Literature DB >> 27773604

Engineering Escherichia coli to bind to cyanobacteria.

Zijian Zhang1, Liuyi Meng1, Congjian Ni1, Lanqiu Yao1, Fengyu Zhang1, Yuji Jin1, Xuelang Mu1, Shiyu Zhu1, Xiaoyu Lu1, Shiyu Liu1, Congyu Yu1, Chenggong Wang1, Pu Zheng1, Jie Wu1, Li Kang2, Haoqian M Zhang3, Qi Ouyang4.   

Abstract

We engineered Escherichia coli cells to bind to cyanobacteria by heterologously producing and displaying lectins of the target cyanobacteria on their surface. To prove the efficacy of our approach, we tested this design on Microcystis aeruginosa with microvirin (Mvn), the lectin endogenously produced by this cyanobacterium. The coding sequence of Mvn was C-terminally fused to the ice nucleation protein NC (INPNC) gene and expressed in E. coli. Results showed that E. coli cells expressing the INPNC::Mvn fusion protein were able to bind to M. aeruginosa and the average number of E. coli cells bound to each cyanobacterial cell was enhanced 8-fold. Finally, a computational model was developed to simulate the binding reaction and help reconstruct the binding parameters. To our best knowledge, this is the first report on the binding of two organisms in liquid culture mediated by the surface display of lectins and it may serve as a novel approach to mediate microbial adhesion.
Copyright © 2016 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.

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Keywords:  Binding; Cyanobacteria; Escherichia coli; Lectin; Microvirin; Surface display

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Year:  2016        PMID: 27773604     DOI: 10.1016/j.jbiosc.2016.09.010

Source DB:  PubMed          Journal:  J Biosci Bioeng        ISSN: 1347-4421            Impact factor:   2.894


  1 in total

1.  Surface Display of Small Affinity Proteins on Synechocystis sp. Strain PCC 6803 Mediated by Fusion to the Major Type IV Pilin PilA1.

Authors:  Ivana Cengic; Mathias Uhlén; Elton P Hudson
Journal:  J Bacteriol       Date:  2018-07-25       Impact factor: 3.490

  1 in total

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