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dc.contributor.authorBarnea, Eilon
dc.contributor.authorDel Val, Margarita
dc.contributor.authorAdmon, Arie 
dc.contributor.authorLorente, Elena 
dc.contributor.authorPalomo-Sanz, Concepcion 
dc.contributor.authorMir-Gerrero, Carmen 
dc.contributor.authorLópez, Daniel 
dc.date.accessioned2020-06-15T07:18:33Z
dc.date.available2020-06-15T07:18:33Z
dc.date.issued2019
dc.identifier.citationJ Proteome Res . 2019 Sep 6;18(9):3512-3520.es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/10399
dc.description.abstractPeptides generated by proteases in the cytosol must be translocated to endoplasmic reticulum lumen by the transporter associated with antigen processing (TAP) prior to their assembly with major histocompatibility complex (MHC) class I molecules. Nonfunctional TAP complexes produce a drastic decrease of the MHC class I/peptide complexes presented on the cell surface. Previously, the cellular MHC class I ligandome from TAP-deficient cell lines was determined, but similar analysis from normal tissues remains incomplete. Using high-throughput mass spectrometry to analyze the MHC-bound peptide pools isolated from ex vivo spleen cells of TAP-deficient mice, we identified 210 TAP-independent ligands naturally presented by murine MHC class I molecules. This ligandome showed increased peptide lengths, presence of multiple nested set peptides, and low theoretical MHC binding affinity. The gene ontology enrichment analysis of parental proteins of this TAP-independent subligandome showed almost exclusively enrichment in tissue-specific biological processes related to the immune system as would be expected. Also, cellular components of the extracellular space (namely proteins outside the cell but still within the organism excluding the extracellular matrix) were specifically associated with TAP-independent antigen processing from these ex vivo mice cells. In addition, functional protein association network analysis revealed low protein-protein interactions between parental proteins from the TAP-independent ligandome. Finally, predominant endoproteolytic peptidase specificity for Leu/Phe residues in the P1 position of the scissile bond at both ligand termini was found for the ex vivo TAP-independent ligands. These data indicate that the TAP-independent ligandome from ex vivo cells derives from a more diverse collection of both endoprotease activities and parental proteins and where the cell origin and contribution of the extracellular environment are more relevant than in its equivalent cell lines.es_ES
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Economy grants SAF2014-58052 and “Acción Estratégica en Salud” MPY 388/18 to D.L., and by Israel Science Foundation, grant No. 1435/16 to A. A. The funding agencies had no role in the study design, data collection, analysis decision to publish, or preparation of the manuscript.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Chemical Society (ACS) es_ES
dc.relation.isversionofPostprintes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleNatural Spleen Cell Ligandome in Transporter Antigen Processing-Deficient Mice.es_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID31361958es_ES
dc.format.volume18es_ES
dc.format.number9es_ES
dc.format.page3512-3520es_ES
dc.identifier.doi10.1021/acs.jproteome.9b00416es_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)
dc.contributor.funderIsrael Science Foundation
dc.description.peerreviewedes_ES
dc.identifier.e-issn1535-3907es_ES
dc.relation.publisherversionhttps://doi.org/10.1021/acs.jproteome.9b00416es_ES
dc.identifier.journalJournal of proteome researches_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/SAF2014-58052es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/MPY 388/18es_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/435/16es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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