Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 1992 Dec;56(4):622-47.
doi: 10.1128/mr.56.4.622-647.1992.

Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin

B D Spangler  1
Affiliations
Review

Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin

B D Spangler. Microbiol Rev. 1992 Dec.

Abstract

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.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Infect Immun. 1992 Feb;60(2):406-15 - PubMed
    1. J Biol Chem. 1992 Jan 15;267(2):1020-6 - PubMed
    1. J Biol Chem. 1992 Feb 15;267(5):3230-5 - PubMed
    1. Nature. 1992 Feb 6;355(6360):561-4 - PubMed
    1. Nature. 1992 Feb 20;355(6362):748-50 - PubMed

Publication types

MeSH terms

LinkOut - more resources