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