Article
The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes.
Molecular microbiology - 1 Sept 2006
Bouckaert Julie, Mackenzie Jenny, de Paz José L, Chipwaza Beatrice, Choudhury Devapriya, Zavialov Anton, Mannerstedt Karin, Anderson Jennifer, Piérard Denis, Wyns Lode, Seeberger Peter H, Oscarson Stefan, De Greve Henri, Knight Stefan D
Abstract excerpt
Type-1 fimbriae are important virulence factors for the establishment of Escherichia coli urinary tract infections. Bacterial adhesion to the high-mannosylated uroplakin Ia glycoprotein receptors of bladder epithelium is mediated by the FimH adhesin. Previous studies have attributed differences in mannose-sensitive adhesion phenotypes between faecal and uropathogenic E. coli to sequence variation in the FimH...
Topics
- Adhesins, Escherichia coli
- Amino Acid Sequence
- Bacterial Adhesion
- Carbohydrate Sequence
- Escherichia coli
- Fimbriae Proteins
- Fimbriae, Bacterial
- Hemagglutination
- Mannose
- Mannosides
- Microarray Analysis
- Molecular Sequence Data