| Literature DB >> 27773604 |
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.Entities:
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