RT Journal Article
T1 Synergistic Action of Actinoporin Isoforms from the SameSea Anemone Species Assembled into Functionally ActiveHeteropores
A1 Rivera de la Torre, Esperanza
A1 García Linares, Sara
A1 Alegre Cebollada, Jorge
A1 Lacadena, Javier
A1 Gavilanes, José G.
A1 Martínez del Pozo, Alvaro
AB Among the toxic polypeptides secreted in the venom of sea anemones, actinoporins are the pore-forming toxins whose toxic activity relies on the formation of oligomeric pores within biological membranes. Intriguingly, actinoporins appear as multigene families that give rise to many protein isoforms in the same individual displaying high sequence identities but large functional differences. However, the evolutionary advantage of producing such similar isotoxins is not fully understood. Here,using sticholysins I and II (StnI and StnII) from the sea anemone Stichodactyla helianthus, it is shown that actinoporin isoforms can potentiate each other’s activity. Through hemolysis and calcein releasing assays, it is revealed that mixtures of StnI and StnII are more lytic than equivalent preparations of the corresponding isolated isoforms. It is then proposed that this synergy is due to the assembly of heteropores because (i) StnI and StnII can be chemically cross-linked at the membrane and (ii) the affinity of sticholysin mixtures for the membrane is increased with respect to any of them acting in isolation, as revealed by isothermal titration calorimetry experiments. These results help us understand the multigene nature of actinoporins and may be extended to other families of toxins that require oligomerization to exert toxicity.
PB ASBMB American Society for Biochemistry and Molecular Biology
SN 1083-351X (Online)
YR 2016
FD 2016
LK https://hdl.handle.net/20.500.14352/24534
UL https://hdl.handle.net/20.500.14352/24534
LA eng
NO Ministerio de Ciencia e Innovación (MICINN)
NO Ramón y Cajal
DS Docta Complutense
RD 30 abr 2024