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dc.contributor.author | Barriga, Alejandro | |
dc.contributor.author | Lorente, Elena | |
dc.contributor.author | Johnstone, Carolina | |
dc.contributor.author | Mir-Gerrero, Carmen | |
dc.contributor.author | Val, Margarita del | |
dc.contributor.author | Lopez, Daniel | |
dc.date.accessioned | 2018-12-18T14:05:20Z | |
dc.date.available | 2018-12-18T14:05:20Z | |
dc.date.issued | 2014-09 | |
dc.identifier.citation | PLoS One. 2014 Sep 30;9(9):e106772 | es_ES |
dc.identifier.issn | 1932-6203 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/6886 | |
dc.description.abstract | CD8(+) T cells identify and kill infected cells through the specific recognition of short viral antigens bound to human major histocompatibility complex (HLA) class I molecules. The colossal number of polymorphisms in HLA molecules makes it essential to characterize the antigen-presenting properties common to large HLA families or supertypes. In this context, the HLA-B*27 family comprising at least 100 different alleles, some of them widely distributed in the human population, is involved in the cellular immune response against pathogens and also associated to autoimmune spondyloarthritis being thus a relevant target of study. To this end, HLA binding assays performed using nine HLA-B*2705-restricted ligands endogenously processed and presented in virus-infected cells revealed a common minimal peptide motif for efficient binding to the HLA-B*27 family. The motif was independently confirmed using four unrelated peptides. This experimental approach, which could be easily transferred to other HLA class I families and supertypes, has implications for the validation of new bioinformatics tools in the functional clustering of HLA molecules, for the identification of antiviral cytotoxic T lymphocyte responses, and for future vaccine development. | es_ES |
dc.description.sponsorship | This work was supported by grants to D. L. from the Spanish “Ministerio de Economía y Competitividad”. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Public Library of Science (PLOS) | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject.mesh | Amino Acid Motifs | es_ES |
dc.subject.mesh | Animals | es_ES |
dc.subject.mesh | Antigen Presentation | es_ES |
dc.subject.mesh | Antigens, Viral, Tumor | 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 | Ligands | es_ES |
dc.subject.mesh | Mice | es_ES |
dc.subject.mesh | Protein Binding | es_ES |
dc.subject.mesh | Protein Stability | es_ES |
dc.subject.mesh | Respiratory Syncytial Virus, Human | es_ES |
dc.subject.mesh | Viral Proteins | es_ES |
dc.title | A common minimal motif for the ligands of HLA-B*27 class I molecules | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución 4.0 Internacional | * |
dc.identifier.pubmedID | 25268942 | es_ES |
dc.format.volume | 9 | es_ES |
dc.format.number | 9 | es_ES |
dc.format.page | e106772 | es_ES |
dc.identifier.doi | 10.1371/journal.pone.0106772 | es_ES |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | |
dc.description.peerreviewed | Sí | es_ES |
dc.identifier.e-issn | 1932-6203 | es_ES |
dc.relation.publisherversion | https://doi.org/10.1371/journal.pone.0106772 | es_ES |
dc.identifier.journal | PloS one | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología | es_ES |
dc.repisalud.institucion | ISCIII | es_ES |
dc.rights.accessRights | open access | es_ES |