ArticleMicrobial cell factories2013
Surface display of recombinant proteins on Escherichia coli by BclA exosporium of Bacillus anthracis.
Article in Microbial cell factories, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Ectopical expression of bacterial collagen-like protein supports its role as adhesin in host-parasite coevolution.Royal Society open science · 2024Article
- Enhancement of protein thermostability by three consecutive mutations using loop-walking method and machine learning.Scientific reports · 2021Article
- Surface Display of Complex Enzymes by in Situ SpyCatcher-SpyTag Interaction.Chembiochem : a European journal of chemical biology · 2020Article
- Sea Bass Immunization to Downsize the Betanodavirus Protein Displayed in the Surface of Inactivated Repair-Less Bacteria.Vaccines · 2019Article
- Autodisplay of an avidin with biotin-binding activity on the surface of Escherichia coli.Biotechnology letters · 2018Article
- A nanobody:GFP bacterial platform that enables functional enzyme display and easy quantification of display capacity.Microbial cell factories · 2016Article
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Authors and funding
6 authors.
Funding
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Abstract
backgroundThe anchoring motif is one of the most important aspects of cell surface display as well as efficient and stable display of target proteins. Thus, there is currently a need for the identification and isolation of novel anchoring motifs.
resultsA system for the display of recombinant proteins on the surface of Escherichia coli was developed using the Bacillus anthracis exosporal protein (BclA) as a new anchoring motif. For the surface display of recombinant proteins, the BAN display platform was constructed in which a target protein is linked to the C-terminus of N-terminal domain (21 amino acids) of BclA. The potential application of BAN platform for cell surface display was demonstrated with two model proteins of different size, the Bacillus sp. endoxylanase (XynA) and monooxygenase (P450 BM3m2). Through experimental analysis including outer membrane fractionation, confocal microscopy and activity assay, it was clearly confirmed that both model proteins were successfully displayed with high activities on the E. coli cell surface.
conclusionsThese results of this study suggest that the strategy employing the B. anthracis BclA as an anchoring motif is suitable for the display of heterologous proteins on the surface of E. coli and consequently for various biocatalytic applications as well as protein engineering.
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