Heat-labile enterotoxin: beyond G(m1) binding.
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2010-06
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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 G(M1), 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, Benjamin, and Meta J Kuehn (2010). Heat-labile enterotoxin: beyond G(m1) binding. Toxins (Basel), 2(6). pp. 1445–1470. 10.3390/toxins2061445 Retrieved from https://hdl.handle.net/10161/10656.
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