Journal
JOURNAL OF EXPERIMENTAL MEDICINE
Volume 207, Issue 9, Pages 1995-2002Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1084/jem.20101176
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Funding
- National Institutes of Health [1 P01 AI08677-01]
- International AIDS Vaccine Initiative (IAVI)
- CAVD [38619]
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The identification and characterization of conserved epitopes on the HIV-1 viral spike that are immunogenic in humans and targeted by neutralizing antibodies is an important step in vaccine design. Antibody cloning experiments revealed that 32% of all HIV-neutralizing antibodies expressed by the memory B cells in patients with high titers of broadly neutralizing antibodies recognize one or more core epitopes that were not defined. Here, we show that anti-core antibodies recognize a single conserved epitope on the gp120 subunit. Amino acids D474, M475, R476, which are essential for anti-core antibody binding, form an immunodominant triad at the outer domain/inner domain junction of gp120. The mutation of these residues to alanine impairs viral fusion and fitness. Thus, the core epitope, a frequent target of anti-HIV-neutralizing antibodies, including the broadly neutralizing antibody HJ16, is conserved and indispensible for viral infectivity. We conclude that the core epitope should be considered as a target for vaccine design.
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