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Heat-Labile Enterotoxin: Beyond G M1 Binding

1
Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA
2
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
*
Author to whom correspondence should be addressed.
Toxins 2010, 2(6), 1445-1470; https://doi.org/10.3390/toxins2061445
Received: 29 April 2010 / Revised: 22 May 2010 / Accepted: 7 June 2010 / Published: 14 June 2010
(This article belongs to the Special Issue Enterotoxins)
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. View Full-Text
Keywords: heat-labile enterotoxin; ETEC; GM1; lipopolysaccharide; blood antigen heat-labile enterotoxin; ETEC; GM1; lipopolysaccharide; blood antigen
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MDPI and ACS Style

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

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