Sialyloligosaccharide chains of laminin as an extracellular matrix target for S fimbriae of Escherichia coli.
S fimbriae purified from recombinant Escherichia coli HB101(pANN801-13) bound strongly to extracellular matrices of cultured endothelial and epithelial cells; only poor binding was seen with the fimbriae purified from the sfaS mutant strain HB101(pANN801-1321). E. coli HB101(pANN801-13) adhered strongly to laminin immobilized on glass; no adhesion was seen to type I, III, IV, or V collagen. Strain HB101(pANN801-1321) failed to adhere to any of the target proteins. Adhesion to laminin of strain HB101(pANN801-13) was inhibited by sialyl-alpha-2,3-lactose as well as by periodate oxidation and neuraminidase treatment of laminin. In Western blotting, the purified S fimbriae recognized more strongly the A chain than the B chains of laminin.
Virkola
R
R
Department of General Microbiology, University of Helsinki, Finland.
Parkkinen
J
J
Hacker
J
J
Korhonen
T K
TK
D001422:Bacterial Adhesion; D004926:Escherichia coli / Q000472:pathogenicity*; D005109:Extracellular Matrix / Q000382:microbiology*; D016326:Extracellular Matrix Proteins / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D066298:In Vitro Techniques; D007797:Laminin / Q000378:metabolism*; D037102:Lectins; D012795:Sialoglycoproteins / Q000378:metabolism*; D013329:Structure-Activity Relationship
D016326:Extracellular Matrix Proteins; D007797:Laminin; D037102:Lectins; D012795:Sialoglycoproteins