surface display system largely reduces the engineering difficulty and increases the reliability of our engineering. Take all the considerations above, we put yeasts into our plan list. Design of pYD1-20ipaD plasmid for therapeutic yeast engineering One of the most important proteins in type III secretion system (T3SS) of pathogenic Shigella called ipaD is our attack target [25] . Because ipaD is the primary trigger to form translocon pores within the host cell membrane, the inhibition of it would probably inhibit the invasion of Shigella and thus treat the infection [26] [27] . Several single domain antibodies (nanobodies) have been previously reported to target ipaD, the most efficient of which is 20ipaD. Therefore, 20ipaD was chosen for further engineering. To have the yeasts displayed 20ipaD on surface, we adopted the strategy of Aga2 yeast surface display system. Aga2 is a membrane protein of S. cerevisiae, which would be sealed on membrane by the interaction with Aga16. By fusing the Aga2 protein with 20ipaD, the nanobody could thus be brought to the membrane, and that was what we designed as shown in the figure. Additionally, we introduced 3xFLAG tag behind 20ipaD for expression assays like immunofluorescent microscopic imaging, western blot, and FACS. The whole expression module was designed under the control of GAL1 promotor that can be induced by galactose to control the expression of the proteins of interest. We used pYD1 vector as the backbone which contains ampicillin resistance marker, E. coli replication origin, and tryptophan deficiency marker. These features enable us to store the recombinant plasmids in E. coli, and easily select the yeasts after transformation. Design of pYD1-ipaD plasmid for efficiency detection Shigella is one of the most infectious pathogens characterized by CDC [8] . Considering the health risks that could be risen during the experiments, we replace the real Shigella by yeasts anchored with the targeted epitope protein ipaD. The construction strategy of pYD1-ipaD was same as the pYD1-20ipaD discussed above except for the replacement of FLAG tag with HA tag. The yeasts containing pYD1-ipaD could display the antigen ipaD on their surfaces to mimic Shigella. With this pathogen analog, the binding affinity of the engineered therapeutic yeasts between the fake pathogens could be measured by whole cell ELISA and other binding affinity assays. Design of high production and high binding affinity plasmids for efficiency optimization After the proving the construction and binding capacity of the engineered yeast, optimization would be done to increase the efficiency of the product. Expression efficiency and binding affinity would be the two main aspects of optimization. To increase the expression efficiency of the nanobody, previously reported strong promoters, including SSA1 and PGK1, would be introduced to replace GAL1 promoter [28] . The expression abundancy would be compared, and the optimized promoter would be chosen. To increase the binding affinity of the nanobody, random mutations would be introduced to the 20ipaD sequence by error-prone PCR. The library would be screened for the optimization of nanobody targeting. Design of delivery of the engineered therapeutic yeasts by Shellac-based microcapsules Microbes, especially yeasts, are hard to preserve for a long time under room temperature. Besides, the acidic and digestive environment inside the gut prevents most organisms from getting to the intestine where Shigella locates in. In order to preserve the engineered yeasts and deliver them into the intestine with smallest deficiency, we designed the shellac-cased microcapsules. Shellac is a natural material that can be used as encapsulating material for microcapsules that can wrap and package molecular matters like drugs and cells [29] . The properties of shellac include high intensity, which can protect the encapsuled matters; hydrophobicity, making it easier for storage; only disintegrate at basic solution, which means that the microcapsules would not disintegrate in the acidic environment of stomach, but only dissolve in basic environment of small intestine where the target pathogen resides [30] . Previous research has proven the efficiency of shellac microcapsules delivery of probiotics [31] [32] [33] . With the light of this, we also designed the capsulation for the engineered yeasts. By producing the microcapsule powder of yeasts, they can be subsequently packaged into macro capsule entities and be productized.","breadcrumbs":"Project » Description » Yeast","id":"57","title":"Yeast"},"58":{"body":"L_Design Idea of probiotics The target probiotics, Lactococcus lactis (L. lactis) , is a lactic acid-producing Gram-positive species of bacteria that is used extensively in the food fermentation industry like the production of cheese and yoghurt. Therefore, it is generally considered as safe (GRAS) status by the Food and Drug Administration [34] . Apart from its important function in making food, L. lactis is often applied as the genetically modified organism for disease treatment of animals and humans [35] [36] . In many parts, it acts as an alternative for the gram positive to Bacillus subtilis and Lactobacillus plantarum, while it can also substitute the gram-negative counterpart, Escherichia coli[GarcÃa2012]. The small genome size (2.3 Mbp) that has been fully sequenced, plus the development of successfully compatible tools including cloning and expression systems with customizable options, have turned _L. lactis_into a desirable model for genetic engineering [34] . Design of 20ipad plasmid Due to the wide use of antibiotics, various types of bacteria have developed antibiotic resistance, thus providing great challenge to human health and therapy design. Our team’s target pathogen, the Shigella spp., is no exception. To overcome the issue of antibiotic resistance, we would like to engineer the probiotics to make it an effective tool for the treatment of shigella infections. Through literature review, it is identified that in the process of shigellosis (also named bacillary dysentery), Shigella uses the type III secretion system (T3SS) to invade colonic epithelial cells. Importantly, one important feature of T3SS is the existence of an extracellular needle with an associated tip complex responsible for assembly of a pore-forming translocon in the host cell membrane [15] . For Shigella flexneri, the tip complex contains invasion plasmid antigen D (IpaD) that not only regulates secretion but also provides the physical platform for the translocon pore [15] [37] . To explore the potential therapeutic avenues for managing infections of Shigella, researchers have developed single-VH domain antibodies (VHHs) that are capable of recognizing distinct epitopes within the antigen IpaD [15] , where one of such VHHs is the 20ipaD applied by our team. In order to have our probiotics L. lactis express the 20ipaD, we firstly constructed the 20ipaD plasmid. For plasmid design, the Usp45 signal peptide was included for secretion to the growth medium, while AcmA3b was included for surface anchoring of the expressed 20ipaD to L. lactis [38] . Flag-tag was added for the convenience of purification. Sequence of 20ipaD was surrounded by two restriction sites (BamHI and SacI respectively). The aim for such a design is that ideally, through the digestion of restriction enzymes, 20ipaD sequence could be obtained. Design of control group (3*Flag tag) with Flag-tag sequence In our future stage, we would fuse the Lactococcus lactis expression vector pNZ8148 with control flag-tag 3 to benefit the examination procedures, here the plasmid containing control group (3 Flag tag) with Flag-tag sequence was designed so that we could get the sequence of control flag-tag 3 from the plasmid. Construction of the plasmid was similar to that of 20ipaD, with Usp45 signal peptide (indicated in yellow) and AcmA3b (indicated in green) included. The sequence of control flag-tag 3 is shown in blue. Two restriction sites for the enzyme NcoI (indicated in dark green) and HindIII (indicated in dark blue) were designed so that during enzymatic digestion, sequence of control flag-tag*3 would be obtained.","breadcrumbs":"Project » Description » Lactococcus","id":"58","title":"Lactococcus"},"59":{"body":"E_design E. coli Nissle 1917, as a probiotic first isolated from the GI tract of healthy soldiers in WWI, has been proven to impose positive impacts on the human GI tract by supression and inhibition of GI tract pathogens. The current trend in developing Nissle for therapeutics is based on the fact that E. coli is one of the most developed model organisms for scientific research. It has a small genome, stability of expression, and is easy to culture. The detailed design of the E. coli surface display system is as follows. Through literature review, We have targeted two different display systems. One is based on E. coli curli operon. The curli fiber is a component of biofilm. The PATCH system developed form previous studies have been effective in displaying protiens of interest. Furthermore, the large capacity of the curli fiber presents multivalency, making it possible to display multiple proteins at arbitrarily close distance to bind simultaneously for the drug effective to take place. The plasmid design referenced the pM1s3ATScsg-Etag plasmid on Addgene (Plasmid #137946) from Neel Joshi Lab with the optimized synthetic curli operon. The other option is based on intimin. Intimin in E. coli has a trans-outer membrane region and a C-terminal repeat of Ig-like and lectin domains that can be used as a potential fusion site for protein display [39] . In some earlier studies, the researchers successfully inserted a fragment of EHEC intimin into a known plasmid vector with a VHH fusing to it and had it successfully express and display the VHH on the bacteria surface [40] . To fully exploit the multivalency advantage of the baterial surface display system, we plan to display more than on kind of nanobodies, so the probiotic can bind to a larger range of pathogens, or it can bind different antigens of the pathogen. It is also important to mention that the target antigen IpaD is highly conservative and exists in all strains of shigella. Also, previous studies have constructed a library of anti-IpaD VHH including VHH 20ipaD, JMKH2, and JPSG3 are found specifically bind to the epitopes in IpaD protein [15] [41] . The affinity of this antigen-VHH pair is considerable when using 20ipaD and JMKH2 [41] .","breadcrumbs":"Project » Description » E. coli","id":"59","title":"E. coli"},"6":{"body":"Team Yixuan Wu (Lisa) UG Class of 2024 Biology Yixuan Liu UG Class of 2024 Biology Sihan Wang UG Class of 2023 Biology Zhujun Yao UG Class of 2024 Biology Lingrui Lai UG Class of 2023 Biology Yuxin Wang UG Class of 2025 Jingyun Jin UG Class of 2024 Biology Chang Shen UG Class of 2025 Yunyi Ru UG Class of 2023 Biology Renwei Gao UG Class of 2023 Biology Qizhou Jiang UG Class of 2025","breadcrumbs":"Team » Team » Biology","id":"6","title":"Biology"},"60":{"body":"[4] Carayol, N. and Guy Nhieu. (2013). The Inside Story of Shigella Invasion of Intestinal Epithelial Cells. Cold Spring Harbor Perspectives in Medicine. Retrieved March 28, 2022, from http://perspectivesinmedicine.cshlp.org/content/3/10/a016717.full [6] Zaidi, M. B., & Estrada-GarcÃa, T. (2014, June 1). shigella: A highly virulent and elusive pathogen. Current tropical medicine reports. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4126259/ [2] O' Neill, J. (2014, December). Antimicrobial resistance: Tackling a crisis for the health and wealth of nations . Retrieved March 28, 2022, from https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf [1] Langdon, A., Crook, N., & Dantas, G. (2016). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome Medicine, 8(1). https://doi.org/10.1186/s13073-016-0294-z [3] Centers for Disease Control and Prevention. (2015, April 2). Multidrug-resistant shigellosis spreading in the United States. [8] Centers for Disease Control and Prevention. (2020, October 8). Antibiotic resistance and Shigella infections. Centers for Disease Control and Prevention. Retrieved March 28, 2022, from https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html [7] Hussen, S., Mulatu, G., & Yohannes Kassa, Z. (2019). Prevalence of shigella species and its drug resistance pattern in Ethiopia: A systematic review and meta-analysis. Annals of Clinical Microbiology and Antimicrobials, 18(1). https://doi.org/10.1186/s12941-019-0321-1 [5] Gray, M. D., Lacher, D. W., Leonard, S. R., Abbott, J., Zhao, S., Lampel, K. A., Prothery, E., Gouali, M., Weill, F.-X., & Maurelli, A. T. (2015, May 14). Prevalence of shiga toxin-producing Shigella species isolated from French travellers returning from the Caribbean: An emerging pathogen with international implications. Clinical Microbiology and Infection. Retrieved March 28, 2022, from https://www.sciencedirect.com/science/article/pii/S1198743X15004437 [42] Huruy, K., Kassu, A., Mulu, A., Gebretsadik, S., Andargie, G., Tadesse, T., Birhan, W., Worku, N., Ghebreselassie, D., Belyhun, Y., Yifru, S., Adugna, S., & Tiruneh, M. (2008). High Level of Antimicrobial Resistance in Shigella Species Isolated From Diarrhoeal Patients in University of Gondar Teaching Hospital, Gondar, Ethiopia . Retrieved March 28, 2022, from https://pharmacologyonline.silae.it/files/archives/2008/vol2/29_Huruy.pdf [10] Casabonne, C., González, A., Aquili, V., & Balagué, C. (2016, November 22). Prevalence and virulence genes of Shigella spp.. isolated from patients with diarrhea in Rosario, Argentina. Japanese Journal of Infectious Diseases. Retrieved March 28, 2022, from https://www.jstage.jst.go.jp/article/yoken/69/6/69_JJID.2015.459/_article/-char/ja/ . [4] Carayol, N. and Guy Nhieu. (2013). The Inside Story of Shigella Invasion of Intestinal Epithelial Cells. Cold Spring Harbor Perspectives in Medicine. Retrieved March 28, 2022, from http://perspectivesinmedicine.cshlp.org/content/3/10/a016717.full [2] O' Neill, J. (2014, December). Antimicrobial resistance: Tackling a crisis for the health and wealth of nations . Retrieved March 28, 2022, from https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf [3] Centers for Disease Control and Prevention. (2015, April 2). Multidrug-resistant shigellosis spreading in the United States. [8] Centers for Disease Control and Prevention. (2020, October 8). Antibiotic resistance and Shigella infections. Centers for Disease Control and Prevention. Retrieved March 28, 2022, from https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html [7] Hussen, S., Mulatu, G., & Yohannes Kassa, Z. (2019). Prevalence of shigella species and its drug resistance pattern in Ethiopia: A systematic review and meta-analysis. Annals of Clinical Microbiology and Antimicrobials, 18(1). https://doi.org/10.1186/s12941-019-0321-1 [5] Gray, M. D., Lacher, D. W., Leonard, S. R., Abbott, J., Zhao, S., Lampel, K. A., Prothery, E., Gouali, M., Weill, F.-X., & Maurelli, A. T. (2015, May 14). Prevalence of shiga toxin-producing Shigella species isolated from French travellers returning from the Caribbean: An emerging pathogen with international implications. Clinical Microbiology and Infection. Retrieved March 28, 2022, from https://www.sciencedirect.com/science/article/pii/S1198743X15004437 [42] Huruy, K., Kassu, A., Mulu, A., Gebretsadik, S., Andargie, G., Tadesse, T., Birhan, W., Worku, N., Ghebreselassie, D., Belyhun, Y., Yifru, S., Adugna, S., & Tiruneh, M. (2008). High Level of Antimicrobial Resistance in Shigella Species Isolated From Diarrhoeal Patients in University of Gondar Teaching Hospital, Gondar, Ethiopia . Retrieved March 28, 2022, from https://pharmacologyonline.silae.it/files/archives/2008/vol2/29_Huruy.pdf [10] Casabonne, C., González, A., Aquili, V., & Balagué, C. (2016, November 22). Prevalence and virulence genes of Shigella spp.. isolated from patients with diarrhea in Rosario, Argentina. Japanese Journal of Infectious Diseases. Retrieved March 28, 2022, from https://www.jstage.jst.go.jp/article/yoken/69/6/69_JJID.2015.459/_article/-char/ja/ [43] Shah, T., Baloch, Z., Shah, Z., Cui, X., & Xia, X. (2021, June 20). The intestinal microbiota: Impacts of antibiotics therapy, colonization resistance, and diseases. International journal of molecular sciences. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8235228/ [12] Kim, S., Covington, A., & Pamer, E. G. (2017, September). The intestinal microbiota: Antibiotics, colonization resistance, and enteric pathogens. Immunological reviews. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6026851/ [11] Francino, M. P. (2016, January 1). Antibiotics and the human gut microbiome: Dysbioses and accumulation of resistances. Frontiers. Retrieved March 28, 2022, from https://www.frontiersin.org/articles/10.3389/fmicb.2015.01543/full [14] Roehrich, A. D., Guillossou, E., Blocker, A. J., & Martinez-Argudo, I. (2013, February). Shigella IpaD has a dual role: Signal transduction from the type III secretion system needle tip and intracellular secretion regulation. Molecular microbiology. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575693/ [16] Tremblay, J.M., Mukherjee, J., Leysath, C.E., Debatis, M., Ofori, K., Baldwin, K., Boucher, C., Peters, R., Beamer, G., Sheoran, A., Bedenice, D., Tzipori, S., & Shoemaker, C.B. (2013, December). A single VHH-based toxin-neutralizing agent and an effector antibody protect mice against challenge with shiga toxins 1 and 2. Infection and immunity. Retrieved March 28, 2022, from https://pubmed.ncbi.nlm.nih.gov/24082082/ [17] De Greve H., Virdi V., Bakshi S., & Depicker A. (2019, December 9). Simplified monomeric VHH-FC antibodies provide new opportunities for passive immunization. Current opinion in biotechnology. Retrieved March 28, 2022, from https://pubmed.ncbi.nlm.nih.gov/31810049/ [18] Sicard, D., Jean Luc, J., Legras, L. (2011). Bread, beer and wine: Yeast domestication in the Saccharomyces sensu stricto complex. Comptes Rendus Biologies, Elsevier, 2011, 229 - 236. ⟨10.1016/j.crvi.2010.12.016⟩. ⟨hal-02653082⟩ [19] Holt, S., Miks, M. H., de Carvalho, B. T., Foulquié-Moreno, M. R., Thevelein, J. M. (2019 May) The molecular biology of fruity and floral aromas in beer and other alcoholic beverages, FEMS Microbiology Reviews, 43(3), 193–222, https://doi.org/10.1093/femsre/fuy041 [20] Piskur, J., Langkjaer, R. B. (2004). Yeast genome sequencing: the power of comparative genomics. Molecular microbiology, 53(2), 381–389. https://doi.org/10.1111/j.1365-2958.2004.04182.x [21] Gaziano, R., Sabbatini, S., Roselletti, E., Perito, S., Monari, C. (2020). Saccharomyces cerevisiae-Based Probiotics as Novel Antimicrobial Agents to Prevent and Treat Vaginal Infections. Frontiers in microbiology, 11, 718. https://doi.org/10.3389/fmicb.2020.00718 [22] Palma, M. L., Zamith-Miranda, D., Martins, F. S., Bozza, F. A., Nimrichter, L., Montero-Lomeli, M., Marques, E. T., Jr, Douradinha, B. (2015). Probiotic Saccharomyces cerevisiae strains as biotherapeutic tools: is there room for improvement?. 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J., Picking, W. L., & Picking, W. D. (2009). Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction. Infection and immunity, 77(7), 2754–2761. https://doi.org/10.1128/IAI.00190-09 [8] Centers for Disease Control and Prevention. (2020). Shigella-Shigellosis. https://www.cdc.gov/shigella/index.html [28] Peng, B., Williams, T. C., Henry, M., Nielsen, L. K., Vickers, C. E. (2015). Controlling heterologous gene expression in yeast cell factories on different carbon substrates and across the diauxic shift: a comparison of yeast promoter activities. Microbial cell factories, 14, 91. https://doi.org/10.1186/s12934-015-0278-5 [29] Huang, X., Gänzle, M., Zhang, H., Zhao, M., Fang, Y., Nishinari, K. (2020). Microencapsulation of probiotic lactobacilli with shellac as moisture barrier and to allow controlled release. Journal of the Science of Food and Agriculture. 101. 10.1002/jsfa.10685. [30] Huang. X., Zhang, H., Peng, S., Zhao, M., Fang, Y. (2019). Tianrankeshixing Bicaichongjiao zai Gongnengzufenweinanghua zhongde Yingyonngyanjiujinzhan [Recent Progress in the Application Shellac as a Natural Edible Wall Material in the Microencapsulation of Functional Ingredients]. Shipinkexue [Food Science], 40(7), 317-324. [31] Mei, S., Han, P., Wu, H., Shi, J., Tang, L., Jiang, Z. (2018). One-pot fabrication of chitin-shellac composite microspheres for efficient enzyme immobilization. Journal of biotechnology, 266, 1–8. https://doi.org/10.1016/j.jbiotec.2017.11.015 [32] Gately, N. M., Kennedy, J. E. (2017). The Development of a Melt-Extruded Shellac Carrier for the Targeted Delivery of Probiotics to the Colon. Pharmaceutics, 9(4), 38. https://doi.org/10.3390/pharmaceutics9040038 [33] Hamad, S. A., Stoyanov, S. D., Paunov, V. N. (2013). Triggered release kinetics of living cells from composite microcapsules. Physical chemistry chemical physics: PCCP, 15(7), 2337–2344. https://doi.org/10.1039/c2cp42100c [35] Braat, H., Rottiers, P., Hommes, D. W., Huyghebaert, N., Remaut, E., Remon, J. P., . . . Steidler, L. (2006). A phase I trial with transgenic bacteria expressing interleukin-10 in Crohn's disease. Clin Gastroenterol Hepatol, 4(6), 754-759. doi:10.1016/j.cgh.2006.03.028 [36] de Moreno de LeBlanc, A., Del Carmen, S., Chatel, J. M., Azevedo, V., Langella, P., Bermudez-Humaran, L., & LeBlanc, J. G. (2016). Evaluation of the biosafety of recombinant lactic acid bacteria designed to prevent and treat colitis. J Med Microbiol, 65(9), 1038-1046. doi:10.1099/jmm.0.000323 [GarcÃa2012] GarcÃa-Fruitós, E. (2012). Lactic acid bacteria: a promising alternative for recombinant protein production. Microbial Cell Factories, 11(1), 157. doi:10.1186/1475-2859-11-157 [37] Muthuramalingam, M., Whittier, S. K., Picking, W. L., & Picking, W. D. (2021). The Shigella Type III Secretion System: An Overview from Top to Bottom. Microorganisms, 9(2). doi:10.3390/microorganisms9020451 [38] Plavec, T. V., & Berlec, A. (2019). Surface Anchoring on Lactococcus lactis by Covalent Isopeptide Bond. Acta Chim Slov, 66(1), 18-27. [34] Song, A. A.-L., In, L. L. A., Lim, S. H. E., & Rahim, R. A. (2017). A review on Lactococcus lactis: from food to factory. Microbial Cell Factories, 16(1), 55. doi:10.1186/s12934-017-0669-x [15] Barta ML, Shearer JP, Arizmendi O, Tremblay JM, Mehzabeen N, Zheng Q, et al. Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem 2017, 292(40), 16677–87. [41] Sierocki, R.; Jneid, B.; Delgado, M. L. O.; Plaisance, M.; Maillère, B.; Nozach, H.; Simon, S. An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLOS Neglected Tropical Diseases 2021, 15(3): e0009231 [39] (14) Sadana, P., Monnich, M., Unverzagt, C. and Scrima, A. Structure of the Y. pseudotuberculosis adhesin InvasinE. Protein Sci 2017, 26: 1182–1195. [40] Salema, V., Marın, E., Martınez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., et al. Selection of single domain antibodies from immune libraries displayed on the surface of E. coli cells with two b-domains of opposite topologies. PLoS One 2013, 8: e75126.","breadcrumbs":"Project » Description » References","id":"60","title":"References"},"61":{"body":"Engineering Cycle This page will give a detailed explanation about the engineering cycle. To make yeast capable of displaying the target nanobody 20ipaD on the cell surface, 20ipaD gene was inserted behind the yeast membrane-sealed protein Aga 2; therefore, Aga 2 would bring the nanobody to the cell surface. The recombinant plasmid pYD1-20ipaD was successfully built, which was supported by PCR amplification data and sequencing data. Apart from yeast, Lactococcus lactis and Escherichia coli were also chosen as probiotics for surface displace of nanobodies at the beginning, where 20ipaD/JPS-G3 and control 3xFLAG tags were inserted into pNZ8148 (L. lactis) and pET30a (E. coli) for expression respectively. However, due to failure in transformation and plasmid construction, only yeast was selected as the final product.","breadcrumbs":"Project » Engineering » Introduction","id":"61","title":"Introduction"},"62":{"body":"","breadcrumbs":"Project » Engineering » Engineering Cycle","id":"62","title":"Engineering Cycle"},"63":{"body":"y-engineering-cycle-high-resolution Cycle 1 Design We located a single-domain antibody (VHH) named 20ipaD from the database, whose binding ability with the needle tip protein ipaD of Shigella type III secretion system has be testified [1] [2] . Peptide sequences of 20ipaD from Barta et al (2017). Codon optimization was performed to get DNA sequences. Two flank sequences containing XhoI and ApaI cutting sites as well as C-terminal Flag-tag were added to the ipaD DNA sequence. Build Designed 20ipaD sequences were chemically de novo synthesized and sent in pUC19. XhoI and ApaI double-digestion enabled us to ligate the 20ipaD DNA sequence into pYD1, a plasmid allowing the surface display of the gene it carries in yeast. The ligation of 20ipaD into pYD1 generates a DNA sequencing coding a recombinant protein of 20ipaD and Aga2, a yeast extracellular membrane protein. pYD1 also contained a replication origin recognized by bacteria and an ampicillin resistance gene. After plasmid ligation, recombinant plasmids were transferred into E. coli to get a clone via ampicillin selection. Cloned plasmids were then transferred into yeast cells. Yeast cells containing the plasmid were selected by tryptophane-deficient medium. Expression of the recombinant protein was induced by add galactose. Test After transformation of recombinant plasmid into E. coli and single colony collection, we perform enzyme digestion and gel electrophoresis to check if the ligation and transformation is successful. For expression assay, we incubated induced yeast cells with anti-flag-tag primary antibody. After incubating with FITC conjugated secondary antibody, cells were examined under florescence microscopy and flow cytometry. Learn Recombinant proteins were observed to express on the cell surfaces on a portion of the cell population. We therefore planned to further testify the effectiveness of our recombinant protein. Though previous modeling through Rosetta suggested that the recombinant Aga2 region as well as the linkers sequences do not undermine the correct folding of the VHH part, we still sought for a experimental support as well as a way to quantify the binding affinity. Cycle 2 Design In this cycle, we aimed to test binding affinity between the recombinant nanobody and the ipaD epitopes. ipaD were retrieved from NCBI database. Codon optimization was also performed to collect the DNA sequence. Similar to 20ipaD, flank regions were inserted into ipaD except the substitution of Flag-tag to HA-tag. Build Synthesized ipaD sequences were got from the same company. Using the same method, we expressed ipaD recombinant protein of the yeast surface. Cycle 3 Design In this cycle, we aims to improve the expression level of the recombinant protein. Energy flows within the yeast cells would be controlled to concentrate more on protein production rather than other metabolic activities. We started by looking for a strong and continuously expressed promoter to drive the expression of 20ipaD recombinant protein. At the same time, we also tried to reduce other cellular activities. Cycle 4 Design In this cycle, we aims to improve the binding affinity of the recombinant protein with the antigen epitope. We would perform error prone PCRs to introduce mutations into 20ipaD sequences. Concentrations of the nucleotide analogs would be controlled so that only point mutants would be produced. All mutants would be screened to identify binding affinity improvements. To reduce the workload of screening, we would perform a modeling prescreen. In the prescreen, we would predict how single amino acid change influence the binding affinity between 20ipaD and ipaD.","breadcrumbs":"Project » Engineering » Yeast","id":"63","title":"Yeast"},"64":{"body":"Cycle 1 Design At first, we wanted to obtain the sequence of both 20ipaD and control flag-tag so that we could amplify them via PCR reaction. The 20ipaD is one of the single-VH domain antibodies (VHHs) capable of recognizing distinct epitopes within the antigen IpaD of pathogen Shigella. In this way, we hoped that by fusing 20ipaD and control flag-tag into the Lactococcus lactis expression vector pNZ8148, we would achieve the surface display and expression of 20ipaD on Lactococcus lactis . Build To obtain the sequence of 20ipaD, we constructed the plasmid with the 20ipaD sequence surrounded by two different restriction sites of enzymes BamHI and SacI. In this way, through the restrictive digestion of Bam HI and Sac I, ideally the sequence of 20ipaD would be obtained. The similar construction was also applied with the sequence of control flag-tag, where the enzymes used for restrictive digestion were changed to be NcoI and HindIII. Test After successfully received the synthesized plasmid sequence for 20ipaD and control flag-tag, we conducted the digestion of BamHI and SacI for the obtain of 20ipaD sequence, and the digestion of Nco I and Hind III for the obtain of control flag-tag sequence. Gel electrophorese was applied to confirm the size of the sequence. Control flag-tag sequence was successfully obtained. However, according to the gel picture, the band of 20ipaD showed a very different size from that in theory. Learn We checked the source of error and found that the designed sequence of 20ipaD has been inserted into the pUC19 vector when being synthesized by the company. Unfortunately, pUC19 vector also contained a restriction site for BamHI itself, thus leading to a different enzymatic digestion than what we have expected before. Cycle 2 Design Since pUC19 vector also contained a restriction site for BamHI itself, which would lead to unspecific enzymatic digestion and the failure of getting 20ipaD sequence, we redesigned the experimental steps in order to overcome such a problem. Build In this try, we would do the PCR amplification of 20ipaD sequence to insert it directly into the pNZ8148 vector first. This would circumvent the enzymatic digestion of pUC19 vector by BamHI that had the insertion of 20ipaD. Learn From this process we learnt that when the synthesized plasmid went wrong from our expectations, apart from directly asking the company to redo the synthesis, we could also alter the steps of ligation via PCR reaction to solve the problem. Cycle 3 Design We wanted to insert the engineered pNZ8148 vector with 20ipaD into the strain Lactococcus lactis NZ9000. According to literature review, electroporation is the commonly used technique to insert vectors into Lactococcus lactis . Build When the OD600 of Lactococcus lactis reached 0.3, the bacteria would be subjected to electroporation. The bacteria would be washed with liquid detergent I containing 0.5mol∙L-1 sucrose and 10% glycerol for the insertion of 0.2 μg vector. The pulse of electroporation was delivered by a Gene-Pulser (Scientz) at 25μF and 2.5kV, while the electroporation cuvette (0.2cm in size) was connected in parallel to a 400-Ω resistor (the parameters were searched online and were consulted from technician at Scientz). According to multiple researches done previously, the transformation efficiency would be the highest is the recovery time is 1.5h after electroporation. Test The process of electroporation was not successful because we failed to insert the vector into Lactococcus lactis . Learn We suspect that the making of electrocompetent cells might be the source of failure. After checking with the team advisor, we found that the type of glycerol used was intended for protein purification, which could cause problems for the electrocompetent cell. Cycle 4 Design To further increase efficiency, after doing more literature reviews we added the pretreatment of Lactococcus lactis with lithium acetate (LiAc) and/or dithiothreitol (DTT). We also substituted the type of glycerol used based on the previous error analysis. Build According to the newly found protocol, the Lactococcus lactis was firstly suspended at room temperature for 30 min in 8ml of 100mM LiAc, 10mM DTT, 0.6M sucrose, and 10mM Tris-HCl (pH=7.5). Following the treatment, Lactococcus lactis was pelleted and was resuspended in 1.5ml microcentrifuge tube, and was then washed as previously described. Afterwards, electroporation was conducted as previously described.","breadcrumbs":"Project » Engineering » Lactococcus lactis","id":"64","title":"Lactococcus lactis"},"65":{"body":"E. coli Engineering Cycle Cycle 1 Design Initially, we planned to try three different nanobodies (20ipaD, JPS-G3, and JMK-H2) agianst the Shigella antigen ipaD from a research paper [1] . We also wanted to try two different surface display systems, beta domain of the E. coli outer membrane protein intimin [3] and the E. coli curli fiber protein, csg B [4] . Our target probiotic is E. coli Nissle 1917 [4] . By inserting the target nanobody sequence behind intimin or csg B, reconstructing the plasmid pET30a and transforming the plasmid into E. coli Nissle 1917, we expect the protein to be displayed on the surface of E. coli , so that it can capture the pathogen via antigen-antibody binding. Build & Test We designed the following sequences to make the recombinant protein. intimin-20ipaD-3xFLAG csgB-JMK-H2-3xFLAG JPS-G3-3xFLAG ipaD-3xHA However, due to limitations in budget & time for gene synthesis, we only have JPS-G3-3xFLAG and ipaD-3xHA (inserted into pUC19 plasmids). By plasmid extraction, double digestion ( Bam HI & Xho I) and PCR, we successfully obtained the sequences and verified the accuracy by Sanger sequencing, but we don't have csgB or intimin for surface display. Learn Complex sequences including potential harmful genes may impact synthesis efficiency. Cycle 2 Design Alternatively, we chose the curli fiber csg A [5] sequence for surface display. Build & Test We designed the following sequences: csgA-JPS-G3-3xFLAG csgA-ipaD-3xHA (displaying the antigen on the surface of E. coli BL21 to mimic Shigella flexneri , so that the effectiveness can be evaluated) csg A gene is obtained from the E. coli strains (pGEX-4T-1-csgA-shMT) provided by the XJLTU iGEM team via PCR. To connect different parts, we plan to use overlapping PCR.","breadcrumbs":"Project » Engineering » Escherichia coli","id":"65","title":"Escherichia coli"},"66":{"body":"Salema, V., MarÃn, E., MartÃnez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., Teira, X., Gutierrez, C., Bodelón, G., & Fernández, L. Ã. (2013). Selection of Single Domain Antibodies from Immune Libraries Displayed on the Surface of E. coli Cells with Two β-Domains of Opposite Topologies. PLoS ONE , 8(9), e75126. https://doi.org/10.1371/journal.pone.0075126 Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998 Barta, M. L., Shearer, J. P., Arizmendi, O., Tremblay, J. M., Mehzabeen, N., Zheng, Q., Battaile, K. P., Lovell, S., Tzipori, S., Picking, W. D., Shoemaker, C. B., & Picking, W. L. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem, 292(40), 16677-16687. https://doi.org/10.1074/jbc.M117.802231 Sierocki, R., Jneid, B., Orsini Delgado, M. L., Plaisance, M., Maillere, B., Nozach, H., & Simon, S. (2021). An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLoS Negl Trop Dis, 15(3), e0009231. https://doi.org/10.1371/journal.pntd.0009231","breadcrumbs":"Project » Engineering » Reference","id":"66","title":"Reference"},"67":{"body":"Experiments","breadcrumbs":"Project » Experiments » Yeast","id":"67","title":"Yeast"},"68":{"body":"Phases : 1. Stock vectors preparation and vectors storage; 2. Stock gene preparation and amplification; 3. Gene cloning, plasmid construction, storage, and verification; 4. Yeast transformation, protein display, and detection Phase I: Stock vectors preparation and vectors storage By the end of this phase, we would get: One tube of pYD1 vector stock solution One glycerol stock containing E. coli DH5α that were transformed with pYD1 vectors Phase II : Gene cloning, plasmid construction, storage, and verification By the end of this step, we would get: One tube of pY20ipaD recombinant stock solution (not pure) One glycerol stock containing E. coli DH5α that were transformed with pYD1 vectors Phase IV : Yeast transformation, protein display, and detection By the end of this phase, we would get: Glycerol stock of yeast that were transformed with recombinant plasmids Induced yeasts (display the nanobody on the surface)","breadcrumbs":"Project » Experiments » Experiment Overview","id":"68","title":"Experiment Overview"},"69":{"body":"Yeast Lab Notes","breadcrumbs":"Project » Experiments » Lab Notes","id":"69","title":"Lab Notes"},"7":{"body":"Sichang He (Steven) UG Class of 2024 Data Science Jasmine Santos UG Class of 2024 Biology Yuxiang He UG Class of 2025 Zhenyu Xu UG Class of 2024 Physics","breadcrumbs":"Team » Team » Modeling","id":"7","title":"Modeling"},"70":{"body":"\"One-step Method Competent Cell Preparation Kit\" from Beyotime was used for this experiment. The protocol follows the manual of the product [1] . E.coli_competent_cell_transformation Plasmid_Extraction Genetic_cloning_Enzyme_digestion_ligation \"DNA Agarose Gel Recycle Kit\" from Beyotime was used for this experiment. The protocol follows the manual of the product. [2] Gel_Purification.pdf \"Frozen-EZ Yeast Transformation II Kit\" from Zymo was used for this experiment. The protocol follows the manual of the product. [3] Yeast_Induction.pdf Fluorescence_Activated_Cell_Sorting.pdf \"FLAG Tag Immuno-precipitation Kit (Immunomagnetic Beads Method)\" from Beyotime was used for this experiment. The protocol follows the manual of the product [4] . Protein_Purification.pdf “TIANprep Mini Plasmid kit†was used for this experiment. The protocol follows the manual of the product [5] . Plasmid_Extraction.pdf","breadcrumbs":"Project » Experiments » Protocols","id":"70","title":"Protocols"},"71":{"body":"","breadcrumbs":"Project » Experiments » Escherichia coli","id":"71","title":"Escherichia coli"},"72":{"body":"Group E Workflow Group E. coli Experimental Procedures 1. Cloning 2. Recombinant Protein Expression 2.1 Express the Protein in E. coli DE3 Cytoplasm 3 different VHHs (JPS-G3, JMK-H2, 20ipaD) and 1 antigen (ipaD) are expressed separately in E. coli DE3 for protein purification. As is shown in the diagram below ( Figure 1 ), the DNA sequences of the proteins are bind to different detection tags (VHHs - FLAG-tag, antigen - HA-tag) and inserted into pET41a plasmids for bacterial transformation and protein purification. The pET41a plasmid contains a T7 promoter and a T7 terminator for high-level protein expression in E. coli DE3, and a GST tag with a Tb (thrombin) site for protein purification. After transformation, the exogenous proteins will be expressed by the bacteria. Fig.1 | Schematic Representation of the Protein Expression & Purification Process 2.2 Protein Purification and Affinity Test Next, we use the GST tag to purify the recombinant protein. The target proteins will be extracted via GSH-GST interaction, and the remaining GST tag will be cut by thrombin. Then, we can get the purified recombinant proteins (target protein + detection tag). Lastly, co-IP (immuno-precipitation) followed by Western analysis will be used to test the affinity between VHHs and the antigen. As is shown in the figure below ( Figure 2 ), by adding anti-FLAG antibodies and anti-HA antibodies to the samples, we can pull down the recombinant proteins with corresponding tags. If adding either anti-FLAG antibodies or anti-HA antibodies leads to a positive result in 'FLAG-VHH + HA-ipaD', we can say that there is high affinity between the expressed VHHs and the antigen. Fig.2 | Expected Western Blot Results of the co-IP Experiment 3. Surface Display 3.1 Surface Display via csgA CsgA, or major curlin subunit, is a component of biofilm. The design was a modified version of the PATCH system from Neel Joshi lab. It is composed of a temperature-controlled promoter, Csg synthetic operon, and the VHH targeting Type III secretion system. The design is predicted to be beneficial in a therapeutic context because biofilm formation effectively inhibits the invasion of shigella into epithelial cells. 3.2 Surface Display via intimin 3.3 Detecting E. coli surface display Congo red binding assay We use a quantitative congo-red binding assay to detect the expression of curli fibers. Congo red is a dye that binds to the hydroxyl group of polypeptide chains in amyloid through hydrogen bonds. A control group with no curli expression and a group with curli expression are cultured under the same condition. The 490nm absorbance of both groups are measured to quantify the amount of congo red not in binding with curli fiber (1) (2) . Whole cell filtration ELISA To detect the expression of curli fibers on the cell surface, we perform whole-cell ELISA. Whole-cell ELISA requires the cells to be seeded to the bottoms of the wells, providing conditions to detect proteins in whole cells (3) (4) . 