The Caveolin-1 Binding Domain of HIV-1 Glycoprotein gp41 Is an Efficient B Cell Epitope Vaccine Candidate against Virus Infection

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...

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Published inImmunity (Cambridge, Mass.) Vol. 21; no. 5; pp. 617 - 627
Main Authors Hovanessian, Ara G., Briand, Jean-Paul, Said, Elias A., Svab, Josette, Ferris, Stephane, Dali, Hayet, Muller, Sylviane, Desgranges, Claude, Krust, Bernard
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.11.2004
Elsevier Limited
Elsevier
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Summary: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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ISSN:1074-7613
1097-4180
DOI:10.1016/j.immuni.2004.08.015