We are analyzing https://link.springer.com/article/10.1007/bf01872268.

Title:
Role of membrane gangliosides in the binding and action of bacterial toxins | The Journal of Membrane Biology
Description:
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 ofE. 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.
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google, scholar, pubmed, biol, fishman, chem, usa, moss, proc, natl, acad, sci, membrane, toxin, cell, infect, article, cholera, nature, van, biochem, cuatrecasas, biochemistry, london, res, heyningen, rev, dis, holmgren, gangliosides, brady, habermann, gill, receptors, access, pharmacol, biophys, svennerholm, privacy, cookies, content, journal, bacterial, toxins, arch, microbiol, wiegandt, publish, search, plasma,

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month download article/chapter heat-labile enterotoxin ofe activating adenylate cyclase activates adenylate cyclase cell surface receptors privacy choices/manage cookies full article pdf membrane biology aims european economic area oligosaccharide chains exposed ganglioside gm1 acs symposium series american chemical society elsevier/north holland fifteenth joint conference cholera toxin binds toxin-resistant cells toxin-receptor complexes conditions privacy policy cell surface glycolipids metabolic neurology branch american physiological society tetanus toxin physiological receptors accepting optional cookies cyclic nucleotide res check access instant access main content log cell surface receptor bacterial toxins cholera toxin journal finder publish plasma membrane intracellular signaling fishman rights binding site related subjects receptors article fishman toxin appears privacy policy personal data article log books a membrane gangliosides optional cookies cholera prophylactics article cite manage preferences

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         description: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 ofE. 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.
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