Journal
CELL HOST & MICROBE
Volume 26, Issue 5, Pages 623-+Publisher
CELL PRESS
DOI: 10.1016/j.chom.2019.09.016
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Funding
- Collaboration for AIDS Vaccine Discovery grants from the Bill and Melinda Gates Foundation [OPP1114725, OPP1032144]
- European Union [681137]
- FRISBI [ANR-10-INBS-05-02]
- GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- Institut Pasteur
- ANRS
- Vaccine Research Institute
- Gilead HIV cure program
- Bill and Melinda Gates Foundation [OPP1114725] Funding Source: Bill and Melinda Gates Foundation
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Potent and broadly neutralizing antibodies (bnAbs) are the hallmark of HIV-1 protection by vaccination. The membrane-proximal external region (MPER) of the HIV-1 gp41 fusion protein is targeted by the most broadly reactive HIV-1 neutralizing antibodies. Here, we examine the structural and molecular mechansims of neutralization by anti-MPER bnAb, LN01, which was isolated from lymph-node-derived germinal center B cells of an elite controller and exhibits broad neutralization breadth. LN01 engages both MPER and the transmembrane (TM) region, which together form a continuous helix in complex with LN01. The tilted TM orientation allows LN01 to interact simultaneously with the peptidic component of the MPER epitope and membrane via two specific lipid binding sites of the antibody paratope. Although LN01 carries a high load of somatic mutations, most key residues interacting with the MPER epitope and lipids are germline encoded, lending support for the LN01 epitope as a candidate for lineage-based vaccine development.
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