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dc.contributor.authorHerrero, Laura
dc.contributor.authorMonroy, Noemi 
dc.contributor.authorGonzalez Portal, Maria Eugenia 
dc.date.accessioned2019-06-17T10:42:10Z
dc.date.available2019-06-17T10:42:10Z
dc.date.issued2013-01-08
dc.identifier.citationBiochemistry. 2013; 52: 171-177es_ES
dc.identifier.issn0006-2960es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/7779
dc.description.abstractHuman immunodeficiency virus type 1 (HIV-1) Vpu is an integral membrane protein that belongs to the viroporin family. Viroporins interact with cell membranes, triggering membrane permeabilization and promoting release of viral particles. In vitro electrophysiological methods have revealed changes in membrane ion currents when Vpu is present; however, in vivo the molecular mechanism of Vpu at the plasma membrane is still uncertain. We used the yeast Saccharomyces cerevisiae as a genetic model system to analyze how Vpu ion channel impacts cellular homeostasis. Inducible expression of Vpu impaired cell growth, suggesting that this viral protein is toxic to yeast cultures. This toxicity decreased with extracellular acidic pH. Also, Vpu toxicity diminished as the extracellular K(+) concentration was increased. However, expression of the Vpu protein suppresses the growth defect of K(+) uptake-deficient yeast (Δtrk1,2). The phenotype rescue of these highly hyperpolarized cells was almost total when they were grown in medium supplemented with high concentrations of KCl (100 mM) at pH 7.0 but was significantly reduced when the extracellular K(+) concentration or pH was decreased. These results indicate that Vpu has the ability to modify K(+) transport in both yeast strains. Here, we show also that Vpu confers tolerance to the aminoglycoside antibiotic hygromycin B in Δtrk1,2 yeast. Our results suggest that Vpu interferes with cell growth of wild-type yeast but improves proliferation of the hyperpolarized trk1,2 mutant by inducing plasma membrane depolarization. Furthermore, evaluation of the ion channel activity of the Vpu protein in Δtrk1,2 yeast could aid in the development of a high-throughput screening assay for molecules that target the retroviral protein.es_ES
dc.description.sponsorshipThis study was supported by Grants PI PI05/00013 and PI08/0912 from Fondo de Investigación Sanitaria. L.H. and N.M. were holders of Predoctoral Fellowships from Instituto de Salud Carlos III.es_ES
dc.language.isoenges_ES
dc.publisherACS Publications es_ES
dc.type.hasVersionSMURes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshBiological Transport es_ES
dc.subject.meshGene Expression es_ES
dc.subject.meshHIV Infections es_ES
dc.subject.meshHIV-1 es_ES
dc.subject.meshHuman Immunodeficiency Virus Proteins es_ES
dc.subject.meshHumans es_ES
dc.subject.meshPotassium es_ES
dc.subject.meshSaccharomyces cerevisiae es_ES
dc.subject.meshViral Regulatory and Accessory Proteins es_ES
dc.subject.meshHost-Pathogen Interactions es_ES
dc.subject.meshViroporines_ES
dc.subject.meshIon Channels es_ES
dc.subject.meshHIV-1 Vpues_ES
dc.subject.meshCell Membrane Permeability es_ES
dc.subject.meshModels, Biologicales_ES
dc.titleHIV-1 Vpu Protein Mediates the Transport of Potassium in Saccharomyces cerevisiaees_ES
dc.typejournal articlees_ES
dc.rights.licenseAttribution-NonCommercial-Share Alike 4.0 Internacional*
dc.identifier.pubmedID23240720es_ES
dc.format.volume52es_ES
dc.format.number1es_ES
dc.format.page177es_ES
dc.identifier.doi10.1021/bi3011175es_ES
dc.contributor.funderInstituto de Salud Carlos III 
dc.description.peerreviewedes_ES
dc.identifier.e-issn1520-4995es_ES
dc.relation.publisherversionhttps://doi.org/10.1021/bi3011175es_ES
dc.identifier.journalBiochemistryes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/PI05/00013es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/PI08/0912es_ES
dc.rights.accessRightsopen accesses_ES


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Attribution-NonCommercial-Share Alike 4.0 Internacional
Este Item está sujeto a una licencia Creative Commons: Attribution-NonCommercial-Share Alike 4.0 Internacional