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dc.contributor.author | Infantes, Susana | |
dc.contributor.author | Lorente, Elena | |
dc.contributor.author | Barnea, Eilon | |
dc.contributor.author | Beer, Ilan | |
dc.contributor.author | Barriga, Alejandro | |
dc.contributor.author | Lasala, Fatima | |
dc.contributor.author | Jimenez, Mercedes | |
dc.contributor.author | Admon, Arie | |
dc.contributor.author | Lopez, Daniel | |
dc.date.accessioned | 2020-04-23T06:59:10Z | |
dc.date.available | 2020-04-23T06:59:10Z | |
dc.date.issued | 2013-04-12 | |
dc.identifier.citation | J Biol Chem . 2013 Apr 12;288(15):10882-9. | es_ES |
dc.identifier.issn | 0021-9258 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/9694 | |
dc.description.abstract | The 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.sponsorship | This 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.iso | eng | es_ES |
dc.publisher | American Society for Biochemistry and Molecular Biology (ASBMB) | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject.mesh | Amino Acid Motifs | es_ES |
dc.subject.mesh | Cell Line | es_ES |
dc.subject.mesh | HLA-B27 Antigen | es_ES |
dc.subject.mesh | Humans | es_ES |
dc.subject.mesh | Peptides | es_ES |
dc.subject.mesh | Protein Binding | es_ES |
dc.subject.mesh | Spondylarthropathies | es_ES |
dc.title | Natural HLA-B*2705 protein ligands with glutamine as anchor motif: implications for HLA-B27 association with spondyloarthropathy | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución-NoComercial-CompartirIgual 4.0 Internacional | * |
dc.identifier.pubmedID | 23430249 | es_ES |
dc.format.volume | 288 | es_ES |
dc.format.number | 15 | es_ES |
dc.format.page | 10882-9 | es_ES |
dc.identifier.doi | 10.1074/jbc.M113.455352 | es_ES |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | |
dc.contributor.funder | Israel Science Foundation | |
dc.description.peerreviewed | No | es_ES |
dc.identifier.e-issn | 1083-351X | es_ES |
dc.relation.publisherversion | https://doi.org/10.1074/jbc.M113.455352 | es_ES |
dc.identifier.journal | The Journal of biological chemistry | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología | es_ES |
dc.repisalud.institucion | ISCIII | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/ISF 916/05 | es_ES |
dc.rights.accessRights | open access | es_ES |