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J. Biol. Chem., Vol. 279, Issue 2, 1151-1160, January 9, 2004

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An Endogenous HIV Envelope-derived Peptide without the Terminal NH₃⁺ Group Anchor Is Physiologically Presented by Major Histocompatibility Complex Class I Molecules^*

Yolanda Samino, Daniel López, Sara Guil, Patricia de León, and Margarita Del Val

From the Centro Nacional de Microbiología. Instituto de Salud Carlos III, E-28220 Madrid, Spain

Cytotoxic 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-2D^d. 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 D^d 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 D^d. 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.

Received for publication, May 21, 2003 , and in revised form, October 24, 2003.

^* This 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.

Supported by Ministerio de Educación y Ciencia.

To whom correspondence should be addressed: Centro Nacional de Microbiología. Instituto de Salud Carlos III, Ctra. Pozuelo, km 2, E-28220 Majadahonda (Madrid), Spain. Tel.: 34-915-097-943; Fax: 34-915-097-919; E-mail: mdval{at}isciii.es.

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