Binding and hemagglutinating properties of the B subunit(s) of heat-labile enterotoxin isolated from human enterotoxigenic Escherichia coli.

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 Lett

authors

Sugii S,Tsuji T

doi

10.1016/0378-1097(90)90256-p

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

45-50

issue

1-3

eissn

0378-1097

issn

1574-6968

journal_volume

54

pub_type

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