3.4 Detecting the Binding Affinity Between E. coli Expressing VHHs and the antigen Aggregation Assay using OD600 measurements (5) Ag (antigen)-only E. coli , Nb (nanobody, i.e., VHHs)-only E. coli and the mixture of the two are cultured separately in LB liquid medium for 24 hours. OD600 of their supernatant are measured immediately/after 24 hours to see whether there is significant difference between the Ag-only group, Nb-only group, and mixture group. A significant low OD600 in the mixture group indicates that the E. coli expressing VHHs and antigens bind to each other, form assembly, and sink. Observing the Morphologies using Confocal Microscopy (5) GFP and m Cherry genes were expressed respectively in Ag-only E. coli and Nb-only E. coli . When observing the morphology via a confocal microscope, we should see that most neighbors of a certain bacterium should have opposite colors. Lab Notes E. coli Lab Notes Protocols E. coli Protocols","breadcrumbs":"Project » Experiments » Experiment Overview","id":"72","title":"Experiment Overview"},"73":{"body":"","breadcrumbs":"Project » Experiments » Lactococcus lactis","id":"73","title":"Lactococcus lactis"},"74":{"body":"L_Workflow","breadcrumbs":"Project » Experiments » Experiment Overview","id":"74","title":"Experiment Overview"},"75":{"body":"Because of financial and logistical reasons, wet lab experiments of group L were halted. We therefore can only present the experimental procedures and protocols designed by our members.","breadcrumbs":"Project » Experiments » Lab Notes","id":"75","title":"Lab Notes"},"76":{"body":"Group L intends to display 20ipaD, a nanobody against Shigella, onto L.lactis. The plasmid construction is performed in E. coli and then transformed into L.lactis. Electroporation_protocol_for_Lactococcus_lactis.pdf gel_extraction_protocol.pdf Plasmid_extraction_of_L.lactis__Gram_positive_bacteria_.pdf Protocol_for_activating_and_preparing_glycerol_stock.pdf Protocol_for_extracting_DNA_from_Lactococcus_Lactis_NZ9000.pdf Protocol_for_ligation.pdf Protocol_for_medium_making.pdf Protocol_for_restriction_enzyme_digestion.pdf plasmid extraction and gel purification are the same as Group Y. Solarbio_protocol_of_DNA_extraction.pdf Beyotime One-step Method Competent Cell Preparation Kit. https://www.beyotime.com/product/D0301.htm Beyotime DNA Agarose Gel Recycle Kit. https://www.beyotime.com/product/D0056.htm Zymo Frozen-EZ_Yeast_Transformation_II_Kit. https://files.zymoresearch.com/protocols/_t2001_frozen-ez_yeast_transformation_ii.pdf Beyotime FLAG Tag Immuno-precipitation Kit (Immunomagnetic Beads Method). https://m.beyotime.com/Manual/P2181%20Flag%E6%A0%87%E7%AD%BE%E8%9B%8B%E7%99%BD%E5%85%8D%E7%96%AB%E6%B2%89%E6%B7%80%E8%AF%95%E5%89%82%E7%9B%92(%E7%A3%81%E7%8F%A0%E6%B3%95).pdf TIANprep Mini Plasmid kit. https://en.tiangen.com/download/manual.html?one=34&two=1085&three=1086&id=4307","breadcrumbs":"Project » Experiments » Protocols","id":"76","title":"Protocols"},"77":{"body":"","breadcrumbs":"Project » Notebook","id":"77","title":"Project"},"78":{"body":"Implementation The end-products of our project are small tablets or capsules that contain dry powders of probiotics that express anti-Shigella antibodies on their surface. Our products serve the dual roles of Shigella infection precaution as well as disease therapy. The abilities of room temperature storage provide our tablets with cost reduction for storage and transportation. Tablets should be taken when facing potential exposure to Shigella infection sources, such as drinking unsanitary water in high diarrhea incidence areas. In consideration of the prevalent transmission pathways of Shigella, we also suggest people whose family members have developed Shigella infections and children in school with diarrhea cases take our tablets to prevent person-to-person transmission, which is the major form of Shigella spreading [1] .","breadcrumbs":"Project » Implementation » Infection Precaution","id":"78","title":"Infection Precaution"},"79":{"body":"Due to intracellular pathogen nature of Shigella, the effect of antibodies reduces as pathogens evade into the cells. The ability of reprogramming the infected cells to form protrusion adjacent cells allows Shigella to spread within intestine epithelial cells, reducing the chance of exposing to body internal environment [2] . This special characteristic implies antibody may not be a one-size-fits-all solution for different stages of infection. We call for the combination of clinical phases of antibiotics treatment with our tablets together.","breadcrumbs":"Project » Implementation » Infection Therapy","id":"79","title":"Infection Therapy"},"8":{"body":"Jiani Chen UG Class of 2023 Biology Yang Yu UG Class of 2023 Biology","breadcrumbs":"Team » Team » Advisor","id":"8","title":"Advisor"},"80":{"body":"Along with the high household transmission rates, Shigella also display high secondary infection rates. Therefore, we suggest families with members developing Shigella to take our pills for a time period to provide continuously protection apart from keep good hygiene conditions. In the meanwhile, patients who have developed Shigella infection before should also take our tablets when facing a second exposure.","breadcrumbs":"Project » Implementation » Prognosis and Secondary infection","id":"80","title":"Prognosis and Secondary infection"},"81":{"body":"People who exposed to potential Shigella infection source, especially in a household environment. Children in school with Shigella cases reported. People with antibiotic allergy that cannot use clinical antibiotic treatment. Government that aims to provide low cost solution for Shigella incidence in low- and middle- income, less developed region.","breadcrumbs":"Project » Implementation » End Users","id":"81","title":"End Users"},"82":{"body":"Our product contains exogenous antibody proteins. Therefore, allergy test may need to be performed to prevent possible anaphylaxis. Besides, considering the pathogenesis and transmission pathway of Shigella, our products may not be a one-size-fits all solution for all infection stages but focuses more on the prevention of infection.","breadcrumbs":"Project » Implementation » Caveats","id":"82","title":"Caveats"},"83":{"body":"Kotloff, K. L., Riddle, M. S., Platts-Mills, J. A., Pavlinac, P., & Zaidi, A. K. M. (2018). Shigellosis. The Lancet, 391(10122), 801-812. https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8 Sansonetti, P. J., Mounier, J., Prévost, M. C., & Mège, R.-M. (1994). Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell, 76(5), 829-839. https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1","breadcrumbs":"Project » Implementation » References","id":"83","title":"References"},"84":{"body":"Partnership","breadcrumbs":"Project » Partnership » Meeting with XJLTU","id":"84","title":"Meeting with XJLTU"},"85":{"body":"They plan to develop a biofilter core to replace current industry filter cores for heavy metal wastewater. Specifically, they plan to engineer E. coli to express csgA protein at high levels and immobilize the bacteria into a filter. In that way, the heavy metal ions in the wastewater can be captured by csgA protein that is expressed by E. coli located in the filter.","breadcrumbs":"Project » Partnership » XJLTU's Project","id":"85","title":"XJLTU's Project"},"86":{"body":"They would like to know how we will interact with and educate the public. A: We have made questionnaires to evaluate their knowledge related to antibiotics, probiotics, and microorganisms. We are also planning to make some handouts and deliver a lecture about it in a high school. They were interested in the specific design of our plasmids. Specifically, it's about how and why we choose each part of the plasmid for surface display. A: We applied three microorganisms and the whole team was divided into three groups, each responsible for E. coli, Yeast cell and Lactococcus lactis. All groups applied a strategy which conjugates the targeted nanobody with a surface protein that is to be expressed, transported and located to the extracellular space. The surface protein and the targeted nanobody were connected with a linker sequence, and each nanobody is marked with at least one protein tag for their identification. We also provided links to igem parts so they can check it directly.","breadcrumbs":"Project » Partnership » Questions & Advice From XJLTU","id":"86","title":"Questions & Advice From XJLTU"},"87":{"body":"Will the biofilter be blocked due to E. coli proliferation? A: The microorganisms are immobilized in filters, and the filtration condition may not allow E. coli to grow at such a speed. The csgA protein's ability to absorb heavy metal ions under different conditions (like pH) can be tested through experiments. For example, we can put csg protein into a certain amount of wastewater, then adjust the pH and check the remaining concentration of metal ions in time, so we can acquire a proper pH for the protein to capture heavy metal ions.","breadcrumbs":"Project » Partnership » Questions & Advice From DKU","id":"87","title":"Questions & Advice From DKU"},"88":{"body":"Model for bacteria growth The XJLTU team developed a model for predicting bacteria growth, and it may also be applied to our situation by adjusting some of the parameters. Quantified expression of csg through controlling IPTG concentration The XJLTU team intended to control the expression of csg protein by adjusting the amount of IPTG inducer, which can also be a helpful approach for our team to check the relationship between the cell-cell adhesion affinity and the number of expressed nanobodies. However, as we also applied the TlpA promotor, it may influence the actual expression to a great extent and cause a big difference from the theoretical calculation. As a result, this approach remains to be a concern. Detection and measurement of displayed csg protein. The XJLTU team controlled the expression level by adjusting inducer concentration and estimated the expression by calculating theoretically. The condition of csg and heavy metal ions after the death of E. coli cells We consider that the heavy metal ions will remain captured, as protein itself has a great affinity to the heavy metal ions. But, it remains to be seen whether the released protein will leak out from the filter.","breadcrumbs":"Project » Partnership » Discussion Topics","id":"88","title":"Discussion Topics"},"89":{"body":"The novel drug we proposed was to anchor nanobodies on the surface of probiotics, including yeast, Lactococcus, and E. coli, which were then delivered to the gut through a shellac-membraned capsule to combat against pathogens like Shigella. Multiple objectives have been achieved to prove our product.","breadcrumbs":"Project » Proof of Concept » Overview","id":"89","title":"Overview"},"9":{"body":"Lingfeng Huang, Ph.D. Associate Professor of Biology, Duke Kunshan University","breadcrumbs":"Team » Team » Principal Investigator","id":"9","title":"Principal Investigator"},"90":{"body":"In order to enable yeast to express surface protein conjugated with target proteins, we cloned the nanobody gene sequence and the antigen gene sequences into the vectors. The vector pYD1 is a yeast surface display unit where the surface-sealed protein Aga2 was controlled by GAL1 promoter. Using XhoI and ApaI, the nanobody gene 20ipaD and the antigen gene ipaD was cloned into the corresponding restriction sites. The gene segment of 20ipaD was ~500bp, while that of ipaD was ~1000bp. The PCR results that amplify an originally ~400bp fragment of empty vector supported the success in plasmid construction (Figure 1, Figure 2). Sequencing data of the region further confirmed the construction of correct plasmids (Figure 3).","breadcrumbs":"Project » Proof of Concept » Construction of recombinant plasmids for yeast surface display","id":"90","title":"Construction of recombinant plasmids for yeast surface display"},"91":{"body":"Using the plasmids constructed in the previous steps, baker's yeast EBY100 was transformed. Considering the TRP1 maker in the plasmid, the yeast was selected on the SCDAA medium where tryptophan was absent. Colonies appeared after incubation, indicating the success of engineered probiotic construction (Figure 4). The yeasts that were transformed with recombinant plasmids were now able to display the nanobodies on their surface. Then, the yeasts were induced by galactose, which can promote the transcriptional activity of GAL1 promoter. After 24h induction, a portion of the cells were shown to display the anticipated proteins on their surface by immunofluorescent microscopic imaging (Figure 5). y-fig-1 y-fig-2 y-fig3 y-fig4 y-fig5","breadcrumbs":"Project » Proof of Concept » Construction of engineered yeasts that display nanobodies and capable for use","id":"91","title":"Construction of engineered yeasts that display nanobodies and capable for use"},"92":{"body":"As a drug of a novel strategy to target the pathogen, our engineered probiotics should combat the pathogenic Shigella by displaying nanobodies on surfaces to efficiently get over the antibiotic resistance problem. To prove the feasibility and efficiency of this proposed drug, evidence from different aspects should be taken into consideration. First, the most solid and important evidence should be the entity of the imagined product. In wet lab, we have shown the success construction of nanobody-displaying yeasts, proving the possibility and authenticity of producing such engineered probiotics. Second, whether the probiotic works to inhibit pathogen would be another important evidence to prove the efficiency of this drug. We also shown the success of pathogen-mimicking yeasts construction and proposed the binding affinity assay that could prove the inhibition feature of the engineered probiotics. Third, evidence for optimization possibility is required to prove the improvement potential of the drug. For the collection of evidence from this aspect, multiple expression enhancement elements refitting and mutation-screening binding affinity enhancement were designed to get the optimized combination of expression abundancy and binding affinity. Last but not least, a solid storage and delivery method should be risen as evidence proving the practicability and productization ability. The shellac-based microcapsulation plus tablet/capsule wrapping theoretically achieved the room temperature storage and intestine-target release of engineered probiotics, thus proving the reliability of low-cost production and storage of the whole drug and the target specificity of the efficient component.","breadcrumbs":"Project » Proof of Concept » Summary and conclusion","id":"92","title":"Summary and conclusion"},"93":{"body":"Results This page will give a detailed record about the experiment results, future plans & project achievements.","breadcrumbs":"Project » Results » Introduction","id":"93","title":"Introduction"},"94":{"body":"","breadcrumbs":"Project » Results » Experiment Results","id":"94","title":"Experiment Results"},"95":{"body":"Summary of Lab Design In order to decorate the yeast surface with nanobodies against the pathogen, we designed the vector which contains the nanobody gene behind a membrane-sealed protein. The overall experiment design could be divided into 3 phases. In phase I, the expected vector that could potentially express our designed module would be constructed and stored. In phase II, the expression vector would be transformed into yeast and detected for its expression abundance and location. In phase III, the binding affinity and inhibitory efficiency on pathogen would be tested. Due to the limitation of materials and time under the background of local pandemic situation, the experiments only accomplished Phase I & II. Genes of nanobody and pathogen were harvested The DNA sequence of nanobody 20ipaD and antigen ipaD were obtained from Sangon in the form of pUC19 plasmid insertions, which were stored inside E. coli. The storage bacteria were amplified, and plasmids containing sequences of interest were extracted with Plasmid mini-prep kit from TIangen. Those plasmids were digested by XhoI and ApaI, and the sequences of interest were recycled by agarose gel recycle kit from Beyotime ( Fig1 ). Recombinant plasmids were constructed The purified ipaD and 20ipaD DNA segments mentioned in the previous section, along with the pYD1 vector digested by XhoI & ApaI, were ligated, and transformed into DH5α cells that were selected by ampicillin. Colony direct PCR was applied to inspect the plasmid condition of the colonies formed. pYD1-forward and pyd1-reverse primers were used to show the size of Aga2-Protein, thus verifying the sequence between the primer pairs ( Table 1 ). The size of pYD1-ipaD plasmid primer box should be about 1500bp, while the size of pYD1-20ipaD should be about 1000bp. As shown in Fig2 a , sample “2-3â€, “2-5†meet the requirement for pYD1-ipaD, so the bacteria in those colonies contain the recombinant plasmid pYD1-ipaD. Additionally, all samples in lane 1~10 met the requirement for pYD1-ipaD, which indicates the bacteria in those colonies contain pYD1-20ipad recombinant plasmids ( Fig2 b ). Those colonies were amplified, and the plasmids were extracted. Sequencing data further supported the successful construction of the recombinant plasmids ( Fig3 ). Recombinant plasmids were transformed into yeast EBY100 We performed yeast transformation using constructed pYD1-ipaD and pYD1-20ipaD plasmids. Yeast competent cells were prepared by Frozen-EZ Yeast transformation II kit (Zymo Research, T2001). The yeasts were successfully transformed by chemical method using carrier DNA and PEG/LiAc. The plasmids and competent cells were thawed on ice. 10μL of Carrier DNA and 2μg of plasmid was added into 100μL of competent cells. Then 500μL of PEF/LiAc solution was added. The tube was inverted 6-8 times and incubated at 30°C with an inversion at 10-minute interval. Then, 20μL of DMSO was added to increase the transformation efficiency. Then, the tube was incubated under 42°C with an inversion of 5-minute interval. The cells were centrifuged at 12000rpm for 5 seconds and incubated with YPD medium for 1 hour at 30°C. After incubation, the cells were pelleted and resuspend by 100μL of 0.9% NaCl, 50μL of which were spread onto SDCAA medium, and another 50μL of cells onto YPD medium. The plates were incubated at 30°C for 2 days. The result of the plates was positive ( Fig4 ). SDCAA plates, which are the selective plates lack of tryptophan, has demonstrated fewer colony growth compared to YPD plates, indicating successful transformation. Single colonies were taken and incubated at 30°C in SDCAA liquid medium for amplification. Nanobody and antigen were expressed and displayed on yeast surface The yeasts that were transformed with pYD1-ipaD, pYD1-20ipaD, and pYD1 were amplified in SDCAA liquid medium for 36h. The cells were harvested by centrifuge at 5000xg for 5 minutes and diluted in SGCAA liquid containing the induction agent galactose to obtain an OD600=0.5. Four milliliters of each diluted cells were transferred into new culture tubes and induced at 21°C for 24h. An additional prep of EBY100 cells without plasmids were also diluted to OD600=0.5 and induced in SGCAA for 24h. The induced cells were harvested and washed with PBS. The yeasts containing pYD1-ipaD were inoculated with rabbit anti-HA tag antibodies, while the yeasts containing pYD1-20ipaD, pYD1, or no plasmids were inoculated with rabbit anti-FLAG tag antibodies and BSA. After washed with PBS, the cells were inoculated with FITC-conjugated goat anti-rabbit immunoglobin antibodies and BSA without light. The cells were washed twice with PBS before imaged under UV-light. As Fig5 shows, the yeasts containing pYD1-ipaD and pYD1-20ipaD emitted green fluorescence, whereas the yeasts containing empty plasmids, or no plasmids did not. This fluorescence pattern proved the yeasts indeed expressed and displayed the nanobody and the antigen on their surfaces, which announced the success of engineering. y-fig-1 y-fig-2 y-fig3 y-fig4 y-fig5","breadcrumbs":"Project » Results » Yeast","id":"95","title":"Yeast"},"96":{"body":"","breadcrumbs":"Project » Results » Lactococcus lactis","id":"96","title":"Lactococcus lactis"},"97":{"body":"Summary of Experiment Design We plan to display the nanobody JPS-G3 agianst the Shigella antigen ipaD on the surface of E. coli Nissle 1917 via the curli fiber protein csg A [1] . We expect the engineered E. coli Nissle 1917 to be capable of capturing the pathogen Shigella flexneri via antigen-antibody specific binding. Plasmid Extraction pUC19-JPS-G3-3xHA and pUC19-ipaD-3xHA were extracted using the TIANGEN plasmid extraction kit. Target Sequence Amplification Using following primers ( Table 1 ), the JPS-G3-3xHA and ipaD-3xHA sequences were successfully amplified, and the results were verified by gel electrophoresis ( Figure 1 ). PCR products were purified for further manipulation. Table 1 | PCR Primers Used Name Sequence (5' -> 3') Endonuclease Site ipaD_FW CGCGGATCCATGAATATTACAACTC Bam HI ipaD_RV GGCCTCGAGTCAAGCGTAG Xho I JPS-G3_FW CGCGGATCCGGAAGTACACAAGTACAGCTAG Bam HI JPS-G3_RV CGCGGATCCGGAAGTACACAAGTACAGCTAG Xho I Figure 1 | Gel Electrophoresis Result for Target Sequence Amplification Molecular Cloning for Cytoplasmic Protein Expression In order to construct the recombinant plasmids pET30a-ipaD-3xHA and pET30a-JPS-G3-3xFLAG, the PCR products obtained from the last step were digested by endonucleases Bam HI and Xho I to create sticky ends. Meanwhile, the pET30a plasmids were transformed into E. coli DH5a competent cells for propagation. After transformation and overnight culture, the extracted plasmids were also digested with endonucleases Bam HI and Xho I to create sticky ends. Afterwards, the digested plasmids and target sequences were ligated and transformed into E. coli DH5a competent cells ( Figure 2 ). Figure 2 | Plates for pET30a-ipaD-3xHA (i-1 & i-2) and pET30a-JPS-G3-3xFLAG (J-1 & J-2). Single colonies were picked from the plates and the inserted sequence were verified by colony PCR ( Figure 3 ) and Sanger sequencing. Figure 3 | Gel Electrophoresis Result for Colony PCR Overlap Extension PCR In order to construct the recombinant DNA sequences csgA-JPS-G3-3xFLAG and csgA-ipaD-3xHA, the following overlap extension PCR primers are used ( Table 2 ). Table 2 | Overlap Extension PCR Primers Name Sequence (5' -> 3') Endonuclease Site OvF_csgA-shMT CCGCGTGGATCCATGAAACTTTTAAAAGTAG Bam HI OvR1_csgA-shMT TAGCTGTACTTGTGTACTTCCCCGCTGCCGCCGTACTGATGA / OvR2_csgA-shMT TAGTCAGAGTTGTAATATTCATCCGCTGCCGCCGTACTGATGA / OvF_JPS-G3 CATCAGTACGGCGGCAGCGGGGAAGTACACAAGTACAGCTAGC / OvR_JPS-G3 GAATCTCGAGTTATTTGTCGTCGTCATCC Xho I OvF_ipaD CATCAGTACGGCGGCAGCGGATGAATATTACAACTCTGACTAAT / OvR_ipaD GGCCTCGAGTCAAGCGTAGTCAGGTAC Xho I However, due to time limitation, this part has not been successfully implemented.","breadcrumbs":"Project » Results » Escherichia coli","id":"97","title":"Escherichia coli"},"98":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改)","breadcrumbs":"Project » Results » Project Achievements & Analysis Summary","id":"98","title":"Project Achievements & Analysis Summary"},"99":{"body":"Constructed the recombinant xxx plasmid, and transformed it into xxx strain. Expressed xxx protein. Effectiveness tested by xxx.","breadcrumbs":"Project » Results » 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Shigella, as one of the most antibiotic resistant pathogens, poses a great threat to food safety especially in developing areas. 10 million will be subject to mortalities caused by shigella infection by 2050. Distribution of antibiotics is the main treatment as of today. It is costly and time consuming. Side effects include degration of GI tract microbiome, and the emergence of more antibiotic resistant strains. We are in an endless race against pathogens. Antibiotics are our weapons. Mutations are their strategies to survival. Now, DKU iGEM team has proposed an alternative to jump out of this race and possibly, go far beyond. Antibody therapy is a popular topic in therapeutics. It is different from antibiotics and can be more effective when triggering the host immune system. However, conventional antibodies have a high cost because of the complicated synthesis procedure. It can also be vulnerable to proteosomes in the GI tract. Thus we propose a novel method to display nanobodies on the surface of probiotics. It exploits the natural pathogen inhibition effects of the probiotics. It also explores possibilities of antibody therapy mass production. Click on the left menu to learn more about the details.","breadcrumbs":"Home","id":"0","title":"Home"},"1":{"body":"","breadcrumbs":"Team » Team","id":"1","title":"Team"},"10":{"body":"Jiani Chen Yang Yu","breadcrumbs":"Team » Team » Advisor","id":"10","title":"Advisor"},"100":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161301 | Single Domain Antibody 20ipaD Conjugated Aga2 Express Module | http://parts.igem.org/Part:BBa_K4161301 | | BBa_K4161508 | Composite part | http://parts.igem.org/Part:BBa_K4161508 |","breadcrumbs":"Parts » Part Collection » Key composite segment","id":"100","title":"Key composite segment"},"101":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161302 | pYD1 plasmid | http://parts.igem.org/Part:BBa_K4161302 |","breadcrumbs":"Parts » Part Collection » Vector","id":"101","title":"Vector"},"102":{"body":"","breadcrumbs":"Parts » Improve","id":"102","title":"Parts"},"103":{"body":"","breadcrumbs":"Safety » Safety","id":"103","title":"Safety"},"104":{"body":"The Duke Kunshan University (DKU) iGEM team sets safety as an integral part of science. It includes protection for sensitive groups and the environment. For this reason, safety was considered from two perspectives—inside and outside the laboratory. For more detailed information, please check our safety form.","breadcrumbs":"Safety » Introduction","id":"104","title":"Introduction"},"105":{"body":"All laboratories of universities in China must be accredited by the Office under the Ministry of Environment following the standard. This year, the project was conducted in the BSL-1 laboratory. Team members wore lab coats and gloves during experiments. Experiments related to bacteria were performed in the biosafety cabinet and near butane burners. Before laboratory started, the team received safety training including how to use equipment properly, following laboratorial hygiene rules and proper disposal of hazardous substances. Also, experiments were first presented in detail by our two supervisors to eliminate biosafety concerns.","breadcrumbs":"Safety » Lab Safety","id":"105","title":"Lab Safety"},"106":{"body":"Protein expression for diagnostic tests was performed in non-pathogenic Escherichia coli strains (E.coli Nissle 1917), Lactococcus Lactis NZ9000 and yeast (EBY100). These gene carriers are probiotic or at least harmless. They do not possess serious illnesses or lead to other problems to people or the environment. In addition, they are in whitelist, belonging to BSL-1 organisms.","breadcrumbs":"Safety » Microorganisms review","id":"106","title":"Microorganisms review"},"107":{"body":"The engineered probiotics were designed to express 20ipad nanobody on their surface by transforming recombinant plasmids with optimized genes. Thus, they can combine with the antigen on the surface of Shigella. Since Shigella is one of the BSL-2 organisms, we decide to express our targeted antigen in probiotics that we used to express the antibody. We optimized the DNA sequences which code the antigen by using machine-learning software. Using yeast as an example, amino acids are essential for the growth of yeast. Amino acids are absorbed by human bodies in the small intestine. There is a competitive absorption of amino acids between intestinal epithelial cells and yeast. This prevents the overgrowth of yeast cells, preventing the destruction of bacterial flora structure. Using yeast as gene carriers limits the leak of antibiotics resistance genes, compared with using bacteria as carriers. In addition, galactose was used to induce the expression of the antibody and antigen. Since we used antibiotics resistance genes, we also pay attention to the potential risks of the leak of antibiotics resistance genes during wetlab process. Discarded liquids and plates that contain antibiotics were placed in specific vessels and then autoclaved.","breadcrumbs":"Safety » Experiments","id":"107","title":"Experiments"},"108":{"body":"Part of planned experiments had to be done by using harmful reagents or procedures. All team members follow the rules under the guideline provided by our lab manager and assistants during experiment safety training. UV light was used to sterilize the biosafety cabinets and equipment inside the cabinets. Safety measures were taken to avoid people`s direct exposure to UV light. Gel imaging system was used for visualizing agarose gel, combined with standard laboratory procedures with blue light transilluminator. Antibiotics were used to select transformants. They can be harmful to sensitive groups. Situations of allergy of team members were collected. Antibiotics were well stored and Handled with proper safety measures according to disposal protocols. Other hazardous chemicals , such as Tris-HCl and methyl alcohol were stored and relevant procedures were conducted in chemical ventilation cabinets. Liquid waste was handled with appropriate safety measures.","breadcrumbs":"Safety » Harmful reagents and procedures","id":"108","title":"Harmful reagents and procedures"},"109":{"body":"Team members followed all the government and university guidelines based on the pandemic situation of Covid-19 in China. For April and May, team`s meetings were online because of school closure and in-person activities were allowed after deblocking. Covid-19 tests were performed regularly and all team members got vaccinated. When wetlabs began, team members` attendance was recorded. The usage of lab equipment was registered. All working surfaces were cleaned with disinfectant fluid before and after conducting wetlabs.","breadcrumbs":"Safety » Covid-19 associated safety measures","id":"109","title":"Covid-19 associated safety measures"},"11":{"body":"Lingfeng Huang","breadcrumbs":"Team » Team » Principal Investigator","id":"11","title":"Principal Investigator"},"110":{"body":"","breadcrumbs":"Human Practices » Human Practice","id":"110","title":"Human Practice"},"111":{"body":"We interviewed Huansheng Cao, Assistant professor of Environmental Science at Duke Kunshan University for suggestions on our initial lab plans. In the interview, team members Yuxin Wang and Chang Shen presented the main design, bacterial surface display, to consult Prof Cao on its feasibility. After confirming the rich research foundations of our plan, he encouraged us to add computational elements to our lab design. As a scientist working in computational biology and bioinformatics, he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody and the antigen unit. As a well-trained biologist, he also suggested fitting our design to more than one model organisms, which shows integration in our drug design. The interview was full of enthusiasm, so we were able to come across many other topics. We discussed the trends in bioinformatics and biotechnology, including bacteria-based bioelectricity, and the relationship between human longevity and gut microbiota. This interview was both encouraging and informative, and contributed greatly to the first stage of human practice. photo","breadcrumbs":"Human Practices » Interview with Prof Cao","id":"111","title":"Interview with Prof Cao"},"112":{"body":"We participated in 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. It encourages students to participate in scientific research, technological development, and entrepreneurship. During the final pitch, Lisa Wu and Lingrui Lai made the presentation about our project of Shigella treatment using the concept of of synthetic biology. Lingrui went through the basic concept of shigella and synthetic biology, then, the current challenges that we are facing for shigella treatment and our suggestions. Lisa introduced the methodology involved and techniques used in our project. At the end they stressed the significance of our project. Judgers include Kai Huang (Division Chair of Natural and Applied Sciences of DKU), Joohyun Lee (Assistant professor of biology of DKU), Anastasia Tsigkou (Associate Professor of Biology of DKU), Ming-Chun Huang (Associate professor of data and computational science of DKU), Liqi Ren (Associate Director for Innovation and Entrepreneurship). After the presentation, Prof. Lee and Dr. Tsigkou presented valuable questions and suggestions. Prof. Lee recognized the difficulty of antibody therapy and informed us of the clear restrictions of FDI approval. We assured him that our project nanobodies are thoroughly researched, and that we will continue to modify the project to enhance biosafety. Dr. Tsigkou asked us about the binding affinity test and false positive. This is a question that did not come to us then, so we answered that the detection is conduct through fluorescence microscopy. After discussion with our PI, Prof. Linfeng Huang, we decide that we will use the pull down method in the detection of binding affinity. We will conduct the experiment by pulling down on both sides of the nanobody-antigen complex. For false positives, DKU iGEM member Lingrui Lai suggested isotype testing.","breadcrumbs":"Human Practices » 2022 College Student Innovation and Entrepreneurship Training Program","id":"112","title":"2022 College Student Innovation and Entrepreneurship Training Program"},"113":{"body":"After we successfully predicted the 3d structure of fusion protein-antibody complex by using Robetta and Alphafold2, the focus shift to how the fusion protein will influence the binding (docking) between antibody and antigen. We plan to get some insights about this from computer modeling before the wet lab begins. We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University for suggestions on our protein docking simulation. At the beginning, team leader Lisa Wu introduced the synthetic biology part of our project. Modeling team leader Zhenyu Xu introduced the progress of protein structure prediction and the need for protein docking simulation. As a scientist working in modern medicine, Prof. Floyd pointed us to some useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These software are powerful at predicting the docking scenario and are used by many researchers, with many online teaching resources accessible. To improve the speed of computer modeling, Prof. Floyd emphasized the preprocessing of protein structures. Namely, the antigen structure. He suggested us delete the floating molecules outside the binding sites and keep those inside, since we only care about the binding scenario. He also pointed that virtual screening could help if we want to do more mutations to the binding sites. Concerning the fusion protein-antibody complex models, since they are the optimal prediction given by Robetta and Alphafold2, we assume these models do not need preprocessing anymore. For docking, he suggested us try rigid docking first, and then flexible docking if we want to get closer to reality.","breadcrumbs":"Human Practices » Interview with Prof Floyd","id":"113","title":"Interview with Prof Floyd"},"114":{"body":"In order to have better educational effect and promote our project , we organized the Journal Club activity in the Duke Kunshan community. The first Journal Club was held on April 30th, 2022. At the very beginning of the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us and introduced in detail what systems biology is and the basic methods of studying systems biology. This journal club event mainly focused on COVID-19 and then developed into three sub-topics including the antigen test for SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the iGEM team, around 10 freshman students with various backgrounds participated in the sharing and raised many inspiring questions.","breadcrumbs":"Human Practices » Journal Club","id":"114","title":"Journal Club"},"115":{"body":"","breadcrumbs":"Human Practices » Interview with Dr. Neel Joshi","id":"115","title":"Interview with Dr. Neel Joshi"},"116":{"body":"Dr. Neel Joshi is an expert in bioengineering with tracks in human disease and new therapies. In his 2019 and 2021 literature, he and his team described genetically engineering E. coli Nissle 1917 to treat some gastrointestinal diseases like bowel inflammation, which provide essential references for our project. To further understand the logics and advantages of this bioengineered model, we invited Dr. Joshi for an interview. Dr. Joshi interview photo 1","breadcrumbs":"Human Practices » Introduction","id":"116","title":"Introduction"},"117":{"body":"Q: What stimulated you and your team to develop the surface-displaced single domain antibodies? What practical problems do you think this model can solve? A: Although the nanobodies have great potentials in treating gastrointestinal diseases, it is somewhat hard to deliver those nanobodies directly to the digestive track. Therefore, the probiotics can serve as a scaffold to make the delivery of nanobodies easy. Q: But why did you choose to display the nanobodies on the surface? Why not directly make the bacteria synthesize nanobodies and release them? A: The surface display resolution has the property of multi-valency. By displaying the nanobodies on the surface, we would have the potential to space the binding domains together to bind to a pathogen surface. It could increase binding affinity and decrease the dissociation constant. It can also diffusion into different directions and increase the local concentration. Q: What about the method of drug delivery? That is to say, how do you decide to send the engineered probiotics to human gastrointestinal track? And could you explain why you use that delivery method? A: We only proposed an approach of micro biological therapy. But to deliver the bacteria, I think it can be freeze-dried to produce a freeze-dried product. Because a large portion of the geographical locations that suffered from these gut problems are the poor areas, and those areas do not have the condition to store the bacteria that require a very low temperature. The freeze-dried products do not require that strict storage conditions, so they are more available in those areas. Q: Why pBbB8k plasmid backbone with kanamycin selection marker? (what's the difference between pUC19, which is our choice, and pBbB8K?) A: pBbB8k is a rather arbitrary choice, we simply chose it because it was used due to antibiotics incompatibility in the previous experiment. When doing in vivo studies, we engineered plasmids from the original E. coli Nissle genome, the pMUT plasmids. These plasmids are more stable than the pBbB8K. For pUC19, I don’t see problems with the expression of pUC19 plasmid. However, you do need to consider if your antibiotic resistant marker in the plasmid is compatible with the shigella testing. If shigella is killed due to the antibiotic selecting E. coli, it can be a problem. Q: What are the setbacks of the Probiotic-associated therapeutic curli hybrids (PATCH) system? A: The first is safety concerns of curli fibers. It has been known that curli fibers induce various types of diseases, including neurological diseases, etc. The other is inherit disadvantages for E. coli to produce curli fibers in vivo. However, we have been able to shown effective production of curli fiber in vivo by measuring the amount of curli fibers coming from the fecal samples. Q: What if the E. coli went out of control and grow infinitely in the gut, disrupting the original gastrointestinal microorganism environment? A: This is a very popular question when it comes to distributing microbes to gut. Actually, we could use some of the auxotrophic strains to limit the growth of the bacteria. And I think there are many “switches†that can turn on the suicide program of those bacteria. But in this case, I think E. coli Nissle 1917 is a very safe bacteria, it has already been identified as a harmless bacterium, so there should be less safety issues of this strain.","breadcrumbs":"Human Practices » Interview Content","id":"117","title":"Interview Content"},"118":{"body":"Q: Is it possible to apply magnetic triggers to shigella infection and cooperate this into the PATCH system? A: Magnetic triggers are mostly applied in cancer treatment. This is because in cancer, you know the spot of the disease. In bacterial infection it’s hard to locate. Q: In Barta et al., the authors described the different indexes of the nanobodies, including binding domains and neutralization effects. What is your rationale when choosing the nanobodies? A: It really depends on how you generate the nanobodies. When different parts of the pathogen are used in Alpaca immunizations, the nanobodies will vary. When displaying the nanobodies, some work and others don’t. We assume this is because of folding problems, but we did not figure out the exact reason. Q: What do you think about sequence optimization in silica? Do you have experience working with this? Do you have any suggestions? A: I would suggest generating different mutations in the sequence and do some docking analysis. Then generate the mutations and do wet labs. Q: Our project aims to tackle the antibiotic resistance problem worldwide. Would the PATCH system generate drug resistance issues? A: This is possible. For example, a mutation in the binding domain of the antigen might cause binding problems. However, I would say the selective pressure by the nanobody is smaller compared to that of the antibiotic. This is because antibiotic kills the pathogen, while PATCH only binds to the pathogen, keeping it from invasive activities. Q: We are worried that the proteins in the GI tract environment would coat the surface of the probiotic, which would cause dysfunction of the nanobodies. How did your team encounter this problem? A: The animal model was effective, which was sufficient to show that the GI tract environment did not inhibit the binding activity. The curli production is continuous in vivo, which provides adequate chance for the binding to occur. However, the proteases in the GI tract is something to consider.","breadcrumbs":"Human Practices » Q&A Section","id":"118","title":"Q&A Section"},"119":{"body":"Dr. Joshi provided lots of perspectives from a brand-new aspect, which were extra inspirable for the whole team. First, Dr. Joshi elaborated on the practical problems that this model could potentially resolve. That the probiotic expression system could make the delivery of nanobodies easier expanded our understanding of the model as the delivery problem does not only exist in the step of bacteria delivery, it starts from the delivery of the essential nanobodies. Next, the freeze-dry delivery approach gives a less stricter storage condition of this drug, making it more available in poor areas, which corresponds with our assumed delivery method. As for the safety problem that the public is most interested in, Dr. Joshi proposed to use some molecular switches to eliminate those bacteria in addition to using safe strains like Nissle, giving important clue and indication for our project design. In the Q&A section, questions regarding drug localization, drug resistance, choice of nanobodies were mentioned by team members. Dr. Joshi gave many valuable advices depending on the questions. Overall, the interview was successful, and we were able to arm ourselves with adequate knowledge for the wet lab.","breadcrumbs":"Human Practices » Summary and Reflection","id":"119","title":"Summary and Reflection"},"12":{"body":"","breadcrumbs":"Team » Team » The whole team","id":"12","title":"The whole team"},"120":{"body":"Club expo figure 1 We participated in 2022 online DKU club expo, introducing IGEM club to international students. Our club is meant to share knowledge and techniques of biosynthesis and to seek for potential team members of DKU IGEM team next year. The relevant club activities are conducted in the form of student presentation and speeches given by guest speakers. The IGEM team composition has also been introduced to DKU students from class of 2026. We divided IGEM teamwork into 4 parts, biological experiments, modelling, wiki design and human practice. For the offline club expo, we also made a small presentation to spread common knowledge about probiotics and provided our advice for consuming commercial probiotic products. Our central idea is that the aim of commercial probiotic products should be limited to minor gut discomforts or hoping to improve general health, and long-term consumption is not suggested by doctors we consulted. Also, we introduced some potential harms of consuming probiotics, trying