2026-08-29T10:01:23Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/96992024-09-27T22:10:15Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Samino, Yolanda
author
Lopez, Daniel
author
Guil, Sara
author
de León, Patricia
author
Val, Margarita del
funder
Unión Europea
funder
Ministerio de Educación y Ciencia (España)
funder
Comunidad de Madrid (España)
funder
Instituto de Salud Carlos III
funder
Red de Investigación Cooperativa en Investigación en Sida (España)
2020-04-23T07:01:37Z
2020-04-23T07:01:37Z
2004-01-09
J Biol Chem. 2004 Jan 9;279(2):1151-60. Epub 2003 Oct 28.
10.1074/jbc.M305343200
0021-9258
The Journal of biological chemistry
14583622
http://hdl.handle.net/20.500.12105/9699
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-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.
eng
An endogenous HIV envelope-derived peptide without the terminal NH3+ group anchor is physiologically presented by major histocompatibility complex class I molecules
journal article
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AnEndogenousHIVEnvelope_2004.pdf.txt