Presentation of the functional receptor-binding domain of the bacterial adhesin F17a-G on bacteriophage M13.
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.
Van Gerven
Nani
N
Onderzoeksgroep Genetische Virologie, Faculteit van de Wetenschappen, Vrije Universiteit Brussel, Pleinlaan 2, Brussels, 1050 Belgium. Nani.Van.Gerven@vub.ac.be
De Greve
Henri
H
Hernalsteens
Jean-Pierre
JP
D018829:Adhesins, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D017104:Bacteriophage M13 / Q000235:genetics / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D051379:Mice; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism
D018829:Adhesins, Bacterial; D011993:Recombinant Fusion Proteins