Open AccessBinding and hemagglutinating properties of the B subunit(s) of heat‐labile enterotoxin isolated from human enteroxigenic Escherichia coli
Author(s) -
Sugii Shunji,
Tsuji Takao
Publication year - 1990
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.1574-6968.1990.tb03970.x
Subject(s) - enterotoxin , heat labile enterotoxin , enterotoxigenic escherichia coli , ganglioside , hemagglutination , escherichia coli , neuraminidase , melibiose , microbiology and biotechnology , biochemistry , biology , protein subunit , chemistry , virology , enzyme , virus , gene , maltose
The binding and hemagglutinating activities of the B subunit(s)_of the heat‐labile enterotoxin (LT h ‐B) isolated from human enterotoxigenic Escherichia coli were investigated. The binding of 125 I‐labeled LT h ‐B to neuraminidase‐treated human type B erythrocytes was most effectively inhibited by ganglioside GM 1 . 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 GM 1 . Preincubation of the LT h ‐B with ganglioside GM 1 gave much stronger hemagglutination than LT h ‐B alone. These results suggest that the predominant binding substance for LT h ‐B on neuraminidase‐treated human type B erythrocytes is ganglioside GM 1 , but indicate that the interaction of LT h ‐B with ganglioside GM 1 is different in hemagglutination.