Induction of human immunodeficiency virus (HIV-1) envelope specific cell-mediated immunity by a non-homologous synthetic peptide
Autor: | Jean-Pierre M'Bika, Jean-Michel Biquard, Velibor Krsmanovic, Alain J. Cozzone, Ammar Achour, Damien Ficheux, Marianna Sikorska |
---|---|
Přispěvatelé: | Deleage, Gilbert |
Rok vydání: | 2007 |
Předmět: |
Spectrometry
Mass Electrospray Ionization Immunogen Science Molecular Sequence Data Peptide HIV Infections envelope Biology Major histocompatibility complex HIV Seronegativity Immunology/Immunity to Infections MHC class I [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology Animals Humans Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Multidisciplinary MHC Class I Gene Gene Products env MHC restriction Virology peptide Cell biology Phenotype Sense strand chemistry synthetic Case-Control Studies Immunology/Immune Response biology.protein HIV-1 Medicine Rabbits Virology/Host Antiviral Responses T-Lymphocytes Cytotoxic Research Article |
Zdroj: | PLoS ONE PLoS ONE, Vol 2, Iss 11, p e1214 (2007) |
ISSN: | 1932-6203 |
Popis: | BACKGROUND: Cell 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 FINDINGS: The 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/SIGNIFICANCE: For 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.BACKGROUND: Cell 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 FINDINGS: The 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/SIGNIFICANCE: For 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: | OpenAIRE |
Externí odkaz: |