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Peptides as models for the structure and function of viral capsid proteins : insights on dengue virus capsid

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dc.contributor.authorFreire, João Miguel
dc.contributor.authorVeiga, Ana Salomé
dc.contributor.authorde la Torre, Beatriz G.
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorAndreu, David
dc.contributor.authorDa Poian, Andrea T.
dc.contributor.authorCastanho, Miguel A. R. B.
dc.date.accessioned2014-03-06T17:22:44Z
dc.date.available2014-03-06T17:22:44Z
dc.date.issued2013
dc.description© 2013 Wiley Periodicals Inc.eng
dc.description.abstractThe structural organization of viral particles is among the most astonishing examples of molecular self-assembly in nature, involving proteins, nucleic acids, and, sometimes, lipids. Proper assembly is essential to produce well structured infectious virions. A great variety of structural arrangements can be found in viral particles. Nucleocapsids, for instance, may display highly ordered geometric shapes or consist in macroscopically amorphous packs of the viral genome. Alphavirus and flavivirus are viral genera that exemplify these extreme cases, the former comprising viral particles structured with a T=4 icosahedral symmetry, whereas flavivirus capsids have no regular geometry. Dengue virus is a member of flavivirus genus and is used in this article to illustrate how viral protein-derived peptides can be used advantageously over full-length proteins to unravel the foundations of viral supramolecular assemblies. Membrane- and viral RNA-binding data of capsid protein-derived dengue virus peptides are used to explain the amorphous organization of the viral capsid. Our results combine bioinformatic and spectroscopic approaches using two- or three-component peptide and/or nucleic acid and/or lipid systems.eng
dc.description.sponsorshipContract grant sponsor: Fundação para a Ciência e Tecnologia—Ministério da Educação e Ciência (FCT-MEC, Portugal) Contract grant numbers: PTDC/QUI-BIQ/112929/2009; SFRH/BD/70423/2010 Contract grant sponsor: Fundação Calouste Gulbenkian Contract grant sponsor: International Research Staff Exchange Scheme project MEMPEPACROSS (EU) Contract grant numbers: FP7-PEOPLE IRSES; FP7-HEALTH-F3–2008-223414 Contract grant sponsor: Spanish Ministry of Economy and Competitivity Contract grant number: SAF2011–24899 Contract grant sponsor: Conselho Nacional de Desenvolvimento Cientıfico e Tecnologico (CNPq) Contract grant number: 550114/2010-6 Contract grant sponsor: Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) Contract grant number: E-26/102.919/2011 Contract grant sponsor: National Institute of Science and Technology in Dengue (INCT-Dengue) Contract grant sponsor: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil) Contract grant number: PVE 171/2012eng
dc.identifier.citationBiopolymers (Pept Sci) 100: 325–336, 2013eng
dc.identifier.issn0006-3525
dc.identifier.urihttp://dx.doi.org/10.1002/bip.22266
dc.identifier.urihttp://hdl.handle.net/10451/10696
dc.language.isootherpor
dc.peerreviewedyespor
dc.publisherWileyeng
dc.relation.publisherversionThe definitive version is available at http://onlinelibrary.wiley.com/eng
dc.subjectFlaviviruseng
dc.subjectDengue viruseng
dc.subjectNucleocapsideng
dc.subjectViraleng
dc.subjectPeptideseng
dc.subjectNucleic acid interactioneng
dc.titlePeptides as models for the structure and function of viral capsid proteins : insights on dengue virus capsideng
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumber223414
oaire.awardNumber247513
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/223414
oaire.awardURIinfo:eu-repo/grantAgreement/EC/FP7/247513
oaire.citation.endPage336por
oaire.citation.startPage325por
oaire.citation.titleBiopolymers (Peptide Science)eng
oaire.citation.volume100por
oaire.fundingStreamFP7
oaire.fundingStreamFP7
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
project.funder.nameEuropean Commission
rcaap.rightsclosedAccesspor
rcaap.typearticlepor
relation.isProjectOfPublication14f452b3-0b2b-4e53-afd8-7347e8a323a9
relation.isProjectOfPublication9a14f3fc-9671-4460-8a00-79594f5854e0
relation.isProjectOfPublication.latestForDiscovery9a14f3fc-9671-4460-8a00-79594f5854e0

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