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Psd2 pea defensin shows a preference for mimetic membrane rafts enriched with glucosylceramide and ergosterol

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dc.contributor.authorAmaral, Virginia Sara Grancieri
dc.contributor.authorFernandes, Caroline Mota
dc.contributor.authorFelício, Mário Romão
dc.contributor.authorValle, Aline Sol
dc.contributor.authorQuintana, Paula G.
dc.contributor.authorAlmeida, Caroline Correa
dc.contributor.authorBarreto-Bergter, Eliana
dc.contributor.authorGonçalves, Sónia
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorKurtenbach, Eleonora
dc.date.accessioned2019-04-16T11:19:28Z
dc.date.available2019-04-16T11:19:28Z
dc.date.issued2019
dc.description© 2019 Elsevier B.V. All rights reservedpt_PT
dc.description.abstractPsd2 is a pea defensin with 47 amino acid residues that inhibits the growth of fungal species by an uncharacterized mechanism. In this work, Psd2 interactions with model membranes mimicking the lipid compositions of different organisms were evaluated. Protein-lipid overlay assays indicated that Psd2 recognizes Fusarium solani glucosylceramide (GlcCerF.solani) and ergosterol (Erg) in addition to phosphatidylcholine (POPC) and some phosphatidylinositol species, such as PtdIns (3)P, (5)P and (3,5)P2, suggesting that these lipids may play important roles as Psd2 targets. Assays using lipid vesicles were also performed to study the behaviour and dynamics that occur after peptide-membrane interactions. Surface plasmon resonance analysis showed that Psd2 has a higher affinity for pure POPC and POPC-based vesicles containing GlcCer and Erg at a 70:30 proportion than for vesicles containing cholesterol (Chol). Partition experiments by fluorescence spectroscopy showed a decrease in Trp42 quantum yield of Psd2 in the presence of GlcCerF.solani and Erg, individually or in simultaneously enriched membranes. The partition coefficient (Kp) obtained indicated a Psd2 partition preference for this vesicles, confirmed by quenching assays using acrylamide and 5/16-doxyl-stearic acid. Furthermore, we showed that the presence of C8C9 double bonds and a methyl group at position C9 of the sphingoid base backbone of GlcCer was relevant to Psd2 activity against Aspergillus nidulans. These results are consistent with the selectivity of Psd2 against fungi and its lack of toxicity in human erythrocytes. Psd2 represents a promising natural compound for the treatment of fungal infections.pt_PT
dc.description.sponsorshipThe authors acknowledge Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, Brasil), Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ, Brasil) and Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brasil) for funding, including fellowship to V.S.G.A. Authors also acknowledge Fundação para a Ciência e a Tecnologia – Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal) for funding, including fellowship SFRH/BD/100517/2014 to M.R.F., Marie Sklodowska-Curie Research and Innovation Staff Exchange (MSCARISE, European Union) project INPACT (call H2020-MSCA-RISE-2014, grant agreement 644167), and FP7-PEOPLE IRSES (International Research Staff Exchange Scheme, European Union).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBBA - Biomembranes 1861 (2019) 713–728pt_PT
dc.identifier.doi10.1016/j.bbamem.2018.12.020pt_PT
dc.identifier.issn0005-2736
dc.identifier.urihttp://hdl.handle.net/10451/37917
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relation644167pt_PT
dc.relationPhotoswitchable peptides as new antimicrobial and anticancer agents
dc.relation.publisherversionhttps://www.sciencedirect.com/journal/biochimica-et-biophysica-acta-bba-biomembranespt_PT
dc.subjectPisum sativum defensin2 (Psd2)pt_PT
dc.subjectPlant defensinspt_PT
dc.subjectAntimicrobial peptidespt_PT
dc.subjectFluorescence spectroscopypt_PT
dc.subjectGlucosylceramide (GlcCer)pt_PT
dc.subjectErgosterolpt_PT
dc.titlePsd2 pea defensin shows a preference for mimetic membrane rafts enriched with glucosylceramide and ergosterolpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitlePhotoswitchable peptides as new antimicrobial and anticancer agents
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/SFRH%2FBD%2F100517%2F2014/PT
oaire.citation.endPage728pt_PT
oaire.citation.startPage713pt_PT
oaire.citation.titleBiochimica et Biophysica Acta (BBA) - Biomembranespt_PT
oaire.citation.volume1861pt_PT
oaire.fundingStreamOE
person.familyNameRomão Felício
person.familyNameAbreu
person.familyNameSantos
person.givenNameMário
person.givenNameSónia
person.givenNameNuno
person.identifier384205
person.identifier.ciencia-idF811-74AE-412A
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.orcid0000-0002-9398-2140
person.identifier.orcid0000-0003-2903-4282
person.identifier.orcid0000-0002-0580-0475
person.identifier.ridJ-8517-2014
person.identifier.ridH-9482-2017
person.identifier.ridN-7248-2013
person.identifier.scopus-author-id57144367400
person.identifier.scopus-author-id35602210000
person.identifier.scopus-author-id55940818300
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication8d7bbafe-ae5e-418e-8224-6af22991a3e7
relation.isAuthorOfPublicationc077a1e4-3d11-47c7-b5d4-29a5a4190a35
relation.isAuthorOfPublication4656d912-5a2d-4c80-8921-2bcba3aa441a
relation.isAuthorOfPublication.latestForDiscoveryc077a1e4-3d11-47c7-b5d4-29a5a4190a35
relation.isProjectOfPublicatione944118c-7234-4e6e-bf1c-92e157b51d91
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