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

Heat-Labile Enterotoxin: Beyond G M1 Binding

1,* email and 2email
Received: 29 April 2010; in revised form: 22 May 2010 / Accepted: 7 June 2010 / Published: 14 June 2010
(This article belongs to the Special Issue Enterotoxins)
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Abstract: 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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

AMA Style

Mudrak B, Kuehn MJ. Heat-Labile Enterotoxin: Beyond G M1 Binding. Toxins. 2010; 2(6):1445-1470.

Chicago/Turabian Style

Mudrak, Benjamin; Kuehn, Meta J. 2010. "Heat-Labile Enterotoxin: Beyond G M1 Binding." Toxins 2, no. 6: 1445-1470.


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