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dc.contributor.authorGuil, Sara
dc.contributor.authorRodríguez-Castro, Marta
dc.contributor.authorAguilar, Francisco 
dc.contributor.authorVillasevil, Eugenia M
dc.contributor.authorAntón, Luis C
dc.contributor.authorVal, Margarita del
dc.identifier.citationJ Biol Chem. 2006 Dec 29;281(52):39925-34. Epub 2006 Nov 6.es_ES
dc.description.abstractCD8(+) T lymphocytes recognize infected cells that display virus-derived antigenic peptides complexed with major histocompatibility complex class I molecules. Peptides are mainly byproducts of cellular protein turnover by cytosolic proteasomes. Cytosolic tripeptidyl-peptidase II (TPPII) also participates in protein degradation. Several peptidic epitopes unexpectedly do not require proteasomes, but it is unclear which proteases generate them. We studied antigen processing of influenza virus nucleoprotein epitope NP(147-155), an archetype epitope that is even destroyed by a proteasome-mediated mechanism. TPPII, with the assistance of endoplasmic reticulum trimming metallo-aminopeptidases, probably ERAAP (endoplasmic reticulum aminopeptidase associated with antigen processing), was crucial for nucleoprotein epitope generation both in the presence of functional proteasomes and when blocked by lactacystin, as shown with specific chemical inhibitors and gene silencing. Different protein contexts and subcellular targeting all allowed epitope processing by TPPII as well as trimming. The results show the plasticity of the cell's assortment of proteases for providing ligands for recognition by antiviral CD8(+) T cells. Our observations identify for the first time a set of proteases competent for antigen processing of an epitope that is susceptible to destruction by proteasomes.es_ES
dc.description.sponsorshipThis work was supported in part by grants from Spanish Ministerio de Educación y Ciencia and from Instituto de Salud Carlos III (to M. D. V.), by a grant from Spanish Ministerio de Educación y Ciencia (to L. C. A.), by an institutional grant from the Fundación Ramón Areces to the Centro de Biología Molecular Severo Ochoa, and by a grant from Comunidad de Madrid (to M. D. V. and L. C. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.es_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biology (ASBMB) es_ES
dc.subject.meshAcetylcysteine es_ES
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAminopeptidases es_ES
dc.subject.meshAnimals es_ES
dc.subject.meshAntigen Presentation es_ES
dc.subject.meshAntigens, Viral es_ES
dc.subject.meshDipeptidyl-Peptidases and Tripeptidyl-Peptidases es_ES
dc.subject.meshEpitopes, T-Lymphocyte es_ES
dc.subject.meshHistocompatibility Antigens Class I es_ES
dc.subject.meshHydrolysis es_ES
dc.subject.meshInfluenza A virus es_ES
dc.subject.meshL Cells es_ES
dc.subject.meshMice es_ES
dc.subject.meshMice, Inbred BALB C es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshNucleoproteins es_ES
dc.subject.meshProteasome Endopeptidase Complex es_ES
dc.subject.meshProteasome Inhibitors es_ES
dc.subject.meshRNA-Binding Proteins es_ES
dc.subject.meshSerine Endopeptidases es_ES
dc.subject.meshSerine Proteinase Inhibitors es_ES
dc.subject.meshT-Lymphocytes, Cytotoxic es_ES
dc.subject.meshVaccinia virus es_ES
dc.subject.meshViral Core Proteins es_ES
dc.titleNeed for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimentales_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.contributor.funderMinisterio de Educación y Ciencia (España)
dc.contributor.funderInstituto de Salud Carlos III 
dc.contributor.funderFundación Ramón Areces
dc.contributor.funderComunidad de Madrid 
dc.identifier.journalThe Journal of biological chemistryes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.rights.accessRightsopen accesses_ES

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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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