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dc.contributor.authorLopez, Daniel 
dc.contributor.authorGarcía-Calvo, Margarita
dc.contributor.authorSmith, Geoffrey L
dc.contributor.authorDel Val, Margarita
dc.identifier.citationJ Immunol. 2010 May 1;184(9):5193-9. doi: 10.4049/jimmunol.1000050. Epub 2010 Mar 26.es_ES
dc.description.abstractCD8(+) cytotoxic T lymphocytes recognize infected cells in which MHC class I molecules present pathogen-derived peptides that have been processed mainly by proteasomes. Many infections induce a set of proteases, the caspases involved in apoptosis or inflammation. In this study, we report that processing and presentation of a short vaccinia virus-encoded Ag can take place also by a nonproteasomal pathway, which was blocked in infected cells with chemical inhibitors of caspases. By cleaving at noncanonical sites, at least two caspases generated antigenic peptides recognized by T lymphocytes. The sites and the peptidic products were partially overlapping but different to those used and produced by proteasomes in vitro. Antigenic natural peptides produced in infected cells by either pathway were quantitatively and qualitatively similar. Finally, coexpression of the natural vaccinia virus protein B13, which is an inhibitor of caspases and apoptosis, impaired Ag presentation by the caspase pathway in infected cells. These data support the hypothesis that numerous cellular proteolytic systems, including those induced during infection, such as caspases involved in apoptosis or in inflammation, contribute to the repertoire of presented peptides, thereby facilitating immunosurveillance.es_ES
dc.description.sponsorshipThis work was supported by grants provided by the European Union, Ministerio de Ciencia e Innovación, Comunidad de Madrid, and Instituto de Salud Carlos III (to M.D.V.) and Programa Ramón y Cajal, Comunidad de Madrid, and Instituto de Salud Carlos III (to D.L.). G.L.S. is a Wellcome Principal Research Fellow.es_ES
dc.publisherAmerican Association of Immunologists (AAI) es_ES
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAnimals es_ES
dc.subject.meshAntigen Presentation es_ES
dc.subject.meshApoptosis es_ES
dc.subject.meshCD8-Positive T-Lymphocytes es_ES
dc.subject.meshCaspases es_ES
dc.subject.meshCell Line es_ES
dc.subject.meshH-2 Antigens es_ES
dc.subject.meshHistocompatibility Antigen H-2D es_ES
dc.subject.meshImmediate-Early Proteins es_ES
dc.subject.meshImmunodominant Epitopes es_ES
dc.subject.meshMice es_ES
dc.subject.meshMice, Inbred BALB C es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshMuromegalovirus es_ES
dc.subject.meshPeptides es_ES
dc.subject.meshProteasome Endopeptidase Complex es_ES
dc.subject.meshSignal Transduction es_ES
dc.subject.meshVaccinia virus es_ES
dc.titleCaspases in virus-infected cells contribute to recognition by CD8+ T lymphocyteses_ES
dc.typejournal articlees_ES
dc.rights.licenseAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.contributor.funderEuropean Union
dc.contributor.funderMinisterio de Ciencia e Innovación (España)
dc.contributor.funderComunidad de Madrid 
dc.contributor.funderInstituto de Salud Carlos III 
dc.identifier.journalJournal of immunology (Baltimore, Md. : 1950)es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.rights.accessRightsopen accesses_ES

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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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