Abstract:
: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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Sugii S,Tsuji Tdoi
10.1016/0378-1097(90)90256-psubject
Has Abstractpub_date
1990-01-01 00:00:00pages
45-50issue
1-3eissn
0378-1097issn
1574-6968journal_volume
54pub_type
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