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@@ -435,7 +435,7 @@ Using the same method described in cycle 1-3, the contact efficacy of SVP-GNA fu
<figcaption class="figure-note"><strong>Fig.14</strong>| (A) Lethality data of SVPs with control over 24, 48, and 72 hours; data are the means of ± SD of three parallel replicate experiments (B) Survival plot of the SVPs along with supernatant of BL21(DE3) as control</figcaption></figure> <br><br>
<div class="subhead">Learn</div> <hr style="border: 2px #7078A9 solid; width: 60%;"><br>
The remarkable potency of SVPs, exemplified by rCtx-4, substantiates the efficacy of our engineering endeavors. Specifically, rCtx-4 displays a phenomenal 100% lethality of female <i>T. urticae</i> in merely 2 days. In the future, we hope that we will be able to provide a collection of SVPs and MVPs, suppressing drug resistance development. <br><br>
-To further optimize venom peptide production, we revisited the initial objective of extracellular expression, which can reduce production time and costs. Given the limitations of E. coli secretion systems, we therefore initiated engineering efforts using an eukaryotic chassis, <i>P. pastoris</i>. <br>
+To further optimize venom peptide production, we revisited the initial objective of extracellular expression, which can reduce production time and costs. Given the limitations of <i>E. coli</i> secretion systems, we therefore initiated engineering efforts using an eukaryotic chassis, <i>P. pastoris</i>. <br>
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@@ -453,14 +453,14 @@ To further optimize venom peptide production, we revisited the initial objective
<div class="contentprotocolhead">Design</div>
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Inspired by the interview we conducted with Professor Elaine Fitches(link hp), we decided to replace <i>E. coli</i> with <i>P. pastoris</i> (strain SMD1168H) as the chassis. With secretory tags, <i>P. pastoris</i> can hopefully secrete venom peptides, which can reduce the time and costs involved in sonication cell lysis. <br><br>
- We opted to synthesize several neurotoxins including Mbla, rCtx-4, HxTx-Hv1h, and Cs1A, which target a diverse range of molecular targets. Fusion proteins between them and GNA with a linker sequence of GGGGSAAA is engineered onto the vector pGAPZaB[15][Fig.15]. At the N-terminus of the toxin sequence, the P. pastoris secretory tag—the α-factor—is annexed to secrete the venoms extracellularly. Meanwhile, a polyhistidine tag is fused at the C-terminus, which could be used for optional protein purification[10]. <br><br>
+ We opted to synthesize several neurotoxins including Mbla, rCtx-4, HxTx-Hv1h, and Cs1A, which target a diverse range of molecular targets. Fusion proteins between them and GNA with a linker sequence of GGGGSAAA is engineered onto the vector pGAPZaB[15][Fig.15]. At the N-terminus of the toxin sequence, the <i>P. pastoris</i> secretory tag—the α-factor—is annexed to secrete the venoms extracellularly. Meanwhile, a polyhistidine tag is fused at the C-terminus, which could be used for optional protein purification[10]. <br><br>
<figure style="text-align: center;"><img src="https://static.igem.wiki/teams/5184/engineering/engineering-fig-15.webp" style="width: 50vw;display: inline-block;"><br>
- <figcaption class="figure-note"><strong>Fig.15</strong>| (A)Integration of venom peptide coding sequence into P. pastoris GAP integration locus (B) Integration loci after integration of GNA-SVP-His</figcaption></figure> <br><br>
+ <figcaption class="figure-note"><strong>Fig.15</strong>| (A)Integration of venom peptide coding sequence into <i>P. pastoris</i> GAP integration locus (B) Integration loci after integration of GNA-SVP-His</figcaption></figure> <br><br>
<div class="contentprotocolhead">Build</div> <hr style="border: 2px #7078A9 solid; width: 60%;"><br>
Digesting pGAPZaB with endonuclease Bsmb1, we linearized the sequences of rCtx4-GNA and Cs1A-GNA, exposing their homologous wall[Fig.16]. <br><br>
<figure style="text-align: center;"><img src="https://static.igem.wiki/teams/5184/engineering/engineering-fig-16.webp" style="width: 50vw;display: inline-block;"><br>
- <figcaption class="figure-note"><strong>Fig.16</strong>| Bsmb1-digested DNA sequences for integration into P. pastoris via HR</figcaption></figure> <br><br>
- By electrotransforming these two linearized sequences into competent cells of SMD1168H strain, the sequences are expected to be integrated into the yeast genome. We successfully obtained the yeast cultures. However, due to time limitations, we weren't able to perform colony PCR to verify our results. In the remaining time of October, we will continue exploring P. pastoris as the chassis, including the validation, fermentation, and expression of rCtx-4-GNA and Cs1A-GNA and other designs.
+ <figcaption class="figure-note"><strong>Fig.16</strong>| Bsmb1-digested DNA sequences for integration into <i>P. pastoris</i> via HR</figcaption></figure> <br><br>
+ By electrotransforming these two linearized sequences into competent cells of SMD1168H strain, the sequences are expected to be integrated into the yeast genome. We successfully obtained the yeast cultures. However, due to time limitations, we weren't able to perform colony PCR to verify our results. In the remaining time of October, we will continue exploring <i>P. pastoris</i> as the chassis, including the validation, fermentation, and expression of rCtx-4-GNA and Cs1A-GNA and other designs.
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@@ -513,7 +513,7 @@ In order to achieve better repellent effects, we decide to synthesize 9HZ and 9H
<p style="font-family: 'poppinsmedium';
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- color: white;"> We investigated the synthesis of the 9HZ and 9H10epoZ and the expression of enzymes found in eukaryotic cells using E. coli as chassis through truncating the N-terminus anchor region and introducing a SpyTag-SpyCatcher system.
+ color: white;"> We investigated the synthesis of the 9HZ and 9H10epoZ and the expression of enzymes found in eukaryotic cells using <i>E. coli</i> as chassis through truncating the N-terminus anchor region and introducing a SpyTag-SpyCatcher system.
<br>Click on the titles below for more details.</p>
<div class="accordion engineering" style="width: 100%;">
<div class="contentBx engineering">