biostudies-literature00540Mudrak BNIAID NIH HHS1445-70https://www.ebi.ac.uk/biostudies/studies/S-EPMC3153253biostudies-literatureUnknown2(6)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.ToxinsHeat-labile enterotoxin: beyond G(m1) binding.PMC3153253R01AI064464R01AI079068R01 AI079068R01 AI064464Kuehn MJMudrak B54falseHeat-labile enterotoxin: beyond G(m1) binding.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.2010-01-01T00:00:00Z2010 Jun2024-11-20T18:53:23.971Z2019-03-27T03:07:51ZS-EPMC31532532206964610.3390/toxins2061445