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Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide
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...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080760/ https://www.ncbi.nlm.nih.gov/pubmed/18043730 http://dx.doi.org/10.1371/journal.pone.0001214 |
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author | Achour, Ammar Biquard, Jean-Michel Krsmanovic, Velibor M'Bika, Jean-Pierre Ficheux, Damien Sikorska, Marianna Cozzone, Alain J. |
author_facet | Achour, Ammar Biquard, Jean-Michel Krsmanovic, Velibor M'Bika, Jean-Pierre Ficheux, Damien Sikorska, Marianna Cozzone, Alain J. |
author_sort | Achour, Ammar |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2080760 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-20807602007-11-28 Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide Achour, Ammar Biquard, Jean-Michel Krsmanovic, Velibor M'Bika, Jean-Pierre Ficheux, Damien Sikorska, Marianna Cozzone, Alain J. PLoS One Research Article 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. Public Library of Science 2007-11-28 /pmc/articles/PMC2080760/ /pubmed/18043730 http://dx.doi.org/10.1371/journal.pone.0001214 Text en Achour et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Achour, Ammar Biquard, Jean-Michel Krsmanovic, Velibor M'Bika, Jean-Pierre Ficheux, Damien Sikorska, Marianna Cozzone, Alain J. Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide |
title | Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide |
title_full | Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide |
title_fullStr | Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide |
title_full_unstemmed | Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide |
title_short | Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologous Synthetic Peptide |
title_sort | induction of human immunodeficiency virus (hiv-1) envelope specific cell-mediated immunity by a non-homologous synthetic peptide |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2080760/ https://www.ncbi.nlm.nih.gov/pubmed/18043730 http://dx.doi.org/10.1371/journal.pone.0001214 |
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