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PMID: 6752418 Published · ppublish English Journal Article Review

Role of membrane gangliosides in the binding and action of bacterial toxins.

The Journal of membrane biology ·Vol. 69 ·No. 2 ·1982-00-00 ·Pages 85-97

Fishman PH

Abstract

Gangliosides are complex glycosphingolipids that contain from one to several residues of sialic acid. They are present in the plasma membrane of vertebrate cells with their oligosaccharide chains exposed to the external environment. They have been implicated as cell surface receptors and several bacterial toxins have been shown to interact with them. Cholera toxin, which mediates its effects on cells by activating adenylate cyclase, bind with high affinity and specificity to ganglioside GM1. Toxin-resistant cells which lack GM1 can be sensitized to cholera toxin by treating them with GM1. Cholera toxin specifically protects GM1 from cell surface labeling procedures and only GM1 is recovered when toxin-receptor complexes are isolated by immunoadsorption. These results clearly demonstrate that GM1 is the specific and only receptor for cholera toxin. Although cholera toxin binds to GM1 on the external side of the plasma membrane, it activates adenylate cyclase on the cytoplasmic side of the membrane by ADP-ribosylation of the regulatory component of the cyclase. GM1 in addition to functioning as a binding site for the toxin appears to facilitate its transmembrane movement. The heat-labile enterotoxin of E. coli is very similar to cholera toxin in both form and function and can also use GM1 as a cell surface receptor. The potent neurotoxin, tetanus toxin, has a high affinity for gangliosides GD1b and GT1b and binds to neurons which contain these gangliosides. It is not yet clear whether these gangliosides are the physiological receptors for tetanus toxin. By applying the techniques that established GM1 as the receptor for cholera toxin, the role of gangliosides as receptors for tetanus toxin as well as physiological effectors may be elucidated.

MeSH Terms
Adenosine Diphosphate Ribose/metabolism Adenylyl Cyclases/metabolism Animals Bacterial Toxins/metabolism Binding Sites Cell Membrane/metabolism Cholera Toxin/metabolism G(M1) Ganglioside/metabolism Gangliosides/metabolism Kinetics Membrane Lipids/metabolism Membrane Proteins/metabolism Receptors, Cell Surface Receptors, Immunologic/metabolism
Chemicals
Bacterial Toxins Gangliosides Membrane Lipids Membrane Proteins Receptors, Cell Surface Receptors, Immunologic choleragen receptor Adenosine Diphosphate Ribose G(M1) Ganglioside Cholera Toxin Adenylyl Cyclases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Fishman P H
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Article Info
Journal
The Journal of membrane biology
Abbr.
J Membr Biol
ISSN
0022-2631
DOI
10.1007/BF01872268
Published
1982-00-00
Pages
85-97
Language
English
Region
United States
NLM ID
0211301
Subset
IM
External Links
PubMed source DOI: 10.1007/BF01872268 View journal details
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