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dc.contributor.authorLorente, Elena 
dc.contributor.authorFontela, Miguel G 
dc.contributor.authorBarnea, Eilon
dc.contributor.authorMartin-Galiano, Antonio Javier 
dc.contributor.authorMir-Gerrero, Carmen 
dc.contributor.authorGalocha, Begoña 
dc.contributor.authorAdmon, Arie 
dc.contributor.authorLauzurica, Pilar 
dc.contributor.authorLópez, Daniel 
dc.date.accessioned2020-06-18T07:07:57Z
dc.date.available2020-06-18T07:07:57Z
dc.date.issued2020-06
dc.identifier.citationMol Cell Proteomics. 2020 Jun;19(6):994-1004.es_ES
dc.identifier.issn1535-9476es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/10488
dc.descriptiones_ES
dc.descriptionThe mass spectrometry data have been deposited to the MassIVE repository (http://massive.ucsd.edu) with the data set identifier MSV000084718.
dc.description.abstractThe HLA-B*27:05 allele and the endoplasmic reticulum-resident aminopeptidases are strongly associated with AS, a chronic inflammatory spondyloarthropathy. This study examined the effect of ERAP2 in the generation of the natural HLA-B*27:05 ligandome in live cells. Complexes of HLA-B*27:05-bound peptide pools were isolated from human ERAP2-edited cell clones, and the peptides were identified using high-throughput mass spectrometry analyses. The relative abundance of a thousand ligands was established by quantitative tandem mass spectrometry and bioinformatics analysis. The residue frequencies at different peptide position, identified in the presence or absence of ERAP2, determined structural features of ligands and their interactions with specific pockets of the antigen-binding site of the HLA-B*27:05 molecule. Sequence alignment of ligands identified with species of bacteria associated with HLA-B*27-dependent reactive arthritis was performed. In the absence of ERAP2, peptides with N-terminal basic residues and minority canonical P2 residues are enriched in the natural ligandome. Further, alterations of residue frequencies and hydrophobicity profile at P3, P7, and PΩ positions were detected. In addition, several ERAP2-dependent cellular peptides were highly similar to protein sequences of arthritogenic bacteria, including one human HLA-B*27:05 ligand fully conserved in a protein from Campylobacter jejuni These findings highlight the pathogenic role of this aminopeptidase in the triggering of AS autoimmune disease.es_ES
dc.description.sponsorshipMinisterio de Ciencia, Innovación y Universidades (MPY 388/18, MPY 483 1346/16, SAF2014–58052) Israel Science Foundation (No. 1435/16)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/4.0/*
dc.titleModulation of Natural HLA-B*27:05 Ligandome by Ankylosing Spondylitis-associated Endoplasmic Reticulum Aminopeptidase 2 (ERAP2).es_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID32265295es_ES
dc.format.volume19es_ES
dc.format.number6es_ES
dc.format.page994-1004es_ES
dc.identifier.doi10.1074/mcp.RA120.002014es_ES
dc.contributor.funderMinisterio de Ciencia, Innovación y Universidades (España)es_ES
dc.contributor.funderIsrael Science Foundationes_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn1535-9484es_ES
dc.relation.publisherversionhttps://doi.org/10.1074/mcp.RA120.002014es_ES
dc.identifier.journalMolecular & Cellular Proteomicses_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu_repo/grantAgreement/ES/MPY 388/18es_ES
dc.relation.projectIDinfo:eu_repo/grantAgreement/ES/MPY 483 1346/16es_ES
dc.relation.projectIDinfo:eu_repo/grantAgreement/ES/SAF2014–58052es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución 4.0 Internacional
This item is licensed under a: Atribución 4.0 Internacional