The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface

Simple item page
dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorAlm, Ida
dc.contributor.authorMaula, Terhi
dc.contributor.authorGavilanes Franco, José Gregorio
dc.contributor.authorSlotte, Johan
dc.contributor.authorMartínez Del Pozo, Álvaro
dc.date.accessioned2024-02-01T12:24:25Z
dc.date.available2024-02-01T12:24:25Z
dc.date.issued2015-03-25
dc.description.abstractActinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members. These proteins remain stably folded in water, but upon interaction with lipid bilayers, they oligomerize to form a pore. This event is triggered by the presence of sphingomyelin (SM), but cholesterol (Chol) facilitates pore formation. Membrane attachment and pore formation require changes involving long-distance rearrangements of residues located at the protein-membrane interface. The influence of Chol on membrane recognition, oligomerization, and/or pore formation is now studied using StnII variants, which are characterized in terms of their ability to interact with model membranes in the presence or absence of Chol. The results obtained frame Chol not only as an important partner for SM for functional membrane recognition but also as a molecule which significantly reduces the structural requirements for the mentioned conformational rearrangements to occur. However, given that the DOPC:SM:Chol vesicles employed display phase coexistence and have domain boundaries, the observed effects could be also due to the presence of these different phases on the membrane. In addition, it is also shown that the Arg51 guanidinium group is strictly required for membrane recognition, independently of the presence of Chol.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipMINECO
dc.description.statuspub
dc.identifier.doi10.3390/md13041647
dc.identifier.issn1660-3397
dc.identifier.officialurlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4413179/
dc.identifier.urihttps://hdl.handle.net/20.500.14352/97665
dc.issue.number4
dc.journal.titleMarine Drugs
dc.language.isoeng
dc.page.final1665
dc.page.initial1647
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)
dc.relation.projectIDBFU2012-32404
dc.rights.accessRightsopen access
dc.subject.cdu577.1
dc.subject.keywordActinoporin
dc.subject.keywordEquinatoxin
dc.subject.keywordPore-forming toxin
dc.subject.keywordSphingomyelin
dc.subject.keywordSphingomyelin
dc.subject.ucmBiología molecular (Biología)
dc.subject.unesco2406 Biofísica
dc.titleThe Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface
dc.typejournal article
dc.type.hasVersionAM
dc.volume.number13
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication4e3f8ba2-146e-4aed-9f47-f48cde58a795
relation.isAuthorOfPublication4d35a8a6-8bd3-4ff4-b179-57581d8d36d8
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
Download
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
2015_GarciaLinares.pdf
Size:
1.22 MB
Format:
Adobe Portable Document Format
downoload Download
Collections
Artículos