Abstract
CHOLERA toxin, a protein of molecular weight 84,000, comprising five or six B and one A subunits, produces massive diarrhoea in man and other mammals by altering the transport of salt and water across the intestinal epithelium1–4. These effects are mediated by a sequence of events leading to an increase in the concentration of cyclic AMP in the epithelial cells. The sequence involves binding of the toxin through its B subunits to specific receptors which seem to be the mono-sialoganglioside galactosyl-N-acetyl-galactosaminyl-(N-acetyl-neuraminyl)-galactosyl-glucosyl-ceramide (GM1), and subsequent activation of adenyl cyclase5–7. We report here experiments which show that cholera toxin reacts with lipid bilayers containing GM1 to form channels which allow ions present in the aqueous solution to traverse the membrane.
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TOSTESON, M., TOSTESON, D. Bilayers containing gangliosides develop channels when exposed to cholera toxin. Nature 275, 142–144 (1978). https://doi.org/10.1038/275142a0
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DOI: https://doi.org/10.1038/275142a0
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