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.
Type
Journal articleSubject
ETECGM1
blood antigen
heat-labile enterotoxin
lipopolysaccharide
Animals
Bacterial Toxins
Enterotoxins
Escherichia coli Proteins
G(M1) Ganglioside
Glycosides
Humans
Lipopolysaccharides
Protein Binding
Triterpenes
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https://hdl.handle.net/10161/10656Published Version (Please cite this version)
10.3390/toxins2061445Publication Info
Mudrak, Benjamin; & Kuehn, Meta J (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.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Margarethe Joanna Kuehn
Associate Professor of Biochemistry
Enterotoxigenic E. coli (ETEC) causes traveler's diarrhea and infant mortality in
underdeveloped countries, and Pseudomonas aeruginosa is an opportunistic pathogen
for immunocompromised patients. Like all gram negative bacteria studied to date, ETEC
and P. aeruginosa produce small outer membrane vesicles that can serve as delivery
"bombs" to host tissues. Vesicles contain a subset of outer membrane and
soluble periplasmic proteins and lipids. In tissues and sera of infected hosts,

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