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

TitlePresentation of the functional receptor-binding domain of the bacterial adhesin F17a-G on bacteriophage M13.
Publication TypeJournal Article
Year of Publication2008
AuthorsVan Gerven, N., H. De Greve, and J-P. Hernalsteens
JournalAntonie Van Leeuwenhoek
Volume93
Issue1-2
Pagination219-26
Date Published2008 Jan-Feb
ISSN0003-6072
KeywordsAdhesins, Bacterial, Animals, Bacteriophage M13, Enzyme-Linked Immunosorbent Assay, Fimbriae, Bacterial, Mice, Protein Structure, Tertiary, Recombinant Fusion Proteins
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.

DOI10.1007/s10482-007-9195-x
Alternate JournalAntonie Van Leeuwenhoek
PubMed ID17701282