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

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Date
2010-06
Authors
Mudrak, Benjamin
Kuehn, Meta J
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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 article
Subject
ETEC
GM1
blood antigen
heat-labile enterotoxin
lipopolysaccharide
Animals
Bacterial Toxins
Enterotoxins
Escherichia coli Proteins
G(M1) Ganglioside
Glycosides
Humans
Lipopolysaccharides
Protein Binding
Triterpenes
Permalink
https://hdl.handle.net/10161/10656
Published Version (Please cite this version)
10.3390/toxins2061445
Publication 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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Scholars@Duke

Kuehn

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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