Novel cell-binding activity specific for N-acetyl-D-glucosamine in an Escherichia coli strain.
Escherichia coli strains isolated from patients with different levels of urinary tract infection and from healthy persons were tested for their ability to haemagglutinate endo-beta-galactosidase-treated human erythrocytes. Among the 104 strains studied one revealed a strong agglutination reaction with the enzyme-treated erythrocytes. From the monosaccharides tested N-acetyl-D-glucosamine inhibited agglutination most effectively. Orosomucoid and asialo-orosomucoid had no effect on the haemagglutination whereas beta-galactosidase treated asialo-orosomucoid was inhibitory. These findings indicate that the E. coli strain studied contains a novel cell-binding activity with specificity for terminal N-acetyl-D-glucosamine residues.
D000117:Acetylglucosamine / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D005944:Glucosamine / Q000031:analogs & derivatives*; D006026:Glycoside Hydrolases; D006386:Hemagglutination Tests; D006801:Humans; D014552:Urinary Tract Infections / Q000382:microbiology; D001616:beta-Galactosidase / Q000378:metabolism
D006026:Glycoside Hydrolases; C026093:keratan-sulfate endo-1,4-beta-galactosidase; D001616:beta-Galactosidase; D005944:Glucosamine; D000117:Acetylglucosamine