Fab-dimerized glycan-reactive antibodies neutralize HIV and are prevalent in humans and rhesus macaques
Wilton B Williams,
R. Ryan Meyerhoff,
Nathan I. Nicely,
Allen L. Hsu,
Mario J Borgnia,
Matthew S Lee,
M Anthony Moody,
Thomas B. Kepler,
S. Munir Alam,
Robert J Parks,
Celia C. LaBranche,
Joseph R Francica,
Geoffrey M Lynn,
William E Walkowicz,
Kevin O. Saunders,
Peter D. Kwong,
Robert A. Seder,
George M Shaw,
Barton F Haynes
Posted 30 Jun 2020
bioRxiv DOI: 10.1101/2020.06.30.178921
Posted 30 Jun 2020
The HIV-1 envelope (Env) is comprised by mass of over 50% glycans. A goal of HIV-1 vaccine development is the induction of Env glycan-reactive broadly neutralizing antibodies (bnAbs). The 2G12 bnAb recognizes an Env glycan cluster using a unique variable heavy (VH) domain-swapped conformation that results in fragment antigen-binding (Fab) dimerization. Here we describe Fab-dimerized glycan (FDG)-reactive antibodies without VH-swapped domains from simian-human immunodeficiency virus (SHIV)-infected macaques that neutralized heterologous HIV-1 isolates. FDG precursors were boosted by vaccination in macaques, and were present in HIV-1-naïve humans with an average estimated frequency of one per 340,000 B cells. These data demonstrate frequent HIV-1 Env glycan-reactive bnAb B cell precursors in macaques and humans and reveal a novel strategy for their induction by vaccination. ### Competing Interest Statement The authors have declared no competing interest.
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