Difference between revisions of "Part:BBa K4765001"

 
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__NOTOC__
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<partinfo>BBa_K4765001 short</partinfo>
  
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===Introduction===
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Intimin is a surface display system ,it was first described by Piñero-Lambea et. Al<ref>Piñero-Lambea, C., Bodelón, G., Fernández-Periáñez, R., Cuesta, A. M., Álvarez-Vallina, L., & Fernández, L. Á. (2015). Programming controlled adhesion of E. coli to target surfaces, cells, and tumors with synthetic adhesins. ACS Synthetic Biology, 4(4), 463–473. https://doi.org/10.1021/sb500252a</ref>. and tested by iGEM22_GreatBay_SCIE. It includes a short N-terminal signal peptide to direct its trafficking to the periplasm, a LysM domain for peptidoglycan binding, and a 12-stranded beta-barrel for transmembrane insertion.
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===Usage and Biology===
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The protein attached to the C-terminus of intimin can achieve outer membrane localization. In our project, intimin is fused with antigens, nanobodies, and lectins, facilitating their display on the membrane of Escherichia coli. This approach allows for the binding of E. coli- E. coli and E. coli to cyanobacteria.
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===Characterization===
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==Reference==

Revision as of 04:20, 30 September 2023

intimin

Introduction

Intimin is a surface display system ,it was first described by Piñero-Lambea et. Al[1]. and tested by iGEM22_GreatBay_SCIE. It includes a short N-terminal signal peptide to direct its trafficking to the periplasm, a LysM domain for peptidoglycan binding, and a 12-stranded beta-barrel for transmembrane insertion.

Usage and Biology

The protein attached to the C-terminus of intimin can achieve outer membrane localization. In our project, intimin is fused with antigens, nanobodies, and lectins, facilitating their display on the membrane of Escherichia coli. This approach allows for the binding of E. coli- E. coli and E. coli to cyanobacteria.

Characterization

Reference

  1. Piñero-Lambea, C., Bodelón, G., Fernández-Periáñez, R., Cuesta, A. M., Álvarez-Vallina, L., & Fernández, L. Á. (2015). Programming controlled adhesion of E. coli to target surfaces, cells, and tumors with synthetic adhesins. ACS Synthetic Biology, 4(4), 463–473. https://doi.org/10.1021/sb500252a