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Comparative Study
. 1994 Dec;11(6):533-40.
doi: 10.1007/BF00731304.

Comparison of the Glycolipid-Binding Specificities of Cholera Toxin and Porcine Escherichia Coli Heat-Labile Enterotoxin: Identification of a Receptor-Active Non-Ganglioside Glycolipid for the Heat-Labile Toxin in Infant Rabbit Small Intestine

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Comparative Study

Comparison of the Glycolipid-Binding Specificities of Cholera Toxin and Porcine Escherichia Coli Heat-Labile Enterotoxin: Identification of a Receptor-Active Non-Ganglioside Glycolipid for the Heat-Labile Toxin in Infant Rabbit Small Intestine

S Teneberg et al. Glycoconj J. .

Abstract

The binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxin were investigated by binding of 125I-labelled toxins to reference glycosphingolipids separated on thin-layer chromatograms and coated in microtitre wells. The binding of cholera toxin was restricted to the GM1 ganglioside. The heat-labile toxin showed the highest affinity for GM1 but also bound, though less strongly, to the GM2, GD2 and GD1b gangliosides and to the non-acid glycosphingolipids gangliotetraosylceramide and lactoneotetraosylceramide. The infant rabbit small intestine, a model system for diarrhoea induced by the toxins, was shown to contain two receptor-active glycosphingolipids for the heat-labile toxin, GM1 ganglioside and lactoneotetraosylceramide, whereas only the GM1 ganglioside was receptor-active for cholera toxin. Preliminary evidence was obtained, indicating that epithelial cells of human small intestine also contain lactoneotetraosylceramide and similar sequences. By computer-based molecular modelling, lactoneotetraosylceramide was docked into the active site of the heat-labile toxin, using the known crystal structure of the toxin in complex with lactose. Interactions which may explain the relatively high toxin affinity for this receptor were found.

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