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

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dc.contributor.authorGarcía Ortega, Lucía
dc.contributor.authorAlegre Cebollada, Jorge
dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorBruix, Marta
dc.contributor.authorMartínez Del Pozo, Álvaro
dc.contributor.authorGavilanes, José G.
dc.date.accessioned2023-06-20T00:06:00Z
dc.date.available2023-06-20T00:06:00Z
dc.date.issued2011-09
dc.description.abstractActinoporins 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.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio Español de Ciencia e Innovación
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/12957
dc.identifier.doi10.1016/j.bbamem.2011.05.012
dc.identifier.issn0005-2736
dc.identifier.officialurlhttp://www.elsevier.com/wps/find/journaldescription.cws_home/601272/description#description
dc.identifier.urihttps://hdl.handle.net/20.500.14352/41960
dc.journal.titleBiochimica et Biophysica Acta - Biomembranes
dc.language.isoeng
dc.page.final2288
dc.page.initial2275
dc.publisherElsevier
dc.relation.projectIDBFU2009-10185
dc.relation.projectIDCTQ 2008-00080/BQU
dc.rights.accessRightsopen access
dc.subject.keywordActinoporin
dc.subject.keywordEquinatoxin
dc.subject.keywordSticholysin
dc.subject.keywordMembrane-pore
dc.subject.keywordPore-forming-toxin
dc.subject.ucmBioquímica (Química)
dc.titleThe behaviour of sea anemone actinoporins at the water-membrane interface
dc.typejournal article
dc.volume.number1808
dspace.entity.typePublication
relation.isAuthorOfPublicationb8f84062-84af-45de-876d-9ee1b31aa47a
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication4d35a8a6-8bd3-4ff4-b179-57581d8d36d8
relation.isAuthorOfPublication.latestForDiscoveryb8f84062-84af-45de-876d-9ee1b31aa47a
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