| Autor: |
Ammar Achour, Jean-Michel Biquard, Velibor Krsmanovic, Jean-Pierre M'bika, Damien Ficheux, Marianna Sikorska, Alain J Cozzone |
| Jazyk: |
angličtina |
| Rok vydání: |
2007 |
| Předmět: |
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| Zdroj: |
PLoS ONE, Vol 2, Iss 11, p e1214 (2007) |
| Druh dokumentu: |
article |
| ISSN: |
1932-6203 |
| DOI: |
10.1371/journal.pone.0001214 |
| Popis: |
BackgroundCell mediated immunity, including efficient CTL response, is required to prevent HIV-1 from cell-to-cell transmission. In previous investigations, we have shown that B1 peptide derived by Fourier transformation of HIV-1 primary structures and sharing no sequence homology with the parent proteins was able to generate antiserum which recognizes envelope and Tat proteins. Here we have investigated cellular immune response towards a novel non-homologous peptide, referred to as cA1 peptide.Methodology/principal findingsThe 20 amino acid sequence of cA1 peptide was predicted using the notion of peptide hydropathic properties; the peptide is encoded by the complementary anti-sense DNA strand to the sense strand of previously described non-homologous A1 peptide. In this report we demonstrate that the cA1 peptide can be a target for major histocompatibility complex (MHC) class I-restricted cytotoxic T lymphocytes in HIV-1-infected or envelope-immunized individuals. The cA1 peptide is recognized in association with different MHC class I allotypes and could prime in vitro CTLs, derived from gp160-immunized individuals capable to recognize virus variants.Conclusions/significanceFor the first time a theoretically designed immunogen involved in broad-based cell-immune memory activation is described. Our findings may thus contribute to the advance in vaccine research by describing a novel strategy to develop a synthetic AIDS vaccine. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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