Peptides interfering 3A protein dimerization decrease FMDV multiplication

Mostra el registre complet Registre parcial de l'ítem

• dc.contributor.author González Magaldi, Mónicaca
• dc.contributor.author Vázquez Calvo, Ángelaca
• dc.contributor.author Torre, Beatriz G. de laca
• dc.contributor.author Valle, Javierca
• dc.contributor.author Andreu Martínez, Davidca
• dc.contributor.author Sobrino, Franciscoca
• dc.date.accessioned 2016-02-01T16:11:35Z
• dc.date.available 2016-02-01T16:11:35Z
• dc.date.issued 2015
• dc.description.abstract Nonstructural protein 3A is involved in relevant functions in foot-and-mouth disease virus (FMDV) replication. FMDV 3A can form homodimers and preservation of the two hydrophobic α-helices (α1 and α2) that stabilize the dimer interface is essential for virus replication. In this work, small peptides mimicking residues involved in the dimer interface were used to interfere with dimerization and thus gain insight on its biological function. The dimer interface peptides α1, α2 and that spanning the two hydrophobic α-helices, α12, impaired in vitro dimer formation of a peptide containing the two α-helices, this effect being higher with peptide α12. To assess the effect of dimer inhibition in cultured cells, the interfering peptides were N-terminally fused to a heptaarginine (R7) sequence to favor their intracellular translocation. Thus, when fused to R7, interference peptides (100 μM) were able to inhibit dimerization of transiently expressed 3A, the higher inhibitions being found with peptides α1 and α12. The 3A dimerization impairment exerted by the peptides correlated with significant, specific reductions in the viral yield recovered from peptide-treated FMDV infected cells. In this case, α2 was the only peptide producing significant reductions at concentrations lower than 100 μM. Thus, dimer interface peptides constitute a tool to understand the structure-function relationship of this viral protein and point to 3A dimerization as a potential antiviral target.ca
• dc.description.sponsorship Work at CBMSO was supported by grants BIO2011-24351 from Ministerio de Economía y Competitividad, PLATESA-S2013/ABI-2906 from Comunidad de Madrid, and by an institutional grant from Fundación Ramón Areces to FS. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript Work at UPF was funded by grants SAF2011-24899 from Ministerio de Economía y Competitividad and 2009SGR492 from Generalitat de Catalunya to DA
• dc.format.mimetype application/pdfca
• dc.identifier.citation González-Magaldi M, Vázquez-Calvo Á, de la Torre BG, Valle J, Andreu D, Sobrino F. Peptides interfering 3A protein dimerization decrease FMDV multiplication. PLoS One. 2015; 10(10): e0141415. DOI 10.1371/journal.pone.0141415ca
• dc.identifier.doi http://dx.doi.org/10.1371/journal.pone.0141415
• dc.identifier.issn 1932-6203
• dc.identifier.uri http://hdl.handle.net/10230/25710
• dc.language.iso engca
• dc.publisher Public Library of Science (PLoS)ca
• dc.relation.ispartof PLoS One. 2015; 10(10): e0141415
• dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2011-24351
• dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/SAF2011-24899
• dc.rights © 2015 González-Magaldi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are creditedca
• dc.rights.accessRights info:eu-repo/semantics/openAccessca
• dc.rights.uri http://creativecommons.org/licenses/by/4.0/ca
• dc.subject.other Pèptids -- Síntesica
• dc.subject.other Proteïnesca
• dc.title Peptides interfering 3A protein dimerization decrease FMDV multiplicationca
• dc.type info:eu-repo/semantics/articleca
• dc.type.version info:eu-repo/semantics/publishedVersionca