National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
P01 AI100148
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
P50 GM082545-06
United States
Citation
Journal: Immunity / Year: 2019 Title: Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope. Authors: Till Schoofs / Christopher O Barnes / Nina Suh-Toma / Jovana Golijanin / Philipp Schommers / Henning Gruell / Anthony P West / Franziska Bach / Yu Erica Lee / Lilian Nogueira / Ivelin S ...Authors: Till Schoofs / Christopher O Barnes / Nina Suh-Toma / Jovana Golijanin / Philipp Schommers / Henning Gruell / Anthony P West / Franziska Bach / Yu Erica Lee / Lilian Nogueira / Ivelin S Georgiev / Robert T Bailer / Julie Czartoski / John R Mascola / Michael S Seaman / M Juliana McElrath / Nicole A Doria-Rose / Florian Klein / Michel C Nussenzweig / Pamela J Bjorkman / Abstract: Broadly neutralizing antibodies (bNAbs) against HIV-1 envelope (Env) inform vaccine design and are potential therapeutic agents. We identified SF12 and related bNAbs with up to 62% neutralization ...Broadly neutralizing antibodies (bNAbs) against HIV-1 envelope (Env) inform vaccine design and are potential therapeutic agents. We identified SF12 and related bNAbs with up to 62% neutralization breadth from an HIV-infected donor. SF12 recognized a glycan-dominated epitope on Env's silent face and was potent against clade AE viruses, which are poorly covered by V3-glycan bNAbs. A 3.3Å cryo-EM structure of a SF12-Env trimer complex showed additional contacts to Env protein residues by SF12 compared with VRC-PG05, the only other known donor-derived silentface antibody, explaining SF12's increased neutralization breadth, potency, and resistance to Env mutation routes. Asymmetric binding of SF12 was associated with distinct N-glycan conformations across Env protomers, demonstrating intra-Env glycan heterogeneity. Administrating SF12 to HIV-1-infected humanized mice suppressed viremia and selected for viruses lacking the N448 glycan. Effective bNAbs can therefore be raised against HIV-1 Env's silent face, suggesting their potential for HIV-1 prevention, therapy, and vaccine development.
#170 - Feb 2014 Broadly Neutralizing Antibodies similarity (1)
#256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1)
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Assembly
Deposited unit
A: SF12 Fab Heavy Chain,SF12 Fab Heavy Chain B: SF12 Fab Light Chain,SF12 Fab Light Chain C: SF12 Fab Light Chain,SF12 Fab Light Chain D: SF12 Fab Heavy Chain,SF12 Fab Heavy Chain E: SF12 Fab Light Chain,SF12 Fab Light Chain F: SF12 Fab Heavy Chain,SF12 Fab Heavy Chain
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