to give them a full image of the commonly advertised probiotic products. We brought some experimental equipment, such as microcentrifuge tubes and plates, to introduce some basic experimental skills. Students who attended the club expo got basic knowledge of how to streak in an agar plate and how to use micropipette and centrifuge machines. Besides providing basic knowledge and doing the offline presentation, we prepared some interesting questions related to Biology and gut microbiomes for college students from all majors. They were designed to enlarge their knowledge about gut microbiomes and make biology interesting. The questions include \"how H. pylori were proved to be able to cause ulcers,\" \"pick out the probiotics from several names of microorganisms,\" \"estimate the number of microorganisms in their stomach,\" and so on. Club expo figure 2","breadcrumbs":"Human Practices » Club Expo","id":"120","title":"Club Expo"},"121":{"body":"","breadcrumbs":"Human Practices » GI tract & Probiotics Brochure","id":"121","title":"GI tract & Probiotics Brochure"},"122":{"body":"The human GI (Gastrointestinal) tract consists of stomach (pH = 2), small intestine (pH = 4-5), and large intestine (pH = 7), which comprises 200 m^2 of surface area in total ( Figure 1 ). It is responsible for the digestion of food and absorption of nutrients. Figure_1 Figure 1 | The GI tract. [1]","breadcrumbs":"Human Practices » GI Tract","id":"122","title":"GI Tract"},"123":{"body":"A normal functioning human body contains the visible human organs, such as the heart, lung, brain etc. containing 10^-14 cells (~23000 genes), and the invisible microbiome, which is a group of up to 10^-14 million microbes (~9 million genes) that live in your body. These bacteria help with digestion, destroys harmful bacteria, and helps control your immune system. The interaction between the host (human) and its microbiota is complex; thus, knowing the human microbiome helps with the development of biomarkers for predicting predisposition to diseases, designing targeted therapies, personalized drug therapies and probiotics. Figure_2 Figure 2 | Oversight of major microbial populations in the body sites sampled by human microbiome projects. [2] The GI microbiota contains 10^13 to 10^14 microbial cells. Microbes in gut affect early development, health, and predisposition to disease. The microbial colonization of gut begins at birth. As is shown in Figure 2 , from sampling data of the human microbiome project, in the GI tract, the species Bacteroidetes and Firmicutes have the highest abundance, followed by Proteobacteria , Tenericutes , and others. The microbial population in different areas of the GI tract are influenced by diet and the physical conditions in the area. In the stomach and small intestine, the low pH level prevents the growth and colonization of many microbials; however, Firmicutes , Bacteroidetes , and Actinobacteria are commonly found in the gastric fluid, while Firmicutes and Proteobacteria are common in the mucus layer of the stomach. Some pathogens, such as Helicobacter pylori , are also discovered in the gastric mucosa. Figure_3 Figure 3 | Different microenvironments in the large intestine. [2] The microbiome in the large intestine generally serves as an in vivo fermentation vessel, with the microbiota using nutrients derived from the digestion of food ( Figure 3 ). The essential biochemical and metabolic contributions of intestinal microorganisms contain different types of vitamins (e.g., thiamine, riboflavin, pyridoxine, B12, K, etc.), amino acids (e.g., asparagine, glutamate, methionine, etc.), gases (e.g., CO2, CH4, H2), odor, organic acids, glycosidase reactions, and steroid metabolism. As a result, the pathological changes in the GI tract microbiome may lead to deficiencies in important metabolic reactions (e.g., lack of vitamin B12 may lead to pernicious anemia – the red blood cells cannot function well).","breadcrumbs":"Human Practices » GI Microbiome","id":"123","title":"GI Microbiome"},"124":{"body":"Currently, physicians usually recommend using antibiotics when treating GI tract bacterial infections. However, since antibiotics usually also kill the beneficial microbiota, it increases the risk of developing IBD (inflammatory bowel disease) after treatment. IBD is characterized of chronic inflammation of the GI tract, which may result in irreversible damage. In addition, some antibiotics can cause ADR (adverse drug reaction) and allergies. Therefore, the development of alternative treatment methods, such as the use of probiotics, have attracted much attention. Unlike antibiotics, probiotics do not kill all the bacteria in an unbolted way. They help inhibit the growth of pathogens and preserve the healthy microbiota via competitive exclusion, anti-adherence, etc. Recently, engineered probiotics have also become a hot topic for new drug development.","breadcrumbs":"Human Practices » GI Microbiome, Antibiotics, and Probiotics","id":"124","title":"GI Microbiome, Antibiotics, and Probiotics"},"125":{"body":"Brock, T. D., Madigan, M. T., Martinko, J. M., & Parker, J. (2003). Brock biology of microorganisms. Upper Saddle River (NJ): Prentice-Hall, 2003. Peate, I. (2018). Anatomy and physiology, 9. The gastrointestinal system. British Journal of Healthcare Assistants, 12(3), 110–114. https://doi.org/10.12968/bjha.2018.12.3.110","breadcrumbs":"Human Practices » Reference","id":"125","title":"Reference"},"126":{"body":"photo Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo In GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo In probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Education","id":"126","title":"Education"},"127":{"body":"photo Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo In GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo In probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Education » Education","id":"127","title":"Education"},"128":{"body":"","breadcrumbs":"Awards » Entrepreneurship","id":"128","title":"Awards"},"129":{"body":"","breadcrumbs":"Awards » Hardware","id":"129","title":"Awards"},"13":{"body":"","breadcrumbs":"Team » Attributions » Attributions","id":"13","title":"Attributions"},"130":{"body":"","breadcrumbs":"Awards » Inclusivity","id":"130","title":"Awards"},"131":{"body":"","breadcrumbs":"Awards » Measurement","id":"131","title":"Awards"},"132":{"body":"Models are powerful tools in terms of imagining reasonable future scenarios. Also, assumptions and results from the model push us to reflect on the present situation and make adjustments to our existing plans and experiments, which might also develop our final goal into a more realistic version. There are 2 modeling sections in our project: Visualization This section mainly shows the structure of proteins and their docking results, and also tries to provide guides for future experiment design. Description and Prediction of durg efficacy This section mainly describes the efficiency of protein expression, and tries to predict the scenario after a patient takes the drug.","breadcrumbs":"Awards » Model » Model","id":"132","title":"Model"},"133":{"body":"","breadcrumbs":"Awards » Model » Visualization","id":"133","title":"Visualization"},"134":{"body":"We used online softwares to help us visualize the 3D protein structures and modeled their docking scenarios, and then we evaluated their stability by using some common parameters. This section aims to visually display the protein structure synthesized in this project and provide ideas or directions for future experiments or experimental teams","breadcrumbs":"Awards » Model » Overview:","id":"134","title":"Overview:"},"135":{"body":"Our team designed DNA sequences for fusion protein-nanobody complex ourselves and these newly designed protein's 3D structures are unknown. A protein's 3D structure determines its functionality, which, in our case, would be the nanobody's docking on the membrane and its binding to the antigen. Protein structure prediction Based on the amino acid sequence of the protein, various algorithms can predict the protein's 3D structure. These algorithms use machine learning to learn from databases of known amino acid sequences and structures. It would intuitively indicate whether the designs are feasible by checking their structures. Prediction service We use Robetta and AlphaFold to predict the structure of the proteins we designed. Robetta [1] is an online public service to predict protein structure. It is based on the algorithms of Rosetta from the Rosetta Commons. Robetta is a protein structure prediction server developed by the Baker lab at the University of Washington. At it's core is the Rosetta macromolecular modeling suite developed by the Rosetta Commons, a multi-institutional collaborative research and software development group. Robetta's primary service is to predict the 3-dimensional structure of a protein given the amino acid sequence. AlphaFold [2] is a prediction software that can structure the 3D model of a protein based on its amino acid sequence, using a combination of bioinformatics and physical approaches. We run models on AlphaFold (Phenix version) [3] Colab notebook and it will automatically give the highest-scoring model. This Colab notebook is derived from ColabFold [4] and the DeepMind AlphaFold2 Colab [5] Robetta [1] and AlphaFold Colab notebook [3] both accept single-letter code amino acid sequences and generate Protein Database (PDB) files, which contains information about the protein's structure. Robetta produces 5 models of different configuration with same score for each sequence. Alphafold automatically produces the model with highest score. We view these pdb files in PyMOL [6] , a powerful tool for 3D structure visualization. Protein structure evaluation Assessment of these resultant structures from Robetta and Alphafold2 is needed for deciding which structure is more credible and can be used in future anlysis. There are several parameters to consider: ramachandran plot, overall G-factors, atomic Z-score RMS, percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, overall quality factor, and Z-score. We use online server SAVES v6.0 [7] and ProSA [8] for the validation. Parameters Ramachandran plot: Ramachandran plot shows the theoretical conformation of amino acid residues and is mainly used to evaluate the model quality after homologous modeling. It considers whether the conformation of amino acids is reasonable. Based on an analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions. [7] Atomic Z-score RMS: Z-score root mean square deviation (Z-score RMS) measures the \"average magnitude of the volume irregularities in the structure.\" [9] Z-score RMS for a good model should be around 1.0. Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile: Indicate whether the atomic model is compatible with its amino acid sequence. It should be higher than 80% for a good model. [7] Overall quality factor: An overall score for the model provided by SAVES server [7] , ranging from 0 to 100. It should be higher than 80 for a good model. Z-score: Indicate whether the z-score of the input structure is within the range of scores typically found for native proteins of similar size [8] . All the structures shown later are the highest scoring structures. Protein structure alignment After the evaluation of models we got from Robetta [1] and AlphaFold Colab notebook [3] , we can compare the antibody structure in the model with its original structure by using PyMOL [6] alignment. If RMSD (root mean square deviation) value is very low, we regard two structures similar, which means the nanobody in our fusion-nanobody complex will theoretically function well.","breadcrumbs":"Awards » Model » Part 1: General pattern","id":"135","title":"Part 1: General pattern"},"136":{"body":"We have successfully expressed the fusion protein-nanobody complex, which is Yeast-20ipaD. Here is the highest-scoring structure of Yeast-20ipaD ( Figure 1 ). Figure 1 | 3D structure of Yeast-20ipaD complex Ramachandran plot of the above structure showed that 85.1% of residues are in the most favorite regions, and 11.9% are in the allowed regions; 1.9% of the residues are in the generously allowed regions and 1.1% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.536, which is a little bit out of range. A very good model would have a value close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 92.39%. The overall quality factor is 82.89, which is acceptable. ProSA calculated Z-score is -8.7, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure can be regarded as a good model of Yeast-20ipaD. Figure 2 | Alignment of 20ipaD between itself in complex and it's original structure. The alignment between 20ipaD in the complex and 20ipaD's original structure shows that our complex can have good effect theoretically ( Figure 2 ). The RMSD value is tested to be 0.807, which means the complex have little influence on the structure of 20ipaD.","breadcrumbs":"Awards » Model » Part 2: Yeast-20ipaD visualization","id":"136","title":"Part 2: Yeast-20ipaD visualization"},"137":{"body":"Interaction imformation (binding sites) of 20ipaD and ipaD is found in the paper: Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion [10] . Since the alignment shows that the 20ipaD in complex is almost the same with it's original structure, we can default the binding sites unchanged. Below is the binding sites between 20ipaD and ipaD ( Figure 3 ). Figure 3 | Binding sites between 20ipaD and Ipad We provided the interaction information for online server HADDOCK [11] to simulate the docking between the complex and ipaD. Below is the docking structure ( Figure 4 ). Figure 4 | Docking between 20ipaD (in complex) and IpaD Ramachandran plot of the above structure showed that 85.0% of residues are in the most favorite regions, and 12.7% are in the allowed regions; 1.2% of the residues are in the generously allowed regions and 1.0% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.441, which is relatively close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 87.61%. The overall quality factor is 85.53, which is acceptable. ProSA calculated Z-score is -7.16, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure indicates that 20ipaD can bind with IpaD well theoretically. Below is the alignment between our docking result and the original docking between 20ipaD and IpaD. RMSD is 0.36, which is very small and acceptable. Figure 5 | Alignment between Yeast-20ipaD-IpaD and 20ipaD-IpaD. All the above shows that our Yeast-20ipaD complex could theoretically work well when binding with IpaD.","breadcrumbs":"Awards » Model » Part 3: Docking modeling","id":"137","title":"Part 3: Docking modeling"},"138":{"body":"In this section, we would like to show other possible combinations of fusion protein-nanobody complex that might theoretically function well. To do this, we modeled their 3D structures and their docking scenarios, and analyzed them. This could be helpful for future experiment and future teams. Robetta https://robetta.bakerlab.org AlphaFold https://www.nature.com/articles/s41586-021-03819-2 AlphaFold(Phenix Version) <https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf old2/AlphaFold2.ipynb> ColabFold <https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol d2.ipynb> AlphaFold2 <https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks /AlphaFold.ipynb> PyMOL https://pymol.org/2/ SAVES https://saves.mbi.ucla.edu/ Prosa https://prosa.services.came.sbg.ac.at/prosa.php Deviations from standard atomic volumes as a quality measure for protein crystal structures <https://pubmed.ncbi.nlm.nih.gov/8950272/#:~:text=Deviations%20of%20the%20atomic %20volumes%20from%20the%20standard,magnitude%20of%20the%20volume%20irregularitie s%20in%20the%20structure.> HADDOCK online server https://wenmr.science.uu.nl/haddock2.4/ Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion. DOI: 10.1074/jbc.M117.802231 https://pubmed.ncbi.nlm.nih.gov/28842484/","breadcrumbs":"Awards » Model » Part 4: Other combinations of probiotic-nanobody complex","id":"138","title":"Part 4: Other combinations of probiotic-nanobody complex"},"139":{"body":"","breadcrumbs":"Awards » Model » Description and Prediction of drug efficacy","id":"139","title":"Description and Prediction of drug efficacy"},"14":{"body":"","breadcrumbs":"Team » Attributions » Biology team","id":"14","title":"Biology team"},"140":{"body":"Wet lab results showed that we have successfully expressed 20ipaD on the surface of Yeast. Our goal is to describe efficiency of expression and predict the scenario after the drug is released in the patient's jejunal.","breadcrumbs":"Awards » Model » Overview:","id":"140","title":"Overview:"},"141":{"body":"To describe how efficient is Yeast concerning the expression of 20ipaD, we manually calculated the efficiency by counting the number of Yeast cells that expressed 20ipaD and the total number of Yeast cells ( Figure 1 ). Figure 1 | Fluorescent cells for Yeast cells that obviously expressed 20ipaD. Dark cells for no or very little expression","breadcrumbs":"Awards » Model » Part 1: Protein expression efficiency","id":"141","title":"Part 1: Protein expression efficiency"},"142":{"body":"","breadcrumbs":"Awards » Model » Part 2: Prediction of post-medication scenario","id":"142","title":"Part 2: Prediction of post-medication scenario"},"143":{"body":"","breadcrumbs":"Awards » Plant","id":"143","title":"Awards"},"144":{"body":"","breadcrumbs":"Awards » Software","id":"144","title":"Awards"},"145":{"body":"","breadcrumbs":"Awards » Sustainable » Sustainable Development Goals (SDGs)","id":"145","title":"Sustainable Development Goals (SDGs)"},"146":{"body":"Scientific research has always had far-reaching significance in our study and daily routine, and even in the development of the whole society. Scientific research can comprehend us a better understanding of the nature and properties of matter. Analyzing the research objects elaboratively can accelerate the development of human knowledge accumulation. Our project follows a shared blueprint for peace and prosperity for people and the planet whose heart is the 17 sustainable development goals (UN, 2022). We respond to the urgent call for action by all countries that end poverty and other deprivations, improve health and education, reduce inequality, and spur economic growth (UN, 2022). This year, our team aims to provide a biological method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . Our method can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity while having stronger pathogen inhibition compared to traditional probiotic treatment (Langdon et al., 2016). Project “GutGuard†is mainly based on Goals 3, 9, 17","breadcrumbs":"Awards » Sustainable » Introduction","id":"146","title":"Introduction"},"147":{"body":"Ensure healthy lives and promoting well-being for all persons with disabilities We prospect our team’s project can make our local community and even the world conscious of the prominence of life and health, especially the gut problem. The gut problem may cause a person to struggle to absorb nutrients and regulate blood sugar. Additionally, weight loss or gain may be caused by bacteria overgrowth or lack of nutrients. The current therapeutics is antibiotics and the potential problem with the usage of antibiotics is that taking antibiotics too often or for the wrong reasons can change bacteria so much that antibiotics do not work against them (Cronan, 2019). Moreover, long-term use of antibiotics in late adulthood may be a risk factor for all-cause and cardiovascular mortality (Heianza, 2020). As the current therapies of antibiotics promote Shigella to develop antibiotic resistance, we are inspired by this problem and focus on shigella’s drug. Reducing antibiotic resistance and minimizing the side effects including the degradation of GI tract microbiome diversity can be achieved compared to the traditional probiotic treatment (Langdon et al., 2016). We mainly worked toward contributing to target 3.5 (Strength the prevention and treatment of substance abuse, including narcotic drug abuse and harmful use of alcohol) (UN, 2022).","breadcrumbs":"Awards » Sustainable » Goal 3| Good health and well-being","id":"147","title":"Goal 3| Good health and well-being"},"148":{"body":"Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation We are capable to lead a new approach and ideologically telling certain product developers to dare to innovate and not to stick to antibiotics to create drugs. To contribute to the goal, we aimed at target 9.5 (Enhance scientific research, upgrade the technological capabilities of industrial sectors in all countries, in particular developing countries, including, by 2030, encouraging innovation and substantially increasing the number of research and development workers per 1 million people and public and private research and development spending) (UN, 2022). We proposed a novel scientific solution to an existing global problem. We mainly focused on a novel method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . While meeting the goal, our laboratory team did various ways (using three different cells for trial: E. coli, Yeast and Lactococcus lactis) to achieve and increase the possibility of success. Additionally, our team collaborates with other iGEM teams from developing countries to contribute to scientific advancement there.","breadcrumbs":"Awards » Sustainable » Goal 9| Industry, Innovation and Infrastructure","id":"148","title":"Goal 9| Industry, Innovation and Infrastructure"},"149":{"body":"Strengthen the means of implementation and revitalize the global partnership for sustainable development We, as a team, share and hold the view of win-win cooperation. We know that iGEM is not just a competition, but a platform for mutual communication and cooperation. We welcome various teams coming from different backgrounds and help to create solutions to the question. Our team strictly followed target 17.16 (Enhance the global partnership for sustainable development, complemented by multi-stakeholder partnerships that mobilize and share knowledge, expertise, technology, and financial resources, to support the achievement of the sustainable development goals in all countries, in particular developing countries.) (UN, 2022). Our team played an active part in collaborating with other iGEM teams (LZU and XJLTU) to gain insights into local society and comprehend more knowledge. This kind of collaboration enriched us and ensured the sharing of knowledge and raising of awareness on both sides.","breadcrumbs":"Awards » Sustainable » Goal 17| Partnerships for the goals","id":"149","title":"Goal 17| Partnerships for the goals"},"15":{"body":"Biology Team leader. In charge of wet lab organization and human practice organizations. Designed the overall topic and approach of the problem to tackle with synthetic biology design. Designer of E.coli csgA surface display and lab experiments of the E. coli group.","breadcrumbs":"Team » Attributions » Yixuan Wu (Lisa)","id":"15","title":"Yixuan Wu (Lisa)"},"150":{"body":"To sum up, we address and fulfill sustainable development goals 3, 9, and 17 . While meeting the goal of displaying nanobodies on the surface of the probiotics to battle antibiotic-resistant pathogens, we can also contribute to improved healthcare globally in the sustainable development aspect. It can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity. The inhibition of the pathogen will be stronger compared to traditional probiotic treatment. Our methods are easy to use and can be improved for further applications.","breadcrumbs":"Awards » Sustainable » Conclusion","id":"150","title":"Conclusion"},"151":{"body":"United Nations. (2022). The 17 goals | sustainable development. United Nations. https://sdgs.un.org/goals United Nations. (2022). #ENVISION2030: 17 goals to transform the world for persons with disabilities enable. United Nations. https://www.un.org/development/desa/disabilities/envision2030.html Langdon, A., Crook, N., & Dantas, G. (2016, April 13). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome medicine. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831151/ Cronan, K. M. (Ed.). (2019, July). The danger of antibiotic overuse (for parents) - nemours kidshealth. KidsHealth. Retrieved September 28, 2022, from https://kidshealth.org/en/parents/antibiotic-overuse.html Heianza, Y., Ma, W., Li, X., Cao, Y., Chan, A. T., Rimm, E. B., Hu, F. B., Rexrode, K. M., Manson, J. A. E., & Qi, L. (2020). Duration and life-stage of antibiotic use and risks of all-cause and cause-specific mortality. Circulation Research, 126(3), 364–373. https://doi.org/10.1161/circresaha.119.315279","breadcrumbs":"Awards » Sustainable » References","id":"151","title":"References"},"152":{"body":"Attribution 4.0 International (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/ ======================================================================= Creative Commons Corporation (\"Creative Commons\") is not a law firm and does not provide legal services or legal advice. Distribution of Creative Commons public licenses does not create a lawyer-client or other relationship. Creative Commons makes its licenses and related information available on an \"as-is\" basis. Creative Commons gives no warranties regarding its licenses, any material licensed under their terms and conditions, or any related information. Creative Commons disclaims all liability for damages resulting from their use to the fullest extent possible. 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Except for the limited purpose of indicating that material is shared under a Creative Commons public license or as otherwise permitted by the Creative Commons policies published at creativecommons.org/policies, Creative Commons does not authorize the use of the trademark \"Creative Commons\" or any other trademark or logo of Creative Commons without its prior written consent including, without limitation, in connection with any unauthorized modifications to any of its public licenses or any other arrangements, understandings, or agreements concerning use of licensed material. For the avoidance of doubt, this paragraph does not form part of the public licenses. Creative Commons may be contacted at creativecommons.org.","breadcrumbs":"LICENSE","id":"152","title":"LICENSE"},"16":{"body":"Co-established the project topic. In charge of lab design and wet lab for the yeast group. Also assisted in Wiki writing and expert interview.","breadcrumbs":"Team » Attributions » Yuxin Wang","id":"16","title":"Yuxin Wang"},"17":{"body":"In charge of background research, E. coli group lab design, wet labs & wiki writing. Hosted journal clubs and science lectures for human practice.","breadcrumbs":"Team » Attributions » Yunyi Ru","id":"17","title":"Yunyi Ru"},"18":{"body":"Designed lactococcus lab procedures and in charge of lactococcus and yeast lab experiments. Conducted expert interviews for human practice.","breadcrumbs":"Team » Attributions » Zhujun Yao","id":"18","title":"Zhujun Yao"},"19":{"body":"Proposed the project topic, participated in plasmid design and workflow design of E.coli group, participated in wet labs and background research. Helped conduct collaboration with XJLTU as a part of human practice.","breadcrumbs":"Team » Attributions » Chang Shen","id":"19","title":"Chang Shen"},"2":{"body":"Yixuan Wu (Lisa) Yixuan Liu Sihan Wang Zhujun Yao Lingrui Lai Yuxin Wang Jingyun Jin Chang Shen Yunyi Ru Renwei Gao Qizhou Jiang","breadcrumbs":"Team » Biology","id":"2","title":"Biology"},"20":{"body":"Responsible for wet lab design and experiment for yeast group. Contribute to Human Practice with Conference of China iGEMer Community.","breadcrumbs":"Team » Attributions » Lingrui Lai","id":"20","title":"Lingrui Lai"},"21":{"body":"Helped conduct human practices and wetlabs for the yeast group. Designed the safety and education wiki and organized local high school activities education.","breadcrumbs":"Team » Attributions » Qizhou Jiang","id":"21","title":"Qizhou Jiang"},"22":{"body":"Helped with background research, designed lab detection protocols for the lactococcus group, conducted wetlab experiments, helped with human practice organization including journal club organization and wiki writing.","breadcrumbs":"Team » Attributions » Sihan Wang","id":"22","title":"Sihan Wang"},"23":{"body":"Organized and chaired the iGEM2022 Journal Club Seminar ever since 2021. Actively participate in human practice part including designing and popularizing events in local collegiate school. Help conduct wet labs.","breadcrumbs":"Team » Attributions » Yixuan Liu","id":"23","title":"Yixuan Liu"},"24":{"body":"Fund manager of the team, in charge of labware purchasing, helped with background research and survey distribution as a part of human practice.","breadcrumbs":"Team » Attributions » Renwei Gao","id":"24","title":"Renwei Gao"},"25":{"body":"Helped design survey as a part of human practice, helped with E. coli wet lab experiments.","breadcrumbs":"Team » Attributions » Jingyun Jin","id":"25","title":"Jingyun Jin"},"26":{"body":"","breadcrumbs":"Team » Attributions » Modeling team","id":"26","title":"Modeling team"},"27":{"body":"Organized protein structure and docking modeling. Helped conduct human practice. Shot and edited the promotion video. Wiki writing.","breadcrumbs":"Team » Attributions » Zhenyu Xu","id":"27","title":"Zhenyu Xu"},"28":{"body":"Main Wiki developer and technical support. Built the Wiki infrastructure. Set up and maintains the GitLab repository for team communication and Wiki editing. Introduced Git and GitLab to the team and helped the team adopt to the workflow on GitLab. Helped with protein modeling using RoseTTAFold, Robetta, and PyMOL.","breadcrumbs":"Team » Attributions » Sichang He (Steven)","id":"28","title":"Sichang He (Steven)"},"29":{"body":"Conceptualized cell surface display technology project during preliminary brainstorming and provided proof of concept through review of related literature. Wrote the project abstract and refined general methodology framework. Built protein models for candidate microbes via Alphafold and Haddock and evaluated fidelity of each model via quantiative metrics. Modelled growth of chosen microbe model computationally.","breadcrumbs":"Team » Attributions » Jasmine Santos","id":"29","title":"Jasmine Santos"},"3":{"body":"Sichang He (Steven) Jasmine Santos Yuxiang He Zhenyu Xu","breadcrumbs":"Team » Modeling","id":"3","title":"Modeling"},"30":{"body":"Built a 3D model for the drug delivery system.","breadcrumbs":"Team » Attributions » Yuxiang He","id":"30","title":"Yuxiang He"},"31":{"body":"","breadcrumbs":"Team » Attributions » Advising support","id":"31","title":"Advising support"},"32":{"body":"Overall project advising, principal investigator.","breadcrumbs":"Team » Attributions » Linfeng Huang","id":"32","title":"Linfeng Huang"},"33":{"body":"Oversee wet lab experiments and overall project advising.","breadcrumbs":"Team » Attributions » Jiani Chen","id":"33","title":"Jiani Chen"},"34":{"body":"Oversee wet lab experiments, helped optimize lab protocols and troubleshooting.","breadcrumbs":"Team » Attributions » Yang Yu","id":"34","title":"Yang Yu"},"35":{"body":"Thanks to the generous funding support of Duke Kunshan University Natural Science Divisions, Wang-Cai Biochemistry Lab, Synear Food Molecular Biology Lab, DKU Innovation and Entrepreneurship Initiative, and Marcia B. France, DKU Dean of Undergraduate Studies. Thanks to free licenses provided by SnapGene.","breadcrumbs":"Team » Attributions » Funding support","id":"35","title":"Funding support"},"36":{"body":"Thanks to Dr. Floyd Beckford and Dr. Huansheng Cao at Duke Kunshan University, Dr. Neel Joshi from Northwestern University, and Dr. Jisheng Lin at Sinovac Biotech CO.,LTD. for providing effective advice on our project design and development.","breadcrumbs":"Team » Attributions » Communications support","id":"36","title":"Communications support"},"37":{"body":"We collaborated with LZU, another iGEM team focusing on probiotics, on education. We found that there are many misleading claims about probiotics and their effects in the market, so we planned to conduct science promotion in local areas to improve people's understanding of probiotics. We chose a local international university to give a lecture on science popularization, and more than 300 middle and high school students and teachers attended.","breadcrumbs":"Team » Collaborations » Collaborations","id":"37","title":"Collaborations"},"38":{"body":"","breadcrumbs":"Project » Communication","id":"38","title":"Communication"},"39":{"body":"We had science communications during different stages of our project. We designed these communications to have different manner, audience and scope, aiming at informing, educating, raising awareness of the topic of Gastrointestinal health, and increasing the sense of wonder about fighting against antibiotic resistance.","breadcrumbs":"Project » Overview","id":"39","title":"Overview"},"4":{"body":"Jiani Chen Yang Yu","breadcrumbs":"Team » Advisor","id":"4","title":"Advisor"},"40":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Socially-Oriented Questionnaire","id":"40","title":"Socially-Oriented Questionnaire"},"41":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus. In addition, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating.","breadcrumbs":"Project » On-Campus Communication","id":"41","title":"On-Campus Communication"},"42":{"body":"In order to carry out science communications on a larger scale, we participated the 9th CCiC Conference (Conference of China iGEMer Community), which is a national summit independently initiated by Chinese iGEM teams, aiming to provide a platform for iGEM teams to share resources and promote mutual learning and communication. We made poster and presented at the conference, answering questions from the audience and judges. After the conference, we collaborated with team LZU on science popularization about probiotics.","breadcrumbs":"Project » CCiC: iGEM community in China","id":"42","title":"CCiC: iGEM community in China"},"43":{"body":"In the later stage of the experiment, in order to better promote the knowledge of synthetic biology and gastrointestinal health in the local area, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers.We distributed science manuals to everyone in the audience and introduced the GI tract, dysentery, probiotic therapy, and antibiotic resistance.","breadcrumbs":"Project » Local School Education","id":"43","title":"Local School Education"},"44":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the communication and cooperation with other Chinese IGEM teams enabled us to learn more knowledge, and also to understand the current issues of synthetic biology in China that deserve attention. The science popularization and education in local schools also gave us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Project » Summary","id":"44","title":"Summary"},"45":{"body":"","breadcrumbs":"Project » Communication » Communication","id":"45","title":"Communication"},"46":{"body":"We had science communications during different stages of our project. We designed these communications to have different manner, audience and scope, aiming at informing, educating, raising awareness of the topic of Gastrointestinal health, and increasing the sense of wonder about fighting against antibiotic resistance.","breadcrumbs":"Project » Communication » Overview","id":"46","title":"Overview"},"47":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Communication » Socially-Oriented Questionnaire","id":"47","title":"Socially-Oriented Questionnaire"},"48":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus. In addition, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating.","breadcrumbs":"Project » Communication » On-Campus Communication","id":"48","title":"On-Campus Communication"},"49":{"body":"In order to carry out science communications on a larger scale, we participated the 9th CCiC Conference (Conference of China iGEMer Community), which is a national summit independently initiated by Chinese iGEM teams, aiming to provide a platform for iGEM teams to share resources and promote mutual learning and communication. We made poster and presented at the conference, answering questions from the audience and judges. After the conference, we collaborated with team LZU on science popularization about probiotics.","breadcrumbs":"Project » Communication » CCiC: iGEM community in China","id":"49","title":"CCiC: iGEM community in China"},"5":{"body":"Lingfeng Huang","breadcrumbs":"Team » Principal Investigator","id":"5","title":"Principal Investigator"},"50":{"body":"In the later stage of the experiment, in order to better promote the knowledge of synthetic biology and gastrointestinal health in the local area, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers.We distributed science manuals to everyone in the audience and introduced the GI tract, dysentery, probiotic therapy, and antibiotic resistance.","breadcrumbs":"Project » Communication » Local School Education","id":"50","title":"Local School Education"},"51":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the communication and cooperation with other Chinese IGEM teams enabled us to learn more knowledge, and also to understand the current issues of synthetic biology in China that deserve attention. The science popularization and education in local schools also gave us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Project » Communication » Summary","id":"51","title":"Summary"},"52":{"body":"We designed cell surface display platforms for probiotics including yeast, E. coli Nissle 1917, and L. lactis . To be specific, the yeast Aga2 surface display platform for nanobodies were developed, We also designed a novel way to detect protein surface expression by using flow cytometry. Another contribution is protein modeling protocol. We designed an integrated protocol involving the usage of PyMol, RobeTTA, and Alphafold2. Through literature review, we were able to determine multiple parameters that measure the accuracy of the protein model, and conducted evaluation on our protein design.","breadcrumbs":"Project » Contribution » Contribution","id":"52","title":"Contribution"},"53":{"body":"Cell surface display platforms can be utilized to cater to many protein engineering and therapeutic drug design purposes. In our case, the therapeutic effect and the nanobody localization on the cellular membrane of yeast yields future possibilities for iGEM teams to utilize this surface display platform based on the yeast Aga2 protein, specifically for therapeutic designs, but possible to be utilized to express other proteins as well.","breadcrumbs":"Project » Contribution » Cell surface display platforms","id":"53","title":"Cell surface display platforms"},"54":{"body":"Online programs are helpful for visualizing and analyzing the structure of different proteins and their docking scenarios. We use Robetta and Alphafold2 to model the structures of our protein, and used HADDOCK to visualize the docking structure. Evaluation focuses on different parameters: Ramachandran plot, Overall G-factors, Atomic Z-score RMS, Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, Overall quality factor, and Z-score. These parameters determine whether a certain structure is stable.","breadcrumbs":"Project » Contribution » Integrated protein modeling protocol","id":"54","title":"Integrated protein modeling protocol"},"55":{"body":"The Shigella species is listed as one of the eight dangerous drug resistant bacteria [1] , with associated mortalities projected to rise to 10 million globally by 2050. The use of conventional antibiotics aggravates the multidrug resistance of most Shigella strains. Besides aiding in the selection of resistant pathogens, antibiotics reduce intestinal species diversity and population, and disrupt the defensive, metabolic, and trophic functions of interdependent microbes [2] . Engineered probiotics with cell surface display systems are promising in tackling this problem due to a weaker selective pressure and specific binding proteins that are less likely to disrupt the host gut microbiome. Through literature review, E. coli Nissle 1917, yeast and L. lactis are chosen for expression because their probiotic nature present no known harm to the GI tract and the convenience in lab culturing. Centers for Disease Control and Prevention. (2019). 