Differences in bindings to the GM1 receptor by heat-labile enterotoxin of human and porcine Escherichia coli strains.

Abstract

Heat-labile enterotoxin producing strains of Escherichia coli were isolated from diarrheal faeces of humans and from the jejunum of pigs which had died of diarrhea. The heat-labile enterotoxin was assayed by three different enzyme-linked immunosorbent assays (ELISA). The first assay was based upon immunological cross-reactions between the heat-labile enterotoxins of E coli and Vibrio cholerae, the second on specific E coli heat-labile enterotoxin antibodies and the third on affinity of the toxin to the presumed cell membrane receptor, the ganglioside GM1. The heat-labile enterotoxins of human and porcine origin bound equally well to the same extent in the ELISA procedure, which utilized immunological cross-reactivity between the heat-labile enterotoxins of E coli and V cholerae. The reactivity, however, was quite different in the GM1-ELISA. The binding affinity was high between GM1 and enterotoxin produced by E coli strains of human origin, whereas the binding affinity was low for enterotoxin from porcine strains.