TY - JOUR
T1 - The caveolin-1 binding domain of HIV-1 glycoprotein gp41 is an efficient B cell epitope vaccine candidate against virus infection
AU - Hovanessian, Ara G.
AU - Briand, Jean Paul
AU - Said, Elias A.
AU - Svab, Josette
AU - Ferris, Stephane
AU - Dali, Hayet
AU - Muller, Sylviane
AU - Desgranges, Claude
AU - Krust, Bernard
N1 - Funding Information:
This work was supported by grants from the Centre National de la Recherche Scientifique, the Institut Pasteur, and the Agence Nationale de la Recherche sur le SIDA. E.A.S. was supported by a grant from SIDACTION. We thank Bryan Williams and Reuben Siraganian for critically reading the manuscript and Emmanuelle Perret for confocal microscopy.
PY - 2004/11
Y1 - 2004/11
N2 - Caveolin-1 is a scaffolding protein that organizes and concentrates specific ligands within the caveolae membranes. We identified a conserved caveolin-1 binding motif in the HIV-1 transmembrane envelope glycoprotein gp41 and designed several synthetic peptides, referred to as CBD1, corresponding to the consensus caveolin-1 binding domain in gp41. In rabbits, these peptides elicit the production of antibodies that inhibit infection of primary CD4 + T lymphocytes by various primary HIV-1 isolates. Interestingly, gp41 exists as a stable complex with caveolin-1 in HIV-infected cells. Anti-CBD1 peptide antibodies, therefore, might be functional by inhibiting the potential interaction of gp41 with caveolin-1. Because of their capacity to elicit antibodies that inhibit the different clades of HIV-1, CBD1-based peptides may represent a novel synthetic universal B cell epitope vaccine candidate for HIV/AIDS. Moreover, such peptides could also have an application as a therapeutic vaccine since CBD1-specific antibodies are rare in HIV-infected individuals from several geographic origins.
AB - Caveolin-1 is a scaffolding protein that organizes and concentrates specific ligands within the caveolae membranes. We identified a conserved caveolin-1 binding motif in the HIV-1 transmembrane envelope glycoprotein gp41 and designed several synthetic peptides, referred to as CBD1, corresponding to the consensus caveolin-1 binding domain in gp41. In rabbits, these peptides elicit the production of antibodies that inhibit infection of primary CD4 + T lymphocytes by various primary HIV-1 isolates. Interestingly, gp41 exists as a stable complex with caveolin-1 in HIV-infected cells. Anti-CBD1 peptide antibodies, therefore, might be functional by inhibiting the potential interaction of gp41 with caveolin-1. Because of their capacity to elicit antibodies that inhibit the different clades of HIV-1, CBD1-based peptides may represent a novel synthetic universal B cell epitope vaccine candidate for HIV/AIDS. Moreover, such peptides could also have an application as a therapeutic vaccine since CBD1-specific antibodies are rare in HIV-infected individuals from several geographic origins.
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U2 - 10.1016/j.immuni.2004.08.015
DO - 10.1016/j.immuni.2004.08.015
M3 - Article
C2 - 15539149
AN - SCOPUS:8544258110
SN - 1074-7613
VL - 21
SP - 617
EP - 627
JO - Immunity
JF - Immunity
IS - 5
ER -
