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Heat-Labile Enterotoxin: Beyond G M1 Binding

Author(s): Benjamin Mudrak | Meta J. Kuehn

Journal: Toxins
ISSN 2072-6651

Volume: 2;
Issue: 6;
Start page: 1445;
Date: 2010;
Original page

Keywords: heat-labile enterotoxin | ETEC | GM1 | lipopolysaccharide | blood antigen

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.