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.
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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