title: Heat-labile enterotoxin: beyond G(m1) binding.
abstract: 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.
authors: Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA. bm36@duke.edu
authors: Benjamin
authors: B
authors: Mudrak
authors: Meta J
authors: MJ
authors: Kuehn
mesh_terms: D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism*; D004768:Enterotoxins / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D005677:G(M1) Ganglioside / Q000378:metabolism; D006027:Glycosides / Q000378:metabolism; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism; D011485:Protein Binding; D014315:Triterpenes / Q000378:metabolism
chemical_list: D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D006027:Glycosides; D008070:Lipopolysaccharides; D014315:Triterpenes; C001883:stichoposide; D005677:G(M1) Ganglioside; C027538:heat-labile enterotoxin, E coli