Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores

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 i...

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Detalhes bibliográficos
Autores: Rivera de la Torre, Esperanza, García Linares, Sara, Alegre Cebollada, Jorge, Lacadena García-Gallo, Francisco Javier, Gavilanes, José G., Martínez Del Pozo, Álvaro
Formato: artículo
Fecha de publicación:2016
País:España
Recursos:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/24534
Acesso em linha:https://hdl.handle.net/20.500.14352/24534
Access Level:acceso abierto
Palavra-chave:577.1
pore-forming-toxin
sticholysin
equinatoxin
erythrocyte
toxin
oligomerization
crosslinking
lysis
lipid-protein interaction
ion channel
Bioquímica (Medicina)
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oai_identifier_str oai:docta.ucm.es:20.500.14352/24534
network_acronym_str ES
network_name_str España
repository_id_str
spelling Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active HeteroporesRivera de la Torre, EsperanzaGarcía Linares, SaraAlegre Cebollada, JorgeLacadena García-Gallo, Francisco JavierGavilanes, José G.Martínez Del Pozo, Álvaro577.1pore-forming-toxinsticholysinequinatoxinerythrocytetoxinoligomerizationcrosslinkinglysislipid-protein interactionion channelBioquímica (Medicina)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.ASBMB American Society for Biochemistry and Molecular BiologyUniversidad Complutense de Madrid20162016-01-0120162016-01-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/24534reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/245342026-06-02T12:44:21Z
dc.title.none.fl_str_mv Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
title Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
spellingShingle Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
Rivera de la Torre, Esperanza
577.1
pore-forming-toxin
sticholysin
equinatoxin
erythrocyte
toxin
oligomerization
crosslinking
lysis
lipid-protein interaction
ion channel
Bioquímica (Medicina)
title_short Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
title_full Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
title_fullStr Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
title_full_unstemmed Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
title_sort Synergistic Action of Actinoporin Isoforms from the Same Sea Anemone Species Assembled into Functionally Active Heteropores
dc.creator.none.fl_str_mv Rivera de la Torre, Esperanza
García Linares, Sara
Alegre Cebollada, Jorge
Lacadena García-Gallo, Francisco Javier
Gavilanes, José G.
Martínez Del Pozo, Álvaro
author Rivera de la Torre, Esperanza
author_facet Rivera de la Torre, Esperanza
García Linares, Sara
Alegre Cebollada, Jorge
Lacadena García-Gallo, Francisco Javier
Gavilanes, José G.
Martínez Del Pozo, Álvaro
author_role author
author2 García Linares, Sara
Alegre Cebollada, Jorge
Lacadena García-Gallo, Francisco Javier
Gavilanes, José G.
Martínez Del Pozo, Álvaro
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
pore-forming-toxin
sticholysin
equinatoxin
erythrocyte
toxin
oligomerization
crosslinking
lysis
lipid-protein interaction
ion channel
Bioquímica (Medicina)
topic 577.1
pore-forming-toxin
sticholysin
equinatoxin
erythrocyte
toxin
oligomerization
crosslinking
lysis
lipid-protein interaction
ion channel
Bioquímica (Medicina)
description 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.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016-01-01
2016
2016-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/24534
url https://hdl.handle.net/20.500.14352/24534
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv ASBMB American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv ASBMB American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869411644304523264
score 15,301629

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