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Synergistic action of actinoporin isoforms from the same sea anemone species assembled into functionally active heteropores



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Rivera de Torre, Esperanza and García Linares, Sara and Alegre Cebollada, Jorge and Lacadena, Javier and Gavilanes, José G. and Martínez del Pozo, Álvaro (2016) Synergistic action of actinoporin isoforms from the same sea anemone species assembled into functionally active heteropores. The Journal of Biological Chemistry, 291 (18). ISSN 0021-9258, ESSN: 1083-351X (In Press)

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Official URL: http://www.jbc.org/content/early/2016/04/27/jbc.M115.710491


Among the toxic polypeptides secreted in the venom of sea anemones, actinoporins are pore forming toxins whose toxic activity relies on the formation of oligomeric pores within biological membranes. Intriguingly, actinoporins appear as multigene families which 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 since (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 to understand the multigene nature of actinoporins and may be extended to other families of toxins that require oligomerization to exert toxicity.

Item Type:Article
Uncontrolled Keywords:pore-forming-toxin, sticholysin, equinatoxin, erythrocyte, toxin, oligomerization, cross-linking, lysis, lipid-protein interaction, ion channel
Subjects:Sciences > Chemistry > Molecular biology
Sciences > Chemistry > Biochemistry
ID Code:37499
Deposited On:12 May 2016 08:01
Last Modified:12 Jun 2017 10:21

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