Heat-labile enterotoxin: beyond G(m1) binding.

Journal Article (Journal Article;Review)

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.

Full Text

Duke Authors

Cited Authors

  • Mudrak, B; Kuehn, MJ

Published Date

  • June 2010

Published In

Volume / Issue

  • 2 / 6

Start / End Page

  • 1445 - 1470

PubMed ID

  • 22069646

Pubmed Central ID

  • PMC3153253

Electronic International Standard Serial Number (EISSN)

  • 2072-6651

Digital Object Identifier (DOI)

  • 10.3390/toxins2061445

Language

  • eng

Conference Location

  • Switzerland