N-Acetyl-d-glucosamine specific hemagglutinin receptor ofVibrio choleraeO1 in chicken erythrocyte membranes

Abstract

N-Acetyl-D-glucosamine specific cell-associated hemagglutinin (HA)/lectin, previously purified from a strain of Vibrio cholerae O1, had been established as an adhesin molecule of V. cholerae O1 cells. This communication records the isolation and purification of the glycoprotein receptor of the N-acetyl-D-glucosamine specific HA of the V. cholerae O1 strain from chicken erythrocyte membranes. The most salient feature of this study is that the pretreatment of partially purified glycoprotein with purified HA could completely inhibit the hemagglutinating activity of the V. cholerae O1 strain with chicken erythrocytes.

Secretory protein Rv1987, a ‘probable chitinase’ fromMycobacterium tuberculosisis a novel chitin and cellulose binding protein lacking enzymatic function

“…Bordetella pertussis has been shown to secrete hemagglutinins containing carbohydrate recognition domains, which are involved in the adherence of bacteria to epithelial cells by binding to glycoconjugates on cell membranes [33], [34]. Another hemagglutinin of V. cholerae has been reported to be specific for Nacetyl-D-glucosamine, the monomeric subunit of chitin, and mediating binding of the bacterial cells to rabbit intestinal epithelial cells [35]. Furthermore, it has been shown that Klebsiella pneumoniae is internalized efficiently by cultured human epithelial cells, presumably via an N-glycosylated receptor containing N-acetyl-glucosamine residues [36].…”