2019 AR Threats Report. https://www.cdc.gov/drugresistance/biggest-threats.html Francino, M. P. (2016, January 1). Antibiotics and the human gut microbiome: Dysbioses and accumulation of resistances. Frontiers. Retrieved March 28, 2022, from https://www.frontiersin.org/articles/10.3389/fmicb.2015.01543/full","breadcrumbs":"Project » Description » Project Description","id":"55","title":"Project Description"},"56":{"body":"","breadcrumbs":"Project » Engineering » Engineering Cycle","id":"56","title":"Engineering Cycle"},"57":{"body":"This page will give a detailed explanation about the engineering cycle. To make yeast capable of displaying the target nanobody 20ipaD on the cell surface, 20ipaD gene was inserted behind the yeast membrane-sealed protein Aga 2; therefore, Aga 2 would bring the nanobody to the cell surface. The recombinant plasmid pYD1-20ipaD was successfully built, which was supported by PCR amplification data and sequencing data. Apart from yeast, Lactococcus lactis and Escherichia coli were also chosen as probiotics for surface displace of nanobodies at the beginning, where 20ipaD/JPS-G3 and control 3xFLAG tags were inserted into pNZ8148 (L. lactis) and pET30a (E. coli) for expression respectively. However, due to failure in transformation and plasmid construction, only yeast was selected as the final product.","breadcrumbs":"Project » Engineering » Introduction","id":"57","title":"Introduction"},"58":{"body":"","breadcrumbs":"Project » Engineering » Engineering Cycle","id":"58","title":"Engineering Cycle"},"59":{"body":"Cycle 1 Design We located a single-domain antibody (VHH) named 20ipaD from the database, whose binding ability with the needle tip protein ipaD of Shigella type III secretion system has be testified (Barta et al., 2017; Sierocki et al., 2021). Peptide sequences of 20ipaD from Barta et al (2017). Codon optimization was performed to get DNA sequences. Two flank sequences containing XhoI and ApaI cutting sites as well as C-terminal Flag-tag were added to the ipaD DNA sequence. Build Designed 20ipaD sequences were chemically de novo synthesized and sent in pUC19. XhoI and ApaI double-digestion enabled us to ligate the 20ipaD DNA sequence into pYD1, a plasmid allowing the surface display of the gene it carries in yeast. The ligation of 20ipaD into pYD1 generates a DNA sequencing coding a recombinant protein of 20ipaD and Aga2, a yeast extracellular membrane protein. pYD1 also contained a replication origin recognized by bacteria and an ampicillin resistance gene. After plasmid ligation, recombinant plasmids were transferred into E. coli to get a clone via ampicillin selection. Cloned plasmids were then transferred into yeast cells. Yeast cells containing the plasmid were selected by tryptophane-deficient medium. Expression of the recombinant protein was induced by add galactose. Test After transformation of recombinant plasmid into E. coli and single colony collection, we perform enzyme digestion and gel electrophoresis to check if the ligation and transformation is successful. For expression assay, we incubated induced yeast cells with anti-flag-tag primary antibody. After incubating with FITC conjugated secondary antibody, cells were examined under florescence microscopy and flow cytometry. Learn Recombinant proteins were observed to express on the cell surfaces on a portion of the cell population. We therefore planned to further testify the effectiveness of our recombinant protein. Though previous modeling through Rosetta suggested that the recombinant Aga2 region as well as the linkers sequences do not undermine the correct folding of the VHH part, we still sought for a experimental support as well as a way to quantify the binding affinity. Cycle 2 Design In this cycle, we aimed to test binding affinity between the recombinant nanobody and the ipaD epitopes. ipaD were retrieved from NCBI database. Codon optimization was also performed to collect the DNA sequence. Similar to 20ipaD, flank regions were inserted into ipaD except the substitution of Flag-tag to HA-tag. Build Synthesized ipaD sequences were got from the same company. Using the same method, we expressed ipaD recombinant protein of the yeast surface. Test Learn Cycle 3 Design In this cycle, we aims to improve the expression level of the recombinant protein. Energy flows within the yeast cells would be controlled to concentrate more on protein production rather than other metabolic activities. We started by looking for a strong and continuously expressed promoter to drive the expression of 20ipaD recombinant protein. At the same time, we also tried to reduce other cellular activities. Cycle 4 Design In this cycle, we aims to improve the binding affinity of the recombinant protein with the antigen epitope. We would perform error prone PCRs to introduce mutations into 20ipaD sequences. Concentrations of the nucleotide analogs would be controlled so that only point mutants would be produced. All mutants would be screened to identify binding affinity improvements. To reduce the workload of screening, we would perform a modeling prescreen. In the prescreen, we would predict how single amino acid change influence the binding affinity between 20ipaD and ipaD.","breadcrumbs":"Project » Engineering » Yeast","id":"59","title":"Yeast"},"6":{"body":"","breadcrumbs":"Team » The whole team","id":"6","title":"The whole team"},"60":{"body":"Cycle 1 Design At first, we wanted to obtain the sequence of both 20ipaD and control flag-tag so that we could amplify them via PCR reaction. The 20ipaD is one of the single-VH domain antibodies (VHHs) capable of recognizing distinct epitopes within the antigen IpaD of pathogen Shigella. In this way, we hoped that by fusing 20ipaD and control flag-tag into the Lactococcus lactis expression vector pNZ8148, we would achieve the surface display and expression of 20ipaD on Lactococcus lactis . Build To obtain the sequence of 20ipaD, we constructed the plasmid with the 20ipaD sequence surrounded by two different restriction sites of enzymes BamHI and SacI. In this way, through the restrictive digestion of Bam HI and Sac I, ideally the sequence of 20ipaD would be obtained. The similar construction was also applied with the sequence of control flag-tag, where the enzymes used for restrictive digestion were changed to be NcoI and HindIII. Test After successfully received the synthesized plasmid sequence for 20ipaD and control flag-tag, we conducted the digestion of BamHI and SacI for the obtain of 20ipaD sequence, and the digestion of Nco I and Hind III for the obtain of control flag-tag sequence. Gel electrophorese was applied to confirm the size of the sequence. Control flag-tag sequence was successfully obtained. However, according to the gel picture, the band of 20ipaD showed a very different size from that in theory. Learn We checked the source of error and found that the designed sequence of 20ipaD has been inserted into the pUC19 vector when being synthesized by the company. Unfortunately, pUC19 vector also contained a restriction site for BamHI itself, thus leading to a different enzymatic digestion than what we have expected before. Cycle 2 Design Since pUC19 vector also contained a restriction site for BamHI itself, which would lead to unspecific enzymatic digestion and the failure of getting 20ipaD sequence, we redesigned the experimental steps in order to overcome such a problem. Build In this try, we would do the PCR amplification of 20ipaD sequence to insert it directly into the pNZ8148 vector first. This would circumvent the enzymatic digestion of pUC19 vector by BamHI that had the insertion of 20ipaD. Learn From this process we learnt that when the synthesized plasmid went wrong from our expectations, apart from directly asking the company to redo the synthesis, we could also alter the steps of ligation via PCR reaction to solve the problem. Cycle 3 Design We wanted to insert the engineered pNZ8148 vector with 20ipaD into the strain Lactococcus lactis NZ9000. According to literature review, electroporation is the commonly used technique to insert vectors into Lactococcus lactis . Build When the OD600 of Lactococcus lactis reached 0.3, the bacteria would be subjected to electroporation. The bacteria would be washed with liquid detergent I containing 0.5mol∙L-1 sucrose and 10% glycerol for the insertion of 0.2 μg vector. The pulse of electroporation was delivered by a Gene-Pulser (Scientz) at 25μF and 2.5kV, while the electroporation cuvette (0.2cm in size) was connected in parallel to a 400-Ω resistor (the parameters were searched online and were consulted from technician at Scientz). According to multiple researches done previously, the transformation efficiency would be the highest is the recovery time is 1.5h after electroporation. Test The process of electroporation was not successful because we failed to insert the vector into Lactococcus lactis . Learn We suspect that the making of electrocompetent cells might be the source of failure. After checking with the team advisor, we found that the type of glycerol used was intended for protein purification, which could cause problems for the electrocompetent cell. Cycle 4 Design To further increase efficiency, after doing more literature reviews we added the pretreatment of Lactococcus lactis with lithium acetate (LiAc) and/or dithiothreitol (DTT). We also substituted the type of glycerol used based on the previous error analysis. Build According to the newly found protocol, the Lactococcus lactis was firstly suspended at room temperature for 30 min in 8ml of 100mM LiAc, 10mM DTT, 0.6M sucrose, and 10mM Tris-HCl (pH=7.5). Following the treatment, Lactococcus lactis was pelleted and was resuspended in 1.5ml microcentrifuge tube, and was then washed as previously described. Afterwards, electroporation was conducted as previously described.","breadcrumbs":"Project » Engineering » Lactococcus lactis","id":"60","title":"Lactococcus lactis"},"61":{"body":"E. coli Engineering Cycle Cycle 1 Design Initially, we planned to try three different nanobodies (20ipaD, JPS-G3, and JMK-H2) agianst the Shigella antigen ipaD from a research paper [1] . We also wanted to try two different surface display systems, beta domain of the E. coli outer membrane protein intimin [2] and the E. coli curli fiber protein, csg B [3] . Our target probiotic is E. coli Nissle 1917 [3] . By inserting the target nanobody sequence behind intimin or csg B, reconstructing the plasmid pET30a and transforming the plasmid into E. coli Nissle 1917, we expect the protein to be displayed on the surface of E. coli , so that it can capture the pathogen via antigen-antibody binding. Build & Test We designed the following sequences to make the recombinant protein. intimin-20ipaD-3xFLAG csgB-JMK-H2-3xFLAG JPS-G3-3xFLAG ipaD-3xHA However, due to limitations in budget & time for gene synthesis, we only have JPS-G3-3xFLAG and ipaD-3xHA (inserted into pUC19 plasmids). By plasmid extraction, double digestion ( Bam HI & Xho I) and PCR, we successfully obtained the sequences and verified the accuracy by Sanger sequencing, but we don't have csgB or intimin for surface display. Learn Complex sequences including potential harmful genes may impact synthesis efficiency. Cycle 2 Design Alternatively, we chose the curli fiber csg A [4] sequence for surface display. Build & Test We designed the following sequences: csgA-JPS-G3-3xFLAG csgA-ipaD-3xHA (displaying the antigen on the surface of E. coli BL21 to mimic Shigella flexneri , so that the effectiveness can be evaluated) csg A gene is obtained from the E. coli strains (pGEX-4T-1-csgA-shMT) provided by the XJLTU iGEM team via PCR. To connect different parts, we plan to use overlapping PCR.","breadcrumbs":"Project » Engineering » Escherichia coli","id":"61","title":"Escherichia coli"},"62":{"body":"Barta, M., Shearer, J., Arizmendi, O., Tremblay, J., Mehzabeen, N., Zheng, Q., . . . Picking, W. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. Journal of Biological Chemistry , 292, jbc.M117.802231. doi:10.1074/jbc.M117.802231 Salema, V., MarÃn, E., MartÃnez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., Teira, X., Gutierrez, C., Bodelón, G., & Fernández, L. Ã. (2013). Selection of Single Domain Antibodies from Immune Libraries Displayed on the Surface of E. coli Cells with Two β-Domains of Opposite Topologies. PLoS ONE , 8(9), e75126. https://doi.org/10.1371/journal.pone.0075126 Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998 Barta, M. L., Shearer, J. P., Arizmendi, O., Tremblay, J. M., Mehzabeen, N., Zheng, Q., Battaile, K. P., Lovell, S., Tzipori, S., Picking, W. D., Shoemaker, C. B., & Picking, W. L. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem, 292(40), 16677-16687. https://doi.org/10.1074/jbc.M117.802231 Sierocki, R., Jneid, B., Orsini Delgado, M. L., Plaisance, M., Maillere, B., Nozach, H., & Simon, S. (2021). An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLoS Negl Trop Dis, 15(3), e0009231. https://doi.org/10.1371/journal.pntd.0009231","breadcrumbs":"Project » Engineering » Reference","id":"62","title":"Reference"},"63":{"body":"","breadcrumbs":"Project » Experiments » Experiment","id":"63","title":"Experiment"},"64":{"body":"This page will give a detailed record about the experiment process, including the lab notes and protocols.","breadcrumbs":"Project » Experiments » Introduction","id":"64","title":"Introduction"},"65":{"body":"","breadcrumbs":"Project » Experiments » Experiment","id":"65","title":"Experiment"},"66":{"body":"Lab Notes Protocols","breadcrumbs":"Project » Experiments » Yeast","id":"66","title":"Yeast"},"67":{"body":"Lab Notes Protocols","breadcrumbs":"Project » Experiments » Lactococcus lactis","id":"67","title":"Lactococcus lactis"},"68":{"body":"Lab Notes Please see attached. E. coli Lab Notes Protocols Please see attached. E. coli Protocols","breadcrumbs":"Project » Experiments » Escherichia coli","id":"68","title":"Escherichia coli"},"69":{"body":"","breadcrumbs":"Project » Notebook","id":"69","title":"Project"},"7":{"body":"","breadcrumbs":"Team » Team » Team","id":"7","title":"Team"},"70":{"body":"","breadcrumbs":"Project » Implementation » Implementation","id":"70","title":"Implementation"},"71":{"body":"The end-products of our project are small tablets or capsules that contain dry powders of probiotics that express anti-Shigella antibodies on their surface. Our products serve the dual roles of Shigella infection precaution as well as disease therapy. The abilities of room temperature storage provide our tablets with cost reduction for storage and transportation. Tablets should be taken when facing potential exposure to Shigella infection sources, such as drinking unsanitary water in high diarrhea incidence areas. In consideration of the prevalent transmission pathways of Shigella, we also suggest people whose family members have developed Shigella infections and children in school with diarrhea cases take our tablets to prevent person-to-person transmission, which is the major form of Shigella spreading (Kotloff et al., 2018).","breadcrumbs":"Project » Implementation » Infection Precaution","id":"71","title":"Infection Precaution"},"72":{"body":"Due to intracellular pathogen nature of Shigella, the effect of antibodies reduces as pathogens evade into the cells. The ability of reprogramming the infected cells to form protrusion adjacent cells allows Shigella to spread within intestine epithelial cells, reducing the chance of exposing to body internal environment (Sansonetti et al., 1994). This special characteristic implies antibody may not be a one-size-fits-all solution for different stages of infection. We call for the combination of clinical phases of antibiotics treatment with our tablets together.","breadcrumbs":"Project » Implementation » Infection Therapy","id":"72","title":"Infection Therapy"},"73":{"body":"Along with the high household transmission rates, Shigella also display high secondary infection rates. Therefore, we suggest families with members developing Shigella to take our pills for a time period to provide continuously protection apart from keep good hygiene conditions. In the meanwhile, patients who have developed Shigella infection before should also take our tablets when facing a second exposure.","breadcrumbs":"Project » Implementation » Prognosis and Secondary infection","id":"73","title":"Prognosis and Secondary infection"},"74":{"body":"People who exposed to potential Shigella infection source, especially in a household environment. Children in school with Shigella cases reported. People with antibiotic allergy that cannot use clinical antibiotic treatment. Government that aims to provide low cost solution for Shigella incidence in low- and middle- income, less developed region.","breadcrumbs":"Project » Implementation » End Users","id":"74","title":"End Users"},"75":{"body":"Our product contains exogenous antibody proteins. Therefore, allergy test may need to be performed to prevent possible anaphylaxis. Besides, considering the pathogenesis and transmission pathway of Shigella, our products may not be a one-size-fits all solution for all infection stages but focuses more on the prevention of infection. Kotloff, K. L., Riddle, M. S., Platts-Mills, J. A., Pavlinac, P., & Zaidi, A. K. M. (2018). Shigellosis. The Lancet, 391(10122), 801-812. https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8 Sansonetti, P. J., Mounier, J., Prévost, M. C., & Mège, R.-M. (1994). Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell, 76(5), 829-839. https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1","breadcrumbs":"Project » Implementation » Caveats","id":"75","title":"Caveats"},"76":{"body":"","breadcrumbs":"Project » Partnership » Meeting with XJLTU","id":"76","title":"Meeting with XJLTU"},"77":{"body":"They plan to develop a biofilter core to replace current industry filter cores for heavy metal wastewater. Specifically, they plan to engineer E. coli to express csgA protein at high levels and immobilize the bacteria into a filter. In that way, the heavy metal ions in the wastewater can be captured by csgA protein that is expressed by E. coli located in the filter.","breadcrumbs":"Project » Partnership » XJLTU's Project","id":"77","title":"XJLTU's Project"},"78":{"body":"They would like to know how we will interact with and educate the public. A: We have made questionnaires to evaluate their knowledge related to antibiotics, probiotics, and microorganisms. We are also planning to make some handouts and deliver a lecture about it in a high school. They were interested in the specific design of our plasmids. Specifically, it's about how and why we choose each part of the plasmid for surface display. A: We applied three microorganisms and the whole team was divided into three groups, each responsible for E. coli, Yeast cell and Lactococcus lactis. All groups applied a strategy which conjugates the targeted nanobody with a surface protein that is to be expressed, transported and located to the extracellular space. The surface protein and the targeted nanobody were connected with a linker sequence, and each nanobody is marked with at least one protein tag for their identification. We also provided links to igem parts so they can check it directly.","breadcrumbs":"Project » Partnership » Questions & Advice From XJLTU:","id":"78","title":"Questions & Advice From XJLTU:"},"79":{"body":"Will the biofilter be blocked due to E. coli proliferation? A: The microorganisms are immobilized in filters, and the filtration condition may not allow E. coli to grow at such a speed. The csgA protein's ability to absorb heavy metal ions under different conditions (like pH) can be tested through experiments. For example, we can put csg protein into a certain amount of wastewater, then adjust the pH and check the remaining concentration of metal ions in time, so we can acquire a proper pH for the protein to capture heavy metal ions.","breadcrumbs":"Project » Partnership » Questions & Advice From DKU:","id":"79","title":"Questions & Advice From DKU:"},"8":{"body":"Yixuan Wu (Lisa) Yixuan Liu Sihan Wang Zhujun Yao Lingrui Lai Yuxin Wang Jingyun Jin Chang Shen Yunyi Ru Renwei Gao Qizhou Jiang","breadcrumbs":"Team » Team » Biology","id":"8","title":"Biology"},"80":{"body":"Model for bacteria growth The XJLTU team developed a model for predicting bacteria growth, and it may also be applied to our situation by adjusting some of the parameters. Quantified expression of csg through controlling IPTG concentration The XJLTU team intended to control the expression of csg protein by adjusting the amount of IPTG inducer, which can also be a helpful approach for our team to check the relationship between the cell-cell adhesion affinity and the number of expressed nanobodies. However, as we also applied the TlpA promotor, it may influence the actual expression to a great extent and cause a big difference from the theoretical calculation. As a result, this approach remains to be a concern. Detection and measurement of displayed csg protein. The XJLTU team controlled the expression level by adjusting inducer concentration and estimated the expression by calculating theoretically. The condition of csg and heavy metal ions after the death of E. coli cells We consider that the heavy metal ions will remain captured, as protein itself has a great affinity to the heavy metal ions. But, it remains to be seen whether the released protein will leak out from the filter.","breadcrumbs":"Project » Partnership » Discussion Topics:","id":"80","title":"Discussion Topics:"},"81":{"body":"","breadcrumbs":"Project » Proof of Concept","id":"81","title":"Project"},"82":{"body":"","breadcrumbs":"Project » Results » Results","id":"82","title":"Results"},"83":{"body":"This page will give a detailed record about the experiment results, future plans & project achievements.","breadcrumbs":"Project » Results » Introduction","id":"83","title":"Introduction"},"84":{"body":"","breadcrumbs":"Project » Results » Experiment Results","id":"84","title":"Experiment Results"},"85":{"body":"","breadcrumbs":"Project » Results » Yeast","id":"85","title":"Yeast"},"86":{"body":"","breadcrumbs":"Project » Results » Lactococcus lactis","id":"86","title":"Lactococcus lactis"},"87":{"body":"Summary of Experiment Design We plan to display the nanobody JPS-G3 agianst the Shigella antigen ipaD on the surface of E. coli Nissle 1917 via the curli fiber protein csg A [1] . We expect the engineered E. coli Nissle 1917 to be capable of capturing the pathogen Shigella flexneri via antigen-antibody specific binding. Please check the detailed experiment design at 'design' part. Plasmid Extraction pUC19-JPS-G3-3xHA and pUC19-ipaD-3xHA were extracted using the TIANGEN plasmid extraction kit. Target Sequence Amplification Using following primers ( Table 1 ), the JPS-G3-3xHA and ipaD-3xHA sequences were successfully amplified, and the results were verified by gel electrophoresis ( Figure 1 ). PCR products were purified for further manipulation. Table 1 | PCR Primers Used Name Sequence (5' -> 3') Endonuclease Site ipaD_FW CGCGGATCCATGAATATTACAACTC Bam HI ipaD_RV GGCCTCGAGTCAAGCGTAG Xho I JPS-G3_FW CGCGGATCCGGAAGTACACAAGTACAGCTAG Bam HI JPS-G3_RV CGCGGATCCGGAAGTACACAAGTACAGCTAG Xho I Figure 1 | Gel Electrophoresis Result for Target Sequence Amplification Molecular Cloning for Cytoplasmic Protein Expression In order to construct the recombinant plasmids pET30a-ipaD-3xHA and pET30a-JPS-G3-3xFLAG, the PCR products obtained from the last step were digested by endonucleases Bam HI and Xho I to create sticky ends. Meanwhile, the pET30a plasmids were transformed into E. coli DH5a competent cells for propagation. After transformation and overnight culture, the extracted plasmids were also digested with endonucleases Bam HI and Xho I to create sticky ends. Afterwards, the digested plasmids and target sequences were ligated and transformed into E. coli DH5a competent cells ( Figure 2 ). Figure 2 | Plates for pET30a-ipaD-3xHA (i-1 & i-2) and pET30a-JPS-G3-3xFLAG (J-1 & J-2). Single colonies were picked from the plates and the inserted sequence were verified by colony PCR ( Figure 3 ) and Sanger sequencing. Figure 3 | Gel Electrophoresis Result for Colony PCR Overlap Extension PCR In order to construct the recombinant DNA sequences csgA-JPS-G3-3xFLAG and csgA-ipaD-3xHA, the following overlap extension PCR primers are used ( Table 2 ). Table 2 | Overlap Extension PCR Primers Name Sequence (5' -> 3') Endonuclease Site OvF_csgA-shMT CCGCGTGGATCCATGAAACTTTTAAAAGTAG Bam HI OvR1_csgA-shMT TAGCTGTACTTGTGTACTTCCCCGCTGCCGCCGTACTGATGA / OvR2_csgA-shMT TAGTCAGAGTTGTAATATTCATCCGCTGCCGCCGTACTGATGA / OvF_JPS-G3 CATCAGTACGGCGGCAGCGGGGAAGTACACAAGTACAGCTAGC / OvR_JPS-G3 GAATCTCGAGTTATTTGTCGTCGTCATCC Xho I OvF_ipaD CATCAGTACGGCGGCAGCGGATGAATATTACAACTCTGACTAAT / OvR_ipaD GGCCTCGAGTCAAGCGTAGTCAGGTAC Xho I However, due to time limitation, this part has not been successfully implemented.","breadcrumbs":"Project » Results » Escherichia coli","id":"87","title":"Escherichia coli"},"88":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改)","breadcrumbs":"Project » Results » Project Achievements & Analysis Summary","id":"88","title":"Project Achievements & Analysis Summary"},"89":{"body":"Constructed the recombinant xxx plasmid, and transformed it into xxx strain. Expressed xxx protein. Effectiveness tested by xxx.","breadcrumbs":"Project » Results » Successes","id":"89","title":"Successes"},"9":{"body":"Sichang He (Steven) Jasmine Santos Yuxiang He Zhenyu Xu","breadcrumbs":"Team » Team » Modeling","id":"9","title":"Modeling"},"90":{"body":"Failed to construct and transform the recombinant plasmids in E. coli and L. lactis .","breadcrumbs":"Project » Results » Failures","id":"90","title":"Failures"},"91":{"body":"","breadcrumbs":"Project » Results » Inspirations","id":"91","title":"Inspirations"},"92":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改) Express proteins in well-studied probiotic strains. Insert nanobody sequences after other promoters that can ensure proper expression in vivo . Conduct hemolysis experiments to see the effectiveness of killing Shigella flexneri . Conduct in vivo experiments to test the therapeutic effects in rodent GI system.","breadcrumbs":"Project » Results » Future Plans","id":"92","title":"Future Plans"},"93":{"body":"Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998","breadcrumbs":"Project » Results » Reference","id":"93","title":"Reference"},"94":{"body":"All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Parts","id":"94","title":"Parts"},"95":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. Part Code Part name Website BBa_K4161501 T7 Promoter http://parts.igem.org/Part:BBa_K4161501 BBa_K4161502 GAL1 Promoter http://parts.igem.org/Part:BBa_K4161502 BBa_K4161503 Aga2 http://parts.igem.org/Part:BBa_K4161503 BBa_K4161504 G4S http://parts.igem.org/Part:BBa_K4161504 BBa_K4161505 T7, Xpress http://parts.igem.org/Part:BBa_K4161505 BBa_K4161506 ipaD http://parts.igem.org/Part:BBa_K4161506 BBa_K4161507 HA http://parts.igem.org/Part:BBa_K4161507","breadcrumbs":"Parts » Single element","id":"95","title":"Single element"},"96":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161301 | Single Domain Antibody 20ipaD Conjugated Aga2 Express Module | http://parts.igem.org/Part:BBa_K4161301 | | BBa_K4161508 | Composite part | http://parts.igem.org/Part:BBa_K4161508 |","breadcrumbs":"Parts » Key composite segment","id":"96","title":"Key composite segment"},"97":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. | Part Code | Part name | Website | |--------------|--------------------------------------------------------------|- ----------------------------------------| | BBa_K4161302 | pYD1 plasmid | http://parts.igem.org/Part:BBa_K4161302 |","breadcrumbs":"Parts » Vector","id":"97","title":"Vector"},"98":{"body":"All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Part Collection » Parts","id":"98","title":"Parts"},"99":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. 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Shigella, as one of the most antibiotic resistant pathogens, poses a great threat to food safety especially in developing areas. 10 million will be subject to mortalities caused by shigella infection by 2050. Distribution of antibiotics is the main treatment as of today. It is costly and time consuming. Side effects include degration of GI tract microbiome, and the emergence of more antibiotic resistant strains. We are in an endless race against pathogens. Antibiotics are our weapons. Mutations are their strategies to survival. Now, DKU iGEM team has proposed an alternative to jump out of this race and possibly, go far beyond. Antibody therapy is a popular topic in therapeutics. It is different from antibiotics and can be more effective when triggering the host immune system. However, conventional antibodies have a high cost because of the complicated synthesis procedure. It can also be vulnerable to proteosomes in the GI tract. Thus we propose a novel method to display nanobodies on the surface of probiotics. It exploits the natural pathogen inhibition effects of the probiotics. It also explores possibilities of antibody therapy mass production. Click on the left menu to learn more.","breadcrumbs":"Home","id":"0","title":"Home"},"1":{"body":"Team Yixuan Wu (Lisa) UG Class of 2024 Biology Yixuan Liu UG Class of 2024 Biology Sihan Wang UG Class of 2023 Biology Zhujun Yao UG Class of 2024 Biology Lingrui Lai UG Class of 2023 Biology Yuxin Wang UG Class of 2025 Jingyun Jin UG Class of 2024 Biology Chang Shen UG Class of 2025 Yunyi Ru UG Class of 2023 Biology Renwei Gao UG Class of 2023 Biology Qizhou Jiang UG Class of 2025","breadcrumbs":"Team » Biology","id":"1","title":"Biology"},"10":{"body":"","breadcrumbs":"Team » Team » The whole team","id":"10","title":"The whole team"},"100":{"body":"Failed to construct and transform the recombinant plasmids in E. coli and L. lactis .","breadcrumbs":"Project » Results » Failures","id":"100","title":"Failures"},"101":{"body":"","breadcrumbs":"Project » Results » Inspirations","id":"101","title":"Inspirations"},"102":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改) Express proteins in well-studied probiotic strains. Insert nanobody sequences after other promoters that can ensure proper expression in vivo . Conduct hemolysis experiments to see the effectiveness of killing Shigella flexneri . Conduct in vivo experiments to test the therapeutic effects in rodent GI system.","breadcrumbs":"Project » Results » Future Plans","id":"102","title":"Future Plans"},"103":{"body":"Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998","breadcrumbs":"Project » Results » Reference","id":"103","title":"Reference"},"104":{"body":"Model Models are powerful tools in terms of imagining reasonable future scenarios. Also, assumptions and results from the model push us to reflect on the present situation and make adjustments to our existing plans and experiments, which might also develop our final goal into a more realistic version. There are 3 modeling sections in our project: Visualization This section mainly shows the structure of proteins and their docking results, and also tries to provide guides for future experiment design. Description and Prediction of durg efficacy This section mainly describes the efficiency of protein expression, and tries to predict the scenario after a patient takes the drug. Hardware This section shows the 3D model of the micro-capsule where Yeast cells are sealed in. The micro-capsule is made of shellac, and the pH-dependent solubility that prefers a mild basic environment makes shellac perfect for releasing probiotics in intestines.","breadcrumbs":"Model » Visualization","id":"104","title":"Visualization"},"105":{"body":"We used online softwares to help us visualize the 3D protein structures and modeled their docking scenarios, and then we evaluated their stability by using some common parameters. This section aims to visually display the protein structure synthesized in this project and provide ideas or directions for future experiments or experimental teams Part 1: General pattern Our team designed DNA sequences for fusion protein-nanobody complex ourselves and these newly designed protein's 3D structures are unknown. A protein's 3D structure determines its functionality, which, in our case, would be the nanobody's docking on the membrane and its binding to the antigen. Protein structure prediction Based on the amino acid sequence of the protein, various algorithms can predict the protein's 3D structure. These algorithms use machine learning to learn from databases of known amino acid sequences and structures. It would intuitively indicate whether the designs are feasible by checking their structures. Prediction service We use Robetta and AlphaFold to predict the structure of the proteins we designed. Robetta [1] is an online public service to predict protein structure. It is based on the algorithms of Rosetta from the Rosetta Commons. Robetta is a protein structure prediction server developed by the Baker lab at the University of Washington. At it's core is the Rosetta macromolecular modeling suite developed by the Rosetta Commons, a multi-institutional collaborative research and software development group. Robetta's primary service is to predict the 3-dimensional structure of a protein given the amino acid sequence. AlphaFold [2] is a prediction software that can structure the 3D model of a protein based on its amino acid sequence, using a combination of bioinformatics and physical approaches. We run models on AlphaFold (Phenix version) [3] Colab notebook and it will automatically give the highest-scoring model. This Colab notebook is derived from ColabFold [4] and the DeepMind AlphaFold2 Colab [5] Robetta [1] and AlphaFold Colab notebook [3] both accept single-letter code amino acid sequences and generate Protein Database (PDB) files, which contains information about the protein's structure. Robetta produces 5 models of different configuration with same score for each sequence. Alphafold automatically produces the model with highest score. We view these pdb files in PyMOL [6] , a powerful tool for 3D structure visualization. Protein structure evaluation Assessment of these resultant structures from Robetta and Alphafold2 is needed for deciding which structure is more credible and can be used in future anlysis. There are several parameters to consider: ramachandran plot, overall G-factors, atomic Z-score RMS, percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, overall quality factor, and Z-score. We use online server SAVES v6.0 [7] and ProSA [8] for the validation. Parameters Ramachandran plot: Ramachandran plot shows the theoretical conformation of amino acid residues and is mainly used to evaluate the model quality after homologous modeling. It considers whether the conformation of amino acids is reasonable. Based on an analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good quality model would be expected to have over 90% in the most favoured regions. [7] Atomic Z-score RMS: Z-score root mean square deviation (Z-score RMS) measures the \"average magnitude of the volume irregularities in the structure.\" [9] Z-score RMS for a good model should be around 1.0. Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile: Indicate whether the atomic model is compatible with its amino acid sequence. It should be higher than 80% for a good model. [7] Overall quality factor: An overall score for the model provided by SAVES server [7] , ranging from 0 to 100. It should be higher than 80 for a good model. [10] Z-score: Indicate whether the z-score of the input structure is within the range of scores typically found for native proteins of similar size [8] . All the structures shown later are the highest scoring structures. Protein structure alignment After the evaluation of models we got from Robetta [1] and AlphaFold Colab notebook [3] , we can compare the antibody structure in the model with its original structure by using PyMOL [6] alignment. If RMSD (root mean square deviation) value is very low, we regard two structures similar, which means the nanobody in our fusion-nanobody complex will theoretically function well. Part 2: Yeast-20ipaD visualization We have successfully expressed the fusion protein-nanobody complex, which is Yeast-20ipaD. Here is the highest-scoring structure of Yeast-20ipaD ( Figure 1 ). Figure 1 | 3D structure of Yeast-20ipaD complex Ramachandran plot of the above structure showed that 85.1% of residues are in the most favorite regions, and 11.9% are in the allowed regions; 1.9% of the residues are in the generously allowed regions and 1.1% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.536, which is a little bit out of range. A very good model would have a value close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 92.39%. The overall quality factor is 82.89, which is acceptable. ProSA calculated Z-score is -8.7, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure can be regarded as a good model of Yeast-20ipaD. Figure 2 | Alignment of 20ipaD between itself in complex and it's original structure. The alignment between 20ipaD in the complex and 20ipaD's original structure shows that our complex can have good effect theoretically ( Figure 2 ). The RMSD value is tested to be 0.807, which means the complex have little influence on the structure of 20ipaD. Part 3: Docking modeling Interaction imformation (binding sites) of 20ipaD and ipaD is found in the paper: Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion [11] . Since the alignment shows that the 20ipaD in complex is almost the same with it's original structure, we can default the binding sites unchanged. Below is the binding sites between 20ipaD and ipaD ( Figure 3 ). Figure 3 | Binding sites between 20ipaD and Ipad We provided the interaction information for online server HADDOCK [12] to simulate the docking between the complex and ipaD. Below is the docking structure ( Figure 4 ). Figure 4 | Docking between 20ipaD (in complex) and IpaD Ramachandran plot of the above structure showed that 85.0% of residues are in the most favorite regions, and 12.7% are in the allowed regions; 1.2% of the residues are in the generously allowed regions and 1.0% in the disallowed regions. The Atomic-Z-score RMS is tested to be 1.441, which is relatively close to 1. The percentage of the amino acids have scored >= 0.2 in the 3D/1D profile is 87.61%. The overall quality factor is 85.53, which is acceptable. ProSA calculated Z-score is -7.16, which falls in the range of scores typically found for experimentally determined (X-ray, NMR) structure for native proteins of similar size in PDB database. The calculated average energy over 40 residues is always under 0. Overall, the above structure indicates that 20ipaD can bind with IpaD well theoretically. Below is the alignment between our docking result and the original docking between 20ipaD and IpaD. RMSD is 0.36, which is very small and acceptable. Figure 5 | Alignment between Yeast-20ipaD-IpaD and 20ipaD-IpaD. All the above shows that our Yeast-20ipaD complex could theoretically work well when binding with IpaD. Part 4: Other combinations of probiotic-nanobody complex In this section, we would like to show other possible combinations of fusion protein-nanobody complex that might theoretically function well. To do this, we modeled their 3D structures and their docking scenarios, and analyzed them. This could be helpful for future experiment and future teams. Table 1 | Evaluation of other combinations of probiotic-nanobody complex The E. coli Intimin protein complex has good results in 4 out of 5 quantitative parameters, making it a great model. First, its Ramachandran plot reveals a good distribution in favored regions. 