Heat-Labile Enterotoxin: Beyond G M1 BindingAuthor(s): Benjamin Mudrak | Meta J. Kuehn
Journal: Toxins ISSN 2072-6651
Volume: 2; Issue: 6; Start page: 1445; Date: 2010;
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.