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Presentation of the functional receptor-binding domain of the bacterial adhesin F17a-G on bacteriophage M13.

作者信息

Van Gerven Nani, De Greve Henri, Hernalsteens Jean-Pierre

机构信息

Onderzoeksgroep Genetische Virologie, Faculteit van de Wetenschappen, Vrije Universiteit Brussel, Pleinlaan 2, Brussels, 1050 Belgium.

出版信息

Antonie Van Leeuwenhoek. 2008 Jan-Feb;93(1-2):219-26. doi: 10.1007/s10482-007-9195-x. Epub 2007 Aug 15.

DOI:10.1007/s10482-007-9195-x
PMID:17701282
Abstract

Bovine enterotoxigenic Escherichia coli (ETEC) carrying F17a fimbriae attach to the intestinal epithelium by means of the F17a-G adhesin. Since filamentous bacteriophages can be employed for the display of foreign peptides, we tested the applicability of this system to F17a-G. The receptor-binding domain of the F17a-G adhesin was expressed on bacteriophage M13, as an amino-terminal fusion with the phage protein pIII. This domain retained its N-acetyl-beta-D: -glucosamine binding activity. The phage presenting the fimbrial receptor-binding domain elicited an IgG response against F17a-G after intraperitoneal immunisation of mice.

摘要

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