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. 1993 Oct;61(10):4480–4484. doi: 10.1128/iai.61.10.4480-4484.1993

Sialyloligosaccharide chains of laminin as an extracellular matrix target for S fimbriae of Escherichia coli.

R Virkola 1, J Parkkinen 1, J Hacker 1, T K Korhonen 1
PMCID: PMC281183  PMID: 8104897

Abstract

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.

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Selected References

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