Journal
SCIENCE
Volume 352, Issue 6287, Pages 828-833Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aae0474
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Funding
- Intramural Research Programs of the Vaccine Research Center and Division of Intramural Research, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health
- International AIDS Vaccine Initiative's (IAVI's) Neutralizing Antibody Consortium
- Bill & Melinda Gates Foundation
- Ministry of Foreign Affairs of Denmark, Irish Aid
- Ministry of Finance of Japan
- Ministry of Foreign Affairs of the Netherlands
- Norwegian Agency for Development Cooperation (NORAD)
- UK Department for International Development (DFID)
- U.S. Agency for International Development (USAID)
- NIH [R01GM079238, P01GM56550, R01GM116654]
- U.S. Department of Energy, Basic Energy Sciences, Office of Science, [W-31-109-Eng-38]
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The HIV-1 fusion peptide, comprising 15 to 20 hydrophobic residues at the N terminus of the Env-gp41 subunit, is a critical component of the virus-cell entry machinery. Here, we report the identification of a neutralizing antibody, N123-VRC34.01, which targets the fusion peptide and blocks viral entry by inhibiting conformational changes in gp120 and gp41 subunits of Env required for entry. Crystal structures of N123-VRC34.01 liganded to the fusion peptide, and to the full Env trimer, revealed an epitope consisting of the N-terminal eight residues of the gp41 fusion peptide and glycan N88 of gp120, and molecular dynamics showed that the N-terminal portion of the fusion peptide can be solvent-exposed. These results reveal the fusion peptide to be a neutralizing antibody epitope and thus a target for vaccine design.
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