The behaviour of sea anemone actinoporins at the water-membrane interface

Actinoporins constitute a group of small and basic α-pore forming toxins produced by sea anemones. They display high sequence identity and appear as multigene families. They show a singular behaviour at the water-membrane interface: In aqueous solution, actinoporins remain stably folded but, upon in...

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Detalles Bibliográficos
Autores: García Ortega, Lucía, Alegre Cebollada, Jorge, García Linares, Sara, Bruix, Marta, Martínez Del Pozo, Álvaro, Gavilanes, José G.
Tipo de recurso: artículo
Fecha de publicación:2011
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/41960
Acceso en línea:https://hdl.handle.net/20.500.14352/41960
Access Level:acceso abierto
Palabra clave:Actinoporin
Equinatoxin
Sticholysin
Membrane-pore
Pore-forming-toxin
Bioquímica (Química)
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spelling The behaviour of sea anemone actinoporins at the water-membrane interfaceGarcía Ortega, LucíaAlegre Cebollada, JorgeGarcía Linares, SaraBruix, MartaMartínez Del Pozo, ÁlvaroGavilanes, José G.ActinoporinEquinatoxinSticholysinMembrane-porePore-forming-toxinBioquímica (Química)Actinoporins constitute a group of small and basic α-pore forming toxins produced by sea anemones. They display high sequence identity and appear as multigene families. They show a singular behaviour at the water-membrane interface: In aqueous solution, actinoporins remain stably folded but, upon interaction with lipid bilayers, become integral membrane structures. These membranes contain sphingomyelin, display phase coexistence, or both. The water soluble structures of the actinoporins equinatoxin II (EqtII) and sticholysin II (StnII) are known in detail. The crystalline structure of a fragaceatoxin C (FraC) nonamer has been also determined. The three proteins fold as a β-sandwich motif flanked by two α-helices, one of them at the N-terminal end. Four regions seem to be especially important: A cluster of aromatic residues, a phosphocholine binding site, an array of basic amino acids, and the N-terminal α-helix. Initial binding of the soluble monomers to the membrane is accomplished by the cluster of aromatic amino acids, the array of basic residues, and the phosphocholine binding site. Then, the N-terminal α-helix detaches from the β-sandwich, extends, and lies parallel to the membrane. Simultaneously, oligomerization occurs. Finally, the extended N-terminal α-helix penetrates the membrane to build a toroidal pore. This model has been however recently challenged by the cryo-EM reconstruction of FraC bound to phospholipid vesicles. Actinoporins structural fold appears across all eukaryotic kingdoms in other functionally unrelated proteins. Many of these proteins neither bind to lipid membranes nor induce cell lysis. Finally, studies focusing on the therapeutic potential of actinoporins also abound.ElsevierUniversidad Complutense de Madrid20112011-09-0120112011-09-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/41960reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/419602026-06-02T12:44:21Z
dc.title.none.fl_str_mv The behaviour of sea anemone actinoporins at the water-membrane interface
title The behaviour of sea anemone actinoporins at the water-membrane interface
spellingShingle The behaviour of sea anemone actinoporins at the water-membrane interface
García Ortega, Lucía
Actinoporin
Equinatoxin
Sticholysin
Membrane-pore
Pore-forming-toxin
Bioquímica (Química)
title_short The behaviour of sea anemone actinoporins at the water-membrane interface
title_full The behaviour of sea anemone actinoporins at the water-membrane interface
title_fullStr The behaviour of sea anemone actinoporins at the water-membrane interface
title_full_unstemmed The behaviour of sea anemone actinoporins at the water-membrane interface
title_sort The behaviour of sea anemone actinoporins at the water-membrane interface
dc.creator.none.fl_str_mv García Ortega, Lucía
Alegre Cebollada, Jorge
García Linares, Sara
Bruix, Marta
Martínez Del Pozo, Álvaro
Gavilanes, José G.
author García Ortega, Lucía
author_facet García Ortega, Lucía
Alegre Cebollada, Jorge
García Linares, Sara
Bruix, Marta
Martínez Del Pozo, Álvaro
Gavilanes, José G.
author_role author
author2 Alegre Cebollada, Jorge
García Linares, Sara
Bruix, Marta
Martínez Del Pozo, Álvaro
Gavilanes, José G.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv Actinoporin
Equinatoxin
Sticholysin
Membrane-pore
Pore-forming-toxin
Bioquímica (Química)
topic Actinoporin
Equinatoxin
Sticholysin
Membrane-pore
Pore-forming-toxin
Bioquímica (Química)
description Actinoporins constitute a group of small and basic α-pore forming toxins produced by sea anemones. They display high sequence identity and appear as multigene families. They show a singular behaviour at the water-membrane interface: In aqueous solution, actinoporins remain stably folded but, upon interaction with lipid bilayers, become integral membrane structures. These membranes contain sphingomyelin, display phase coexistence, or both. The water soluble structures of the actinoporins equinatoxin II (EqtII) and sticholysin II (StnII) are known in detail. The crystalline structure of a fragaceatoxin C (FraC) nonamer has been also determined. The three proteins fold as a β-sandwich motif flanked by two α-helices, one of them at the N-terminal end. Four regions seem to be especially important: A cluster of aromatic residues, a phosphocholine binding site, an array of basic amino acids, and the N-terminal α-helix. Initial binding of the soluble monomers to the membrane is accomplished by the cluster of aromatic amino acids, the array of basic residues, and the phosphocholine binding site. Then, the N-terminal α-helix detaches from the β-sandwich, extends, and lies parallel to the membrane. Simultaneously, oligomerization occurs. Finally, the extended N-terminal α-helix penetrates the membrane to build a toroidal pore. This model has been however recently challenged by the cryo-EM reconstruction of FraC bound to phospholipid vesicles. Actinoporins structural fold appears across all eukaryotic kingdoms in other functionally unrelated proteins. Many of these proteins neither bind to lipid membranes nor induce cell lysis. Finally, studies focusing on the therapeutic potential of actinoporins also abound.
publishDate 2011
dc.date.none.fl_str_mv 2011
2011-09-01
2011
2011-09-01
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/20.500.14352/41960
url https://hdl.handle.net/20.500.14352/41960
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 Elsevier
publisher.none.fl_str_mv Elsevier
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
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score 15,301629

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