The GafD protein of the G (F17) fimbrial complex confers adhesiveness of Escherichia coli to laminin.
Escherichia coli IHE11088(pRR-5) expressing the G (F17) fimbria adhered to immobilized laminin as well as to reconstituted basement membranes. No adhesion was seen with the plasmidless strain IHE11088 or with the deletion derivative IHE11088(pHUB110), which expresses the G-fimbrial filament with a defective GafD lectin and lacks N-acetyl-D-glucosamine-specific binding. Adhesion of IHE11088(pRR-5) to laminin and to reconstituted basement membranes was specifically inhibited by N-acetyl-D-glucosamine, and adhesion was abolished after N-glycosidase F treatment of laminin. The results show that the GafD lectin binds to laminin carbohydrate and suggest a novel function for the F17 fimbria in binding to mammalian basement membranes.
Saarela
S
S
Department of Biosciences, University of Helsinki, Finland.
Westerlund-Wikström
B
B
Rhen
M
M
Korhonen
T K
TK
D000117:Acetylglucosamine / Q000378:metabolism; D018829:Adhesins, Bacterial / Q000235:genetics / Q000502:physiology*; D000818:Animals; D001422:Bacterial Adhesion / Q000235:genetics / Q000502:physiology*; D001485:Basement Membrane / Q000378:metabolism / Q000382:microbiology; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D029968:Escherichia coli Proteins; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000502:physiology*; D066298:In Vitro Techniques; D007797:Laminin / Q000378:metabolism*; D037102:Lectins / Q000235:genetics / Q000502:physiology*; D051379:Mice
D018829:Adhesins, Bacterial; D029968:Escherichia coli Proteins; D016326:Extracellular Matrix Proteins; C092493:GafD protein, E coli; D007797:Laminin; D037102:Lectins; D036781:Fimbriae Proteins; D000117:Acetylglucosamine