Sticholysin I–II oligomerization in the absence of membranes

Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI...

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Detalles Bibliográficos
Autores: García Linares, Sara, Amigot Sánchez, Rafael, García Montoya, Carmen, Alfonso, Carlos, Luque Ortega, Juan Román, Gavilanes, José G., Martínez Del Pozo, Álvaro, Palacios Ortega, Juan
Tipo de recurso: artículo
Fecha de publicación:2022
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/72007
Acceso en línea:https://hdl.handle.net/20.500.14352/72007
Access Level:acceso abierto
Palabra clave:577.1
actinoporins analytical
ultracentrifugation
pore-forming proteins
sedimentation velocity
Bioquímica (Biología)
2302 Bioquímica
Descripción
Sumario:Sticholysins are pore-forming toxins produced by the sea anemone Stichodactyla helianthus. When they encounter a sphingomyelin-containing membrane, these proteins bind to it and oligomerize, a process that ends in pore formation. Mounting evidence indicates that StnII can favour the activity of StnI. Previous results have shown that these two isotoxins can oligomerize together. Furthermore, StnII appeared to potentiate the activity of StnI through the membrane-binding step of the process. Hence, isotoxin interaction should occur prior to membrane encounter. Here, we have used analytical ultracentrifugation to investigate the oligomerization of Stns in solution, both separately and together. Our results indicate that while StnI seems to be more prone to oligomerize in water solution than StnII, a small percentage of StnII in StnI–StnII mixtures promotes oligomerization.