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dc.contributor.authorLorente, Elena 
dc.contributor.authorBarriga, Alejandro 
dc.contributor.authorJohnstone, Carolina 
dc.contributor.authorMir-Gerrero, Carmen 
dc.contributor.authorJimenez, Mercedes 
dc.contributor.authorLópez, Daniel 
dc.date.accessioned2019-12-02T13:11:44Z
dc.date.available2019-12-02T13:11:44Z
dc.date.issued2013
dc.identifier.citationPLoS One. 2013 Nov 1;8(11):e79596.es_ES
dc.identifier.issn1932-6203es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/8726
dc.description.abstractIn the classical human leukocyte antigen (HLA) class I antigen processing and presentation pathway, the antigenic peptides are generated from viral proteins by multiple proteolytic cleavages of the proteasome (and in some cases other cytosolic proteases) and transported to the endoplasmic reticulum (ER) lumen where they are exposed to aminopeptidase activity. In human cells, two different ER-resident enzymes, ERAP1 and ERAP2, can trim the N-terminally extended residues of peptide precursors. In this study, the possible cooperative effect of generating five naturally processed HLA-B27 ligands by both proteases was analyzed. We identified differences in the products obtained with increased detection of natural HLA-B27 ligands by comparing double versus single enzyme digestions by mass spectrometry analysis. These in vitro data suggest that each enzyme can use the degradation products of the other as a substrate for new N-terminal trimming, indicating concerted aminoproteolytic activity of ERAP 1 and ERAP2.es_ES
dc.description.sponsorshipThis work was supported by grants to D. L. from the Ministerio de Ciencia e Innovación. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.es_ES
dc.language.isoenges_ES
dc.publisherPublic Library of Sciencees_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAminopeptidases es_ES
dc.subject.meshHLA-B27 Antigen es_ES
dc.subject.meshHumans es_ES
dc.subject.meshLigands es_ES
dc.subject.meshMinor Histocompatibility Antigens es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshProtein Multimerization es_ES
dc.subject.meshProtein Structure, Quaternary es_ES
dc.subject.meshRespiratory Syncytial Virus, Humanes_ES
dc.subject.meshViral Proteins es_ES
dc.subject.meshProteolysis es_ES
dc.titleConcerted in vitro trimming of viral HLA-B27-restricted ligands by human ERAP1 and ERAP2 aminopeptidaseses_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID24223975es_ES
dc.format.volume8es_ES
dc.format.number11es_ES
dc.format.pagee79596es_ES
dc.identifier.doi10.1371/journal.pone.0079596es_ES
dc.contributor.funderMinisterio de Ciencia e Innovación (España)
dc.description.peerreviewedes_ES
dc.identifier.e-issn1932-6203es_ES
dc.relation.publisherversionhttps://doi.org/10.1371/journal.pone.0079596es_ES
dc.identifier.journalPloS onees_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución 4.0 Internacional
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