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Parainfluenza fusion peptide promotes membrane fusion by assembling into oligomeric porelike structures

2022Artigo científico Acesso aberto
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dc.contributor.authorValério, Mariana
dc.contributor.authorMendonça, Diogo A.
dc.contributor.authorMorais, João
dc.contributor.authorBuga, Carolina C.
dc.contributor.authorCruz, Carlos H.
dc.contributor.authorCastanho, Miguel A. R. B.
dc.contributor.authorMelo, Manuel N.
dc.contributor.authorSoares, Cláudio M.
dc.contributor.authorVeiga, Ana Salomé
dc.contributor.authorLousa, Diana
dc.date.accessioned2023-05-24T14:32:37Z
dc.date.available2023-05-24T14:32:37Z
dc.date.issued2022
dc.description© 2022 The Authors. Published by American Chemical Societypt_PT
dc.description.abstractParamyxoviruses are enveloped viruses harboring a negative-sense RNA genome that must enter the host’s cells to replicate. In the case of the parainfluenza virus, the cell entry process starts with the recognition and attachment to target receptors, followed by proteolytic cleavage of the fusion glycoprotein (F) protein, exposing the fusion peptide (FP) region. The FP is responsible for binding to the target membrane, and it is believed to play a crucial role in the fusion process, but the mechanism by which the parainfluenza FP (PIFP) promotes membrane fusion is still unclear. To elucidate this matter, we performed biophysical experimentation of the PIFP in membranes, together with coarse grain (CG) and atomistic (AA) molecular dynamics (MD) simulations. The simulation results led to the pinpointing of the most important PIFP amino acid residues for membrane fusion and show that, at high concentrations, the peptide induces the formation of a water-permeable porelike structure. This structure promotes lipid head intrusion and lipid tail protrusion, which facilitates membrane fusion. Biophysical experimental results validate these findings, showing that, depending on the peptide/lipid ratio, the PIFP can promote fusion and/or membrane leakage. Our work furthers the understanding of the PIFP-induced membrane fusion process, which might help foster development in the field of viral entry inhibition.pt_PT
dc.description.sponsorshipThis work was financially supported by FCT-Fundação para a Ciência e a Tecnologia, Portugal, through project PTDC/CCI-BIO/28200/2017 and by the European Union (H2020-FETOPEN-2018-2019-2020-01, grant no. 828774). This work was also financially supported by Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE2020_Programa Operacional Competitividade e Internacionalização (POCI). M.V. and D.A.M. thank FCT for their PhD fellowships (SFRH/BD/148542/2019 and PD/BD/136752/2018, respectively). M.N.M. thanks FCT for the Post-Doc fellowship CEECIND/04124/2017. M.N.M. and D.L. thank the MACC for the computing hours in their HPC center (CPCA/A0/7329/2020 and CPCA/A0/7305/2020).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationACS Chem. Biol. 2022, 17, 7, 1831–1843pt_PT
dc.identifier.doi10.1021/acschembio.2c00208pt_PT
dc.identifier.eissn1554-8937
dc.identifier.issn1554-8929
dc.identifier.urihttp://hdl.handle.net/10451/57580
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherACS Publicationspt_PT
dc.relationLISBOA-01-0145-FEDER-007660pt_PT
dc.relationUsing computational and experimental methods to provide a global characterization of viral fusion peptides
dc.relation''One size fits all'' unique drug to eradicate multiple viral species simultaneously from the central nervous system of co-infected individuals
dc.relationDengue fusion peptide: from molecular properties to the design of therapeutic applications
dc.relationTargeting brain-resident viruses across the blood-brain barrier using peptide drugs.
dc.relationNot Available
dc.relation.publisherversionhttps://pubs.acs.org/journal/acbcctpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/pt_PT
dc.titleParainfluenza fusion peptide promotes membrane fusion by assembling into oligomeric porelike structurespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleUsing computational and experimental methods to provide a global characterization of viral fusion peptides
oaire.awardTitle''One size fits all'' unique drug to eradicate multiple viral species simultaneously from the central nervous system of co-infected individuals
oaire.awardTitleDengue fusion peptide: from molecular properties to the design of therapeutic applications
oaire.awardTitleTargeting brain-resident viruses across the blood-brain barrier using peptide drugs.
oaire.awardTitleNot Available
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FCCI-BIO%2F28200%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/EC/H2020/828774/EU
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F148542%2F2019/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/OE/PD%2FBD%2F136752%2F2018/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/CEEC IND 2017/CEECIND%2F04124%2F2017%2FCP1428%2FCT0008/PT
oaire.citation.endPage1843pt_PT
oaire.citation.issue7pt_PT
oaire.citation.startPage1831pt_PT
oaire.citation.titleACS Chemical Biologypt_PT
oaire.citation.volume17pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamH2020
oaire.fundingStreamOE
oaire.fundingStreamCEEC IND 2017
person.familyNameMendonça
person.familyNameC. Buga
person.familyNameCastanho
person.familyNameVeiga
person.givenNameDiogo
person.givenNameCarolina
person.givenNameMiguel
person.givenNameAna Salome
person.identifier.ciencia-id2F1E-8D99-DA70
person.identifier.ciencia-id551F-AAA3-F281
person.identifier.orcid0000-0001-8003-4662
person.identifier.orcid0000-0003-4109-8502
person.identifier.orcid0000-0001-7891-7562
person.identifier.orcid0000-0002-9892-2243
person.identifier.scopus-author-id56605575600
person.identifier.scopus-author-id56745037100
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameEuropean Commission
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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