Open AccessBinding of K99 fimbriae of enterotoxigenic Escherichia coli to pig small intestinal mucin glycopeptides
Author(s) -
Mattias Lindahl,
Ingemar Carlstedt
Publication year - 1990
Publication title -
journal of general microbiology/journal of general microbiology
Language(s) - English
Resource type - Journals
eISSN - 2059-9323
pISSN - 0022-1287
DOI - 10.1099/00221287-136-8-1609
Subject(s) - enterotoxigenic escherichia coli , fimbria , mucin , microbiology and biotechnology , escherichia coli , glycopeptide , mucus , biology , binding site , chemistry , small intestine , glycoprotein , pilus , sialic acid , biochemistry , enterotoxin , ecology , gene , antibiotics
Binding of purified K99 fimbriae to cryostat sections of pig small intestine was detected. Binding sites were located in the mucus layer, but not in the submucosal connective tissue. High-Mr mucin glycopeptides from pig small intestine were found to bind to K99-fimbriated enterotoxigenic Escherichia coli, in contrast to non-fimbriated cells. Sialic acid specificity of K99 fimbriae was demonstrated by the significant reduction in binding upon desialylation of mucin glycopeptides. The binding was saturable and the dissociation constant was estimated to be 6 x 10(-7) M. Fimbriated bacteria were calculated to possess 2.3 x 10(3) binding sites per cell.