83% of its residues are in the core regions, 14.7% are in the allowed regions, 1.3% are in the general regions and 0.9% in the disallowed regions. Second, the % amino acids having scored 0.2 in 3D/1D profile is 85.91%, higher than the standard 80%. Its atomic model is therefore fairly compatible with its amino acid sequence. Third, its overall quality factor, that accounts for the error value of individual residue, is at 92, surpassing the 80 score cut-off. Its Z-score is also within the range of scores found for native proteins of similar size. The main downside to this model is that Z-score is not around one,showing that it has greater average magnitude of the volume irregularities in the structure. The E. coli CsgA protein complex is a good model that fulfills 4 out of 5 quantitative parameters. Like Intimin, CsgA’s Ramachandran plot displays a good distribution in favored regions: 83.5% of residues are in the core regions, 12.7% are in the allowed regions, 2.0% are in the general regions and 1.8% in the disallowed regions. The % amino acids having scored 0.2 in 3D/1D profile is 84.27%, higher than the standard 80% but not nearly as high as Intimin. Its overall quality factor is 91,exceeding the 80 score cut-off. The Z-score is within the range of scores found for native proteins of similar size, and like Intimin, the CsgA model’s Z-score is not around one. The Lacto tag 1 protein complex is a good model that fulfills 4 out of 5 quantitative parameters. CsgA’s Ramachandran plot displays a well enough distribution in favored regions: 83.1% of residues are in the core regions, 15.2% are in the allowed regions, 1.5% are in the general regions and 0.2% in the disallowed regions. The % of amino acids having scored 0.2 in 3D/1D profile is 79.97%, close enough to the standard 80% but comparatively low against Intimin and CsgA. Its overall quality factor is 92, surpassing the 80 score cut-off. The Z-score is within the range of scores found for native proteins of similar size, and similar to Intimin and CsGA, the CsgA model’s Z-score is not around one. Overall, all three protein docking jobs show satisfactory results and could be helpful for future experiments and future teams. In light of these promising findings, we encourage future researchers to test these models in the lab, with the E. coli Intimin model that performed the best among the three.","breadcrumbs":"Model » Overview:","id":"105","title":"Overview:"},"106":{"body":"To conclude, we have developed the best 3D model for Yeast-20ipaD and the docking structure between Yeast-20ipaD and IpaD. They are well analyzed and are decided to have good effect theoretically. Moreover, we modeled other 3 possible combinations of fusion protein and nanobody, which might serve as a guidance for future experiment design. Robetta https://robetta.bakerlab.org AlphaFold https://www.nature.com/articles/s41586-021-03819-2 AlphaFold(Phenix Version) < https://colab.research.google.com/github/phenix-project/Colabs/blob/main/alphaf old2/AlphaFold2.ipynb> ColabFold < https://colab.research.google.com/github/sokrypton/ColabFold/blob/main/AlphaFol d2.ipynb> AlphaFold2 < https://colab.research.google.com/github/deepmind/alphafold/blob/main/notebooks /AlphaFold.ipynb> PyMOL https://pymol.org/2/ SAVES https://saves.mbi.ucla.edu/ Prosa https://prosa.services.came.sbg.ac.at/prosa.php Deviations from standard atomic volumes as a quality measure for protein crystal structures https://pubmed.ncbi.nlm.nih.gov/8950272/ HADDOCK online server https://wenmr.science.uu.nl/haddock2.4/ Single-Domain Antibodies Pinpoint Potential Targets within Shigella Invasion Plasmid Antigen D of the Needle Tip Complex for Inhibition of Type III Secretion. DOI: 10.1074/jbc.M117.802231 https://pubmed.ncbi.nlm.nih.gov/28842484/ Homology modeling and virtual screening approaches to identify potent inhibitors of VEB-1 β-lactamase. DOI: 10.1186/1742-4682-10-22 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668210/","breadcrumbs":"Model » Summary","id":"106","title":"Summary"},"107":{"body":"","breadcrumbs":"Model » Description and Prediction of drug efficacy","id":"107","title":"Description and Prediction of drug efficacy"},"108":{"body":"Wet lab results showed that we have successfully expressed 20ipaD on the surface of Yeast. Our goal is to describe efficiency of expression and predict the scenario after the drug is released in the patient's jejunal. Part 1: Protein expression efficiency To describe how efficient is Yeast concerning the expression of 20ipaD, we manually calculated the efficiency by counting the number of Yeast cells that expressed 20ipaD and the total number of Yeast cells ( Figure 1 ).Through separated assessments conducted by two individuals, we found that our model has a 31.25% expression rate with a STD of ± 0.75. Figure 1 | Fluorescent cells for Yeast cells that obviously expressed 20ipaD. Dark cells for no or very little expression Part 2: Prediction of post-medication scenario In this section, we want to predict post-medication scenario by using math modeling. In detail, we want to see how will the number of floating Shigella change after the drug release, this will be depending on natural growth of Shigella, the binding efficiency of 20ipaD and IpaD, the concentration of Yeast cells, and the survival rate of Yeast cells. Yeast cells are sealed in micro-capsules made of shellac before being delivered into bodies. The pH-dependent solubility that prefers a mild basic environment makes shellac perfect for releasing probiotics in jejunal. There are several important assumptions for this model: Each floating Yeast cell carries one 20ipaD; Each floating Shigella cell carries one IpaD; Growth of Shigella cultured in BHI (Brian Heart Infusion) medium is similar with the growth of Shigella in human's jejunal; Each 20ipad binds with one IpaD once; Died Yeast cell cannot display 20ipaD and cannot bind with IpaD; Yeast growth is not considered here since a healthy immune system does not allow overgrowth of the yeast, and the growth of the yeast is very slow in neutral; or even slightly alkaline conditions [13] . Based on these assumptions, the following two equations describe the change in number of shigella and Yeast: dtdL′(t)​=dtdL(t)​−βL(t)D(t) dtD(t)​=γL(t)D(t) L′(t): the log count of the number of shigella in jejunal at time t after drug release; L(t): the log count of the number of shigella in jejunal at time t before drug release; β: the binding efficiency between 20ipaD and IpaD; D(t): the log count of number of Yeast in jejunal at time t after drug release; γ:survival rate of Yeast in jejunal Detail: The natural growth of shigella in jejunal can be described in the form of Gompertz equation [14] : L(t)=A+Cexp[−exp(−B(t−M))] L(t): the log count of the number of shigella in jejunal at time t before drug release; A: the asymptotic log count as t decreases indefinitely; C: the asymptotic amount of growth (log number) that occurs as t increases indefinitely; M: the time at which the absolute growth rate is maximum; B: the relative growth rate at M Parameters A, C, M,and B depend on the environmental conditions: temperature T, pH, and sodium chloride concentration c. In our case, T is defaulted to 37 degrees; the pH is about 6.9 in jejunal and about 7.2 in ileal [15] ; c in jejunal is about 112mM [16] . Translate the concentration into the form of percentage: 100mlxg​58.44g1mol​1L1000ml​=0.012M x=0.65 So, the concentration of sodium chloride is about 0.65% in jejunal. Gompertz equation parameters and calculated growth curve values for Shigella can be found in the paper: Effect of Sodium Chloride, pH and Temperature on Growth of Shigella flexneri [14] . Parameters in our situation do not perfectly fit the calculated ones, but they do fall in a certain range: Lower limit: T=37 degrees, pH=6.5, c=0.5% A=4.53, B=0.493, C=4.47, M=3.68 L(t)=4.53+4.47exp[−exp(−0.493(t−3.68))] dtL(t)​=2.20exp[−exp(−0.493(x−3.68))−0.493(x−3.68)] Higher limit: T=37 degrees, pH=7.5, c=0.5% A=4.26, B=0.435, C=5.41, M=4.54 L(t)=4.26+5.41exp[−exp(−0.435(t−4.54))] dtL(t)​=2.35exp[−exp(−0.435(x−4.54))−0.435(x−4.54)] Since our situation is in this range, so we can have an upper limit and lower limit for the growth scenario of Shigella ( Figure 2 ). Figure 2 | Upper limit and lower limit for Shigella's natural growth in jejunal. The x axis indicates the time with unit of hour; the y axis indicates the log count of number of Shigella. The survival rate of Yeast cells in jejunal varies with time ( Figure 3 ) [15] . Figure 3 | Survival rate of Yeast cells in jejunal with time of digestion. The survival rate is highest at t=2h, when 30.8% of intake Yeast cells are viable. Then, the viability decreases with time, finally 13% of intake Yeast cells are viable at 5h. Part 3: Medication guidance Our drug is designed to 'kill' the Shigella before it invades the surface of jejunal, or more realistically, to decrease the concentration of floating Shigella so that a mass invasion could be avoided or stopped as soon as possible. Based on the information from wet-lab and math modeling, we would like to give a possible conclusion or a medication guidance for the patients and the managers of the healthcare system, so that our vision could be realized. For a single micro-capsule, assume it contains at least 10 billion CFU (colony-forming unit) [17] , then it contains at least 10 billion live Yeast cells. Since the expression rate is about 31.25%, there would be at least 3 billion live Yeast cells that expressed at least one 20ipaD on each of their surfaces. After the capsule reaches jejunal, it will dissolve and start to release Yeast cells. After 2 hours, there will be about 0.9 billion Yeast cells (30.8% of the intake) that are viable to display 20ipaD and bind with IpaD. For Shigella, since the upper limit and lower limit of natural growth are found, we can calculate the maximum population density in the following form: Densitymax​(log10​cfu/ml)=A+C So the uppper limit of the max density at t=5h will be about 5 billion Shigella, and the lower limit will be about 1 billion Shigella. Therefore, it is proper to take 5-6 capsules every 5 hours after the patient start to have symptoms, and distribute 1-5 capsules every 5 hours to the people who might develop symptoms due to living togethor or common life styles.","breadcrumbs":"Model » Overview","id":"108","title":"Overview"},"109":{"body":"To conclude, we have described the 20ipaD expression efficiency of Yeast cell through wet-lab results and predicted the post-medication scenario through math modeling. The expression efficiency is found to be about 31.25%± 0.75, and the upper limit and lower limit of natural growth of Shigella could help us to define a range for Shigella to grow naturally in jejunal. By assuming each capsule contains 10 billion CFU, we are able to give a medication guidance for symptomatic patient to take 5-6 capsules per 5 hours and for potential patients to take 1-5 capsules per 5 hours. In the future, more work can be devoted to deciding the binding efficiency β between Yeast-20ipaD and IpaD, and how much CFU is needed and realistic can a single capsule contain. These work can help us better understand the change of number of Shigella after medication, so that a more precise medication guidance is available. Investigation of the Best Saccharomyces cerevisiae Growth Condition. Electron Physician. DOI: 10.19082/3592 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5308499/ Effect of Sodium Chloride, pH and Temperature on Growth of Shigella flexneri. Journal of Food Protection. DOI:10.4315/0362-028x-52.5.356 https://pubmed.ncbi.nlm.nih.gov/31003269/ Effect of a New Probiotic Saccharomyces cerevisiae Strain on Survival of Escherichia Coli O157:H7 in a Dynamic Gastrointestinal Model. Applied and Environmental Microbiology. DOI:10.1128/AEM.02130-10 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3028742/ The mechanisms of sodium absorption in the human small intestine. The Journal of Clinical Investigation. DOI:10.1172/JCI105781 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC297237/ Choosing the Best Probiotic: How Many CFUs is Enough? https://deerland.com/chew/choosing-best-probiotic-many-cfus-enough/","breadcrumbs":"Model » Summary & Future plan","id":"109","title":"Summary & Future plan"},"11":{"body":"Attributions","breadcrumbs":"Team » Attributions » Biology team","id":"11","title":"Biology team"},"110":{"body":"Probiotics will be sealed in microcapsules( Figure 1 ) made of shellac before being delivered into bodies. The pH-dependent solubility that prefers a mild basic environment makes shellac perfect for releasing probiotics in intestines. Figure 1 | 3D model of the microcapsule Microcapsule is a microscope-scale capsulation format. The probiotics were wrapped by materials that can ensure the reservation, activation, release, and environmental-resistance of the probiotics. It would be presented as powder. “Microencapsulation is a technology that serves as a tool to protect the sensitive and expensive nutrients (Meyers et al., 1998), by providing them with a protective wall, which allows them to get released at a particular site, at a particular time, and under particular conditions.\" [18] To summarize, the technology of microencapsulation is to ensure the safe delivery of sensitive compound. Shellac is a natural polymer that is generally recognized as a safe (GRAS) material. It is insoluble in neutral and acidic aqueous solution but dissolves at alkaline condition [19] . So, shellac is proper for the controlled release of Yeast cells in the intestine. Research has shown that the microcapsules with the addition of shellac \"contributed to better probiotic survivals after freeze drying, simulated digestion,heating and ambient storage, and whey protein isolate (WPI) addition had a synergistic effect.\" [20] Microencapsulation: An overview on concepts, methods, properties and applications in foods. Food Frontiers. https://doi.org/10.1002/fft2.94 Microencapsulation of probiotic lactobacilli with shellac as moisture barrier and to allow controlled release. Journal of the Science of Food and Agriculture. https://doi.org/10.1002/jsfa.10685 Comparison of spray drying, freeze drying and convective hot air drying for the production of a probiotic orange powder. J Funct Foods https://doi.org/10.1016/j.jff.2015.06.001","breadcrumbs":"Model » Hardware","id":"110","title":"Hardware"},"111":{"body":"Parts All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Yeast (Group Y) Parts","id":"111","title":"Yeast (Group Y) Parts"},"112":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. Part Code Part name Link BBa_K4161501 T7 Promoter http://parts.igem.org/Part:BBa_K4161501 BBa_K4161502 GAL1 Promoter http://parts.igem.org/Part:BBa_K4161502 BBa_K4161503 Aga2 http://parts.igem.org/Part:BBa_K4161503 BBa_K4161504 G4S http://parts.igem.org/Part:BBa_K4161504 BBa_K4161505 T7, Xpress http://parts.igem.org/Part:BBa_K4161505 BBa_K4161506 ipaD http://parts.igem.org/Part:BBa_K4161506 BBa_K4161507 HA http://parts.igem.org/Part:BBa_K4161507","breadcrumbs":"Parts » Group Y single elements","id":"112","title":"Group Y single elements"},"113":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. Part Code Part name Link BBa_K4161301 Single Domain Antibody 20ipaD Conjugated Aga2 Express Module http://parts.igem.org/Part:BBa_K4161301 BBa_K4161508 488aa recombinant protein, Aga2 + ipaD http://parts.igem.org/Part:BBa_K4161508","breadcrumbs":"Parts » Group Y key composite segments","id":"113","title":"Group Y key composite segments"},"114":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. Part Code Part name Link BBa_K4161302 pYD1 plasmid http://parts.igem.org/Part:BBa_K4161302","breadcrumbs":"Parts » Group Y vector","id":"114","title":"Group Y vector"},"115":{"body":"","breadcrumbs":"Parts » E.coli Nissle 1917 (Group E) Parts","id":"115","title":"E.coli Nissle 1917 (Group E) Parts"},"116":{"body":"Single elements of Group E include nanobodies, curli protein (csg) operon fragments, linkers, tags, signal peptides, promoters and terminators. A total of 15 parts were documented. Part code Part name Link BBa_K4161001 20IpaD http://parts.igem.org/Part:BBa_K4161001 BBa_K4161002 JMK-H2 http://parts.igem.org/Part:BBa_K4161002 BBa_K4161010 csgA http://parts.igem.org/Part:BBa_K4161010 BBa_K4161011 csgB http://parts.igem.org/Part:BBa_K4161011 BBa_K4161012 csgC http://parts.igem.org/Part:BBa_K4161012 BBa_K4161013 csgE http://parts.igem.org/Part:BBa_K4161013 BBa_K4161014 csgF http://parts.igem.org/Part:BBa_K4161014 BBa_K4161015 csgG http://parts.igem.org/Part:BBa_K4161015 BBa_K4161016 riboJ http://parts.igem.org/Part:BBa_K4161016 BBa_K4161017 Neae: the intimin fragment for surface display http://parts.igem.org/Part:BBa_K4161017 BBa_K4161018 pTlpA promotor C7 variant http://parts.igem.org/Part:BBa_K4161018 BBa_K4161019 FE-36 linker http://parts.igem.org/Part:BBa_K4161019 BBa_K4161020 JPS-G3 http://parts.igem.org/Part:BBa_K4161020 BBa_K4161021 3xFlag http://parts.igem.org/Part:BBa_K4161021 BBa_K4161022 thr terminator http://parts.igem.org/Part:BBa_K4161022","breadcrumbs":"Parts » Group E single elements","id":"116","title":"Group E single elements"},"117":{"body":"Group E's composite parts are designed to express surface protein-nanobody fusion proteins. A total of 4 composite parts are documented. Part code Part name Link BBa_K4161003 csg-JMK-H2, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161003 BBa_K4161004 intimin-20IpaD, Nanobody surface display system based on intimin http://parts.igem.org/Part:BBa_K4161004 BBa_K4161023 csgA-JPS-G3-3xFLAG, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161023 BBa_K4161100 Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161100","breadcrumbs":"Parts » Group E composite segments","id":"117","title":"Group E composite segments"},"118":{"body":"Vectors pET30a and pUC19 are used for recombinant plasmid construction and protein expression. Part code Part name Link BBa_K4161024 pET30a, empty vector http://parts.igem.org/Part:BBa_K4161024 BBa_K4161025 pUC19, empty vector http://parts.igem.org/Part:BBa_K4161025","breadcrumbs":"Parts » Group E vectors","id":"118","title":"Group E vectors"},"119":{"body":"","breadcrumbs":"Parts » L.lactis NZ9000 parts","id":"119","title":"L.lactis NZ9000 parts"},"12":{"body":"Biology Team leader. In charge of wet lab organization, human practice organizations and wiki construction. Designed the overall topic and approach of the problem to tackle with synthetic biology design. Designer of E.coli csgA surface display and lab experiments of the E. coli group.","breadcrumbs":"Team » Attributions » Yixuan Wu (Lisa)","id":"12","title":"Yixuan Wu (Lisa)"},"120":{"body":"Single parts in Group L includes the following elements: Group L parts Part code Part name Link BBa_K4161600 Usp45 nisin promoter http://parts.igem.org/Part:BBa_K4161600 BBa_K4161603 AcmA3b http://parts.igem.org/Part:BBa_K4161603 BBa_K4161602 20ipaD http://parts.igem.org/Part:BBa_K4161602 BBa_K4161604 signalling peptide in L.lactis http://parts.igem.org/Part:BBa_K4161604 BBa_K4161605 Flag-tag http://parts.igem.org/Part:BBa_K4161605","breadcrumbs":"Parts » Group L single elements","id":"120","title":"Group L single elements"},"121":{"body":"The composite element of Group L includes Usp45-signaling peptide in L.lactis-Flagtag-20ipaD-AcmA3b. Part code Part name Link BBa_K4161600 Usp45-signaling peptide in L.lactis-20ipaD-AcmA3b http://parts.igem.org/Part:BBa_K4161997","breadcrumbs":"Parts » Composite elemnent","id":"121","title":"Composite elemnent"},"122":{"body":"","breadcrumbs":"Parts » Group L vector","id":"122","title":"Group L vector"},"123":{"body":"The plasmid backbone of Group L is pNZ8148, a plasmid suitable for L.lactis. Part code Part name Link BBa_K4161601 pNZ8148 http://parts.igem.org/Part:BBa_K4161601","breadcrumbs":"Parts » Composite elemnent","id":"123","title":"Composite elemnent"},"124":{"body":"Parts All genetic parts of group Y can be divided into 3 categories, including single element, key composite segment, and vector.","breadcrumbs":"Parts » Part Collection » Yeast (Group Y) Parts","id":"124","title":"Yeast (Group Y) Parts"},"125":{"body":"The single elements refer to every functional unit of our key genetic parts, like promoter, linker, important polypeptide, etc. A total of seven single elements were documented. Part Code Part name Link BBa_K4161501 T7 Promoter http://parts.igem.org/Part:BBa_K4161501 BBa_K4161502 GAL1 Promoter http://parts.igem.org/Part:BBa_K4161502 BBa_K4161503 Aga2 http://parts.igem.org/Part:BBa_K4161503 BBa_K4161504 G4S http://parts.igem.org/Part:BBa_K4161504 BBa_K4161505 T7, Xpress http://parts.igem.org/Part:BBa_K4161505 BBa_K4161506 ipaD http://parts.igem.org/Part:BBa_K4161506 BBa_K4161507 HA http://parts.igem.org/Part:BBa_K4161507","breadcrumbs":"Parts » Part Collection » Group Y single elements","id":"125","title":"Group Y single elements"},"126":{"body":"The key composite segments are clusters of multiple single elements, they make up the key expression modules or functional units of the genetic model. Two key composite segments were documented. Part Code Part name Link BBa_K4161301 Single Domain Antibody 20ipaD Conjugated Aga2 Express Module http://parts.igem.org/Part:BBa_K4161301 BBa_K4161508 488aa recombinant protein, Aga2 + ipaD http://parts.igem.org/Part:BBa_K4161508","breadcrumbs":"Parts » Part Collection » Group Y key composite segments","id":"126","title":"Group Y key composite segments"},"127":{"body":"Most of our genetic designs were based on the yeast surface display vector pYD1, which is also documented. Part Code Part name Link BBa_K4161302 pYD1 plasmid http://parts.igem.org/Part:BBa_K4161302","breadcrumbs":"Parts » Part Collection » Group Y vector","id":"127","title":"Group Y vector"},"128":{"body":"","breadcrumbs":"Parts » Part Collection » E.coli Nissle 1917 (Group E) Parts","id":"128","title":"E.coli Nissle 1917 (Group E) Parts"},"129":{"body":"Single elements of Group E include nanobodies, curli protein (csg) operon fragments, linkers, tags, signal peptides, promoters and terminators. A total of 15 parts were documented. Part code Part name Link BBa_K4161001 20IpaD http://parts.igem.org/Part:BBa_K4161001 BBa_K4161002 JMK-H2 http://parts.igem.org/Part:BBa_K4161002 BBa_K4161010 csgA http://parts.igem.org/Part:BBa_K4161010 BBa_K4161011 csgB http://parts.igem.org/Part:BBa_K4161011 BBa_K4161012 csgC http://parts.igem.org/Part:BBa_K4161012 BBa_K4161013 csgE http://parts.igem.org/Part:BBa_K4161013 BBa_K4161014 csgF http://parts.igem.org/Part:BBa_K4161014 BBa_K4161015 csgG http://parts.igem.org/Part:BBa_K4161015 BBa_K4161016 riboJ http://parts.igem.org/Part:BBa_K4161016 BBa_K4161017 Neae: the intimin fragment for surface display http://parts.igem.org/Part:BBa_K4161017 BBa_K4161018 pTlpA promotor C7 variant http://parts.igem.org/Part:BBa_K4161018 BBa_K4161019 FE-36 linker http://parts.igem.org/Part:BBa_K4161019 BBa_K4161020 JPS-G3 http://parts.igem.org/Part:BBa_K4161020 BBa_K4161021 3xFlag http://parts.igem.org/Part:BBa_K4161021 BBa_K4161022 thr terminator http://parts.igem.org/Part:BBa_K4161022","breadcrumbs":"Parts » Part Collection » Group E single elements","id":"129","title":"Group E single elements"},"13":{"body":"Co-established the project topic. In charge of lab design and wet lab for the yeast group. Also assisted in Wiki writing and expert interview.","breadcrumbs":"Team » Attributions » Yuxin Wang","id":"13","title":"Yuxin Wang"},"130":{"body":"Group E's composite parts are designed to express surface protein-nanobody fusion proteins. A total of 4 composite parts are documented. Part code Part name Link BBa_K4161003 csg-JMK-H2, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161003 BBa_K4161004 intimin-20IpaD, Nanobody surface display system based on intimin http://parts.igem.org/Part:BBa_K4161004 BBa_K4161023 csgA-JPS-G3-3xFLAG, Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161023 BBa_K4161100 Csg surface display system on E. coli Nissle 1917 http://parts.igem.org/Part:BBa_K4161100","breadcrumbs":"Parts » Part Collection » Group E composite segments","id":"130","title":"Group E composite segments"},"131":{"body":"Vectors pET30a and pUC19 are used for recombinant plasmid construction and protein expression. Part code Part name Link BBa_K4161024 pET30a, empty vector http://parts.igem.org/Part:BBa_K4161024 BBa_K4161025 pUC19, empty vector http://parts.igem.org/Part:BBa_K4161025","breadcrumbs":"Parts » Part Collection » Group E vectors","id":"131","title":"Group E vectors"},"132":{"body":"","breadcrumbs":"Parts » Part Collection » L.lactis NZ9000 parts","id":"132","title":"L.lactis NZ9000 parts"},"133":{"body":"Single parts in Group L includes the following elements: Group L parts Part code Part name Link BBa_K4161600 Usp45 nisin promoter http://parts.igem.org/Part:BBa_K4161600 BBa_K4161603 AcmA3b http://parts.igem.org/Part:BBa_K4161603 BBa_K4161602 20ipaD http://parts.igem.org/Part:BBa_K4161602 BBa_K4161604 signalling peptide in L.lactis http://parts.igem.org/Part:BBa_K4161604 BBa_K4161605 Flag-tag http://parts.igem.org/Part:BBa_K4161605","breadcrumbs":"Parts » Part Collection » Group L single elements","id":"133","title":"Group L single elements"},"134":{"body":"The composite element of Group L includes Usp45-signaling peptide in L.lactis-Flagtag-20ipaD-AcmA3b. Part code Part name Link BBa_K4161600 Usp45-signaling peptide in L.lactis-20ipaD-AcmA3b http://parts.igem.org/Part:BBa_K4161997","breadcrumbs":"Parts » Part Collection » Composite elemnent","id":"134","title":"Composite elemnent"},"135":{"body":"","breadcrumbs":"Parts » Part Collection » Group L vector","id":"135","title":"Group L vector"},"136":{"body":"The plasmid backbone of Group L is pNZ8148, a plasmid suitable for L.lactis. Part code Part name Link BBa_K4161601 pNZ8148 http://parts.igem.org/Part:BBa_K4161601","breadcrumbs":"Parts » Part Collection » Composite elemnent","id":"136","title":"Composite elemnent"},"137":{"body":"Our part BBa_K4161301 is an improvement of part BBa_K416000 from iGEM10_NYU (2010). In 2010, iGEM10_NYU designed the part “BBa_K416000†which was the CDS of Aga2 protein for yeast surface display. The part was achieved by deleting the stop codon of the Aga2 CDS region from vector pCTCON2 so that the element can be fused with other fragments to express fusion proteins. On the basis of this part, we designed the integrated expression module “BBa_K4161301â€. This part integrated the yeast surface protein Aga2, GAL1 promotor, nanobody 20ipaD, and 3xFLAG tag sequences, which make it a complete expression module that is controllable. The addition of GAL1 promotor ensures the whole surface display part would only be induced by galactose and denied the leaky expression. The nanobody segment provides the real function for the whole module so that it can bind to its corresponding antigen to inhibit pathogens like Shigella. Additionally, the 3xFLAG tag eases the detection of the expression of this module.","breadcrumbs":"Parts » Improve » Part improvement","id":"137","title":"Part improvement"},"138":{"body":"Safety The Duke Kunshan University (DKU) iGEM team sets safety as an integral part of science. It includes protection for sensitive groups and the environment. For this reason, safety was considered from two perspectives—inside and outside the laboratory. For more detailed information, please check our safety form.","breadcrumbs":"Safety » Introduction","id":"138","title":"Introduction"},"139":{"body":"All laboratories of universities in China must be accredited by the Office under the Ministry of Environment following the standard. This year, the project was conducted in the BSL-1 laboratory. Team members wore lab coats and gloves during experiments. Experiments related to bacteria were performed in the biosafety cabinet and near butane burners. Before laboratory started, the team received safety training including how to use equipment properly, following laboratorial hygiene rules and proper disposal of hazardous substances. Also, experiments were first presented in detail by our two supervisors to eliminate biosafety concerns.","breadcrumbs":"Safety » Lab Safety","id":"139","title":"Lab Safety"},"14":{"body":"In charge of background research, E. coli group lab design, wet labs & wiki writing. Hosted journal clubs and science lectures for human practice.","breadcrumbs":"Team » Attributions » Yunyi Ru","id":"14","title":"Yunyi Ru"},"140":{"body":"Protein expression for diagnostic tests was performed in non-pathogenic Escherichia coli strains (E.coli Nissle 1917), Lactococcus lactis NZ9000 and yeast (EBY100). These gene carriers are probiotic or at least harmless. They do not possess serious illnesses or lead to other problems to people or the environment. In addition, they are in whitelist, belonging to BSL-1 organisms.","breadcrumbs":"Safety » Microorganisms review","id":"140","title":"Microorganisms review"},"141":{"body":"The engineered probiotics were designed to express 20ipad nanobody on their surface by transforming recombinant plasmids with optimized genes. Thus, they can combine with the antigen on the surface of Shigella. Since Shigella is one of the BSL-2 organisms, we decide to express our targeted antigen in probiotics that we used to express the antibody. We optimized the DNA sequences which code the antigen by using machine-learning software. Using yeast as an example, amino acids are essential for the growth of yeast. Amino acids are absorbed by human bodies in the small intestine. There is a competitive absorption of amino acids between intestinal epithelial cells and yeast. This prevents the overgrowth of yeast cells, preventing the destruction of bacterial flora structure. Using yeast as gene carriers limits the leak of antibiotics resistance genes, compared with using bacteria as carriers. In addition, galactose was used to induce the expression of the antibody and antigen. Since we used antibiotics resistance genes, we also pay attention to the potential risks of the leak of antibiotics resistance genes during wetlab process. Discarded liquids and plates that contain antibiotics were placed in specific vessels and then autoclaved.","breadcrumbs":"Safety » Experiments","id":"141","title":"Experiments"},"142":{"body":"Part of planned experiments had to be done by using harmful reagents or procedures. All team members follow the rules under the guideline provided by our lab manager and assistants during experiment safety training. UV light was used to sterilize the biosafety cabinets and equipment inside the cabinets. Safety measures were taken to avoid people`s direct exposure to UV light. Gel imaging system was used for visualizing agarose gel, combined with standard laboratory procedures with blue light transilluminator. Antibiotics were used to select transformants. They can be harmful to sensitive groups. Situations of allergy of team members were collected. Antibiotics were well stored and Handled with proper safety measures according to disposal protocols. Other hazardous chemicals , such as Tris-HCl and methyl alcohol were stored and relevant procedures were conducted in chemical ventilation cabinets. Liquid waste was handled with appropriate safety measures.","breadcrumbs":"Safety » Harmful reagents and procedures","id":"142","title":"Harmful reagents and procedures"},"143":{"body":"Team members followed all the government and university guidelines based on the pandemic situation of Covid-19 in China. For April and May, team`s meetings were online because of school closure and in-person activities were allowed after deblocking. Covid-19 tests were performed regularly and all team members got vaccinated. When wetlabs began, team members` attendance was recorded. The usage of lab equipment was registered. All working surfaces were cleaned with disinfectant fluid before and after conducting wetlabs.","breadcrumbs":"Safety » Covid-19 associated safety measures","id":"143","title":"Covid-19 associated safety measures"},"144":{"body":"Antibiotic resistance is a problem in its scale and subtlety. Shigella infection has its significance in antibiotic resistance because of its identity as one of the most antibiotic resistant bacterias recognized by CDC. In our integrated human practice, we followed the procedure of research-design-engagement-modification.","breadcrumbs":"Human Practices » Integrated Human Practice","id":"144","title":"Integrated Human Practice"},"145":{"body":"The subtlety of antibiotic resistance did not come to mind until some of the team members took the microbiology class at DKU: From the amazing lectures given by Dr. Linfeng Huang, we realized that the race against bacterial infection is largely dependent on discoveries of newly synthesized drugs. People modify the drug molecule by perhaps a small sidechain, changing the chemical property but perhaps not changing the chemical property. This can lead to significant advances because it can possibly alter the pathogen's ability to recognize the drug, therefore no longer maintain its resistance. Antibiotics are thus labeled as the best weapon. It is almost always the solution to infections. It can be bought at ordinary pharmacies, and are consumed at a scale larger than ever. From talking with the people around us, we realized that the lack of knowledge of antibiotic resistance exists as possibly a larger threat than the pathogen itself. We ask ourselves: What if one day, we have exhausted all the combinations of chemicals? What if we lose the race because we have strengthened antibiotic resistance to the point of no return? And clearly this has been considered. The field of immunology has become more heated than ever before. What if we could deploit the weapon that is the gift of the creation-our own immune systems? We looked into nanobody therapy, because it is easy to perform in our lab, and effective nanobodies for Shigella T3SS has been revealed by previous studies.","breadcrumbs":"Human Practices » Recognizing the problem and designing the approach","id":"145","title":"Recognizing the problem and designing the approach"},"146":{"body":"We further consulted experts in this area, including Dr. Neel Joshi from Northwestern University, whose lab had worked on nanobody therapy and bacterial surface display. He answered our questions about the choice of probiotics and gave us more information on the multi-valency potential of the surface display method. He also reminded us that areas with high shigella infection rates and mortality are usally underdeveloped areas, thus we should consider the delivery method to be economic friendly and easy to maintain. In the interview with Dr. Lin from SINOVAC, he suggested that our final design should consider safety, effectiveness and economics. See entrepreneurship for more details. To engage with the general public in our design, we distributed a questionaire and received over 500 responses on what people know about antibiotic resistance and shigella infection, and identified potential barriers of drug distribution to the general public. See our report here.","breadcrumbs":"Human Practices » Engaging stakeholders","id":"146","title":"Engaging stakeholders"},"147":{"body":"In aspect of our design, we adopted the PATCH system by Dr. Neel Joshi, for better multivalency performance. We also changed our design logic: our drug is more vaccine orientated than the conventional drug designs. The drug should be ideal for prevention of regional spread of shigella infection, acting as a blocking agent for further transmission. The delivery method is in freeze-dried powder, delivered in economic-friendly microcapsules. For the advice from Dr. Lin, we made multiple modifications that would promote the safety and effectiveness of our design. See entrepreneurship for more details. As for the general public response, we found one major problem, which is that a significant amount of people see E. coli as the main causative agent for dysentery syndrome. We assessed that this may cause major problems if we reveal our approach as probiotic-nanobody therapy, in specific, yeast and E. coli Nissle 1917 can be subject to public opinions including skepticism. Therefore, we attempted educational approaches to give more information on probiotics at both DKU and local high schools.","breadcrumbs":"Human Practices » Modification","id":"147","title":"Modification"},"148":{"body":"Our integrated human practices influenced our experimental design, and the overall logic of our project. We are able to engage with our stakeholders and the general public, acheiving satisfying outcomes. Engagement is the key to creating a project design with actual social impact, and we will carry this spirit on as we progress further into our project and future careers.","breadcrumbs":"Human Practices » Conclusion","id":"148","title":"Conclusion"},"149":{"body":"Education Overview: We conduct popular science education both on and off campus. On campus, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating. We also cohosted a Biology Seminar Series, inviting Prof. Dong Hyun Jo, from Seoul National University College of Medicine to give a talk on therapeutic revolution for the DKU community. Off campus, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers about our project and synthetic biology. Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo For GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo For probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Off campus education","id":"149","title":"Off campus education"},"15":{"body":"Designed Lactococcus lab procedures and in charge of Lactococcus and yeast lab experiments. Conducted expert interviews for human practice.","breadcrumbs":"Team » Attributions » Zhujun Yao","id":"15","title":"Zhujun Yao"},"150":{"body":"Wang-Cai Biology Seminar Series Wang-Cai Talk In this Wang-Cai biology seminar series, the DKU iGEM team was honored to co-host the speech delivered by Prof. Dong Hyun Jo from Seoul National University College of Medicine. The talk was titled “Therapeutic Revolution: Application of Novel Technologiesâ€, where Dr Jo introduced the brief history and therapeutic development for one specific type of cancer, retinoblastoma. Dr Jo is the assistant professor of Seoul National University College of Medicine in Republic of Korea. He had his medical degree at Seoul National University in 2007. In 2012, Dr Jo received residency at the Department of Ophthalmology, Seoul National University Hospital, and in 2016, he received his PhD at Seoul National University. Dr Jo’s research interest focuses on 3 aspects. The first is the development of novel therapeutic approaches against retinal diseases. The second is the molecular mechanisms of physiological and pathological angiogenesis in the retina and associated organs, the third is translational research on retinoblastoma. At the end of the talk. Dr. Jo shared his career pathway as both a physician and a researcher. The devotion he made to the clinical therapy of retinoblastoma and the improvement of the health of his patients made him feel that biomedical sciences are not limited to theoretical knowledge, but rather quite practical and can benefit the whole population. The experience and thoughts expressed by Dr. Jo greatly inspired us, which allow us to have more understanding of graduate choices and future career plans. Journal club In order to have better educational effect and promote our project , we organized the Journal Club activity in the Duke Kunshan community. The first Journal Club was held on April 30th, 2022. At the very beginning of the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us and introduced in detail what systems biology is and the basic methods of studying systems biology. This journal club event mainly focused on COVID-19 and then developed into three sub-topics including the antigen test for SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the iGEM team, around 10 freshman students with various backgrounds participated in the sharing and raised many inspiring questions.","breadcrumbs":"Awards » On campus education","id":"150","title":"On campus education"},"151":{"body":"We have devoted in several education activities. On-campus education allows us to better transfer knowledge about synthetic biology and shigella treatment to our students, as well as gather fresh blood for the next year's team. The science popularization and education in local school also gives us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Awards » Summary","id":"151","title":"Summary"},"152":{"body":"Education Overview: We conduct popular science education both on and off campus. On campus, we have established a journal club, where different members of the team introduce cutting-edge knowledge about synthetic biology every two weeks, and we are happy to see many freshmen participating. We also cohosted a Biology Seminar Series, inviting Prof. Dong Hyun Jo, from Seoul National University College of Medicine to give a talk on therapeutic revolution for the DKU community. Off campus, we contacted a local international high school and successfully delivered popular science lectures to more than 330 middle and high school students and teachers about our project and synthetic biology. Although iGEM competition has a solid audience base in universities , students in high schools have little knowledge of iGEM competition or give up because of their limitation of conducting wetlabs. There is an increasing trend of taking probiotic products. However, there is lack of common sense of probiotics. photo To narrow the gap between public and science, we contacted with Dipont Huayao Collegiate School Kunshan, a local high school. We introduced iGEM competition and popularize the knowledge of GI tract and probiotics by giving a presentation. In the introduction of iGEM , we introduced biology team, modelling team, wiki team and human practice team, including their responsibility and collaborations between different subgroups. photo For GI tract , we introduced the process of digesting. Functions of each human organ and different intestinal floras were explained in detail. Along with knowledge, we provided two fun facts——“Mom passes gut microbiota to baby†and “Having stomachache and diarrhea before examsâ€. Besides GI tract, we also mentioned the harm that using antibiotics can do to gastrointestinal tract. photo For probiotics , we popularized basic knowledge of probiotics, pointed out issues that taking probiotics improperly will lead to and give our advice. After the speech, 330 high school students and teachers had a better understanding of choosing probiotic products. Students and teachers interested in participating in iGEM competition consulted with us about the future iGEM cooperations. photo","breadcrumbs":"Awards » Education » Off campus education","id":"152","title":"Off campus education"},"153":{"body":"Wang-Cai Biology Seminar Series Wang-Cai Talk In this Wang-Cai biology seminar series, the DKU iGEM team was honored to co-host the speech delivered by Prof. Dong Hyun Jo from Seoul National University College of Medicine. The talk was titled “Therapeutic Revolution: Application of Novel Technologiesâ€, where Dr Jo introduced the brief history and therapeutic development for one specific type of cancer, retinoblastoma. Dr Jo is the assistant professor of Seoul National University College of Medicine in Republic of Korea. He had his medical degree at Seoul National University in 2007. In 2012, Dr Jo received residency at the Department of Ophthalmology, Seoul National University Hospital, and in 2016, he received his PhD at Seoul National University. Dr Jo’s research interest focuses on 3 aspects. The first is the development of novel therapeutic approaches against retinal diseases. The second is the molecular mechanisms of physiological and pathological angiogenesis in the retina and associated organs, the third is translational research on retinoblastoma. At the end of the talk. Dr. Jo shared his career pathway as both a physician and a researcher. The devotion he made to the clinical therapy of retinoblastoma and the improvement of the health of his patients made him feel that biomedical sciences are not limited to theoretical knowledge, but rather quite practical and can benefit the whole population. The experience and thoughts expressed by Dr. Jo greatly inspired us, which allow us to have more understanding of graduate choices and future career plans. Journal club In order to have better educational effect and promote our project , we organized the Journal Club activity in the Duke Kunshan community. The first Journal Club was held on April 30th, 2022. At the very beginning of the meeting, Yuyang, the leader of last year's iGEM team, gave a speech for us and introduced in detail what systems biology is and the basic methods of studying systems biology. This journal club event mainly focused on COVID-19 and then developed into three sub-topics including the antigen test for SARS-CoV-2 introduced by Kathy, human ACE2 receptor & TM air freshening spray presented by Irene, and COVID-19 Vaccines explained by Bruce. Apart from the iGEM team, around 10 freshman students with various backgrounds participated in the sharing and raised many inspiring questions.","breadcrumbs":"Awards » Education » On campus education","id":"153","title":"On campus education"},"154":{"body":"We have devoted in several education activities. On-campus education allows us to better transfer knowledge about synthetic biology and shigella treatment to our students, as well as gather fresh blood for the next year's team. The science popularization and education in local school also gives us the opportunity to communicate with middle and high school students, understand their ideas and answer their doubts.","breadcrumbs":"Awards » Education » Summary","id":"154","title":"Summary"},"155":{"body":"The probiotics market in China is expected to reach a size of USD 13,527.100 million by 2025, growing at a CAGR of 8.81 percent. In 2019, the market was valued at US8,149.466 million [1] . Previous research findings has emphasized on the significance of gut microbiome on human health, and this has opened up the marketing of probiotics. Taking advantage of the booming market and the maturation of bioengineering technology, our project aims to guard our guts through bacteria-bacteria interaction, a method that is an alternative to antibiotics. Some probiotic product utilizing bacteria-bacteria cell interaction has already gone through clinical trials and entered the market, such as Lactobacillus reuteri DSM17648 that treats H.pylori infection [2] . Therefore, it is possible for our product to secure a place in the probiotic market. The terminal of our designed product is a drug used in people. We understand that animal model testings as well as clinical trials are often involved in the process of drug development. What we have reached so far is only a prototype tested in vitro. After the completion of the in vitro testing we will proceed to in vivo models. To improve our plan we interviewed Jisheng Lin from Sinovac Biotech company, to collected feedbacks and suggestions about how to turn our products into commercial ones as well as cautions on putting our products in a real world situation. Here we provide considerations from various aspects of accessing our products into market and our solutions so far.","breadcrumbs":"Awards » Entrepreneurship » Introduction","id":"155","title":"Introduction"},"156":{"body":"\"Safety is always the first concern,\" as suggested by Mr. Lin, \"even it doesn't work well, at least does no harm.