Force Mapping Study of Actinoporin Effect in Membranes Presenting Phase Domains

DC FieldValueLanguage
dc.contributor.authorCosentino, Katia
dc.contributor.authorHermann, Edward
dc.contributor.authorvon Kugelgen, Nicolai
dc.contributor.authorUnsay, Joseph D.
dc.contributor.authorRos, Uris
dc.contributor.authorGarcia-Saez, Ana J.
dc.date.accessioned2021-12-23T16:17:13Z-
dc.date.available2021-12-23T16:17:13Z-
dc.date.issued2021
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/12258-
dc.description.abstractEquinatoxin II (EqtII) and Fragaceatoxin C (FraC) are pore-forming toxins (PFTs) from the actinoporin family that have enhanced membrane affinity in the presence of sphingomyelin (SM) and phase coexistence in the membrane. However, little is known about the effect of these proteins on the nanoscopic properties of membrane domains. Here, we used combined confocal microscopy and force mapping by atomic force microscopy to study the effect of EqtII and FraC on the organization of phase-separated phosphatidylcholine/SM/cholesterol membranes. To this aim, we developed a fast, high-throughput processing tool to correlate structural and nano-mechanical information from force mapping. We found that both proteins changed the lipid domain shape. Strikingly, they induced a reduction in the domain area and circularity, suggesting a decrease in the line tension due to a lipid phase height mismatch, which correlated with proteins binding to the domain interfaces. Moreover, force mapping suggested that the proteins affected the mechanical properties at the edge, but not in the bulk, of the domains. This effect could not be revealed by ensemble force spectroscopy measurements supporting the suitability of force mapping to study local membrane topographical and mechanical alterations by membranotropic proteins.
dc.description.sponsorshipMax Planck SocietyMax Planck SocietyFoundation CELLEX; Bundesministerium fur Bildung and ForschungFederal Ministry of Education & Research (BMBF) [0312040]; Insitutional Strategy of the University of Tubingen (Deutsche Forschungsgemeinschaft) [ZUK 63]; Alexander von Humboldt FoundationAlexander von Humboldt Foundation; International Foundation for ScienceInternational Foundation for Science [4616-2]; German Cancer Research Center; This research was funded by the Max Planck Society, the Bundesministerium fur Bildung and Forschung (Grant No. 0312040). Work of K.C. was partially funded by the Insitutional Strategy of the University of Tubingen (Deutsche Forschungsgemeinschaft, ZUK 63). Work of U.R. at IFIB was funded by the Alexander von Humboldt Foundation. U.R. also acknowledges previous support of this project from the International Foundation for Science (4616-2). J.D.U. was funded by the German Cancer Research Center and the Max Planck Society.
dc.language.isoen
dc.publisherMDPI
dc.relation.ispartofTOXINS
dc.subjectatomic force microscopy
dc.subjectCHOLESTEROL
dc.subjectCURVATURE
dc.subjectEQUINATOXIN-II
dc.subjectFood Science & Technology
dc.subjectforce spectroscopy
dc.subjectLINE TENSION
dc.subjectMECHANISM
dc.subjectmembrane phase domains
dc.subjectMICROSCOPY
dc.subjectOLIGOMERIZATION
dc.subjectpore forming toxins
dc.subjectPORE-FORMING TOXIN
dc.subjectSPHINGOMYELIN
dc.subjectSUPPORTED LIPID-BILAYERS
dc.subjectToxicology
dc.titleForce Mapping Study of Actinoporin Effect in Membranes Presenting Phase Domains
dc.typejournal article
dc.identifier.doi10.3390/toxins13090669
dc.identifier.isiISI:000699963200001
dc.description.volume13
dc.description.issue9
dc.identifier.eissn20726651
dc.publisher.placeST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND
dcterms.isPartOf.abbreviationToxins
dcterms.oaStatusGreen Published, gold
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidCoKa893-
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