The molecular basis of the self/Non-self selectivity of a coelenterate toxin

Coelenterates produce potent hemolysins inhibited by sphingomyelin (SM) Remarkably, instead of this lipid, their membrane contain a phosphono analogue of it. Using coelenterolysin (CL), a toxin produced by the sea anemone Phymactis clematis, we have examined a possible connection between these two p...

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Publicado: 1995
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v216_n1_p348_Meinardi
http://hdl.handle.net/20.500.12110/paper_0006291X_v216_n1_p348_Meinardi
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_0006291X_v216_n1_p348_Meinardi
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spelling paper:paper_0006291X_v216_n1_p348_Meinardi2023-06-08T14:30:09Z The molecular basis of the self/Non-self selectivity of a coelenterate toxin Coelenterates produce potent hemolysins inhibited by sphingomyelin (SM) Remarkably, instead of this lipid, their membrane contain a phosphono analogue of it. Using coelenterolysin (CL), a toxin produced by the sea anemone Phymactis clematis, we have examined a possible connection between these two peculiar traits. Our experiments showed that, while SM binds this lysin and inhibits its hemolytic activity, the endogenous PnSL do neither. In addition, liposomes made of bovine erythrocyte lipids are rapidly disrupted by CL, while those made of P. clematis lipids are completely resistant to it. However, if small amounts of SM are added to the P. clematis lipids, the resulting liposomes become sensitive to CL. Taken together, our results show for the first time that substitution of SM by its phosphono analogue is the molecular basis for the selectivity of an anthozoan toxin. We therefore propose that exotoxin production and membrane composition are coadapted traits that confer on the coelenterates a significant evolutionary advantage. © 1995 Academic Press, Inc. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v216_n1_p348_Meinardi http://hdl.handle.net/20.500.12110/paper_0006291X_v216_n1_p348_Meinardi
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
description Coelenterates produce potent hemolysins inhibited by sphingomyelin (SM) Remarkably, instead of this lipid, their membrane contain a phosphono analogue of it. Using coelenterolysin (CL), a toxin produced by the sea anemone Phymactis clematis, we have examined a possible connection between these two peculiar traits. Our experiments showed that, while SM binds this lysin and inhibits its hemolytic activity, the endogenous PnSL do neither. In addition, liposomes made of bovine erythrocyte lipids are rapidly disrupted by CL, while those made of P. clematis lipids are completely resistant to it. However, if small amounts of SM are added to the P. clematis lipids, the resulting liposomes become sensitive to CL. Taken together, our results show for the first time that substitution of SM by its phosphono analogue is the molecular basis for the selectivity of an anthozoan toxin. We therefore propose that exotoxin production and membrane composition are coadapted traits that confer on the coelenterates a significant evolutionary advantage. © 1995 Academic Press, Inc.
title The molecular basis of the self/Non-self selectivity of a coelenterate toxin
spellingShingle The molecular basis of the self/Non-self selectivity of a coelenterate toxin
title_short The molecular basis of the self/Non-self selectivity of a coelenterate toxin
title_full The molecular basis of the self/Non-self selectivity of a coelenterate toxin
title_fullStr The molecular basis of the self/Non-self selectivity of a coelenterate toxin
title_full_unstemmed The molecular basis of the self/Non-self selectivity of a coelenterate toxin
title_sort molecular basis of the self/non-self selectivity of a coelenterate toxin
publishDate 1995
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v216_n1_p348_Meinardi
http://hdl.handle.net/20.500.12110/paper_0006291X_v216_n1_p348_Meinardi
_version_ 1768541919122554880

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