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dc.contributor.authorLorente, Elena 
dc.contributor.authorInfantes, Susana 
dc.contributor.authorAbia, David
dc.contributor.authorBarnea, Eilon
dc.contributor.authorBeer, Ilan
dc.contributor.authorGarcia, Ruth 
dc.contributor.authorLasala, Fatima
dc.contributor.authorJimenez, Mercedes 
dc.contributor.authorMir-Gerrero, Carmen 
dc.contributor.authorMorreale, Antonio
dc.contributor.authorAdmon, Arie 
dc.contributor.authorLópez, Daniel 
dc.date.accessioned2019-11-06T11:53:28Z
dc.date.available2019-11-06T11:53:28Z
dc.date.issued2012-10-12
dc.identifier.citationJ Biol Chem. 2012 Oct 12;287(42):34895-903. doi: 10.1074/jbc.M112.362293. Epub 2012 Aug 27.es_ES
dc.identifier.issn0021-9258es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/8563
dc.description.abstractThe transporter associated with antigen processing (TAP) enables the flow of viral peptides generated in the cytosol by the proteasome and other proteases to the endoplasmic reticulum, where they complex with nascent human leukocyte antigen (HLA) class I. Later, these peptide-HLA class I complexes can be recognized by CD8(+) lymphocytes. Cancerous cells and infected cells in which TAP is blocked, as well as individuals with unusable TAP complexes, are able to present peptides on HLA class I by generating them through TAP-independent processing pathways. Here, we identify a physiologically processed HLA-E ligand derived from the D8L protein in TAP-deficient vaccinia virus-infected cells. This natural high affinity HLA-E class I ligand uses alternative interactions to the anchor motifs previously described to be presented on nonclassical HLA class I molecules. This octameric peptide was also presented on HLA-Cw1 with similar binding affinity on both classical and nonclassical class I molecules. In addition, this viral peptide inhibits HLA-E-mediated cytolysis by natural killer cells. Comparison between the amino acid sequences of the presenting HLA-E and HLA-Cw1 alleles revealed a shared structural motif in both HLA class molecules, which could be related to their observed similar cross-reactivity affinities. This motif consists of several residues located on the floor of the peptide-binding site. These data expand the role of HLA-E as an antigen-presenting molecule.es_ES
dc.description.sponsorshipThis work was supported by grants from the Ministerio de Ciencia e Innovación and the Fundación para la Investigación y Prevención del SIDA en España (FIPSE) Foundation (to D. L.) and Israel Science Foundation Grant 916/05 (to A. A.).es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyes_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshATP-Binding Cassette Transporters es_ES
dc.subject.meshAmino Acid Motifs es_ES
dc.subject.meshAntigens, Viral es_ES
dc.subject.meshCD8-Positive T-Lymphocytes es_ES
dc.subject.meshCell Line es_ES
dc.subject.meshHLA-C Antigens es_ES
dc.subject.meshHistocompatibility Antigens Class I es_ES
dc.subject.meshHumans es_ES
dc.subject.meshMembrane Proteins es_ES
dc.subject.meshPeptides es_ES
dc.subject.meshVaccinia es_ES
dc.subject.meshVaccinia virus es_ES
dc.subject.meshViral Structural Proteins es_ES
dc.subject.meshAntigen Presentation es_ES
dc.titleA viral, transporter associated with antigen processing (TAP)-independent, high affinity ligand with alternative interactions endogenously presented by the nonclassical human leukocyte antigen E class I moleculees_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID22927436es_ES
dc.format.volume287es_ES
dc.format.number42es_ES
dc.format.page34895-903es_ES
dc.identifier.doi10.1074/jbc.M112.362293es_ES
dc.contributor.funderMinisterio de Ciencia e Innovación (España)
dc.contributor.funderFundación para la Investigación y la Prevención del Sida en España
dc.contributor.funderIsrael Science Foundation
dc.description.peerreviewedes_ES
dc.identifier.e-issn1083-351Xes_ES
dc.relation.publisherversionhttps://doi.org/10.1074/jbc.M112.362293es_ES
dc.identifier.journalThe Journal of biological chemistryes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/916/05es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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