Publication:
Viroporins

dc.contributor.authorGonzalez Portal, Maria Eugenia
dc.contributor.authorCarrasco, Luis
dc.contributor.funderComunidad de Madrid (España)
dc.contributor.funderInstituto de Salud Carlos III
dc.contributor.funderDirección General de Investigación Científica y Técnica (España)
dc.date.accessioned2019-06-17T09:15:09Z
dc.date.available2019-06-17T09:15:09Z
dc.date.issued2003-09-18
dc.description.abstractViroporins are a group of proteins that participate in several viral functions, including the promotion of release of viral particles from cells. These proteins also affect cellular functions, including the cell vesicle system, glycoprotein trafficking and membrane permeability. Viroporins are not essential for the replication of viruses, but their presence enhances virus growth. Comprising some 60-120 amino acids, viroporins have a hydrophobic transmembrane domain that interacts with and expands the lipid bilayer. Some viroporins also contain other motifs, such as basic amino acid residues or a domain rich in aromatic amino acids that confers on the protein the ability to interact with the interfacial lipid bilayer. Viroporin oligomerization gives rise to hydrophilic pores at the membranes of virus-infected cells. As the list of known viroporins steadily grows, recent research efforts focus on deciphering the actions of the viroporins poliovirus 2B, alphavirus 6K, HIV-1 Vpu and influenza virus M2. All these proteins can enhance the passage of ions and small molecules through membranes depending on their concentration gradient. Future work will lengthen the list of viroporins and will provide a deeper understanding of their mechanisms of action.es_ES
dc.description.peerreviewedes_ES
dc.description.sponsorshipThis work was supported by the Comunidad Autonoma de Madrid (082‐0024/2000), Instituto de Salud Carlos III (01/0042) and the DGICYT (PM99‐0002). The authors also acknowledge the institutional grant awarded to the Centro de Biologı́a Molecular ‘Severo Ochoa’ by the Fundación Ramón Areces.es_ES
dc.format.number1es_ES
dc.format.page28-34es_ES
dc.format.volume552es_ES
dc.identifier.citationFEBS Lett. 2003;552(1):28-34.es_ES
dc.identifier.doi10.1016/S0014-5793(03)00780-4es_ES
dc.identifier.e-issn1873-3468es_ES
dc.identifier.issn0014-5793es_ES
dc.identifier.journalFEBS letterses_ES
dc.identifier.pubmedID12972148es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/7778
dc.language.isoenges_ES
dc.publisherFederation of European Biochemical Societies (FEBS)
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/082-0024/2000es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/01/0042es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/PM99-0002es_ES
dc.relation.publisherversionhttps://doi.org/10.1016/S0014-5793(03)00780-4es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiología (CNM)es_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsopen accesses_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAmino Acid Sequencees_ES
dc.subject.meshAmino Acidses_ES
dc.subject.meshAntiviral Agentses_ES
dc.subject.meshCell Membranees_ES
dc.subject.meshCell Membrane Permeabilityes_ES
dc.subject.meshHuman Immunodeficiency Virus Proteinses_ES
dc.subject.meshIon Channelses_ES
dc.subject.meshLipid Bilayerses_ES
dc.subject.meshModels, Moleculares_ES
dc.subject.meshMolecular Sequence Dataes_ES
dc.subject.meshPicornaviridaees_ES
dc.subject.meshProtein Structure, Tertiaryes_ES
dc.subject.meshViral Envelope Proteinses_ES
dc.subject.meshViral Matrix Proteinses_ES
dc.titleViroporinses_ES
dc.typeresearch articlees_ES
dc.type.hasVersionAMes_ES
dspace.entity.typePublication
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