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dc.contributor.authorLorente, Elena 
dc.contributor.authorInfantes, Susana 
dc.contributor.authorBarnea, Eilon
dc.contributor.authorBeer, Ilan
dc.contributor.authorGarcia, Ruth 
dc.contributor.authorAdmon, Arie 
dc.contributor.authorLasala, Fatima
dc.contributor.authorJimenez, Mercedes 
dc.contributor.authorLópez, Daniel 
dc.date.accessioned2020-07-06T05:54:08Z
dc.date.available2020-07-06T05:54:08Z
dc.date.issued2011-01-14
dc.identifier.citationAIDS . 2011 Jan 14;25(2):265-9.es_ES
dc.identifier.issn0269-9370es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/10656
dc.description.abstractIndividuals with nonfunctional transporters associated with antigen processing (TAP) complexes are not particularly susceptible to viral infections or neoplasms. Therefore, their immune system must be reasonably efficient, and the present, though reduced, cytolytic CD8 αβ T subpopulation specific for TAP-independent antigens may be sufficient to establish an immune defense protecting against viral infections in these individuals. The objective of the present study was to identify TAP-independent ligands from HIV gp160 protein. An analysis and comparison of complex human histocompatibility complex (HLA)-bound peptide pools isolated from large quantities of healthy or HIV gp160-expressing human cells was performed using mass spectrometry and bioinformatics tools. A conserved TAP-independent HLA peptide ligand endogenously processed and presented in infected human cells was identified. This ligand originates from the envelope protein bound to the HLA-Cw1 class I molecule with high affinity. It was concluded that HLA class I peptides derived from a large fraction of the N-terminal HIV envelope protein could be presented even in the absence of the TAP complex.es_ES
dc.description.sponsorshipThe present work was supported by grants to D.L. from the Fondo Investigaciones Sanitarias de la Seguridad Social, and the FIPSE Foundation and to A.A. from the Israel Science Foundation ().es_ES
dc.language.isoenges_ES
dc.publisherLippincott, Williams & Wilkinses_ES
dc.relation.isversionofPostprintes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshATP Binding Cassette Transporter, Subfamily B, Member 3es_ES
dc.subject.meshATP-Binding Cassette Transporters es_ES
dc.subject.meshHLA-C Antigens es_ES
dc.subject.meshHumans es_ES
dc.subject.meshLymphocyte Activation es_ES
dc.subject.meshMajor Histocompatibility Complex es_ES
dc.subject.meshProtein Binding es_ES
dc.subject.meshViral Proteins es_ES
dc.titleTAP-independent human histocompatibility complex-Cw1 antigen processing of an HIV envelope protein conserved peptide.es_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID21099670es_ES
dc.format.volume25es_ES
dc.format.number2es_ES
dc.format.page265-9es_ES
dc.identifier.doi10.1097/QAD.0b013e328340fe3ces_ES
dc.contributor.funderFondo de Investigaciones Sanitariases_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn1473-5571es_ES
dc.relation.publisherversionhttps://doi.org/10.1097/QAD.0b013e328340fe3ces_ES
dc.identifier.journalAIDS (London, England)es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu_repo/grantAgreement/ES/ISF 916/05es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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