Comparison of the Glycolipid-Binding Specificities of Cholera-Toxin and Porcin Escherichia-Coli Heart-Labile Enterotoxin - Identification of a Receptor-Active Non-Ganglioside Glycolipid for the Heart-Labile toxin in Infant Rabit Small- Intenstin

Teneberg, Susann and Hirst, Timothy R. and Angstrom, Jonas and Karlsson, Karl-Anders (1994) Comparison of the Glycolipid-Binding Specificities of Cholera-Toxin and Porcin Escherichia-Coli Heart-Labile Enterotoxin - Identification of a Receptor-Active Non-Ganglioside Glycolipid for the Heart-Labile toxin in Infant Rabit Small- Intenstin. Glycoconjugate Journal, 11 (6). pp. 533-540. ISSN 0282-0080. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)

Abstract

The binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxin were investigated by binding of I-125-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.

Item Type: Article
Uncontrolled keywords: GLYCOLIPID RECEPTOR; CHOLERA TOXIN; PORCINE ESCHERICHIA COLI HEAT-LABILE ENTEROTOXIN; INFANT RABBIT INTESTINE
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 18 Jun 2009 08:50
Last Modified: 13 Jun 2014 14:02
Resource URI: https://kar.kent.ac.uk/id/eprint/20070 (The current URI for this page, for reference purposes)
  • Depositors only (login required):