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

Van Gerven N, De Greve H, Hernalsteens JP

Onderzoeksgroep Genetische Virologie, Faculteit van de Wetenschappen, Vrije Universiteit Brussel, Pleinlaan 2, Brussels, 1050, Belgium, Nani.Van.Gerven@vub.ac.be.

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.

Published 17 December 2007 in Antonie Van Leeuwenhoek, 93(1): 219-26.
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