\" Based on Mr. Lin's suggestions as well as our previous thoughts, several sources of safety concerns are listed as follows: First, the plasmid we used for selection contains a bacterial ampicillin resistance gene. though not expressed in yeast due to different promoter and codon structures, potential horizontal gene transfers still leave risks of spread antibiotic resistent genes to other prokaryotes in the intestine. Second, though our vectors cell linage yeast strain EBY100 has been well studied, the genomic background of our engineered yeast is unknown. Our engineering process may alter the growth and metabolic characteristics. Efforts should be given to test if engineered yeast could harm human bodies. Besides, human intestine is a complicated microenvironment comprises of a microbiota yet not fully understood. It is also important to clarify how long does our engineered yeast can survive in human body, whether it gains competitive advantages over native gut microorganisms, and how it alter the structure of gut microbiome. Third, similar to antibody therapies, allergy may be a question to some people. Therefore, an approach should be developed to pre-test patients' irritability. Fourth, as a commercial product, a standard of quality control during each step of the engineering or the drug production is also needed. Entre_image","breadcrumbs":"Awards » Entrepreneurship » Safety","id":"156","title":"Safety"},"157":{"body":"Effectiveness demonstrates the values of our products. We have shown qualitatively the expression of the antibodies and the binding between the antigen and the antibodies. For a real world application, we need to establish standard to access and quantify these values. Moreover, the success in the simplified in vitro assay does not guarantee the effectiveness of the drug to work in a real scenario. Considering the real world application that our products function in human GI tracts, it requires the engineered yeast be able to settle down, proliferate, and bind to Shigella spike proteins. Hence, the growth curve about the engineered yeast in human intestines should also be tested. More importantly, the performance of the drug should also be assessed. Potential questions include whether there is dosage-dependent protection effect, how to assess these effects if they exist, and whether this product focuses on therapy or is precaution oriented.","breadcrumbs":"Awards » Entrepreneurship » Effectiveness","id":"157","title":"Effectiveness"},"158":{"body":"The third aspect related to the economics about our products. Apart from the reagents and consumable usage, stabilities, including plasmid stability and the stability of the phenotype expressions, are important factor influence the cost of production. A passaging lineage stably expression the recombinant antibodies greatly reduce the cost of continuously re-engineering the yeast to harvest antibody expression. Efforts should be devoted to focus on increasing the stability antibody expression during passages.","breadcrumbs":"Awards » Entrepreneurship » Economics","id":"158","title":"Economics"},"159":{"body":"We should also seek for further development of our products in the future, such as increasing the valency of our product so that it can target multiple pathogens at the same time.","breadcrumbs":"Awards » Entrepreneurship » Future","id":"159","title":"Future"},"16":{"body":"Proposed the project topic, participated in plasmid design and workflow design of E.coli group, participated in wet labs and background research. Helped conduct collaboration with XJLTU as a part of human practice.","breadcrumbs":"Team » Attributions » Chang Shen","id":"16","title":"Chang Shen"},"160":{"body":"As many goals are still far from being achieved, here we proposed our future plan altogether with what we have reached. We used two different approaches to remove the influence of ampicillin resistance gene. In the first approach, we designed a PCR-fusion that jumps the whole ampicillin resistant gene and the bacterial replication origin. The resting plasmid contains around 3200bp including the TRP1 gene that is a suitable size for PCR amplification and enables the selection of transformant yeast cells. The alternative approach used CRISPR-Cas9 to integrate the whole \"promoter-Aga2-20ipaD\" cassette into yeast genome. The latter also increases phenotype stability as no plasmid is needed to maintain the phenotype. For expression level assessment, we have already established a system employed ELISA to quantify the expression. However, one drawback of this approach is that it does not differentiate surface displayed antibodies from the antibodies no correctly presented on surface. An improved design uses biotins to labeled all surface proteins followed by avidin affinity binding to isolate these proteins from the protein repertoire. Isolated surface protein can be then analyzed via ELISA. To improve expression level, we have listed a set of developed constitutive yeast promoters as candidates. However, we also realized that promoter engineering processes may be required in the future. For the effectiveness test, we have designed a cell invasion test in vitro. Engineered yeast cells together with Shigella will be applied to Vero cell cultures. Effectiveness will be measured by proportion of cells being infected. To remove the influence of cell lines on the result of invasion test, we plan to substitute the Vero cell lines to epithelial cells in the future. After the completion of in vitro assay, further in vivo assay may be applied.","breadcrumbs":"Awards » Entrepreneurship » Our Solution","id":"160","title":"Our Solution"},"161":{"body":"We realized that what we have built is only a prototype of a Shigella infection precaution drug. There is still a long way to go for optimizing the drug in vitro as well as testing the drug in vivo. However, via a series of design processes, we have developed plans to turn it into real world application. China Probiotics Market Size, Share, Opportunities, COVID-19 Impact, And Trends By Ingredient (Bacteria, Yeast), By Form (Liquid, Dry), By Application (Functional Food And Beverages, Dietary Supplements, Animal Feed), And By End-User (Human, Animal) - Forecasts From 2020 To 2025. (2020). https://www.knowledge-sourcing.com/report/china-probiotics-market#:~:text=China%20probiotics%20market%20is%20estimated,intestinal%20tracts%2C%20and%20bowel%20function Significant Reduction in Helicobacter pylori Load in Humans with Non-viable Lactobacillus reuteri DSM17648: A Pilot Study. (2015). https://pubmed.ncbi.nlm.nih.gov/25481036/","breadcrumbs":"Awards » Entrepreneurship » Conclusion","id":"161","title":"Conclusion"},"162":{"body":"","breadcrumbs":"Awards » Inclusivity","id":"162","title":"Awards"},"163":{"body":"","breadcrumbs":"Awards » Measurement","id":"163","title":"Awards"},"164":{"body":"","breadcrumbs":"Awards » Plant","id":"164","title":"Awards"},"165":{"body":"","breadcrumbs":"Awards » Software","id":"165","title":"Awards"},"166":{"body":"","breadcrumbs":"Awards » Sustainable » Sustainable Development Goals (SDGs)","id":"166","title":"Sustainable Development Goals (SDGs)"},"167":{"body":"Scientific research has always had far-reaching significance in our study and daily routine, and even in the development of the whole society. Scientific research can comprehend us a better understanding of the nature and properties of matter. Analyzing the research objects elaboratively can accelerate the development of human knowledge accumulation. Our project follows a shared blueprint for peace and prosperity for people and the planet whose heart is the 17 sustainable development goals (UN, 2022). We respond to the urgent call for action by all countries that end poverty and other deprivations, improve health and education, reduce inequality, and spur economic growth (UN, 2022). This year, our team aims to provide a biological method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . Our method can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity while having stronger pathogen inhibition compared to traditional probiotic treatment (Langdon et al., 2016). Project “GutGuard†is mainly based on Goals 3, 9, 17","breadcrumbs":"Awards » Sustainable » Introduction","id":"167","title":"Introduction"},"168":{"body":"Ensure healthy lives and promoting well-being for all persons with disabilities We prospect our team’s project can make our local community and even the world conscious of the prominence of life and health, especially the gut problem. The gut problem may cause a person to struggle to absorb nutrients and regulate blood sugar. Additionally, weight loss or gain may be caused by bacteria overgrowth or lack of nutrients. The current therapeutics is antibiotics and the potential problem with the usage of antibiotics is that taking antibiotics too often or for the wrong reasons can change bacteria so much that antibiotics do not work against them (Cronan, 2019). Moreover, long-term use of antibiotics in late adulthood may be a risk factor for all-cause and cardiovascular mortality (Heianza, 2020). As the current therapies of antibiotics promote Shigella to develop antibiotic resistance, we are inspired by this problem and focus on shigella’s drug. Reducing antibiotic resistance and minimizing the side effects including the degradation of GI tract microbiome diversity can be achieved compared to the traditional probiotic treatment (Langdon et al., 2016). We mainly worked toward contributing to target 3.5 (Strength the prevention and treatment of substance abuse, including narcotic drug abuse and harmful use of alcohol) (UN, 2022).","breadcrumbs":"Awards » Sustainable » Goal 3| Good health and well-being","id":"168","title":"Goal 3| Good health and well-being"},"169":{"body":"Build resilient infrastructure, promote inclusive and sustainable industrialization and foster innovation We are capable to lead a new approach and ideologically telling certain product developers to dare to innovate and not to stick to antibiotics to create drugs. To contribute to the goal, we aimed at target 9.5 (Enhance scientific research, upgrade the technological capabilities of industrial sectors in all countries, in particular developing countries, including, by 2030, encouraging innovation and substantially increasing the number of research and development workers per 1 million people and public and private research and development spending) (UN, 2022). We proposed a novel scientific solution to an existing global problem. We mainly focused on a novel method for battling antibiotic-resistant pathogens by displaying nanobodies on the surface of the probiotics . While meeting the goal, our laboratory team did various ways (using three different cells for trial: E. coli, Yeast and Lactococcus lactis ) to achieve and increase the possibility of success. Additionally, our team collaborates with other iGEM teams from developing countries to contribute to scientific advancement there.","breadcrumbs":"Awards » Sustainable » Goal 9| Industry, Innovation and Infrastructure","id":"169","title":"Goal 9| Industry, Innovation and Infrastructure"},"17":{"body":"Responsible for wet lab design and experiment for yeast group. Contribute to Human Practice with Conference of China iGEMer Community.","breadcrumbs":"Team » Attributions » Lingrui Lai","id":"17","title":"Lingrui Lai"},"170":{"body":"Strengthen the means of implementation and revitalize the global partnership for sustainable development We, as a team, share and hold the view of win-win cooperation. We know that iGEM is not just a competition, but a platform for mutual communication and cooperation. We welcome various teams coming from different backgrounds and help to create solutions to the question. Our team strictly followed target 17.16 (Enhance the global partnership for sustainable development, complemented by multi-stakeholder partnerships that mobilize and share knowledge, expertise, technology, and financial resources, to support the achievement of the sustainable development goals in all countries, in particular developing countries.) (UN, 2022). Our team played an active part in collaborating with other iGEM teams (LZU and XJLTU) to gain insights into local society and comprehend more knowledge. This kind of collaboration enriched us and ensured the sharing of knowledge and raising of awareness on both sides.","breadcrumbs":"Awards » Sustainable » Goal 17| Partnerships for the goals","id":"170","title":"Goal 17| Partnerships for the goals"},"171":{"body":"To sum up, we address and fulfill sustainable development goals 3, 9, and 17 . While meeting the goal of displaying nanobodies on the surface of the probiotics to battle antibiotic-resistant pathogens, we can also contribute to improved healthcare globally in the sustainable development aspect. It can not only reduce antibiotic resistance but minimize side effects including the degradation of GI tract microbiome diversity. The inhibition of the pathogen will be stronger compared to traditional probiotic treatment. Our methods are easy to use and can be improved for further applications.","breadcrumbs":"Awards » Sustainable » Conclusion","id":"171","title":"Conclusion"},"172":{"body":"United Nations. (2022). The 17 goals | sustainable development. United Nations. https://sdgs.un.org/goals United Nations. (2022). #ENVISION2030: 17 goals to transform the world for persons with disabilities enable. United Nations. https://www.un.org/development/desa/disabilities/envision2030.html Langdon, A., Crook, N., & Dantas, G. (2016, April 13). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome medicine. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831151/ Cronan, K. M. (Ed.). (2019, July). The danger of antibiotic overuse (for parents) - nemours kidshealth. KidsHealth. Retrieved September 28, 2022, from https://kidshealth.org/en/parents/antibiotic-overuse.html Heianza, Y., Ma, W., Li, X., Cao, Y., Chan, A. T., Rimm, E. B., Hu, F. B., Rexrode, K. M., Manson, J. A. E., & Qi, L. (2020). Duration and life-stage of antibiotic use and risks of all-cause and cause-specific mortality. Circulation Research, 126(3), 364–373. https://doi.org/10.1161/circresaha.119.315279","breadcrumbs":"Awards » Sustainable » References","id":"172","title":"References"},"173":{"body":"Attribution 4.0 International (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/ ======================================================================= Creative Commons Corporation (\"Creative Commons\") is not a law firm and does not provide legal services or legal advice. Distribution of Creative Commons public licenses does not create a lawyer-client or other relationship. Creative Commons makes its licenses and related information available on an \"as-is\" basis. Creative Commons gives no warranties regarding its licenses, any material licensed under their terms and conditions, or any related information. Creative Commons disclaims all liability for damages resulting from their use to the fullest extent possible. 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Except for the limited purpose of indicating that material is shared under a Creative Commons public license or as otherwise permitted by the Creative Commons policies published at creativecommons.org/policies, Creative Commons does not authorize the use of the trademark \"Creative Commons\" or any other trademark or logo of Creative Commons without its prior written consent including, without limitation, in connection with any unauthorized modifications to any of its public licenses or any other arrangements, understandings, or agreements concerning use of licensed material. For the avoidance of doubt, this paragraph does not form part of the public licenses. Creative Commons may be contacted at creativecommons.org.","breadcrumbs":"LICENSE","id":"173","title":"LICENSE"},"18":{"body":"Helped conduct human practices and wetlabs for the yeast group. Designed the safety and education wiki and organized local high school activities education.","breadcrumbs":"Team » Attributions » Qizhou Jiang","id":"18","title":"Qizhou Jiang"},"19":{"body":"Helped with background research, designed lab detection protocols for the lactococcus group, conducted wetlab experiments, helped with human practice organization including journal club organization and wiki writing.","breadcrumbs":"Team » Attributions » Sihan Wang","id":"19","title":"Sihan Wang"},"2":{"body":"Sichang He (Steven) UG Class of 2024 Data Science Jasmine Santos UG Class of 2024 Biology Yuxiang He UG Class of 2025 Zhenyu Xu UG Class of 2024 Physics","breadcrumbs":"Team » Modeling","id":"2","title":"Modeling"},"20":{"body":"Organized and chaired the iGEM2022 Journal Club Seminar ever since 2021. Actively participate in human practice part including designing and popularizing events in local collegiate school. Help conduct wet labs.","breadcrumbs":"Team » Attributions » Yixuan Liu","id":"20","title":"Yixuan Liu"},"21":{"body":"Fund manager of the team, in charge of labware purchasing, helped with background research and survey distribution as a part of human practice.","breadcrumbs":"Team » Attributions » Renwei Gao","id":"21","title":"Renwei Gao"},"22":{"body":"Helped design survey as a part of human practice, helped with E. coli wet lab experiments.","breadcrumbs":"Team » Attributions » Jingyun Jin","id":"22","title":"Jingyun Jin"},"23":{"body":"","breadcrumbs":"Team » Attributions » Modeling team","id":"23","title":"Modeling team"},"24":{"body":"Organized protein structure and docking modeling. Helped conduct human practice. Shot and edited the promotion video. Wiki writing.","breadcrumbs":"Team » Attributions » Zhenyu Xu","id":"24","title":"Zhenyu Xu"},"25":{"body":"Main Wiki developer and technical support. Built the Wiki infrastructure. Set up and maintains the GitLab repository for team communication and Wiki editing. Introduced Git and GitLab to the team and helped the team adopt to the workflow on GitLab. Helped with protein modeling using RoseTTAFold, Robetta, and PyMOL.","breadcrumbs":"Team » Attributions » Sichang He (Steven)","id":"25","title":"Sichang He (Steven)"},"26":{"body":"Conceptualized cell surface display technology project during preliminary brainstorming and provided proof of concept through review of related literature. Wrote the project abstract and refined general methodology framework. Built protein models for candidate microbes via Alphafold and Haddock and evaluated fidelity of each model via quantiative metrics. Modelled growth of chosen microbe model computationally.","breadcrumbs":"Team » Attributions » Jasmine Santos","id":"26","title":"Jasmine Santos"},"27":{"body":"Built a 3D model for the drug delivery system.","breadcrumbs":"Team » Attributions » Yuxiang He","id":"27","title":"Yuxiang He"},"28":{"body":"","breadcrumbs":"Team » Attributions » Advising support","id":"28","title":"Advising support"},"29":{"body":"Overall project advising, principal investigator.","breadcrumbs":"Team » Attributions » Linfeng Huang","id":"29","title":"Linfeng Huang"},"3":{"body":"Jiani Chen UG Class of 2023 Biology Yang Yu UG Class of 2023 Biology","breadcrumbs":"Team » Advisor","id":"3","title":"Advisor"},"30":{"body":"Oversee wet lab experiments and overall project advising.","breadcrumbs":"Team » Attributions » Jiani Chen","id":"30","title":"Jiani Chen"},"31":{"body":"Oversee wet lab experiments, helped optimize lab protocols and troubleshooting.","breadcrumbs":"Team » Attributions » Yang Yu","id":"31","title":"Yang Yu"},"32":{"body":"Thanks to the generous funding support of Duke Kunshan University Natural Science Divisions, Wang-Cai Biochemistry Lab, Synear Food Molecular Biology Lab, DKU Innovation and Entrepreneurship Initiative, and Marcia B. France, DKU Dean of Undergraduate Studies. Thanks to free licenses provided by SnapGene.","breadcrumbs":"Team » Attributions » Funding support","id":"32","title":"Funding support"},"33":{"body":"Thanks to Dr. Floyd Beckford and Dr. Huansheng Cao at Duke Kunshan University, Dr. Neel Joshi from Northwestern University, and Dr. Jisheng Lin at Sinovac Biotech CO.,LTD. for providing effective advice on our project design and development.","breadcrumbs":"Team » Attributions » Communications support","id":"33","title":"Communications support"},"34":{"body":"Collaborations Duke-DKU iGEM History Duke Kunshan University (DKU) is our sister school in Kunshan, China. Like Duke, DKU set out to provide a transformative and innovative education to students around the world. In addition, students are given the opportunity to study abroad in both semesters, further cementing our status as sister schools. Since taking its inaugural class of undergraduate students in 2018, DKU only had its very first iGEM team. Duke, on the other hand, has competed in the competition ever since 2006. Thus, when we learned about their interest in iGEM, we were beyond happy and excited to build a strong partnership between our teams. Our Partnership Since DKU iGEM only started in 2021, we continued to look to Duke iGEM for support and guidance. This year, we are still able to meet on the Duke campus and give each other suggestions. We shared the trouble shooting processes of our wet labs and reached mutual agreement to construct a PCR trouble shooting guide for future iGEM teams to use. dku-duke-group0","breadcrumbs":"Team » Collaborations » Collaboration with Duke iGEM","id":"34","title":"Collaboration with Duke iGEM"},"35":{"body":"CCiC certificate In order to carry out science communications on a larger scale, we participated the 9th CCiC Conference (Conference of China iGEMer Community), which is a national summit independently initiated by Chinese iGEM teams, aiming to provide a platform for iGEM teams to share resources and promote mutual learning and communication. We made poster and presented at the conference, answering questions from the audience and judges. After the conference, we collaborated with team LZU on science popularization about probiotics. CCiC photo","breadcrumbs":"Team » Collaborations » CCiC Meetup","id":"35","title":"CCiC Meetup"},"36":{"body":"Communications We had science communications during different stages of our project. Firstly, we designed a socially-oriented questionnaire to find out how much the public knows about shigella. Then,throughout expert interviews, we managed to gain insights of our project feasibility and possible future directions. Finally, we participated in on-campus communication to let more people know about shigella and surface display technology.","breadcrumbs":"Project » Overview","id":"36","title":"Overview"},"37":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Socially-Oriented Questionnaire","id":"37","title":"Socially-Oriented Questionnaire"},"38":{"body":"We interviewed Huansheng Cao, Assistant professor of Environmental Science at Duke Kunshan University for suggestions on our initial lab plans. In the interview, team members Yuxin Wang and Chang Shen presented the main design, bacterial surface display, to consult Prof Cao on its feasibility. After confirming the rich research foundations of our plan, he encouraged us to add computational elements to our lab design. As a scientist working in computational biology and bioinformatics, he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody and the antigen unit. As a well-trained biologist, he also suggested fitting our design to more than one model organisms, which shows integration in our drug design. The interview was full of enthusiasm, so we were able to come across many other topics. We discussed the trends in bioinformatics and biotechnology, including bacteria-based bioelectricity, and the relationship between human longevity and gut microbiota. This interview was both encouraging and informative, and contributed greatly to the first stage of human practice.","breadcrumbs":"Project » Interview with Prof. Cao","id":"38","title":"Interview with Prof. Cao"},"39":{"body":"After we successfully predicted the 3d structure of fusion protein-antibody complex by using Robetta and Alphafold2, the focus shift to how the fusion protein will influence the binding (docking) between antibody and antigen. We plan to get some insights about this from computer modeling before the wet lab begins. We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University for suggestions on our protein docking simulation. At the beginning, team leader Lisa Wu introduced the synthetic biology part of our project. Modeling team leader Zhenyu Xu introduced the progress of protein structure prediction and the need for protein docking simulation. As a scientist working in modern medicine, Prof. Floyd pointed us to some useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These software are powerful at predicting the docking scenario and are used by many researchers, with many online teaching resources accessible. To improve the speed of computer modeling, Prof. Floyd emphasized the preprocessing of protein structures. Namely, the antigen structure. He suggested us delete the floating molecules outside the binding sites and keep those inside, since we only care about the binding scenario. He also pointed that virtual screening could help if we want to do more mutations to the binding sites. Concerning the fusion protein-antibody complex models, since they are the optimal prediction given by Robetta and Alphafold2, we assume these models do not need preprocessing anymore. For docking, he suggested us try rigid docking first, and then flexible docking if we want to get closer to reality.","breadcrumbs":"Project » Interview with Prof. Beckford","id":"39","title":"Interview with Prof. Beckford"},"4":{"body":"Lingfeng Huang, Ph.D. Associate Professor of Biology, Duke Kunshan University","breadcrumbs":"Team » Principal Investigator","id":"4","title":"Principal Investigator"},"40":{"body":"Introduction Dr. Neel Joshi is an expert in bioengineering with tracks in human disease and new therapies. In his 2019 and 2021 literature, he and his team described genetically engineering E. coli Nissle 1917 to treat some gastrointestinal diseases like bowel inflammation, which provide essential references for our project. To further understand the logics and advantages of this bioengineered model, we invited Dr. Joshi for an interview. Dr. Joshi interview photo 1 Interview Content Q: What stimulated you and your team to develop the surface-displaced single domain antibodies? What practical problems do you think this model can solve? A: Although the nanobodies have great potentials in treating gastrointestinal diseases, it is somewhat hard to deliver those nanobodies directly to the digestive track. Therefore, the probiotics can serve as a scaffold to make the delivery of nanobodies easy. Q: But why did you choose to display the nanobodies on the surface? Why not directly make the bacteria synthesize nanobodies and release them? A: The surface display resolution has the property of multi-valency. By displaying the nanobodies on the surface, we would have the potential to space the binding domains together to bind to a pathogen surface. It could increase binding affinity and decrease the dissociation constant. It can also diffusion into different directions and increase the local concentration. Q: What about the method of drug delivery? That is to say, how do you decide to send the engineered probiotics to human gastrointestinal track? And could you explain why you use that delivery method? A: We only proposed an approach of micro biological therapy. But to deliver the bacteria, I think it can be freeze-dried to produce a freeze-dried product. Because a large portion of the geographical locations that suffered from these gut problems are the poor areas, and those areas do not have the condition to store the bacteria that require a very low temperature. The freeze-dried products do not require that strict storage conditions, so they are more available in those areas. Q: Why pBbB8k plasmid backbone with kanamycin selection marker? (what's the difference between pUC19, which is our choice, and pBbB8K?) A: pBbB8k is a rather arbitrary choice, we simply chose it because it was used due to antibiotics incompatibility in the previous experiment. When doing in vivo studies, we engineered plasmids from the original E. coli Nissle genome, the pMUT plasmids. These plasmids are more stable than the pBbB8K. For pUC19, I don’t see problems with the expression of pUC19 plasmid. However, you do need to consider if your antibiotic resistant marker in the plasmid is compatible with the shigella testing. If shigella is killed due to the antibiotic selecting E. coli, it can be a problem. Q: What are the setbacks of the Probiotic-associated therapeutic curli hybrids (PATCH) system? A: The first is safety concerns of curli fibers. It has been known that curli fibers induce various types of diseases, including neurological diseases, etc. The other is inherit disadvantages for E. coli to produce curli fibers in vivo. However, we have been able to shown effective production of curli fiber in vivo by measuring the amount of curli fibers coming from the fecal samples. Q: What if the E. coli went out of control and grow infinitely in the gut, disrupting the original gastrointestinal microorganism environment? A: This is a very popular question when it comes to distributing microbes to gut. Actually, we could use some of the auxotrophic strains to limit the growth of the bacteria. And I think there are many “switches†that can turn on the suicide program of those bacteria. But in this case, I think E. coli Nissle 1917 is a very safe bacteria, it has already been identified as a harmless bacterium, so there should be less safety issues of this strain. Q&A Section Q: Is it possible to apply magnetic triggers to shigella infection and cooperate this into the PATCH system? A: Magnetic triggers are mostly applied in cancer treatment. This is because in cancer, you know the spot of the disease. In bacterial infection it’s hard to locate. Q: In Barta et al., the authors described the different indexes of the nanobodies, including binding domains and neutralization effects. What is your rationale when choosing the nanobodies? A: It really depends on how you generate the nanobodies. When different parts of the pathogen are used in Alpaca immunizations, the nanobodies will vary. When displaying the nanobodies, some work and others don’t. We assume this is because of folding problems, but we did not figure out the exact reason. Q: What do you think about sequence optimization in silica? Do you have experience working with this? Do you have any suggestions? A: I would suggest generating different mutations in the sequence and do some docking analysis. Then generate the mutations and do wet labs. Q: Our project aims to tackle the antibiotic resistance problem worldwide. Would the PATCH system generate drug resistance issues? A: This is possible. For example, a mutation in the binding domain of the antigen might cause binding problems. However, I would say the selective pressure by the nanobody is smaller compared to that of the antibiotic. This is because antibiotic kills the pathogen, while PATCH only binds to the pathogen, keeping it from invasive activities. Q: We are worried that the proteins in the GI tract environment would coat the surface of the probiotic, which would cause dysfunction of the nanobodies. How did your team encounter this problem? A: The animal model was effective, which was sufficient to show that the GI tract environment did not inhibit the binding activity. The curli production is continuous in vivo, which provides adequate chance for the binding to occur. However, the proteases in the GI tract is something to consider. Summary and Reflection Dr. Joshi provided lots of perspectives from a brand-new aspect, which were extra inspirable for the whole team. First, Dr. Joshi elaborated on the practical problems that this model could potentially resolve. That the probiotic expression system could make the delivery of nanobodies easier expanded our understanding of the model as the delivery problem does not only exist in the step of bacteria delivery, it starts from the delivery of the essential nanobodies. Next, the freeze-dry delivery approach gives a less stricter storage condition of this drug, making it more available in poor areas, which corresponds with our assumed delivery method. As for the safety problem that the public is most interested in, Dr. Joshi proposed to use some molecular switches to eliminate those bacteria in addition to using safe strains like Nissle, giving important clue and indication for our project design. In the Q&A section, questions regarding drug localization, drug resistance, choice of nanobodies were mentioned by team members. Dr. Joshi gave many valuable advices depending on the questions. Overall, the interview was successful, and we were able to arm ourselves with adequate knowledge for the wet lab.","breadcrumbs":"Project » Interview with Dr. Neel Joshi","id":"40","title":"Interview with Dr. Neel Joshi"},"41":{"body":"See Entrepreneurship.","breadcrumbs":"Project » Interview with SINOVAC","id":"41","title":"Interview with SINOVAC"},"42":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus.","breadcrumbs":"Project » On-Campus Communication","id":"42","title":"On-Campus Communication"},"43":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the expert interviews enabled us to reflect on the feasibility and future directions of our lab design. These science communication helped us be more clear about the direction of the experiment and the significance of this project.","breadcrumbs":"Project » Summary","id":"43","title":"Summary"},"44":{"body":"Communications We had science communications during different stages of our project. Firstly, we designed a socially-oriented questionnaire to find out how much the public knows about shigella. Then,throughout expert interviews, we managed to gain insights of our project feasibility and possible future directions. Finally, we participated in on-campus communication to let more people know about shigella and surface display technology.","breadcrumbs":"Project » Communication » Overview","id":"44","title":"Overview"},"45":{"body":"Before the experiment, we designed and published a questionnaire about antibiotic treatment and dysentery on social network platform, and obtained more than 500 responses from people of different regions, age groups and education levels in China. We found that many people, although aware of dysentery, do not know how it is transmitted or the bacteria that causes it. This makes us realize the importance of science popularization. Meanwhile, people have different levels of concern about antibiotic resistance, which means it is necessary for us to focus on antibiotic therapy replacement.","breadcrumbs":"Project » Communication » Socially-Oriented Questionnaire","id":"45","title":"Socially-Oriented Questionnaire"},"46":{"body":"We interviewed Huansheng Cao, Assistant professor of Environmental Science at Duke Kunshan University for suggestions on our initial lab plans. In the interview, team members Yuxin Wang and Chang Shen presented the main design, bacterial surface display, to consult Prof Cao on its feasibility. After confirming the rich research foundations of our plan, he encouraged us to add computational elements to our lab design. As a scientist working in computational biology and bioinformatics, he pointed us to Alphafold2 for the enhancing the binding affinity of our nanobody and the antigen unit. As a well-trained biologist, he also suggested fitting our design to more than one model organisms, which shows integration in our drug design. The interview was full of enthusiasm, so we were able to come across many other topics. We discussed the trends in bioinformatics and biotechnology, including bacteria-based bioelectricity, and the relationship between human longevity and gut microbiota. This interview was both encouraging and informative, and contributed greatly to the first stage of human practice.","breadcrumbs":"Project » Communication » Interview with Prof. Cao","id":"46","title":"Interview with Prof. Cao"},"47":{"body":"After we successfully predicted the 3d structure of fusion protein-antibody complex by using Robetta and Alphafold2, the focus shift to how the fusion protein will influence the binding (docking) between antibody and antigen. We plan to get some insights about this from computer modeling before the wet lab begins. We interviewed Floyd Beckford, Professor of Chemistry at Duke Kunshan University for suggestions on our protein docking simulation. At the beginning, team leader Lisa Wu introduced the synthetic biology part of our project. Modeling team leader Zhenyu Xu introduced the progress of protein structure prediction and the need for protein docking simulation. As a scientist working in modern medicine, Prof. Floyd pointed us to some useful docking software--Autodock, ADFR suite, GOLD, and Maestro. These software are powerful at predicting the docking scenario and are used by many researchers, with many online teaching resources accessible. To improve the speed of computer modeling, Prof. Floyd emphasized the preprocessing of protein structures. Namely, the antigen structure. He suggested us delete the floating molecules outside the binding sites and keep those inside, since we only care about the binding scenario. He also pointed that virtual screening could help if we want to do more mutations to the binding sites. Concerning the fusion protein-antibody complex models, since they are the optimal prediction given by Robetta and Alphafold2, we assume these models do not need preprocessing anymore. For docking, he suggested us try rigid docking first, and then flexible docking if we want to get closer to reality.","breadcrumbs":"Project » Communication » Interview with Prof. Beckford","id":"47","title":"Interview with Prof. Beckford"},"48":{"body":"Introduction Dr. Neel Joshi is an expert in bioengineering with tracks in human disease and new therapies. In his 2019 and 2021 literature, he and his team described genetically engineering E. coli Nissle 1917 to treat some gastrointestinal diseases like bowel inflammation, which provide essential references for our project. To further understand the logics and advantages of this bioengineered model, we invited Dr. Joshi for an interview. Dr. Joshi interview photo 1 Interview Content Q: What stimulated you and your team to develop the surface-displaced single domain antibodies? What practical problems do you think this model can solve? A: Although the nanobodies have great potentials in treating gastrointestinal diseases, it is somewhat hard to deliver those nanobodies directly to the digestive track. Therefore, the probiotics can serve as a scaffold to make the delivery of nanobodies easy. Q: But why did you choose to display the nanobodies on the surface? Why not directly make the bacteria synthesize nanobodies and release them? A: The surface display resolution has the property of multi-valency. By displaying the nanobodies on the surface, we would have the potential to space the binding domains together to bind to a pathogen surface. It could increase binding affinity and decrease the dissociation constant. It can also diffusion into different directions and increase the local concentration. Q: What about the method of drug delivery? That is to say, how do you decide to send the engineered probiotics to human gastrointestinal track? And could you explain why you use that delivery method? A: We only proposed an approach of micro biological therapy. But to deliver the bacteria, I think it can be freeze-dried to produce a freeze-dried product. Because a large portion of the geographical locations that suffered from these gut problems are the poor areas, and those areas do not have the condition to store the bacteria that require a very low temperature. The freeze-dried products do not require that strict storage conditions, so they are more available in those areas. Q: Why pBbB8k plasmid backbone with kanamycin selection marker? (what's the difference between pUC19, which is our choice, and pBbB8K?) A: pBbB8k is a rather arbitrary choice, we simply chose it because it was used due to antibiotics incompatibility in the previous experiment. When doing in vivo studies, we engineered plasmids from the original E. coli Nissle genome, the pMUT plasmids. These plasmids are more stable than the pBbB8K. For pUC19, I don’t see problems with the expression of pUC19 plasmid. However, you do need to consider if your antibiotic resistant marker in the plasmid is compatible with the shigella testing. If shigella is killed due to the antibiotic selecting E. coli, it can be a problem. Q: What are the setbacks of the Probiotic-associated therapeutic curli hybrids (PATCH) system? A: The first is safety concerns of curli fibers. It has been known that curli fibers induce various types of diseases, including neurological diseases, etc. The other is inherit disadvantages for E. coli to produce curli fibers in vivo. However, we have been able to shown effective production of curli fiber in vivo by measuring the amount of curli fibers coming from the fecal samples. Q: What if the E. coli went out of control and grow infinitely in the gut, disrupting the original gastrointestinal microorganism environment? A: This is a very popular question when it comes to distributing microbes to gut. Actually, we could use some of the auxotrophic strains to limit the growth of the bacteria. And I think there are many “switches†that can turn on the suicide program of those bacteria. But in this case, I think E. coli Nissle 1917 is a very safe bacteria, it has already been identified as a harmless bacterium, so there should be less safety issues of this strain. Q&A Section Q: Is it possible to apply magnetic triggers to shigella infection and cooperate this into the PATCH system? A: Magnetic triggers are mostly applied in cancer treatment. This is because in cancer, you know the spot of the disease. In bacterial infection it’s hard to locate. Q: In Barta et al., the authors described the different indexes of the nanobodies, including binding domains and neutralization effects. What is your rationale when choosing the nanobodies? A: It really depends on how you generate the nanobodies. When different parts of the pathogen are used in Alpaca immunizations, the nanobodies will vary. When displaying the nanobodies, some work and others don’t. We assume this is because of folding problems, but we did not figure out the exact reason. Q: What do you think about sequence optimization in silica? Do you have experience working with this? Do you have any suggestions? A: I would suggest generating different mutations in the sequence and do some docking analysis. Then generate the mutations and do wet labs. Q: Our project aims to tackle the antibiotic resistance problem worldwide. Would the PATCH system generate drug resistance issues? A: This is possible. For example, a mutation in the binding domain of the antigen might cause binding problems. However, I would say the selective pressure by the nanobody is smaller compared to that of the antibiotic. This is because antibiotic kills the pathogen, while PATCH only binds to the pathogen, keeping it from invasive activities. Q: We are worried that the proteins in the GI tract environment would coat the surface of the probiotic, which would cause dysfunction of the nanobodies. How did your team encounter this problem? A: The animal model was effective, which was sufficient to show that the GI tract environment did not inhibit the binding activity. The curli production is continuous in vivo, which provides adequate chance for the binding to occur. However, the proteases in the GI tract is something to consider. Summary and Reflection Dr. Joshi provided lots of perspectives from a brand-new aspect, which were extra inspirable for the