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

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dc.contributor.authorRivera de Torre, Esperanza
dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorAlegre Cebollada, Jorge
dc.contributor.authorLacadena, Javier
dc.contributor.authorGavilanes, José G.
dc.contributor.authorMartínez del Pozo, Álvaro
dc.date.accessioned2023-06-18T06:52:11Z
dc.date.available2023-06-18T06:52:11Z
dc.date.issued2016-04-27
dc.description.abstractAmong 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.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.departmentSección Deptal. de Bioquímica y Biología Molecular (Biológicas)
dc.description.facultyFac. de Ciencias Químicas
dc.description.facultyFac. de Ciencias Biológicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia e Innovación (MICINN)
dc.description.sponsorshipUCM collaboration fellowship to ERT
dc.description.sponsorshipRamón y Cajal Award
dc.description.statusinpress
dc.eprint.idhttps://eprints.ucm.es/id/eprint/37499
dc.identifier.doi10.1074/jbc.M115.710491
dc.identifier.issn0021-9258, ESSN: 1083-351X
dc.identifier.officialurlhttp://www.jbc.org/content/early/2016/04/27/jbc.M115.710491
dc.identifier.urihttps://hdl.handle.net/20.500.14352/24452
dc.issue.number18
dc.journal.titleThe Journal of Biological Chemistry
dc.language.isoeng
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dc.relation.projectIDBFU2012-32404
dc.relation.projectIDJAC (RYC-2014-16604)
dc.rights.accessRightsopen access
dc.subject.cdu577.1
dc.subject.keywordpore-forming-toxin
dc.subject.keywordsticholysin
dc.subject.keywordequinatoxin
dc.subject.keyworderythrocyte
dc.subject.keywordtoxin
dc.subject.keywordoligomerization
dc.subject.keywordcross-linking
dc.subject.keywordlysis
dc.subject.keywordlipid-protein interaction
dc.subject.keywordion channel
dc.subject.ucmBiología molecular (Química)
dc.subject.ucmBioquímica (Química)
dc.titleSynergistic action of actinoporin isoforms from the same sea anemone species assembled into functionally active heteropores
dc.typejournal article
dc.volume.number291
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
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