Genetically engineered S and F1C fimbriae differ in their contribution to adherence of Escherichia coli to cultured renal tubular cells.
AUTOR(ES)
Marre, R
RESUMO
Escherichia coli K-12 strains producing S-fimbrial adhesins, F1C fimbriae, and mutagenized fimbriae were tested in a binding assay with a renal tubular cell line. S-fimbrial adhesins and F1C fimbriae mediated binding to tubular cells. The SfaA, SfaG, and SfaS subunits of S fimbriae contributed to attachment. Site-specific mutations in the sfaS gene reduced binding. The inhibition profile of F1C fimbriae resembled that of S fimbriae.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=313672Documentos Relacionados
- Receptor Structure for F1C Fimbriae of Uropathogenic Escherichia coli
- Binding of Escherichia coli S fimbriae to cultured human endothelial cells.
- Gene clusters for S fimbrial adhesin (sfa) and F1C fimbriae (foc) of Escherichia coli: comparative aspects of structure and function.
- F1C fimbriae of a uropathogenic Escherichia coli strain: genetic and functional organization of the foc gene cluster and identification of minor subunits.
- S fimbriae of uropathogenic Escherichia coli bind to primary human renal proximal tubular epithelial cells but do not induce expression of intercellular adhesion molecule 1.
