Functional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus

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dc.contributor.authorRivera de la Torre, Esperanza
dc.contributor.authorPalacios Ortega, Juan
dc.contributor.authorSlotte, J. Peter
dc.contributor.authorGavilanes, José G.
dc.contributor.authorMartínez del Pozo, Álvaro
dc.contributor.authorGarcía Linares, Sara
dc.date.accessioned2023-06-16T15:24:02Z
dc.date.available2023-06-16T15:24:02Z
dc.date.issued2020-11
dc.description.abstractVenoms constitute complex mixtures of many different molecules arising from evolution in processes driven by continuous prey–predator interactions. One of the most common compounds in these venomous cocktails are pore-forming proteins, a family of toxins whose activity relies on the disruption of the plasmatic membranes by forming pores. The venom of sea anemones, belonging to the oldest lineage of venomous animals, contains a large amount of a characteristic group of pore-forming proteins known as actinoporins. They bind specifically to sphingomyelin-containing membranes and suffer a conformational metamorphosis that drives them to make pores. This event usually leads cells to death by osmotic shock. Sticholysins are the actinoporins produced by Stichodactyla helianthus. Three different isotoxins are known: Sticholysins I, II, and III. They share very similar amino acid sequence and three-dimensional structure but display different behavior in terms of lytic activity and ability to interact with cholesterol, an important lipid component of vertebrate membranes. In addition, sticholysins can act in synergy when exerting their toxin action. The subtle, but important, molecular nuances that explain their different behavior are described and discussed throughout the text. Improving our knowledge about sticholysins behavior is important for eventually developing them into biotechnological tools.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipUCM-Banco Santander
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/62276
dc.identifier.doi10.3390/ijms21238915
dc.identifier.issn1661-6596
dc.identifier.officialurlhttps://www.mdpi.com/1422-0067/21/23/8915/htm
dc.identifier.urihttps://hdl.handle.net/20.500.14352/6579
dc.issue.number8915
dc.journal.titleInternational journal of molecular sciences
dc.language.isoeng
dc.page.final24
dc.page.initial1
dc.publisherMDPI
dc.relation.projectIDgrants PR75/18-21561 and PR87/19-22556
dc.rights.accessRightsopen access
dc.subject.cdu577.1
dc.subject.keywordactinoporins
dc.subject.keywordcholesterol
dc.subject.keywordcnidaria
dc.subject.keywordleakage
dc.subject.keywordsphingomyelin
dc.subject.keywordvenom
dc.subject.ucmBiología molecular (Química)
dc.subject.ucmBioquímica (Química)
dc.titleFunctional and Structural Variation among Sticholysins, Pore-Forming Proteins from the Sea Anemone Stichodactyla helianthus
dc.typejournal article
dc.volume.number21
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
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