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Toxins 2010, 2(6), 1445-1470; doi:10.3390/toxins2061445

Heat-Labile Enterotoxin: Beyond G M1 Binding

Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
Author to whom correspondence should be addressed.
Received: 29 April 2010 / Revised: 22 May 2010 / Accepted: 7 June 2010 / Published: 14 June 2010
(This article belongs to the Special Issue Enterotoxins)
View Full-Text   |   Download PDF [2404 KB, 17 June 2010; original version 14 June 2010]   |  


Enterotoxigenic Escherichia coli (ETEC) is a significant source of morbidity and mortality worldwide. One major virulence factor released by ETEC is the heat-labile enterotoxin LT, which is structurally and functionally similar to cholera toxin. LT consists of five B subunits carrying a single catalytically active A subunit. LTB binds the monosialoganglioside GM1, the toxin’s host receptor, but interactions with A-type blood sugars and E. coli lipopolysaccharide have also been identified within the past decade. Here, we review the regulation, assembly, and binding properties of the LT B-subunit pentamer and discuss the possible roles of its numerous molecular interactions.
Keywords: heat-labile enterotoxin; ETEC; GM1; lipopolysaccharide; blood antigen heat-labile enterotoxin; ETEC; GM1; lipopolysaccharide; blood antigen

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Mudrak, B.; Kuehn, M.J. Heat-Labile Enterotoxin: Beyond G M1 Binding. Toxins 2010, 2, 1445-1470.

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