Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection

Detalhes bibliográficos
Autor(a) principal: Freire, João M.
Data de Publicação: 2015
Outros Autores: Santos, Nuno C., Veiga, Ana Salomé, Poian, Andrea T. da, Castanho, Miguel A. R. B.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/23130
Resumo: © 2015 FEBS
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spelling Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfectionAntimicrobialCapsidDengue virusEnvelopeFusionMultifunctional proteins© 2015 FEBSRegardless of the debate on whether there is a place for viruses in the tree of life, it is consensual that they co-evolve with their hosts under the pressure of genome minimization. The abundance of multifunctional viral structural proteins is a consequence of this pressure. The molecular key to multifunctionality is the existence of intrinsically disordered domains together with ordered domains in the same protein. Capsid proteins, the hallmark of viruses, are not exceptions because they have coexisting ordered and disordered domains that are crucial for multifunctionality. It is also frequent to find supercharged proteins (i.e. proteins for which the net charge per unit molecular mass is > +0.75/kDa) among viral capsid proteins. All flaviviruses having annotated proteins in the ExPASy Viralzone database have supercharged capsid proteins. Moreover, cell-penetrating sequences/domains are frequent in viral proteins, even when they are not supercharged. Altogether, the findings strongly suggest that the ability to translocate membranes was acquired, conserved and optimized throughout the evolution of some viral proteins as part of their multifunctionality. The fitness of capsid proteins to translocate membranes carrying genomes was experimentally demonstrated with dengue virus capsid protein. This protein is potentially able to help the fusion process and translocate the RNA genome across the hemifused membrane formed by the viral envelope and the endosomal membrane. In addition, one of the cell-penetrating domains of the capsid protein also has antibacterial activity. This may be reminiscent of parasitic bacteria–bacteria competition for the same host and shed light on the origins of enveloped viruses.The authors acknowledge funding from Fundação para a Ciência e Tecnologia (FCT, Portugal; project HIVER/0002/2013), Conselho Nacional de Desenvolvimento Cientifico e Tecnológico (CNPq, Brazil, Projects 471239/2012-7 and 306669/2013-7), Fundação Carlos Chagas Filho de Amparo -a Pesquisa do Estado do Rio de Janeiro (FAPERJ, Brazil, Projects E-26/111.668/2013 and E-26/201.167/2014), and European Commission, Program H2020, Marie Skłodowska-Curie Actions (MSCA), RISE project grant 644167. M. Castanho acknowledges the support of Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES, Brazil; Project PVE171/2012) and J. Freire acknowledges fellowship SFRH/BD/70423/2010 from FCT, Portugal. A. S. Veiga acknowledges FCT, Portugal, for funding within the FCT Investigator Programme (IF/00803/2012).WileyRepositório da Universidade de LisboaFreire, João M.Santos, Nuno C.Veiga, Ana SaloméPoian, Andrea T. daCastanho, Miguel A. R. B.2016-03-23T14:59:38Z20152015-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/23130engFEBS Journal 282 (2015) 2267–22781742-464Xdoi:10.1111/febs.13274metadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T16:10:58Zoai:repositorio.ul.pt:10451/23130Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:40:35.851974Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
title Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
spellingShingle Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
Freire, João M.
Antimicrobial
Capsid
Dengue virus
Envelope
Fusion
Multifunctional proteins
title_short Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
title_full Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
title_fullStr Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
title_full_unstemmed Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
title_sort Rethinking the capsid proteins of enveloped viruses : multifunctionality from genome packaging to genome transfection
author Freire, João M.
author_facet Freire, João M.
Santos, Nuno C.
Veiga, Ana Salomé
Poian, Andrea T. da
Castanho, Miguel A. R. B.
author_role author
author2 Santos, Nuno C.
Veiga, Ana Salomé
Poian, Andrea T. da
Castanho, Miguel A. R. B.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Freire, João M.
Santos, Nuno C.
Veiga, Ana Salomé
Poian, Andrea T. da
Castanho, Miguel A. R. B.
dc.subject.por.fl_str_mv Antimicrobial
Capsid
Dengue virus
Envelope
Fusion
Multifunctional proteins
topic Antimicrobial
Capsid
Dengue virus
Envelope
Fusion
Multifunctional proteins
description © 2015 FEBS
publishDate 2015
dc.date.none.fl_str_mv 2015
2015-01-01T00:00:00Z
2016-03-23T14:59:38Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10451/23130
url http://hdl.handle.net/10451/23130
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv FEBS Journal 282 (2015) 2267–2278
1742-464X
doi:10.1111/febs.13274
dc.rights.driver.fl_str_mv metadata only access
info:eu-repo/semantics/openAccess
rights_invalid_str_mv metadata only access
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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