Open AccessHemagglutinating activity of the heat‐labile enterotoxin isolated from porcine enterotoxigenic Escherichia coli
Author(s) -
Sugii Shunji,
Tsuji Takao,
Honda Takeshi,
Miwatani Toshio
Publication year - 1988
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.1574-6968.1988.tb02712.x
Subject(s) - enterotoxigenic escherichia coli , enterotoxin , hemagglutination , pronase , melibiose , neuraminidase , microbiology and biotechnology , escherichia coli , heat labile enterotoxin , galactose , hemagglutinin (influenza) , biochemistry , hemagglutination assay , chemistry , biology , lectin , virology , raffinose , virus , sucrose , enzyme , trypsin , titer , gene
The hemagglutinating activity of the heat‐labile enterotoxin (LT p ) isolated from porcine enterotoxigenic Escherichia coli was studied by hemagglutination inhibition. The hemagglutinating activity of LT p was enhanced 64–512‐fold with pronase‐ and neuraminidase‐treated human erythrocytes although both intact human and sheep erythrocytes were not agglutinated by LT p at the highest concentration used. No enhancement was found in hemagglutination of neuraminidase‐treated sheep erythrocytes by LT p . Hemagglutination of pronase‐treated human type A erythrocytes induced by LT p was inhibited by melibiose and galactose among mono‐, di‐, and polysaccharides used as inhibitors. Galactose was a slightly better inhibitor than melibiose. These findings suggest that LT p is a bacterial lectin specific for galactose.