Toxin-induced pore formation is hindered by intermolecular hydrogen bonding in sphingomyelin bilayers

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dc.contributor.authorGarcía Linares, Sara
dc.contributor.authorPalacios Ortega, Juan
dc.contributor.authorYasuda, Tomokazu
dc.contributor.authorÅstrand, Mia
dc.contributor.authorGavilanes, José G.
dc.contributor.authorMartínez del Pozo, Álvaro
dc.contributor.authorSlotte, J. Peter
dc.date.accessioned2023-06-18T06:52:12Z
dc.date.available2023-06-18T06:52:12Z
dc.date.issued2016-03-11
dc.description.abstractSticholysin I and II (StnI and StnII) are pore-forming toxins that use sphingomyelin (SM) for membrane binding. We examined how hydrogen bonding among membrane SMs affected the StnI- and StnII-induced pore formation process, resulting in bilayer permeabilization. We compared toxin-induced permeabilization in bilayers containing either SM or dihydro-SM (lacking the trans 4 double bond of the long-chain base), since their hydrogen-bonding properties are known to differ greatly. We observed that whereas both StnI and StnII formed pores in unilamellar vesicles containing palmitoyl-SM or oleoyl-SM, the toxins failed to similarly form pores in vesicles prepared from dihydro-PSM or dihydro-OSM. In supported bilayers containing OSM, StnII bound efficiently, as determined by surface plasmon resonance. However, StnII binding to supported bilayers prepared from dihydro-OSM was very low under similar experimental conditions. The association of the positively charged StnII (at pH 7.0) with unilamellar vesicles prepared from OSM led to a concentration-dependent increase in vesicle charge, as determined from zeta-potential measurements. With dihydro-OSM vesicles, a similar response was not observed. Benzyl alcohol, which is a small hydrogen-bonding compound with affinity to lipid bilayer interfaces, strongly facilitated StnII-induced pore formation in dihydro-OSM bilayers, suggesting that hydrogen bonding in the interfacial region originally prevented StnII from membrane binding and pore formation. We conclude that interfacial hydrogen bonding was able to affect the membrane association of StnI- and StnII, and hence their pore forming capacity. Our results suggest that other types of protein interactions in bilayers may also be affected by hydrogen-bonding origination from SMs.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.departmentSección Deptal. de Bioquímica y Biología Molecular (Biológicas)
dc.description.facultyFac. de Ciencias Químicas
dc.description.facultyFac. de Ciencias Biológicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia e Innovación (MICINN)
dc.description.statuspub
dc.eprint.idhttps://eprints.ucm.es/id/eprint/37500
dc.identifier.doi10.1016/j.bbamem.2016.03.013
dc.identifier.issn0005-2736
dc.identifier.officialurlhttp://www.sciencedirect.com/science/article/pii/S0005273616300992
dc.identifier.urihttps://hdl.handle.net/20.500.14352/24453
dc.issue.number6
dc.journal.titleBiochimica et Biophysica Acta - Biomembranes
dc.language.isoeng
dc.page.final1195
dc.page.initial1189
dc.publisherElsevier
dc.relation.projectIDBFU2012-32404
dc.rights.accessRightsopen access
dc.subject.cdu577.1
dc.subject.keywordPermeabilization
dc.subject.keywordsurface plasmon resonance
dc.subject.keywordsphingomyelinase
dc.subject.keywordsticholysin
dc.subject.ucmBiología molecular (Química)
dc.subject.ucmBioquímica (Química)
dc.titleToxin-induced pore formation is hindered by intermolecular hydrogen bonding in sphingomyelin bilayers
dc.typejournal article
dc.volume.number1858
dspace.entity.typePublication
relation.isAuthorOfPublication35824f7f-c79d-4928-9728-21124243bf7a
relation.isAuthorOfPublication.latestForDiscovery35824f7f-c79d-4928-9728-21124243bf7a
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