whole team. First, Dr. Joshi elaborated on the practical problems that this model could potentially resolve. That the probiotic expression system could make the delivery of nanobodies easier expanded our understanding of the model as the delivery problem does not only exist in the step of bacteria delivery, it starts from the delivery of the essential nanobodies. Next, the freeze-dry delivery approach gives a less stricter storage condition of this drug, making it more available in poor areas, which corresponds with our assumed delivery method. As for the safety problem that the public is most interested in, Dr. Joshi proposed to use some molecular switches to eliminate those bacteria in addition to using safe strains like Nissle, giving important clue and indication for our project design. In the Q&A section, questions regarding drug localization, drug resistance, choice of nanobodies were mentioned by team members. Dr. Joshi gave many valuable advices depending on the questions. Overall, the interview was successful, and we were able to arm ourselves with adequate knowledge for the wet lab.","breadcrumbs":"Project » Communication » Interview with Dr. Neel Joshi","id":"48","title":"Interview with Dr. Neel Joshi"},"49":{"body":"See Entrepreneurship.","breadcrumbs":"Project » Communication » Interview with SINOVAC","id":"49","title":"Interview with SINOVAC"},"5":{"body":"","breadcrumbs":"Team » The whole team","id":"5","title":"The whole team"},"50":{"body":"As an undergraduate team, we participated in the 2022's College Student Innovation and Entrepreneurship Training Program—a national training program for college students on innovation and entrepreneurship. In this way, we can better promote the topic of synthetic biology to the DKU community and attract more fresh blood to participate in innovation. We made posters and participated in project exhibitions, and were regularly inspected by the jury on campus.","breadcrumbs":"Project » Communication » On-Campus Communication","id":"50","title":"On-Campus Communication"},"51":{"body":"Throughout the project, we never stopped science communication with different groups. The social questionnaire allowed us to identify the need for the program; the school publicity has attracted a batch of fresh blood to join the research and innovation of synthetic biology; the expert interviews enabled us to reflect on the feasibility and future directions of our lab design. These science communication helped us be more clear about the direction of the experiment and the significance of this project.","breadcrumbs":"Project » Communication » Summary","id":"51","title":"Summary"},"52":{"body":"Contribution We designed cell surface display platforms for probiotics including yeast, E. coli Nissle 1917, and L. lactis . To be specific, the yeast Aga2 surface display platform for nanobodies were developed, We also designed a novel way to detect protein surface expression by using flow cytometry. Another contribution is protein modeling protocol. We designed an integrated protocol involving the usage of PyMol, RobeTTA, and Alphafold2. Through literature review, we were able to determine multiple parameters that measure the accuracy of the protein model, and conducted evaluation on our protein design. We also contributed to previous parts by designing our parts with imporvement based on past iGEM teams. Cell surface display platforms can be utilized to cater to many protein engineering and therapeutic drug design purposes. In our case, the therapeutic effect and the nanobody localization on the cellular membrane of yeast yields future possibilities for iGEM teams to utilize this surface display platform based on the yeast Aga2 protein, specifically for therapeutic designs, but possible to be utilized to express other proteins as well.","breadcrumbs":"Project » Contribution » Cell surface display platforms","id":"52","title":"Cell surface display platforms"},"53":{"body":"Online programs are helpful for visualizing and analyzing the structure of different proteins and their docking scenarios. We use Robetta and Alphafold2 to model the structures of our protein, and used HADDOCK to visualize the docking structure. Evaluation focuses on different parameters: Ramachandran plot, Overall G-factors, Atomic Z-score RMS, Percentage of the amino acids having scored >= 0.2 in the 3D/1D profile, Overall quality factor, and Z-score. These parameters determine whether a certain structure is stable. More details please see our Modeling Page","breadcrumbs":"Project » Contribution » Integrated protein modeling protocol","id":"53","title":"Integrated protein modeling protocol"},"54":{"body":"See Improvement","breadcrumbs":"Project » Contribution » Improvement of parts","id":"54","title":"Improvement of parts"},"55":{"body":"Project Description The Shigella species is listed as one of the eight dangerous drug resistant bacteria [1] , with associated mortalities projected to rise to 10 million globally by 2050, if not properly addressed [2] . In the United States alone, over 77,000 antibiotic resistant cases were reported annually and 90% of overall Shigella cases were found to be resistant to the first choice medication ciprofloxacin [3] . Shigella, as a highly infective, enteroinvasive and occasionally toxin-releasing [4] [5] bacterial genus, may cause severe infection and bacterial dysentery in the colorectal mucosa even with as low a dose as 10 - 100 organisms [6] . Shigella-related infections thereby spread rapidly, particularly in low-resource populations [7] and among vulnerable groups including children in care facilities, the homeless, and returned travelers [8] [9] [10] [5] . The use of conventional antibiotics aggravates the multidrug resistance of most Shigella strains. Besides aiding in the selection of resistant pathogens, antibiotics reduce intestinal species diversity and population, and disrupt the defensive, metabolic, and trophic functions of interdependent microbes [11] . Although antibiotics are able to prevent and treat infections, antibiotic exposure to the intestinal microbiota can lead to loss of colonization resistance, rendering the host more susceptible to future invasion [12] [13] . Engineered probiotics with cell surface display systems are an especially promising alternative that improve Shigella eradication rates without heavy reliance on antibiotics. Single VH domain (VHH) antibodies displayed on the probiotic surface reduce virulent activity of Shigella [14] through probiotic-pathogen binding while minimizing toxicity to non-targets [15] [16] . Specifically, these antibodies recognize and target epitopes within the tip complex that is conserved across all pathogens that utilize type III secretion system (T3SS) to translocate effector proteins into the host cells [15] . Innovations in VHH-ipaD binding not only offer a solution that preserves the potency of antibiotics and microbial composition of the gut microbiome, but also illuminates targeted approaches to treat related T3SS bacteria like Salmonella and enterohemorrhagic E. coli, and other novel opportunities for passive immunization [17] . Engineered probiotics with cell surface display systems are an especially promising alternative that improve Shigella eradication rates without heavy reliance on antibiotics. Single VH domain (VHH) antibodies displayed on the probiotic surface reduce virulent activity of Shigella [14] through probiotic-pathogen binding while minimizing toxicity to non-targets [15] [16] . Specifically, these antibodies recognize and target epitopes within the tip complex that is conserved across all pathogens that utilize type III secretion system (T3SS) to translocate effector proteins into the host cells [15] . Innovations in VHH-ipaD binding not only offer a solution that preserves the potency of antibiotics and microbial composition of the gut microbiome, but also illuminates targeted approaches to treat related T3SS bacteria like Salmonella and enterohemorrhagic E. coli, and other novel opportunities for passive immunization [17] .","breadcrumbs":"Project » Description » Background","id":"55","title":"Background"},"56":{"body":"","breadcrumbs":"Project » Description » Design","id":"56","title":"Design"},"57":{"body":"Y_Design Idea of probiotics Saccharomyces cerevisiae, or baker’s yeast, is widely used in food industry and scientific research. Its facultative anaerobic feature enables it to make fluffy bread [18] . Also, its variable metabolism pathways make it a good agent for alcohol fermentation and wine production [19] . Last but not least, the already-annotated genome makes it an excellent model organism for molecular biology research [20] . With all these features, yeasts have been considered to be safe by Food and Drug Administration for a long time. Apart from our treatment strategy, this probiotic has been engineered as new conceptual drugs for other diseases treatment, such as vaginal infections, diarrhea, and irritable bowel syndrome (IBS) [21] [22] . Compared to other prokaryotic probiotics, the eukaryotic yeast could support more complex protein folding, which is favorable for the generation of antibodies of interest. Moreover, previous works have successfully developed a mature Aga proteins yeast surface display system, which have been put in practical use in vaccine selection and sorting [23] [24] . This established surface display system largely reduces the engineering difficulty and increases the reliability of our engineering. Take all the considerations above, we put yeasts into our plan list. Design of pYD1-20ipaD plasmid for therapeutic yeast engineering One of the most important proteins in type III secretion system (T3SS) of pathogenic Shigella called ipaD is our attack target [25] . Because ipaD is the primary trigger to form translocon pores within the host cell membrane, the inhibition of it would probably inhibit the invasion of Shigella and thus treat the infection [26] [27] . Several single domain antibodies (nanobodies) have been previously reported to target ipaD, the most efficient of which is 20ipaD. Therefore, 20ipaD was chosen for further engineering. To have the yeasts displayed 20ipaD on surface, we adopted the strategy of Aga2 yeast surface display system. Aga2 is a membrane protein of S. cerevisiae, which would be sealed on membrane by the interaction with Aga16. By fusing the Aga2 protein with 20ipaD, the nanobody could thus be brought to the membrane, and that was what we designed as shown in the figure. Additionally, we introduced 3xFLAG tag behind 20ipaD for expression assays like immunofluorescent microscopic imaging, western blot, and FACS. The whole expression module was designed under the control of GAL1 promotor that can be induced by galactose to control the expression of the proteins of interest. We used pYD1 vector as the backbone which contains ampicillin resistance marker, E. coli replication origin, and tryptophan deficiency marker. These features enable us to store the recombinant plasmids in E. coli, and easily select the yeasts after transformation. Design of pYD1-ipaD plasmid for efficiency detection Shigella is one of the most infectious pathogens characterized by CDC [8] . Considering the health risks that could be risen during the experiments, we replace the real Shigella by yeasts anchored with the targeted epitope protein ipaD. The construction strategy of pYD1-ipaD was same as the pYD1-20ipaD discussed above except for the replacement of FLAG tag with HA tag. The yeasts containing pYD1-ipaD could display the antigen ipaD on their surfaces to mimic Shigella. With this pathogen analog, the binding affinity of the engineered therapeutic yeasts between the fake pathogens could be measured by whole cell ELISA and other binding affinity assays. Design of high production and high binding affinity plasmids for efficiency optimization After the proving the construction and binding capacity of the engineered yeast, optimization would be done to increase the efficiency of the product. Expression efficiency and binding affinity would be the two main aspects of optimization. To increase the expression efficiency of the nanobody, previously reported strong promoters, including SSA1 and PGK1, would be introduced to replace GAL1 promoter [28] . The expression abundancy would be compared, and the optimized promoter would be chosen. To increase the binding affinity of the nanobody, random mutations would be introduced to the 20ipaD sequence by error-prone PCR. The library would be screened for the optimization of nanobody targeting. Design of delivery of the engineered therapeutic yeasts by Shellac-based microcapsules Microbes, especially yeasts, are hard to preserve for a long time under room temperature. Besides, the acidic and digestive environment inside the gut prevents most organisms from getting to the intestine where Shigella locates in. In order to preserve the engineered yeasts and deliver them into the intestine with smallest deficiency, we designed the shellac-cased microcapsules. Shellac is a natural material that can be used as encapsulating material for microcapsules that can wrap and package molecular matters like drugs and cells [29] . The properties of shellac include high intensity, which can protect the encapsuled matters; hydrophobicity, making it easier for storage; only disintegrate at basic solution, which means that the microcapsules would not disintegrate in the acidic environment of stomach, but only dissolve in basic environment of small intestine where the target pathogen resides [30] . Previous research has proven the efficiency of shellac microcapsules delivery of probiotics [31] [32] [33] . With the light of this, we also designed the capsulation for the engineered yeasts. By producing the microcapsule powder of yeasts, they can be subsequently packaged into macro capsule entities and be productized.","breadcrumbs":"Project » Description » Yeast","id":"57","title":"Yeast"},"58":{"body":"L_Design Idea of probiotics The target probiotics, Lactococcus lactis (L. lactis) , is a lactic acid-producing Gram-positive species of bacteria that is used extensively in the food fermentation industry like the production of cheese and yoghurt. Therefore, it is generally considered as safe (GRAS) status by the Food and Drug Administration [34] . Apart from its important function in making food, L. lactis is often applied as the genetically modified organism for disease treatment of animals and humans [35] [36] . In many parts, it acts as an alternative for the gram positive to Bacillus subtilis and Lactobacillus plantarum, while it can also substitute the gram-negative counterpart, Escherichia coli[GarcÃa2012]. The small genome size (2.3 Mbp) that has been fully sequenced, plus the development of successfully compatible tools including cloning and expression systems with customizable options, have turned _L. lactis_into a desirable model for genetic engineering [34] . Design of 20ipad plasmid Due to the wide use of antibiotics, various types of bacteria have developed antibiotic resistance, thus providing great challenge to human health and therapy design. Our team’s target pathogen, the Shigella spp., is no exception. To overcome the issue of antibiotic resistance, we would like to engineer the probiotics to make it an effective tool for the treatment of shigella infections. Through literature review, it is identified that in the process of shigellosis (also named bacillary dysentery), Shigella uses the type III secretion system (T3SS) to invade colonic epithelial cells. Importantly, one important feature of T3SS is the existence of an extracellular needle with an associated tip complex responsible for assembly of a pore-forming translocon in the host cell membrane [15] . For Shigella flexneri, the tip complex contains invasion plasmid antigen D (IpaD) that not only regulates secretion but also provides the physical platform for the translocon pore [15] [37] . To explore the potential therapeutic avenues for managing infections of Shigella, researchers have developed single-VH domain antibodies (VHHs) that are capable of recognizing distinct epitopes within the antigen IpaD [15] , where one of such VHHs is the 20ipaD applied by our team. In order to have our probiotics L. lactis express the 20ipaD, we firstly constructed the 20ipaD plasmid. For plasmid design, the Usp45 signal peptide was included for secretion to the growth medium, while AcmA3b was included for surface anchoring of the expressed 20ipaD to L. lactis [38] . Flag-tag was added for the convenience of purification. Sequence of 20ipaD was surrounded by two restriction sites (BamHI and SacI respectively). The aim for such a design is that ideally, through the digestion of restriction enzymes, 20ipaD sequence could be obtained. Design of control group (3*Flag tag) with Flag-tag sequence In our future stage, we would fuse the Lactococcus lactis expression vector pNZ8148 with control flag-tag 3 to benefit the examination procedures, here the plasmid containing control group (3 Flag tag) with Flag-tag sequence was designed so that we could get the sequence of control flag-tag 3 from the plasmid. Construction of the plasmid was similar to that of 20ipaD, with Usp45 signal peptide (indicated in yellow) and AcmA3b (indicated in green) included. The sequence of control flag-tag 3 is shown in blue. Two restriction sites for the enzyme NcoI (indicated in dark green) and HindIII (indicated in dark blue) were designed so that during enzymatic digestion, sequence of control flag-tag*3 would be obtained.","breadcrumbs":"Project » Description » Lactococcus","id":"58","title":"Lactococcus"},"59":{"body":"E_design E. coli Nissle 1917, as a probiotic first isolated from the GI tract of healthy soldiers in WWI, has been proven to impose positive impacts on the human GI tract by supression and inhibition of GI tract pathogens. The current trend in developing Nissle for therapeutics is based on the fact that E. coli is one of the most developed model organisms for scientific research. It has a small genome, stability of expression, and is easy to culture. The detailed design of the E. coli surface display system is as follows. Through literature review, We have targeted two different display systems. One is based on E. coli curli operon. The curli fiber is a component of biofilm. The PATCH system developed form previous studies have been effective in displaying protiens of interest. Furthermore, the large capacity of the curli fiber presents multivalency, making it possible to display multiple proteins at arbitrarily close distance to bind simultaneously for the drug effective to take place. The plasmid design referenced the pM1s3ATScsg-Etag plasmid on Addgene (Plasmid #137946) from Neel Joshi Lab with the optimized synthetic curli operon. The other option is based on intimin. Intimin in E. coli has a trans-outer membrane region and a C-terminal repeat of Ig-like and lectin domains that can be used as a potential fusion site for protein display [39] . In some earlier studies, the researchers successfully inserted a fragment of EHEC intimin into a known plasmid vector with a VHH fusing to it and had it successfully express and display the VHH on the bacteria surface [40] . To fully exploit the multivalency advantage of the baterial surface display system, we plan to display more than on kind of nanobodies, so the probiotic can bind to a larger range of pathogens, or it can bind different antigens of the pathogen. It is also important to mention that the target antigen IpaD is highly conservative and exists in all strains of shigella. Also, previous studies have constructed a library of anti-IpaD VHH including VHH 20ipaD, JMKH2, and JPSG3 are found specifically bind to the epitopes in IpaD protein [15] [41] . The affinity of this antigen-VHH pair is considerable when using 20ipaD and JMKH2 [41] .","breadcrumbs":"Project » Description » E. coli","id":"59","title":"E. coli"},"6":{"body":"Team Yixuan Wu (Lisa) UG Class of 2024 Biology Yixuan Liu UG Class of 2024 Biology Sihan Wang UG Class of 2023 Biology Zhujun Yao UG Class of 2024 Biology Lingrui Lai UG Class of 2023 Biology Yuxin Wang UG Class of 2025 Jingyun Jin UG Class of 2024 Biology Chang Shen UG Class of 2025 Yunyi Ru UG Class of 2023 Biology Renwei Gao UG Class of 2023 Biology Qizhou Jiang UG Class of 2025","breadcrumbs":"Team » Team » Biology","id":"6","title":"Biology"},"60":{"body":"[4] Carayol, N. and Guy Nhieu. (2013). The Inside Story of Shigella Invasion of Intestinal Epithelial Cells. Cold Spring Harbor Perspectives in Medicine. Retrieved March 28, 2022, from http://perspectivesinmedicine.cshlp.org/content/3/10/a016717.full [6] Zaidi, M. B., & Estrada-GarcÃa, T. (2014, June 1). shigella: A highly virulent and elusive pathogen. Current tropical medicine reports. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4126259/ [2] O' Neill, J. (2014, December). Antimicrobial resistance: Tackling a crisis for the health and wealth of nations . Retrieved March 28, 2022, from https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf [1] Langdon, A., Crook, N., & Dantas, G. (2016). The effects of antibiotics on the microbiome throughout development and alternative approaches for therapeutic modulation. Genome Medicine, 8(1). https://doi.org/10.1186/s13073-016-0294-z [3] Centers for Disease Control and Prevention. (2015, April 2). Multidrug-resistant shigellosis spreading in the United States. [8] Centers for Disease Control and Prevention. (2020, October 8). Antibiotic resistance and Shigella infections. Centers for Disease Control and Prevention. Retrieved March 28, 2022, from https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html [7] Hussen, S., Mulatu, G., & Yohannes Kassa, Z. (2019). Prevalence of shigella species and its drug resistance pattern in Ethiopia: A systematic review and meta-analysis. Annals of Clinical Microbiology and Antimicrobials, 18(1). https://doi.org/10.1186/s12941-019-0321-1 [5] Gray, M. D., Lacher, D. W., Leonard, S. R., Abbott, J., Zhao, S., Lampel, K. A., Prothery, E., Gouali, M., Weill, F.-X., & Maurelli, A. T. (2015, May 14). Prevalence of shiga toxin-producing Shigella species isolated from French travellers returning from the Caribbean: An emerging pathogen with international implications. Clinical Microbiology and Infection. Retrieved March 28, 2022, from https://www.sciencedirect.com/science/article/pii/S1198743X15004437 [42] Huruy, K., Kassu, A., Mulu, A., Gebretsadik, S., Andargie, G., Tadesse, T., Birhan, W., Worku, N., Ghebreselassie, D., Belyhun, Y., Yifru, S., Adugna, S., & Tiruneh, M. (2008). High Level of Antimicrobial Resistance in Shigella Species Isolated From Diarrhoeal Patients in University of Gondar Teaching Hospital, Gondar, Ethiopia . Retrieved March 28, 2022, from https://pharmacologyonline.silae.it/files/archives/2008/vol2/29_Huruy.pdf [10] Casabonne, C., González, A., Aquili, V., & Balagué, C. (2016, November 22). Prevalence and virulence genes of Shigella spp.. isolated from patients with diarrhea in Rosario, Argentina. Japanese Journal of Infectious Diseases. Retrieved March 28, 2022, from https://www.jstage.jst.go.jp/article/yoken/69/6/69_JJID.2015.459/_article/-char/ja/ . [4] Carayol, N. and Guy Nhieu. (2013). The Inside Story of Shigella Invasion of Intestinal Epithelial Cells. Cold Spring Harbor Perspectives in Medicine. Retrieved March 28, 2022, from http://perspectivesinmedicine.cshlp.org/content/3/10/a016717.full [2] O' Neill, J. (2014, December). Antimicrobial resistance: Tackling a crisis for the health and wealth of nations . Retrieved March 28, 2022, from https://amr-review.org/sites/default/files/AMR%20Review%20Paper%20-%20Tackling%20a%20crisis%20for%20the%20health%20and%20wealth%20of%20nations_1.pdf [3] Centers for Disease Control and Prevention. (2015, April 2). Multidrug-resistant shigellosis spreading in the United States. [8] Centers for Disease Control and Prevention. (2020, October 8). Antibiotic resistance and Shigella infections. Centers for Disease Control and Prevention. Retrieved March 28, 2022, from https://www.cdc.gov/shigella/treatment/antibiotic-resistance-general.html [7] Hussen, S., Mulatu, G., & Yohannes Kassa, Z. (2019). Prevalence of shigella species and its drug resistance pattern in Ethiopia: A systematic review and meta-analysis. Annals of Clinical Microbiology and Antimicrobials, 18(1). https://doi.org/10.1186/s12941-019-0321-1 [5] Gray, M. D., Lacher, D. W., Leonard, S. R., Abbott, J., Zhao, S., Lampel, K. A., Prothery, E., Gouali, M., Weill, F.-X., & Maurelli, A. T. (2015, May 14). Prevalence of shiga toxin-producing Shigella species isolated from French travellers returning from the Caribbean: An emerging pathogen with international implications. Clinical Microbiology and Infection. Retrieved March 28, 2022, from https://www.sciencedirect.com/science/article/pii/S1198743X15004437 [42] Huruy, K., Kassu, A., Mulu, A., Gebretsadik, S., Andargie, G., Tadesse, T., Birhan, W., Worku, N., Ghebreselassie, D., Belyhun, Y., Yifru, S., Adugna, S., & Tiruneh, M. (2008). High Level of Antimicrobial Resistance in Shigella Species Isolated From Diarrhoeal Patients in University of Gondar Teaching Hospital, Gondar, Ethiopia . Retrieved March 28, 2022, from https://pharmacologyonline.silae.it/files/archives/2008/vol2/29_Huruy.pdf [10] Casabonne, C., González, A., Aquili, V., & Balagué, C. (2016, November 22). Prevalence and virulence genes of Shigella spp.. isolated from patients with diarrhea in Rosario, Argentina. Japanese Journal of Infectious Diseases. Retrieved March 28, 2022, from https://www.jstage.jst.go.jp/article/yoken/69/6/69_JJID.2015.459/_article/-char/ja/ [43] Shah, T., Baloch, Z., Shah, Z., Cui, X., & Xia, X. (2021, June 20). The intestinal microbiota: Impacts of antibiotics therapy, colonization resistance, and diseases. International journal of molecular sciences. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8235228/ [12] Kim, S., Covington, A., & Pamer, E. G. (2017, September). The intestinal microbiota: Antibiotics, colonization resistance, and enteric pathogens. Immunological reviews. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6026851/ [11] Francino, M. P. (2016, January 1). Antibiotics and the human gut microbiome: Dysbioses and accumulation of resistances. Frontiers. Retrieved March 28, 2022, from https://www.frontiersin.org/articles/10.3389/fmicb.2015.01543/full [14] Roehrich, A. D., Guillossou, E., Blocker, A. J., & Martinez-Argudo, I. (2013, February). Shigella IpaD has a dual role: Signal transduction from the type III secretion system needle tip and intracellular secretion regulation. Molecular microbiology. Retrieved March 28, 2022, from https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575693/ [16] Tremblay, J.M., Mukherjee, J., Leysath, C.E., Debatis, M., Ofori, K., Baldwin, K., Boucher, C., Peters, R., Beamer, G., Sheoran, A., Bedenice, D., Tzipori, S., & Shoemaker, C.B. (2013, December). A single VHH-based toxin-neutralizing agent and an effector antibody protect mice against challenge with shiga toxins 1 and 2. Infection and immunity. Retrieved March 28, 2022, from https://pubmed.ncbi.nlm.nih.gov/24082082/ [17] De Greve H., Virdi V., Bakshi S., & Depicker A. (2019, December 9). Simplified monomeric VHH-FC antibodies provide new opportunities for passive immunization. Current opinion in biotechnology. Retrieved March 28, 2022, from https://pubmed.ncbi.nlm.nih.gov/31810049/ [18] Sicard, D., Jean Luc, J., Legras, L. (2011). Bread, beer and wine: Yeast domestication in the Saccharomyces sensu stricto complex. Comptes Rendus Biologies, Elsevier, 2011, 229 - 236. ⟨10.1016/j.crvi.2010.12.016⟩. ⟨hal-02653082⟩ [19] Holt, S., Miks, M. H., de Carvalho, B. T., Foulquié-Moreno, M. R., Thevelein, J. M. (2019 May) The molecular biology of fruity and floral aromas in beer and other alcoholic beverages, FEMS Microbiology Reviews, 43(3), 193–222, https://doi.org/10.1093/femsre/fuy041 [20] Piskur, J., Langkjaer, R. B. (2004). Yeast genome sequencing: the power of comparative genomics. Molecular microbiology, 53(2), 381–389. https://doi.org/10.1111/j.1365-2958.2004.04182.x [21] Gaziano, R., Sabbatini, S., Roselletti, E., Perito, S., Monari, C. (2020). Saccharomyces cerevisiae-Based Probiotics as Novel Antimicrobial Agents to Prevent and Treat Vaginal Infections. Frontiers in microbiology, 11, 718. https://doi.org/10.3389/fmicb.2020.00718 [22] Palma, M. L., Zamith-Miranda, D., Martins, F. S., Bozza, F. A., Nimrichter, L., Montero-Lomeli, M., Marques, E. T., Jr, Douradinha, B. (2015). Probiotic Saccharomyces cerevisiae strains as biotherapeutic tools: is there room for improvement?. 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J., Picking, W. L., & Picking, W. D. (2009). Liposomes recruit IpaC to the Shigella flexneri type III secretion apparatus needle as a final step in secretion induction. Infection and immunity, 77(7), 2754–2761. https://doi.org/10.1128/IAI.00190-09 [8] Centers for Disease Control and Prevention. (2020). Shigella-Shigellosis. https://www.cdc.gov/shigella/index.html [28] Peng, B., Williams, T. C., Henry, M., Nielsen, L. K., Vickers, C. E. (2015). Controlling heterologous gene expression in yeast cell factories on different carbon substrates and across the diauxic shift: a comparison of yeast promoter activities. Microbial cell factories, 14, 91. https://doi.org/10.1186/s12934-015-0278-5 [29] Huang, X., Gänzle, M., Zhang, H., Zhao, M., Fang, Y., Nishinari, K. (2020). Microencapsulation of probiotic lactobacilli with shellac as moisture barrier and to allow controlled release. Journal of the Science of Food and Agriculture. 101. 10.1002/jsfa.10685. [30] Huang. X., Zhang, H., Peng, S., Zhao, M., Fang, Y. (2019). Tianrankeshixing Bicaichongjiao zai Gongnengzufenweinanghua zhongde Yingyonngyanjiujinzhan [Recent Progress in the Application Shellac as a Natural Edible Wall Material in the Microencapsulation of Functional Ingredients]. Shipinkexue [Food Science], 40(7), 317-324. [31] Mei, S., Han, P., Wu, H., Shi, J., Tang, L., Jiang, Z. (2018). One-pot fabrication of chitin-shellac composite microspheres for efficient enzyme immobilization. Journal of biotechnology, 266, 1–8. https://doi.org/10.1016/j.jbiotec.2017.11.015 [32] Gately, N. M., Kennedy, J. E. (2017). The Development of a Melt-Extruded Shellac Carrier for the Targeted Delivery of Probiotics to the Colon. Pharmaceutics, 9(4), 38. https://doi.org/10.3390/pharmaceutics9040038 [33] Hamad, S. A., Stoyanov, S. D., Paunov, V. N. (2013). Triggered release kinetics of living cells from composite microcapsules. Physical chemistry chemical physics: PCCP, 15(7), 2337–2344. https://doi.org/10.1039/c2cp42100c [35] Braat, H., Rottiers, P., Hommes, D. W., Huyghebaert, N., Remaut, E., Remon, J. P., . . . Steidler, L. (2006). A phase I trial with transgenic bacteria expressing interleukin-10 in Crohn's disease. Clin Gastroenterol Hepatol, 4(6), 754-759. doi:10.1016/j.cgh.2006.03.028 [36] de Moreno de LeBlanc, A., Del Carmen, S., Chatel, J. M., Azevedo, V., Langella, P., Bermudez-Humaran, L., & LeBlanc, J. G. (2016). Evaluation of the biosafety of recombinant lactic acid bacteria designed to prevent and treat colitis. J Med Microbiol, 65(9), 1038-1046. doi:10.1099/jmm.0.000323 [GarcÃa2012] GarcÃa-Fruitós, E. (2012). Lactic acid bacteria: a promising alternative for recombinant protein production. Microbial Cell Factories, 11(1), 157. doi:10.1186/1475-2859-11-157 [37] Muthuramalingam, M., Whittier, S. K., Picking, W. L., & Picking, W. D. (2021). The Shigella Type III Secretion System: An Overview from Top to Bottom. Microorganisms, 9(2). doi:10.3390/microorganisms9020451 [38] Plavec, T. V., & Berlec, A. (2019). Surface Anchoring on Lactococcus lactis by Covalent Isopeptide Bond. Acta Chim Slov, 66(1), 18-27. [34] Song, A. A.-L., In, L. L. A., Lim, S. H. E., & Rahim, R. A. (2017). A review on Lactococcus lactis: from food to factory. Microbial Cell Factories, 16(1), 55. doi:10.1186/s12934-017-0669-x [15] Barta ML, Shearer JP, Arizmendi O, Tremblay JM, Mehzabeen N, Zheng Q, et al. Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem 2017, 292(40), 16677–87. [41] Sierocki, R.; Jneid, B.; Delgado, M. L. O.; Plaisance, M.; Maillère, B.; Nozach, H.; Simon, S. An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLOS Neglected Tropical Diseases 2021, 15(3): e0009231 [39] (14) Sadana, P., Monnich, M., Unverzagt, C. and Scrima, A. Structure of the Y. pseudotuberculosis adhesin InvasinE. Protein Sci 2017, 26: 1182–1195. [40] Salema, V., Marın, E., Martınez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., et al. Selection of single domain antibodies from immune libraries displayed on the surface of E. coli cells with two b-domains of opposite topologies. PLoS One 2013, 8: e75126.","breadcrumbs":"Project » Description » References","id":"60","title":"References"},"61":{"body":"Engineering Cycle This page will give a detailed explanation about the engineering cycle. To make yeast capable of displaying the target nanobody 20ipaD on the cell surface, 20ipaD gene was inserted behind the yeast membrane-sealed protein Aga 2; therefore, Aga 2 would bring the nanobody to the cell surface. The recombinant plasmid pYD1-20ipaD was successfully built, which was supported by PCR amplification data and sequencing data. Apart from yeast, Lactococcus lactis and Escherichia coli were also chosen as probiotics for surface displace of nanobodies at the beginning, where 20ipaD/JPS-G3 and control 3xFLAG tags were inserted into pNZ8148 (L. lactis) and pET30a (E. coli) for expression respectively. However, due to failure in transformation and plasmid construction, only yeast was selected as the final product.","breadcrumbs":"Project » Engineering » Introduction","id":"61","title":"Introduction"},"62":{"body":"","breadcrumbs":"Project » Engineering » Engineering Cycle","id":"62","title":"Engineering Cycle"},"63":{"body":"y-engineering-cycle-high-resolution Cycle 1 Design We located a single-domain antibody (VHH) named 20ipaD from the database, whose binding ability with the needle tip protein ipaD of Shigella type III secretion system has be testified [1] [2] . Peptide sequences of 20ipaD from Barta et al (2017). Codon optimization was performed to get DNA sequences. Two flank sequences containing XhoI and ApaI cutting sites as well as C-terminal Flag-tag were added to the ipaD DNA sequence. Build Designed 20ipaD sequences were chemically de novo synthesized and sent in pUC19. XhoI and ApaI double-digestion enabled us to ligate the 20ipaD DNA sequence into pYD1, a plasmid allowing the surface display of the gene it carries in yeast. The ligation of 20ipaD into pYD1 generates a DNA sequencing coding a recombinant protein of 20ipaD and Aga2, a yeast extracellular membrane protein. pYD1 also contained a replication origin recognized by bacteria and an ampicillin resistance gene. After plasmid ligation, recombinant plasmids were transferred into E. coli to get a clone via ampicillin selection. Cloned plasmids were then transferred into yeast cells. Yeast cells containing the plasmid were selected by tryptophane-deficient medium. Expression of the recombinant protein was induced by add galactose. Test After transformation of recombinant plasmid into E. coli and single colony collection, we perform enzyme digestion and gel electrophoresis to check if the ligation and transformation is successful. For expression assay, we incubated induced yeast cells with anti-flag-tag primary antibody. After incubating with FITC conjugated secondary antibody, cells were examined under florescence microscopy and flow cytometry. Learn Recombinant proteins were observed to express on the cell surfaces on a portion of the cell population. We therefore planned to further testify the effectiveness of our recombinant protein. Though previous modeling through Rosetta suggested that the recombinant Aga2 region as well as the linkers sequences do not undermine the correct folding of the VHH part, we still sought for a experimental support as well as a way to quantify the binding affinity. Cycle 2 Design In this cycle, we aimed to test binding affinity between the recombinant nanobody and the ipaD epitopes. ipaD were retrieved from NCBI database. Codon optimization was also performed to collect the DNA sequence. Similar to 20ipaD, flank regions were inserted into ipaD except the substitution of Flag-tag to HA-tag. Build Synthesized ipaD sequences were got from the same company. Using the same method, we expressed ipaD recombinant protein of the yeast surface. Cycle 3 Design In this cycle, we aims to improve the expression level of the recombinant protein. Energy flows within the yeast cells would be controlled to concentrate more on protein production rather than other metabolic activities. We started by looking for a strong and continuously expressed promoter to drive the expression of 20ipaD recombinant protein. At the same time, we also tried to reduce other cellular activities. Cycle 4 Design In this cycle, we aims to improve the binding affinity of the recombinant protein with the antigen epitope. We would perform error prone PCRs to introduce mutations into 20ipaD sequences. Concentrations of the nucleotide analogs would be controlled so that only point mutants would be produced. All mutants would be screened to identify binding affinity improvements. To reduce the workload of screening, we would perform a modeling prescreen. In the prescreen, we would predict how single amino acid change influence the binding affinity between 20ipaD and ipaD.","breadcrumbs":"Project » Engineering » Yeast","id":"63","title":"Yeast"},"64":{"body":"Cycle 1 Design At first, we wanted to obtain the sequence of both 20ipaD and control flag-tag so that we could amplify them via PCR reaction. The 20ipaD is one of the single-VH domain antibodies (VHHs) capable of recognizing distinct epitopes within the antigen IpaD of pathogen Shigella. In this way, we hoped that by fusing 20ipaD and control flag-tag into the Lactococcus lactis expression vector pNZ8148, we would achieve the surface display and expression of 20ipaD on Lactococcus lactis . Build To obtain the sequence of 20ipaD, we constructed the plasmid with the 20ipaD sequence surrounded by two different restriction sites of enzymes BamHI and SacI. In this way, through the restrictive digestion of Bam HI and Sac I, ideally the sequence of 20ipaD would be obtained. The similar construction was also applied with the sequence of control flag-tag, where the enzymes used for restrictive digestion were changed to be NcoI and HindIII. Test After successfully received the synthesized plasmid sequence for 20ipaD and control flag-tag, we conducted the digestion of BamHI and SacI for the obtain of 20ipaD sequence, and the digestion of Nco I and Hind III for the obtain of control flag-tag sequence. Gel electrophorese was applied to confirm the size of the sequence. Control flag-tag sequence was successfully obtained. However, according to the gel picture, the band of 20ipaD showed a very different size from that in theory. Learn We checked the source of error and found that the designed sequence of 20ipaD has been inserted into the pUC19 vector when being synthesized by the company. Unfortunately, pUC19 vector also contained a restriction site for BamHI itself, thus leading to a different enzymatic digestion than what we have expected before. Cycle 2 Design Since pUC19 vector also contained a restriction site for BamHI itself, which would lead to unspecific enzymatic digestion and the failure of getting 20ipaD sequence, we redesigned the experimental steps in order to overcome such a problem. Build In this try, we would do the PCR amplification of 20ipaD sequence to insert it directly into the pNZ8148 vector first. This would circumvent the enzymatic digestion of pUC19 vector by BamHI that had the insertion of 20ipaD. Learn From this process we learnt that when the synthesized plasmid went wrong from our expectations, apart from directly asking the company to redo the synthesis, we could also alter the steps of ligation via PCR reaction to solve the problem. Cycle 3 Design We wanted to insert the engineered pNZ8148 vector with 20ipaD into the strain Lactococcus lactis NZ9000. According to literature review, electroporation is the commonly used technique to insert vectors into Lactococcus lactis . Build When the OD600 of Lactococcus lactis reached 0.3, the bacteria would be subjected to electroporation. The bacteria would be washed with liquid detergent I containing 0.5mol∙L-1 sucrose and 10% glycerol for the insertion of 0.2 μg vector. The pulse of electroporation was delivered by a Gene-Pulser (Scientz) at 25μF and 2.5kV, while the electroporation cuvette (0.2cm in size) was connected in parallel to a 400-Ω resistor (the parameters were searched online and were consulted from technician at Scientz). According to multiple researches done previously, the transformation efficiency would be the highest is the recovery time is 1.5h after electroporation. Test The process of electroporation was not successful because we failed to insert the vector into Lactococcus lactis . Learn We suspect that the making of electrocompetent cells might be the source of failure. After checking with the team advisor, we found that the type of glycerol used was intended for protein purification, which could cause problems for the electrocompetent cell. Cycle 4 Design To further increase efficiency, after doing more literature reviews we added the pretreatment of Lactococcus lactis with lithium acetate (LiAc) and/or dithiothreitol (DTT). We also substituted the type of glycerol used based on the previous error analysis. Build According to the newly found protocol, the Lactococcus lactis was firstly suspended at room temperature for 30 min in 8ml of 100mM LiAc, 10mM DTT, 0.6M sucrose, and 10mM Tris-HCl (pH=7.5). Following the treatment, Lactococcus lactis was pelleted and was resuspended in 1.5ml microcentrifuge tube, and was then washed as previously described. Afterwards, electroporation was conducted as previously described.","breadcrumbs":"Project » Engineering » Lactococcus lactis","id":"64","title":"Lactococcus lactis"},"65":{"body":"E. coli Engineering Cycle Cycle 1 Design Initially, we planned to try three different nanobodies (20ipaD, JPS-G3, and JMK-H2) agianst the Shigella antigen ipaD from a research paper [1] . We also wanted to try two different surface display systems, beta domain of the E. coli outer membrane protein intimin [3] and the E. coli curli fiber protein, csg B [4] . Our target probiotic is E. coli Nissle 1917 [4] . By inserting the target nanobody sequence behind intimin or csg B, reconstructing the plasmid pET30a and transforming the plasmid into E. coli Nissle 1917, we expect the protein to be displayed on the surface of E. coli , so that it can capture the pathogen via antigen-antibody binding. Build & Test We designed the following sequences to make the recombinant protein. intimin-20ipaD-3xFLAG