Title | Presentation of the functional receptor-binding domain of the bacterial adhesin F17a-G on bacteriophage M13. |
Publication Type | Journal Article |
Year of Publication | 2008 |
Authors | Van Gerven, N., H. De Greve, and J-P. Hernalsteens |
Journal | Antonie Van Leeuwenhoek |
Volume | 93 |
Issue | 1-2 |
Pagination | 219-26 |
Date Published | 2008 Jan-Feb |
ISSN | 0003-6072 |
Keywords | Adhesins, 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. |
DOI | 10.1007/s10482-007-9195-x |
Alternate Journal | Antonie Van Leeuwenhoek |
PubMed ID | 17701282 |
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