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dc.contributor.authorInfantes, Susana 
dc.contributor.authorLorente, Elena 
dc.contributor.authorBarnea, Eilon
dc.contributor.authorBeer, Ilan
dc.contributor.authorBarriga, Alejandro 
dc.contributor.authorLasala, Fatima
dc.contributor.authorJimenez, Mercedes 
dc.contributor.authorAdmon, Arie
dc.contributor.authorLopez, Daniel 
dc.date.accessioned2020-04-23T06:59:10Z
dc.date.available2020-04-23T06:59:10Z
dc.date.issued2013-04-12
dc.identifier.citationJ Biol Chem . 2013 Apr 12;288(15):10882-9.es_ES
dc.identifier.issn0021-9258es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/9694
dc.description.abstractThe presentation of short viral peptide antigens by human leukocyte antigen (HLA) class I molecules on cell surfaces is a key step in the activation of cytotoxic T lymphocytes, which mediate the killing of pathogen-infected cells or initiate autoimmune tissue damage. HLA-B27 is a well known class I molecule that is used to study both facets of the cellular immune response. Using mass spectrometry analysis of complex HLA-bound peptide pools isolated from large amounts of HLA-B*2705(+) cells, we identified 200 naturally processed HLA-B*2705 ligands. Our analyses revealed that a change in the position (P) 2 anchor motif was detected in the 3% of HLA-B*2705 ligands identified. B*2705 class I molecules were able to bind these six GlnP2 peptides, which showed significant homology to pathogenic bacterial sequences, with a broad range of affinities. One of these ligands was able to bind with distinct conformations to HLA-B27 subtypes differentially associated with ankylosing spondylitis. These conformational differences could be sufficient to initiate autoimmune damage in patients with ankylosing spondylitis-associated subtypes. Therefore, these kinds of peptides (short, with GlnP2, and similar low affinity to all HLA-B27 subtypes tested but with unlike conformations in differentially ankylosing spondylitis-associated subtypes) must not be excluded from future researches involving potential arthritogenic peptides.es_ES
dc.description.sponsorshipThis work was supported by grants from the Programa Ramón y Cajal and the Ministerio de Ciencia e Innovación (to D. L.) and from the Israel Science Foundation (ISF 916/05) (to A. A.).es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biology (ASBMB) es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAmino Acid Motifs es_ES
dc.subject.meshCell Line es_ES
dc.subject.meshHLA-B27 Antigen es_ES
dc.subject.meshHumans es_ES
dc.subject.meshPeptides es_ES
dc.subject.meshProtein Binding es_ES
dc.subject.meshSpondylarthropathies es_ES
dc.titleNatural HLA-B*2705 protein ligands with glutamine as anchor motif: implications for HLA-B27 association with spondyloarthropathyes_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID23430249es_ES
dc.format.volume288es_ES
dc.format.number15es_ES
dc.format.page10882-9es_ES
dc.identifier.doi10.1074/jbc.M113.455352es_ES
dc.contributor.funderMinisterio de Ciencia e Innovación (España) 
dc.contributor.funderIsrael Science Foundation 
dc.description.peerreviewedNoes_ES
dc.identifier.e-issn1083-351Xes_ES
dc.relation.publisherversionhttps://doi.org/10.1074/jbc.M113.455352es_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/ISF 916/05es_ES
dc.rights.accessRightsopen accesses_ES


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Atribución-NoComercial-CompartirIgual 4.0 Internacional
Este Item está sujeto a una licencia Creative Commons: Atribución-NoComercial-CompartirIgual 4.0 Internacional