Binding and hemagglutinating properties of the B subunit(s) of heat-labile enterotoxin isolated from human enterotoxigenic Escherichia coli.
The binding and hemagglutinating activities of the B subunit(s) of the heat-labile enterotoxin (LTh-B) isolated from human enterotoxigenic Escherichia coli were investigated. The binding of 125I-labeled LTh-B to neuraminidase-treated human type B erythrocytes was most effectively inhibited by ganglioside GM1. A number of mono-, di- and polysaccharides, as well as several glycoproteins were at least 500 times less potent inhibitors. However, hemagglutination was effectively inhibited by galactose, melibiose and hog A + H but not by ganglioside GM1. Preincubation of the LTh-B with ganglioside GM1 gave much stronger hemagglutination than LTh-B alone. These results suggest that the predominant binding substance for LTh-B on neuraminidase-treated human type B erythrocytes is ganglioside GM1, but indicate that the interaction of LTh-B with ganglioside GM1 is different in hemagglutination.
Sugii
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S
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Japan.
Tsuji
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T
D001427:Bacterial Toxins / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D001665:Binding Sites; D001667:Binding, Competitive; D004768:Enterotoxins / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D004912:Erythrocytes / Q000378:metabolism; D004926:Escherichia coli / Q000032:analysis* / Q000302:isolation & purification; D029968:Escherichia coli Proteins; D006385:Hemagglutination Inhibition Tests; D006388:Hemagglutinins / Q000302:isolation & purification; D006801:Humans; D066298:In Vitro Techniques; D008968:Molecular Conformation
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D006388:Hemagglutinins; C027538:heat-labile enterotoxin, E coli