Open AccessBinding to erythrocyte membrane glycoproteins and carbohydrate specificity of F41 fimbriae of enterotoxigenic Escherichia coli
Author(s) -
Lindahl Mats,
Wadström Torkel
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01424.x
Subject(s) - fimbria , glycophorin , enterotoxigenic escherichia coli , fucose , hemagglutination , monosaccharide , glycoprotein , galactose , biochemistry , microbiology and biotechnology , chemistry , escherichia coli , lectin , biology , membrane , enterotoxin , antibody , gene , immunology
Haemagglutination of enterotoxigenic Escherichia coli (ETEC) possessing F41 fimbriae was found to be inhibited by N ‐acetylgalactosamine. Other monosaccharides, such as N ‐acetylglucosamine, galactose and fucose were also inhibitors, although less effective than N ‐acetylgalactosamine. Purified F41 fimbriae bound to glycoproteins of human erythrocytes and glycophorin was found to act as an erythrocyte receptor for F41.