csgB-JMK-H2-3xFLAG JPS-G3-3xFLAG ipaD-3xHA However, due to limitations in budget & time for gene synthesis, we only have JPS-G3-3xFLAG and ipaD-3xHA (inserted into pUC19 plasmids). By plasmid extraction, double digestion ( Bam HI & Xho I) and PCR, we successfully obtained the sequences and verified the accuracy by Sanger sequencing, but we don't have csgB or intimin for surface display. Learn Complex sequences including potential harmful genes may impact synthesis efficiency. Cycle 2 Design Alternatively, we chose the curli fiber csg A [5] sequence for surface display. Build & Test We designed the following sequences: csgA-JPS-G3-3xFLAG csgA-ipaD-3xHA (displaying the antigen on the surface of E. coli BL21 to mimic Shigella flexneri , so that the effectiveness can be evaluated) csg A gene is obtained from the E. coli strains (pGEX-4T-1-csgA-shMT) provided by the XJLTU iGEM team via PCR. To connect different parts, we plan to use overlapping PCR.","breadcrumbs":"Project » Engineering » Escherichia coli","id":"65","title":"Escherichia coli"},"66":{"body":"Salema, V., MarÃn, E., MartÃnez-Arteaga, R., Ruano-Gallego, D., Fraile, S., Margolles, Y., Teira, X., Gutierrez, C., Bodelón, G., & Fernández, L. Ã. (2013). Selection of Single Domain Antibodies from Immune Libraries Displayed on the Surface of E. coli Cells with Two β-Domains of Opposite Topologies. PLoS ONE , 8(9), e75126. https://doi.org/10.1371/journal.pone.0075126 Gelfat, I., Aqeel, Y., Tremblay, J. M., Jaskiewicz, J. J., Shrestha, A., Lee, J. N., Hu, S., Qian, X., Magoun, L., Sheoran, A., Bedenice, D., Giem, C., Manjula-Basavanna, A., Osburne, M. S., Tzipori, S., Shoemaker, C. B., Leong, J. M., & Joshi, N. S. (2021). Single domain antibodies against enteric pathogen virulence factors are active as curli fiber fusions on probiotic E. coli Nissle 1917 (p. 2021.06.18.448998). bioRxiv . https://doi.org/10.1101/2021.06.18.448998 Barta, M. L., Shearer, J. P., Arizmendi, O., Tremblay, J. M., Mehzabeen, N., Zheng, Q., Battaile, K. P., Lovell, S., Tzipori, S., Picking, W. D., Shoemaker, C. B., & Picking, W. L. (2017). Single-domain antibodies pinpoint potential targets within Shigella invasion plasmid antigen D of the needle tip complex for inhibition of type III secretion. J Biol Chem, 292(40), 16677-16687. https://doi.org/10.1074/jbc.M117.802231 Sierocki, R., Jneid, B., Orsini Delgado, M. L., Plaisance, M., Maillere, B., Nozach, H., & Simon, S. (2021). An antibody targeting type III secretion system induces broad protection against Salmonella and Shigella infections. PLoS Negl Trop Dis, 15(3), e0009231. https://doi.org/10.1371/journal.pntd.0009231","breadcrumbs":"Project » Engineering » Reference","id":"66","title":"Reference"},"67":{"body":"Experiments","breadcrumbs":"Project » Experiments » Yeast","id":"67","title":"Yeast"},"68":{"body":"Phases : 1. Stock vectors preparation and vectors storage; 2. Stock gene preparation and amplification; 3. Gene cloning, plasmid construction, storage, and verification; 4. Yeast transformation, protein display, and detection Phase I: Stock vectors preparation and vectors storage By the end of this phase, we would get: One tube of pYD1 vector stock solution One glycerol stock containing E. coli DH5α that were transformed with pYD1 vectors Phase II : Gene cloning, plasmid construction, storage, and verification By the end of this step, we would get: One tube of pY20ipaD recombinant stock solution (not pure) One glycerol stock containing E. coli DH5α that were transformed with pYD1 vectors Phase IV : Yeast transformation, protein display, and detection By the end of this phase, we would get: Glycerol stock of yeast that were transformed with recombinant plasmids Induced yeasts (display the nanobody on the surface)","breadcrumbs":"Project » Experiments » Experiment Overview","id":"68","title":"Experiment Overview"},"69":{"body":"Yeast Lab Notes","breadcrumbs":"Project » Experiments » Lab Notes","id":"69","title":"Lab Notes"},"7":{"body":"Sichang He (Steven) UG Class of 2024 Data Science Jasmine Santos UG Class of 2024 Biology Yuxiang He UG Class of 2025 Zhenyu Xu UG Class of 2024 Physics","breadcrumbs":"Team » Team » Modeling","id":"7","title":"Modeling"},"70":{"body":"\"One-step Method Competent Cell Preparation Kit\" from Beyotime was used for this experiment. The protocol follows the manual of the product [1] . E.coli_competent_cell_transformation Plasmid_Extraction Genetic_cloning_Enzyme_digestion_ligation \"DNA Agarose Gel Recycle Kit\" from Beyotime was used for this experiment. The protocol follows the manual of the product. [2] Gel_Purification.pdf \"Frozen-EZ Yeast Transformation II Kit\" from Zymo was used for this experiment. The protocol follows the manual of the product. [3] Yeast_Induction.pdf Fluorescence_Activated_Cell_Sorting.pdf \"FLAG Tag Immuno-precipitation Kit (Immunomagnetic Beads Method)\" from Beyotime was used for this experiment. The protocol follows the manual of the product [4] . Protein_Purification.pdf “TIANprep Mini Plasmid kit†was used for this experiment. The protocol follows the manual of the product [5] . Plasmid_Extraction.pdf","breadcrumbs":"Project » Experiments » Protocols","id":"70","title":"Protocols"},"71":{"body":"","breadcrumbs":"Project » Experiments » Escherichia coli","id":"71","title":"Escherichia coli"},"72":{"body":"Group E Workflow Group E. coli Experimental Procedures 1. Cloning 2. Recombinant Protein Expression 2.1 Express the Protein in E. coli DE3 Cytoplasm 3 different VHHs (JPS-G3, JMK-H2, 20ipaD) and 1 antigen (ipaD) are expressed separately in E. coli DE3 for protein purification. As is shown in the diagram below ( Figure 1 ), the DNA sequences of the proteins are bind to different detection tags (VHHs - FLAG-tag, antigen - HA-tag) and inserted into pET41a plasmids for bacterial transformation and protein purification. The pET41a plasmid contains a T7 promoter and a T7 terminator for high-level protein expression in E. coli DE3, and a GST tag with a Tb (thrombin) site for protein purification. After transformation, the exogenous proteins will be expressed by the bacteria. Fig.1 | Schematic Representation of the Protein Expression & Purification Process 2.2 Protein Purification and Affinity Test Next, we use the GST tag to purify the recombinant protein. The target proteins will be extracted via GSH-GST interaction, and the remaining GST tag will be cut by thrombin. Then, we can get the purified recombinant proteins (target protein + detection tag). Lastly, co-IP (immuno-precipitation) followed by Western analysis will be used to test the affinity between VHHs and the antigen. As is shown in the figure below ( Figure 2 ), by adding anti-FLAG antibodies and anti-HA antibodies to the samples, we can pull down the recombinant proteins with corresponding tags. If adding either anti-FLAG antibodies or anti-HA antibodies leads to a positive result in 'FLAG-VHH + HA-ipaD', we can say that there is high affinity between the expressed VHHs and the antigen. Fig.2 | Expected Western Blot Results of the co-IP Experiment 3. Surface Display 3.1 Surface Display via csgA CsgA, or major curlin subunit, is a component of biofilm. The design was a modified version of the PATCH system from Neel Joshi lab. It is composed of a temperature-controlled promoter, Csg synthetic operon, and the VHH targeting Type III secretion system. The design is predicted to be beneficial in a therapeutic context because biofilm formation effectively inhibits the invasion of shigella into epithelial cells. 3.2 Surface Display via intimin 3.3 Detecting E. coli surface display Congo red binding assay We use a quantitative congo-red binding assay to detect the expression of curli fibers. Congo red is a dye that binds to the hydroxyl group of polypeptide chains in amyloid through hydrogen bonds. A control group with no curli expression and a group with curli expression are cultured under the same condition. The 490nm absorbance of both groups are measured to quantify the amount of congo red not in binding with curli fiber (1) (2) . Whole cell filtration ELISA To detect the expression of curli fibers on the cell surface, we perform whole-cell ELISA. Whole-cell ELISA requires the cells to be seeded to the bottoms of the wells, providing conditions to detect proteins in whole cells (3) (4) . 3.4 Detecting the Binding Affinity Between E. coli Expressing VHHs and the antigen Aggregation Assay using OD600 measurements (5) Ag (antigen)-only E. coli , Nb (nanobody, i.e., VHHs)-only E. coli and the mixture of the two are cultured separately in LB liquid medium for 24 hours. OD600 of their supernatant are measured immediately/after 24 hours to see whether there is significant difference between the Ag-only group, Nb-only group, and mixture group. A significant low OD600 in the mixture group indicates that the E. coli expressing VHHs and antigens bind to each other, form assembly, and sink. Observing the Morphologies using Confocal Microscopy (5) GFP and m Cherry genes were expressed respectively in Ag-only E. coli and Nb-only E. coli . When observing the morphology via a confocal microscope, we should see that most neighbors of a certain bacterium should have opposite colors. Lab Notes E. coli Lab Notes Protocols E. coli Protocols","breadcrumbs":"Project » Experiments » Experiment Overview","id":"72","title":"Experiment Overview"},"73":{"body":"","breadcrumbs":"Project » Experiments » Lactococcus lactis","id":"73","title":"Lactococcus lactis"},"74":{"body":"L_Workflow","breadcrumbs":"Project » Experiments » Experiment Overview","id":"74","title":"Experiment Overview"},"75":{"body":"Because of financial and logistical reasons, wet lab experiments of group L were halted. We therefore can only present the experimental procedures and protocols designed by our members.","breadcrumbs":"Project » Experiments » Lab Notes","id":"75","title":"Lab Notes"},"76":{"body":"Group L intends to display 20ipaD, a nanobody against Shigella, onto L.lactis. The plasmid construction is performed in E. coli and then transformed into L.lactis. Electroporation_protocol_for_Lactococcus_lactis.pdf gel_extraction_protocol.pdf Plasmid_extraction_of_L.lactis__Gram_positive_bacteria_.pdf Protocol_for_activating_and_preparing_glycerol_stock.pdf Protocol_for_extracting_DNA_from_Lactococcus_Lactis_NZ9000.pdf Protocol_for_ligation.pdf Protocol_for_medium_making.pdf Protocol_for_restriction_enzyme_digestion.pdf plasmid extraction and gel purification are the same as Group Y. Solarbio_protocol_of_DNA_extraction.pdf Beyotime One-step Method Competent Cell Preparation Kit. https://www.beyotime.com/product/D0301.htm Beyotime DNA Agarose Gel Recycle Kit. https://www.beyotime.com/product/D0056.htm Zymo Frozen-EZ_Yeast_Transformation_II_Kit. https://files.zymoresearch.com/protocols/_t2001_frozen-ez_yeast_transformation_ii.pdf Beyotime FLAG Tag Immuno-precipitation Kit (Immunomagnetic Beads Method). https://m.beyotime.com/Manual/P2181%20Flag%E6%A0%87%E7%AD%BE%E8%9B%8B%E7%99%BD%E5%85%8D%E7%96%AB%E6%B2%89%E6%B7%80%E8%AF%95%E5%89%82%E7%9B%92(%E7%A3%81%E7%8F%A0%E6%B3%95).pdf TIANprep Mini Plasmid kit. https://en.tiangen.com/download/manual.html?one=34&two=1085&three=1086&id=4307","breadcrumbs":"Project » Experiments » Protocols","id":"76","title":"Protocols"},"77":{"body":"","breadcrumbs":"Project » Notebook","id":"77","title":"Project"},"78":{"body":"Implementation The end-products of our project are small tablets or capsules that contain dry powders of probiotics that express anti-Shigella antibodies on their surface. Our products serve the dual roles of Shigella infection precaution as well as disease therapy. The abilities of room temperature storage provide our tablets with cost reduction for storage and transportation. Tablets should be taken when facing potential exposure to Shigella infection sources, such as drinking unsanitary water in high diarrhea incidence areas. In consideration of the prevalent transmission pathways of Shigella, we also suggest people whose family members have developed Shigella infections and children in school with diarrhea cases take our tablets to prevent person-to-person transmission, which is the major form of Shigella spreading [1] .","breadcrumbs":"Project » Implementation » Infection Precaution","id":"78","title":"Infection Precaution"},"79":{"body":"Due to intracellular pathogen nature of Shigella, the effect of antibodies reduces as pathogens evade into the cells. The ability of reprogramming the infected cells to form protrusion adjacent cells allows Shigella to spread within intestine epithelial cells, reducing the chance of exposing to body internal environment [2] . This special characteristic implies antibody may not be a one-size-fits-all solution for different stages of infection. We call for the combination of clinical phases of antibiotics treatment with our tablets together.","breadcrumbs":"Project » Implementation » Infection Therapy","id":"79","title":"Infection Therapy"},"8":{"body":"Jiani Chen UG Class of 2023 Biology Yang Yu UG Class of 2023 Biology","breadcrumbs":"Team » Team » Advisor","id":"8","title":"Advisor"},"80":{"body":"Along with the high household transmission rates, Shigella also display high secondary infection rates. Therefore, we suggest families with members developing Shigella to take our pills for a time period to provide continuously protection apart from keep good hygiene conditions. In the meanwhile, patients who have developed Shigella infection before should also take our tablets when facing a second exposure.","breadcrumbs":"Project » Implementation » Prognosis and Secondary infection","id":"80","title":"Prognosis and Secondary infection"},"81":{"body":"People who exposed to potential Shigella infection source, especially in a household environment. Children in school with Shigella cases reported. People with antibiotic allergy that cannot use clinical antibiotic treatment. Government that aims to provide low cost solution for Shigella incidence in low- and middle- income, less developed region.","breadcrumbs":"Project » Implementation » End Users","id":"81","title":"End Users"},"82":{"body":"Our product contains exogenous antibody proteins. Therefore, allergy test may need to be performed to prevent possible anaphylaxis. Besides, considering the pathogenesis and transmission pathway of Shigella, our products may not be a one-size-fits all solution for all infection stages but focuses more on the prevention of infection.","breadcrumbs":"Project » Implementation » Caveats","id":"82","title":"Caveats"},"83":{"body":"Kotloff, K. L., Riddle, M. S., Platts-Mills, J. A., Pavlinac, P., & Zaidi, A. K. M. (2018). Shigellosis. The Lancet, 391(10122), 801-812. https://doi.org/https://doi.org/10.1016/S0140-6736(17)33296-8 Sansonetti, P. J., Mounier, J., Prévost, M. C., & Mège, R.-M. (1994). Cadherin expression is required for the spread of Shigella flexneri between epithelial cells. Cell, 76(5), 829-839. https://doi.org/https://doi.org/10.1016/0092-8674(94)90358-1","breadcrumbs":"Project » Implementation » References","id":"83","title":"References"},"84":{"body":"Partnership","breadcrumbs":"Project » Partnership » Meeting with XJLTU","id":"84","title":"Meeting with XJLTU"},"85":{"body":"They plan to develop a biofilter core to replace current industry filter cores for heavy metal wastewater. Specifically, they plan to engineer E. coli to express csgA protein at high levels and immobilize the bacteria into a filter. In that way, the heavy metal ions in the wastewater can be captured by csgA protein that is expressed by E. coli located in the filter.","breadcrumbs":"Project » Partnership » XJLTU's Project","id":"85","title":"XJLTU's Project"},"86":{"body":"They would like to know how we will interact with and educate the public. A: We have made questionnaires to evaluate their knowledge related to antibiotics, probiotics, and microorganisms. We are also planning to make some handouts and deliver a lecture about it in a high school. They were interested in the specific design of our plasmids. Specifically, it's about how and why we choose each part of the plasmid for surface display. A: We applied three microorganisms and the whole team was divided into three groups, each responsible for E. coli, Yeast cell and Lactococcus lactis. All groups applied a strategy which conjugates the targeted nanobody with a surface protein that is to be expressed, transported and located to the extracellular space. The surface protein and the targeted nanobody were connected with a linker sequence, and each nanobody is marked with at least one protein tag for their identification. We also provided links to igem parts so they can check it directly.","breadcrumbs":"Project » Partnership » Questions & Advice From XJLTU","id":"86","title":"Questions & Advice From XJLTU"},"87":{"body":"Will the biofilter be blocked due to E. coli proliferation? A: The microorganisms are immobilized in filters, and the filtration condition may not allow E. coli to grow at such a speed. The csgA protein's ability to absorb heavy metal ions under different conditions (like pH) can be tested through experiments. For example, we can put csg protein into a certain amount of wastewater, then adjust the pH and check the remaining concentration of metal ions in time, so we can acquire a proper pH for the protein to capture heavy metal ions.","breadcrumbs":"Project » Partnership » Questions & Advice From DKU","id":"87","title":"Questions & Advice From DKU"},"88":{"body":"Model for bacteria growth The XJLTU team developed a model for predicting bacteria growth, and it may also be applied to our situation by adjusting some of the parameters. Quantified expression of csg through controlling IPTG concentration The XJLTU team intended to control the expression of csg protein by adjusting the amount of IPTG inducer, which can also be a helpful approach for our team to check the relationship between the cell-cell adhesion affinity and the number of expressed nanobodies. However, as we also applied the TlpA promotor, it may influence the actual expression to a great extent and cause a big difference from the theoretical calculation. As a result, this approach remains to be a concern. Detection and measurement of displayed csg protein. The XJLTU team controlled the expression level by adjusting inducer concentration and estimated the expression by calculating theoretically. The condition of csg and heavy metal ions after the death of E. coli cells We consider that the heavy metal ions will remain captured, as protein itself has a great affinity to the heavy metal ions. But, it remains to be seen whether the released protein will leak out from the filter.","breadcrumbs":"Project » Partnership » Discussion Topics","id":"88","title":"Discussion Topics"},"89":{"body":"The novel drug we proposed was to anchor nanobodies on the surface of probiotics, including yeast, Lactococcus, and E. coli, which were then delivered to the gut through a shellac-membraned capsule to combat against pathogens like Shigella. Multiple objectives have been achieved to prove our product.","breadcrumbs":"Project » Proof of Concept » Overview","id":"89","title":"Overview"},"9":{"body":"Lingfeng Huang, Ph.D. Associate Professor of Biology, Duke Kunshan University","breadcrumbs":"Team » Team » Principal Investigator","id":"9","title":"Principal Investigator"},"90":{"body":"In order to enable yeast to express surface protein conjugated with target proteins, we cloned the nanobody gene sequence and the antigen gene sequences into the vectors. The vector pYD1 is a yeast surface display unit where the surface-sealed protein Aga2 was controlled by GAL1 promoter. Using XhoI and ApaI, the nanobody gene 20ipaD and the antigen gene ipaD was cloned into the corresponding restriction sites. The gene segment of 20ipaD was ~500bp, while that of ipaD was ~1000bp. The PCR results that amplify an originally ~400bp fragment of empty vector supported the success in plasmid construction (Figure 1, Figure 2). Sequencing data of the region further confirmed the construction of correct plasmids (Figure 3).","breadcrumbs":"Project » Proof of Concept » Construction of recombinant plasmids for yeast surface display","id":"90","title":"Construction of recombinant plasmids for yeast surface display"},"91":{"body":"Using the plasmids constructed in the previous steps, baker's yeast EBY100 was transformed. Considering the TRP1 maker in the plasmid, the yeast was selected on the SCDAA medium where tryptophan was absent. Colonies appeared after incubation, indicating the success of engineered probiotic construction (Figure 4). The yeasts that were transformed with recombinant plasmids were now able to display the nanobodies on their surface. Then, the yeasts were induced by galactose, which can promote the transcriptional activity of GAL1 promoter. After 24h induction, a portion of the cells were shown to display the anticipated proteins on their surface by immunofluorescent microscopic imaging (Figure 5). y-fig-1 y-fig-2 y-fig3 y-fig4 y-fig5","breadcrumbs":"Project » Proof of Concept » Construction of engineered yeasts that display nanobodies and capable for use","id":"91","title":"Construction of engineered yeasts that display nanobodies and capable for use"},"92":{"body":"As a drug of a novel strategy to target the pathogen, our engineered probiotics should combat the pathogenic Shigella by displaying nanobodies on surfaces to efficiently get over the antibiotic resistance problem. To prove the feasibility and efficiency of this proposed drug, evidence from different aspects should be taken into consideration. First, the most solid and important evidence should be the entity of the imagined product. In wet lab, we have shown the success construction of nanobody-displaying yeasts, proving the possibility and authenticity of producing such engineered probiotics. Second, whether the probiotic works to inhibit pathogen would be another important evidence to prove the efficiency of this drug. We also shown the success of pathogen-mimicking yeasts construction and proposed the binding affinity assay that could prove the inhibition feature of the engineered probiotics. Third, evidence for optimization possibility is required to prove the improvement potential of the drug. For the collection of evidence from this aspect, multiple expression enhancement elements refitting and mutation-screening binding affinity enhancement were designed to get the optimized combination of expression abundancy and binding affinity. Last but not least, a solid storage and delivery method should be risen as evidence proving the practicability and productization ability. The shellac-based microcapsulation plus tablet/capsule wrapping theoretically achieved the room temperature storage and intestine-target release of engineered probiotics, thus proving the reliability of low-cost production and storage of the whole drug and the target specificity of the efficient component.","breadcrumbs":"Project » Proof of Concept » Summary and conclusion","id":"92","title":"Summary and conclusion"},"93":{"body":"Results This page will give a detailed record about the experiment results, future plans & project achievements.","breadcrumbs":"Project » Results » Introduction","id":"93","title":"Introduction"},"94":{"body":"","breadcrumbs":"Project » Results » Experiment Results","id":"94","title":"Experiment Results"},"95":{"body":"Summary of Lab Design In order to decorate the yeast surface with nanobodies against the pathogen, we designed the vector which contains the nanobody gene behind a membrane-sealed protein. The overall experiment design could be divided into 3 phases. In phase I, the expected vector that could potentially express our designed module would be constructed and stored. In phase II, the expression vector would be transformed into yeast and detected for its expression abundance and location. In phase III, the binding affinity and inhibitory efficiency on pathogen would be tested. Due to the limitation of materials and time under the background of local pandemic situation, the experiments only accomplished Phase I & II. Genes of nanobody and pathogen were harvested The DNA sequence of nanobody 20ipaD and antigen ipaD were obtained from Sangon in the form of pUC19 plasmid insertions, which were stored inside E. coli. The storage bacteria were amplified, and plasmids containing sequences of interest were extracted with Plasmid mini-prep kit from TIangen. Those plasmids were digested by XhoI and ApaI, and the sequences of interest were recycled by agarose gel recycle kit from Beyotime ( Fig1 ). Recombinant plasmids were constructed The purified ipaD and 20ipaD DNA segments mentioned in the previous section, along with the pYD1 vector digested by XhoI & ApaI, were ligated, and transformed into DH5α cells that were selected by ampicillin. Colony direct PCR was applied to inspect the plasmid condition of the colonies formed. pYD1-forward and pyd1-reverse primers were used to show the size of Aga2-Protein, thus verifying the sequence between the primer pairs ( Table 1 ). The size of pYD1-ipaD plasmid primer box should be about 1500bp, while the size of pYD1-20ipaD should be about 1000bp. As shown in Fig2 a , sample “2-3â€, “2-5†meet the requirement for pYD1-ipaD, so the bacteria in those colonies contain the recombinant plasmid pYD1-ipaD. Additionally, all samples in lane 1~10 met the requirement for pYD1-ipaD, which indicates the bacteria in those colonies contain pYD1-20ipad recombinant plasmids ( Fig2 b ). Those colonies were amplified, and the plasmids were extracted. Sequencing data further supported the successful construction of the recombinant plasmids ( Fig3 ). Recombinant plasmids were transformed into yeast EBY100 We performed yeast transformation using constructed pYD1-ipaD and pYD1-20ipaD plasmids. Yeast competent cells were prepared by Frozen-EZ Yeast transformation II kit (Zymo Research, T2001). The yeasts were successfully transformed by chemical method using carrier DNA and PEG/LiAc. The plasmids and competent cells were thawed on ice. 10μL of Carrier DNA and 2μg of plasmid was added into 100μL of competent cells. Then 500μL of PEF/LiAc solution was added. The tube was inverted 6-8 times and incubated at 30°C with an inversion at 10-minute interval. Then, 20μL of DMSO was added to increase the transformation efficiency. Then, the tube was incubated under 42°C with an inversion of 5-minute interval. The cells were centrifuged at 12000rpm for 5 seconds and incubated with YPD medium for 1 hour at 30°C. After incubation, the cells were pelleted and resuspend by 100μL of 0.9% NaCl, 50μL of which were spread onto SDCAA medium, and another 50μL of cells onto YPD medium. The plates were incubated at 30°C for 2 days. The result of the plates was positive ( Fig4 ). SDCAA plates, which are the selective plates lack of tryptophan, has demonstrated fewer colony growth compared to YPD plates, indicating successful transformation. Single colonies were taken and incubated at 30°C in SDCAA liquid medium for amplification. Nanobody and antigen were expressed and displayed on yeast surface The yeasts that were transformed with pYD1-ipaD, pYD1-20ipaD, and pYD1 were amplified in SDCAA liquid medium for 36h. The cells were harvested by centrifuge at 5000xg for 5 minutes and diluted in SGCAA liquid containing the induction agent galactose to obtain an OD600=0.5. Four milliliters of each diluted cells were transferred into new culture tubes and induced at 21°C for 24h. An additional prep of EBY100 cells without plasmids were also diluted to OD600=0.5 and induced in SGCAA for 24h. The induced cells were harvested and washed with PBS. The yeasts containing pYD1-ipaD were inoculated with rabbit anti-HA tag antibodies, while the yeasts containing pYD1-20ipaD, pYD1, or no plasmids were inoculated with rabbit anti-FLAG tag antibodies and BSA. After washed with PBS, the cells were inoculated with FITC-conjugated goat anti-rabbit immunoglobin antibodies and BSA without light. The cells were washed twice with PBS before imaged under UV-light. As Fig5 shows, the yeasts containing pYD1-ipaD and pYD1-20ipaD emitted green fluorescence, whereas the yeasts containing empty plasmids, or no plasmids did not. This fluorescence pattern proved the yeasts indeed expressed and displayed the nanobody and the antigen on their surfaces, which announced the success of engineering. y-fig-1 y-fig-2 y-fig3 y-fig4 y-fig5","breadcrumbs":"Project » Results » Yeast","id":"95","title":"Yeast"},"96":{"body":"","breadcrumbs":"Project » Results » Lactococcus lactis","id":"96","title":"Lactococcus lactis"},"97":{"body":"Summary of Experiment Design We plan to display the nanobody JPS-G3 agianst the Shigella antigen ipaD on the surface of E. coli Nissle 1917 via the curli fiber protein csg A [1] . We expect the engineered E. coli Nissle 1917 to be capable of capturing the pathogen Shigella flexneri via antigen-antibody specific binding. Plasmid Extraction pUC19-JPS-G3-3xHA and pUC19-ipaD-3xHA were extracted using the TIANGEN plasmid extraction kit. Target Sequence Amplification Using following primers ( Table 1 ), the JPS-G3-3xHA and ipaD-3xHA sequences were successfully amplified, and the results were verified by gel electrophoresis ( Figure 1 ). PCR products were purified for further manipulation. Table 1 | PCR Primers Used Name Sequence (5' -> 3') Endonuclease Site ipaD_FW CGCGGATCCATGAATATTACAACTC Bam HI ipaD_RV GGCCTCGAGTCAAGCGTAG Xho I JPS-G3_FW CGCGGATCCGGAAGTACACAAGTACAGCTAG Bam HI JPS-G3_RV CGCGGATCCGGAAGTACACAAGTACAGCTAG Xho I Figure 1 | Gel Electrophoresis Result for Target Sequence Amplification Molecular Cloning for Cytoplasmic Protein Expression In order to construct the recombinant plasmids pET30a-ipaD-3xHA and pET30a-JPS-G3-3xFLAG, the PCR products obtained from the last step were digested by endonucleases Bam HI and Xho I to create sticky ends. Meanwhile, the pET30a plasmids were transformed into E. coli DH5a competent cells for propagation. After transformation and overnight culture, the extracted plasmids were also digested with endonucleases Bam HI and Xho I to create sticky ends. Afterwards, the digested plasmids and target sequences were ligated and transformed into E. coli DH5a competent cells ( Figure 2 ). Figure 2 | Plates for pET30a-ipaD-3xHA (i-1 & i-2) and pET30a-JPS-G3-3xFLAG (J-1 & J-2). Single colonies were picked from the plates and the inserted sequence were verified by colony PCR ( Figure 3 ) and Sanger sequencing. Figure 3 | Gel Electrophoresis Result for Colony PCR Overlap Extension PCR In order to construct the recombinant DNA sequences csgA-JPS-G3-3xFLAG and csgA-ipaD-3xHA, the following overlap extension PCR primers are used ( Table 2 ). Table 2 | Overlap Extension PCR Primers Name Sequence (5' -> 3') Endonuclease Site OvF_csgA-shMT CCGCGTGGATCCATGAAACTTTTAAAAGTAG Bam HI OvR1_csgA-shMT TAGCTGTACTTGTGTACTTCCCCGCTGCCGCCGTACTGATGA / OvR2_csgA-shMT TAGTCAGAGTTGTAATATTCATCCGCTGCCGCCGTACTGATGA / OvF_JPS-G3 CATCAGTACGGCGGCAGCGGGGAAGTACACAAGTACAGCTAGC / OvR_JPS-G3 GAATCTCGAGTTATTTGTCGTCGTCATCC Xho I OvF_ipaD CATCAGTACGGCGGCAGCGGATGAATATTACAACTCTGACTAAT / OvR_ipaD GGCCTCGAGTCAAGCGTAGTCAGGTAC Xho I However, due to time limitation, this part has not been successfully implemented.","breadcrumbs":"Project » Results » Escherichia coli","id":"97","title":"Escherichia coli"},"98":{"body":"(åªæ˜¯ä¸¾ä¾‹ï¼Œè¯·éšæ„更改)","breadcrumbs":"Project » Results » Project Achievements & Analysis Summary","id":"98","title":"Project Achievements & Analysis Summary"},"99":{"body":"Constructed the recombinant xxx plasmid, and transformed it into xxx strain. Expressed xxx protein. Effectiveness tested by xxx.","breadcrumbs":"Project » Results » 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+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item expanded "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item expanded "><a href="software.html" class="active">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -104,6 +104,12 @@
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/sustainable.html b/public/sustainable.html
index e34e39f3ceea1ca5a1dc8f57affdc3d8f9105764..ba27f7e2be6ea574f59f5cac5cea73c762478ae7 100644
--- a/public/sustainable.html
+++ b/public/sustainable.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item expanded "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item expanded "><a href="sustainable.html" class="active">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item "><a href="team.html">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="team.html">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item expanded "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item expanded "><a href="sustainable.html" class="active">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -154,7 +154,7 @@ spending) (UN, 2022).</p>
mainly focused on a novel method for battling antibiotic-resistant pathogens by
<strong>displaying nanobodies on the surface of the probiotics</strong>. While meeting the
goal, our laboratory team did various ways (using three different cells for
-trial: E. coli, Yeast and Lactococcus lactis) to achieve and increase the
+trial: E. coli, Yeast and <em>Lactococcus lactis</em>) to achieve and increase the
possibility of success. Additionally, our team collaborates with other iGEM
teams from developing countries to contribute to scientific advancement there.</p>
<h2 id="goal-17-partnerships-for-the-goals"><a class="header" href="#goal-17-partnerships-for-the-goals">Goal 17| Partnerships for the goals</a></h2>
@@ -204,6 +204,12 @@ Research, 126(3), 364–373. <a href="https://doi.org/10.1161/circresaha.119.315
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
<p>© 2022 - Content on this site is licensed under a
<a href="https://creativecommons.org/licenses/by/4.0/" rel="license">
Creative Commons Attribution 4.0 International license
diff --git a/public/team.html b/public/team.html
index 1d6557c9c063e6bfbe00ad58bbfffaf9b0036bba..92d8ff6f1064e2035787b16349f4e36a14e1aaaf 100644
--- a/public/team.html
+++ b/public/team.html
@@ -39,7 +39,7 @@
<body>
<nav id="sidebar" class="sidebar" aria-label="Table of contents">
<div class="sidebar-scrollbox scroll-smooth">
- <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item expanded "><a href="team.html" class="active">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item expanded "><a href="team.html" class="active">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="hardware.html">Hardware</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
+ <ol class="chapter"><li class="chapter-item "><a href="index.html">Home</a></li><li class="chapter-item expanded "><a href="team.html" class="active">Team</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item expanded "><a href="team.html" class="active">Team</a></li><li class="chapter-item "><a href="attributions.html">Attributions</a></li><li class="chapter-item "><a href="collaborations.html">Collaborations</a></li></ol></li><li class="chapter-item "><a href="communication.html">Project</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="communication.html">Communication</a></li><li class="chapter-item "><a href="contribution.html">Contribution</a></li><li class="chapter-item "><a href="description.html">Description</a></li><li class="chapter-item "><a href="engineering.html">Engineering</a></li><li class="chapter-item "><a href="experiments.html">Experiments</a></li><li class="chapter-item "><a href="notebook.html">Notebook</a></li><li class="chapter-item "><a href="implementation.html">Implementation</a></li><li class="chapter-item "><a href="partnership.html">Partnership</a></li><li class="chapter-item "><a href="proof-of-concept.html">Proof of Concept</a></li><li class="chapter-item "><a href="results.html">Results</a></li></ol></li><li class="chapter-item "><a href="model.html">Model</a></li><li class="chapter-item "><a href="part-collection.html">Parts</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="part-collection.html">Part Collection</a></li><li class="chapter-item "><a href="improve.html">Improve</a></li></ol></li><li class="chapter-item "><a href="safety.html">Safety</a></li><li class="chapter-item "><a href="human-practices.html">Human Practices</a></li><li class="chapter-item "><a href="education.html">Awards</a><a class="toggle"><div>â±</div></a></li><li><ol class="section"><li class="chapter-item "><a href="education.html">Education</a></li><li class="chapter-item "><a href="entrepreneurship.html">Entrepreneurship</a></li><li class="chapter-item "><a href="inclusivity.html">Inclusivity</a></li><li class="chapter-item "><a href="measurement.html">Measurement</a></li><li class="chapter-item "><a href="plant.html">Plant</a></li><li class="chapter-item "><a href="software.html">Software</a></li><li class="chapter-item "><a href="sustainable.html">Sustainable</a></li></ol></li><li class="chapter-item "><a href="LICENSE.html">LICENSE</a></li></ol>
</div>
<div id="sidebar-resize-handle" class="sidebar-resize-handle"></div>
</nav>
@@ -99,112 +99,147 @@
</article>
<main>
<link rel="stylesheet" href="katex/katex.min.css">
-<h1 id="team"><a class="header" href="#team">Team</a></h1>
+<div class="h1-bg">
+ <h1 class>Team</h1>
+ <img src="https://static.igem.wiki/teams/4161/wiki/team-bg.png" />
+</div>
<h2 id="biology"><a class="header" href="#biology">Biology</a></h2>
-<div class="grid items-end grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
+<div class="grid grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
<div>
<img alt="Lisa's Picture" src="https://static.igem.wiki/teams/4161/wiki/lisa-pic.jpg" class="max-w-full" />
<br />
-Yixuan Wu (Lisa)
+<p>Yixuan Wu (Lisa)<br />
+UG Class of 2024<br />
+Biology</p>
</div>
<div>
<img alt="Kathy's Picture" src="https://static.igem.wiki/teams/4161/wiki/yixuanliu-kathy.png" class="max-w-full" />
<br />
-Yixuan Liu
+<p>Yixuan Liu<br />
+UG Class of 2024<br />
+Biology</p>
</div>
<div>
<img alt="Sihan's Picture" src="https://static.igem.wiki/teams/4161/wiki/sihan-pic.jpg" class="max-w-full" />
<br />
-Sihan Wang
+<p>Sihan Wang<br />
+UG Class of 2023<br />
+Biology</p>
</div>
<div>
<img alt="Zhujun's Picture" src="https://static.igem.wiki/teams/4161/wiki/zhujun-pic.png" class="max-w-full" />
<br />
-Zhujun Yao
+<p>Zhujun Yao<br />
+UG Class of 2024<br />
+Biology</p>
</div>
<div>
<img alt="Lingrui's Picture" src="https://static.igem.wiki/teams/4161/wiki/ll-pic.jpg" class="max-w-full" />
<br />
-Lingrui Lai
+<p>Lingrui Lai<br />
+UG Class of 2023<br />
+Biology</p>
</div>
<div>
<img alt="Yuxin's Picture" src="https://static.igem.wiki/teams/4161/wiki/yuxin-wang-profile-photo.jpg" class="max-w-full" />
<br />
-Yuxin Wang
+<p>Yuxin Wang<br />
+UG Class of 2025</p>
</div>
<div>
<img alt="Irene's Picture" src="https://static.igem.wiki/teams/4161/wiki/irene-pic.jpg" class="max-w-full" />
<br />
-Jingyun Jin
+<p>Jingyun Jin<br />
+UG Class of 2024<br />
+Biology</p>
</div>
<div>
<img alt="sc's Picture" src="https://static.igem.wiki/teams/4161/wiki/sc-pic.jpg" class="max-w-full" />
<br />
-Chang Shen
+<p>Chang Shen<br />
+UG Class of 2025</p>
</div>
<div>
<img alt="Yunyi's Picture" src="https://static.igem.wiki/teams/4161/wiki/yunyi-pic.png" class="max-w-full" />
<br />
-Yunyi Ru
+<p>Yunyi Ru<br />
+UG Class of 2023<br />
+Biology</p>
</div>
<div>
-<br />
<img alt="Renwei's Picture" src="https://static.igem.wiki/teams/4161/wiki/renwei-pic.jpg" class="max-w-full" />
<br />
-Renwei Gao
+<p>Renwei Gao<br />
+UG Class of 2023<br />
+Biology</p>
</div>
<div>
<img alt="Qizhou's Picture" src="https://static.igem.wiki/teams/4161/wiki/qizhou-jiang-pic.jpg" class="max-w-full" />
<br />
-Qizhou Jiang
+<p>Qizhou Jiang<br />
+UG Class of 2025</p>
</div>
</div>
<h2 id="modeling"><a class="header" href="#modeling">Modeling</a></h2>
-<div class="grid items-end grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
+<div class="grid grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
<div>
<img alt="Steven's Picture" src="https://static.igem.wiki/teams/4161/wiki/steven-pic.jpg" class="max-w-full" />
<br />
-Sichang He (Steven)
+<p>Sichang He (Steven)<br />
+UG Class of 2024<br />
+Data Science</p>
</div>
<div>
<img alt="Jasmine's Picture" src="https://static.igem.wiki/teams/4161/wiki/jas-pic.jpg" class="max-w-full" />
<br />
-Jasmine Santos
+<p>Jasmine Santos<br />
+UG Class of 2024<br />
+Biology</p>
</div>
<div>
<img alt="Yuxiang's Picture" src="https://static.igem.wiki/teams/4161/wiki/img-1134.jpg" class="max-w-full" />
<br />
-Yuxiang He
+<p>Yuxiang He<br />
+UG Class of 2025</p>
</div>
<div>
<img alt="Bella's Picture" src="https://static.igem.wiki/teams/4161/wiki/bella.jpg" class="max-w-full" />
<br />
-Zhenyu Xu
+<p>Zhenyu Xu<br />
+UG Class of 2024<br />
+Physics</p>
</div>
</div>
<h2 id="advisor"><a class="header" href="#advisor">Advisor</a></h2>
-<div class="grid items-end grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
+<div class="grid grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
<div>
<img alt="Jiani's Picture" src="https://static.igem.wiki/teams/4161/wiki/jiani-pic.jpg" class="max-w-full" />
<br />
-Jiani Chen
+<p>Jiani Chen<br />
+UG Class of 2023<br />
+Biology</p>
</div>
<div>
-<img alt="Steven's Picture" src="https://static.igem.wiki/teams/4161/wiki/yang-yu.jpeg" class="max-w-full" />
+<img alt="Yang's Picture" src="https://static.igem.wiki/teams/4161/wiki/yang-yu.jpeg" class="max-w-full" />
<br />
-Yang Yu
+<p>Yang Yu<br />
+UG Class of 2023<br />
+Biology</p>
</div>
</div>
<h2 id="principal-investigator"><a class="header" href="#principal-investigator">Principal Investigator</a></h2>
-<div class="grid items-end grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
+<div class="grid grid-flow-row grid-cols-2 gap-4 text-center md:grid-cols-4">
<div>
-<img alt="Steven's Picture" src="https://static.igem.wiki/teams/4161/wiki/linfeng-huang.jpeg" class="max-w-full" />
+<img alt="Lingfeng's Picture" src="https://static.igem.wiki/teams/4161/wiki/linfeng-huang.jpeg" class="max-w-full" />
<br />
-Lingfeng Huang
+<p>Lingfeng Huang, Ph.D.<br />
+Associate Professor<br />
+of Biology,<br />
+Duke Kunshan University</p>
</div>
</div>
<h2 id="the-whole-team"><a class="header" href="#the-whole-team">The whole team</a></h2>
-<div class="grid items-end grid-flow-row grid-cols-1 gap-4 text-center">
+<div class="grid grid-flow-row grid-cols-1 gap-4 text-center">
<img alt="Photo of the whole team 1" src="https://static.igem.wiki/teams/4161/wiki/team-photo.jpg" />
<img alt="Photo of the whole team 2" src="https://static.igem.wiki/teams/4161/wiki/groupphoto2.png" />
</div>
@@ -213,6 +248,12 @@ Lingfeng Huang
<footer>
<hr />
+ <div class="flex justify-center">
+ <div class="flex justify-center">
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/ine-official.png" class="h-20 p-10" />
+ <img alt="SnapGene Logo" src="https://static.igem.wiki/teams/4161/wiki/snapgene-logo.png" class="h-20 p-10" />
+ </div>
+ </div>
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