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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todo:paper_0006291X_v216_n1_p348_Meinardi2023-10-03T14:03:45Z The molecular basis of the self/Non-self selectivity of a coelenterate toxin Meinardi, E. Florin-Christensen, M. Paratcha, G. Azcurra, J.M. Florin-Christensen, J. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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. |
| format |
JOUR |
| author |
Meinardi, E. Florin-Christensen, M. Paratcha, G. Azcurra, J.M. Florin-Christensen, J. |
| spellingShingle |
Meinardi, E. Florin-Christensen, M. Paratcha, G. Azcurra, J.M. Florin-Christensen, J. The molecular basis of the self/Non-self selectivity of a coelenterate toxin |
| author_facet |
Meinardi, E. Florin-Christensen, M. Paratcha, G. Azcurra, J.M. Florin-Christensen, J. |
| author_sort |
Meinardi, E. |
| title |
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 |
| url |
http://hdl.handle.net/20.500.12110/paper_0006291X_v216_n1_p348_Meinardi |
| work_keys_str_mv |
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1807316469761966080 |