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Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope

Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope

Till Schoofs, Christopher O Barnes, Nina Suh-Toma, Jovana Golijanin, Philipp Schommers, Henning Gruell, Anthony P West Jr, Franziska Bach, Yu Erica Lee, Lilian Nogueira, Ivelin S Georgiev, Robert T Bailer, etc.

Immunity. 2019 Jun 18;50(6):1513-1529.e9.

PMID: 31126879

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 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 N448gp120 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP145164245	A3 Glycan		145164-24-5	Price

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