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      Heat-Labile Enterotoxin: Beyond G M1 Binding

      review-article
      Author(s): 1 , 2 , *
      Publication date (Electronic):
      Journal: Toxins
      Publisher: MDPI
      Keywords: heat-labile enterotoxin, ETEC, GM1, lipopolysaccharide, blood antigen

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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.

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          Most cited references103

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          Pathogenomics of the virulence plasmids of Escherichia coli.

          Timothy J Johnson, Lisa K Nolan (2009)
          Bacterial plasmids are self-replicating, extrachromosomal elements that are key agents of change in microbial populations. They promote the dissemination of a variety of traits, including virulence, enhanced fitness, resistance to antimicrobial agents, and metabolism of rare substances. Escherichia coli, perhaps the most studied of microorganisms, has been found to possess a variety of plasmid types. Included among these are plasmids associated with virulence. Several types of E. coli virulence plasmids exist, including those essential for the virulence of enterotoxigenic E. coli, enteroinvasive E. coli, enteropathogenic E. coli, enterohemorrhagic E. coli, enteroaggregative E. coli, and extraintestinal pathogenic E. coli. Despite their diversity, these plasmids belong to a few plasmid backbones that present themselves in a conserved and syntenic manner. Thanks to some recent research, including sequence analysis of several representative plasmid genomes and molecular pathogenesis studies, the evolution of these virulence plasmids and the implications of their acquisition by E. coli are now better understood and appreciated. Here, work involving each of the E. coli virulence plasmid types is summarized, with the available plasmid genomic sequences for several E. coli pathotypes being compared in an effort to understand the evolution of these plasmid types and define their core and accessory components.
          Article 0 comments Cited 181 times – based on 0 reviews     Review now
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            Enterotoxigenic Escherichia coli vesicles target toxin delivery into mammalian cells.

            Meta Kuehn, Norman Miller, N C Kesty … (2004)
            Enterotoxigenic Escherichia coli (ETEC) is a prevalent cause of traveler's diarrhea and infant mortality in third-world countries. Heat-labile enterotoxin (LT) is secreted from ETEC via vesicles composed of outer membrane and periplasm. We investigated the role of ETEC vesicles in pathogenesis by analyzing vesicle association and entry into eukaryotic cells. Fluorescently labeled vesicles from LT-producing and LT-nonproducing strains were compared in their ability to bind adrenal and intestinal epithelial cells. ETEC-derived vesicles, but not control nonpathogen-derived vesicles, associated with cells in a time-, temperature-, and receptor-dependent manner. Vesicles were visualized on the cell surface at 4 degrees C and detected intracellularly at 37 degrees C. ETEC vesicle endocytosis depended on cholesterol-rich lipid rafts. Entering vesicles partially colocalized with caveolin, and the internalized vesicles accumulated in a nonacidified compartment. We conclude that ETEC vesicles serve as specifically targeted transport vehicles that mediate entry of active enterotoxin and other bacterial envelope components into host cells. These data demonstrate a role in virulence for ETEC vesicles.
            Article 0 comments Cited 129 times – based on 0 reviews     Review now
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              Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin.

              B D Spangler (1992)
              Cholera and the related Escherichia coli-associated diarrheal disease are important problems confronting Third World nations and any area where water supplies can become contaminated. The disease is extremely debilitating and may be fatal in the absence of treatment. Symptoms are caused by the action of cholera toxin, secreted by the bacterium Vibrio cholerae, or by a closely related heat-labile enterotoxin, produced by Escherichia coli, that causes a milder, more common traveler's diarrhea. Both toxins bind receptors in intestinal epithelial cells and insert an enzymatic subunit that modifies a G protein associated with the adenylate cyclase complex. The consequent stimulated production of cyclic AMP, or other factors such as increased synthesis of prostaglandins by intoxicated cells, initiates a metabolic cascade that results in the excessive secretion of fluid and electrolytes characteristic of the disease. The toxins have a very high degree of structural and functional homology and may be evolutionarily related. Several effective new vaccine formulations have been developed and tested, and a growing family of endogenous cofactors is being discovered in eukaryotic cells. The recent elucidation of the three-dimensional structure of the heat-labile enterotoxin has provided an opportunity to examine and compare the correlations between structure and function of the two toxins. This information may improve our understanding of the disease process itself, as well as illuminate the role of the toxin in studies of signal transduction and G-protein function.
              Article 0 comments Cited 108 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Toxins (Basel)
                Journal ID (publisher-id): toxins
                Title: Toxins
                Publisher: MDPI
                ISSN (Electronic): 2072-6651
                Publication date (Electronic): 14 June 2010
                Publication date Collection: June 2010
                Volume: 2
                Issue: 6
                Pages: 1445-1470
                Affiliations
                [1 ]Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA; Email: bm36@ 123456duke.edu
                [2 ]Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
                Author notes
                [* ] Author to whom correspondence should be addressed; Email: meta.kuehn@ 123456duke.edu ; Tel.: +1-919-684-2545; Fax: +1-919-684-8885.
                Article
                Publisher ID: toxins-02-01445
                DOI: 10.3390/toxins2061445
                PMC ID: 3153253
                PubMed ID: 22069646
                SO-VID: 3e0eb176-b8a0-4309-be78-6ce0b60b8c58
                Copyright © © 2010 by the authors; licensee MDPI, Basel, Switzerland
                License:

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 29 April 2010
                Date revision received : 22 May 2010
                Date accepted : 07 June 2010
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular medicine
                Keywords: heat-labile enterotoxin,etec,gm1,lipopolysaccharide,blood antigen
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: heat-labile enterotoxin, etec, gm1, lipopolysaccharide, blood antigen

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