Hemagglutinating activity of the B subunit(s) of the heat-labile enterotoxin isolated from human enterotoxigenic Escherichia coli |
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| Authors: | Shunji Sugii Takao Tsuji Takeshi Honda Toshio Miwatani |
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| Institution: | Department of Serology and Immunology, School of Medical Technology, Kitasato University, Kitasato, Kanagawa, Japan;Department of Bacteriology and Serrlogy, Research Institute for Microbiol Diseases, Osaka University, Osaka, Japan |
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| Abstract: | Abstract The hemagglutinating activity of the B subunit(s) of the heat-labile toxin (LTh - B) produced by human enterotoxigenic Escherichia coli was studied by hemagglutination and hemagglutination inhibition. Very strong hemagglutination of both neuraminidase- and pronase-treated human erythrocytes was induced by the LTh - B whereas that of intact ones was induced weakly or not at all by the LTh - B at the highest concentration used. Enhancement in hemagglitination of these human erythrocytes by the LTh - B was about 8- to 512-fold for type A and B erythrocytes and 16-fold for type O erthrocytes, respectively. On the other hand, no hemagglutination of intact and treated sheep erythrocytes was found by the LTh - B at the highest concentration used. Hemagglutination of pronase-treated human type B erythrocytes by the LTh - B was inhibited by galactose and melibiose among mono-, di- and polysaccharides used as inhibitors. These findings suggest that the LTh - B is a bacterial lectin specific for galactose-linked residues. |
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| Keywords: | Escherichia coli Enterotoxin heat-labile Haemagglutination (Human strain) |
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