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dc.contributor.authorSamino, Yolanda
dc.contributor.authorLópez, Daniel 
dc.contributor.authorGuil, Sara
dc.contributor.authorde León, Patricia
dc.contributor.authorVal, Margarita del
dc.identifier.citationJ Biol Chem. 2004 Jan 9;279(2):1151-60. Epub 2003 Oct 28.es_ES
dc.description.abstractCytotoxic T lymphocytes (CTL) recognize viral peptidic antigens presented by major histocompatibility complex (MHC) class I molecules on the surface of infected cells. The CTL response is critical in clearance and prevention of HIV infection. Yet, there are no descriptions of physiological peptides derived from the viral envelope protein. In the few reports on endogenous MHC class I viral peptidic ligands from HIV internal proteins, definitive positive identification by mass spectrometry is lacking. The HIV-1 envelope glycoprotein gp160 induces a strong specific CTL response restricted by several human and murine MHC class I molecules, including H-2Dd. Previous analyses showed that this response can be optimally mimicked with the synthetic decameric peptide 318RGPGRAFVTI327. We aim to identify the endogenous natural peptides mediating the response to this epitope. Our data indicate the presence of, at least, two peptidic species of different length and sharing the same antigenic core, which are associated with the Dd presenting molecule in infected cells. One species is at least, probably, the optimal decapeptide. The second species, identified by mass spectrometry for the first time in HIV, is, unexpectedly, a nonamer, which lacks the correctly positioned N-terminal group to bind to Dd. And yet, it is present in similar amounts and, notably, is equally antigenic. Thus, the physiological set of HIV-derived MHC class I ligands is richer and different than expected from studies with synthetic peptides. This may help raise the plasticity and thus the effectiveness of the immune response against the viral infection. These data have implications for HIV vaccine development.es_ES
dc.description.sponsorshipThis work was supported by grants from the European Union, Ministerio de Educación y Ciencia, Comisión Interministerial de Ciencia y Tecnología, Comunidad de Madrid, Instituto de Salud Carlos III, and Red Temática de Investigación Cooperativa en SIDA del Fondo de Investigaciones Sanitarias. 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 Biologyes_ES
dc.relation.isversionofPublisher's versiones_ES
dc.subject.meshAnimals es_ES
dc.subject.meshCell Line es_ES
dc.subject.meshCell Line, Tumor es_ES
dc.subject.meshChromatography, High Pressure Liquid es_ES
dc.subject.meshCytokines es_ES
dc.subject.meshEpitopes es_ES
dc.subject.meshGlycoproteins es_ES
dc.subject.meshHIV es_ES
dc.subject.meshHIV Envelope Protein gp160 es_ES
dc.subject.meshHumans es_ES
dc.subject.meshLigands es_ES
dc.subject.meshMass Spectrometry es_ES
dc.subject.meshMice es_ES
dc.subject.meshMice, Inbred BALB C es_ES
dc.subject.meshPeptides es_ES
dc.subject.meshProtein Structure, Tertiaryes_ES
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization es_ES
dc.subject.meshT-Lymphocytes es_ES
dc.subject.meshVaccinia virus es_ES
dc.titleAn endogenous HIV envelope-derived peptide without the terminal NH3+ group anchor is physiologically presented by major histocompatibility complex class I moleculeses_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.contributor.funderEuropean Uniones_ES
dc.contributor.funderMinisterio de Educación y Ciencia (España)es_ES
dc.contributor.funderComunidad de Madrides_ES
dc.contributor.funderInstituto de Salud Carlos III - ISCIIIes_ES
dc.contributor.funderRed Temática Cooperativa de Investigación en Sida (España)es_ES
dc.identifier.journalThe Journal of biological chemistryes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES

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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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