Broadly neutralizing anti-HIV-1 antibodies tether viral particles at the surface of infected cells

Jérémy Dufloo, Cyril Planchais, Stéphane Frémont, Valérie Lorin, Florence Guivel-Benhassine, Karl Stefic, Nicoletta Casartelli, Arnaud Echard, Philippe Roingeard, Hugo Mouquet, Olivier Schwartz () and Timothée Bruel ()
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Jérémy Dufloo: Université de Paris, CNRS UMR3569, Virus and Immunity Unit
Cyril Planchais: Université de Paris, INSERM U1222, Humoral Immunology Laboratory
Stéphane Frémont: Université de Paris, CNRS UMR3691, Membrane Traffic and Cell Division Unit
Valérie Lorin: Université de Paris, INSERM U1222, Humoral Immunology Laboratory
Florence Guivel-Benhassine: Université de Paris, CNRS UMR3569, Virus and Immunity Unit
Karl Stefic: Service de Bactériologie-Virologie
Nicoletta Casartelli: Université de Paris, CNRS UMR3569, Virus and Immunity Unit
Arnaud Echard: Université de Paris, CNRS UMR3691, Membrane Traffic and Cell Division Unit
Philippe Roingeard: Université de Tours, CHRU de Tours, INSERM U1259 MAVIVH and Plateforme IBiSA de Microscopie Électronique
Hugo Mouquet: Université de Paris, INSERM U1222, Humoral Immunology Laboratory
Olivier Schwartz: Université de Paris, CNRS UMR3569, Virus and Immunity Unit
Timothée Bruel: Université de Paris, CNRS UMR3569, Virus and Immunity Unit

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Broadly neutralizing antibodies (bNAbs) targeting the HIV-1 envelope glycoprotein (Env) are promising molecules for therapeutic or prophylactic interventions. Beyond neutralization, bNAbs exert Fc-dependent functions including antibody-dependent cellular cytotoxicity and activation of the complement. Here, we show that a subset of bNAbs targeting the CD4 binding site and the V1/V2 or V3 loops inhibit viral release from infected cells. We combined immunofluorescence, scanning electron microscopy, transmission electron microscopy and immunogold staining to reveal that some bNAbs form large aggregates of virions at the surface of infected cells. This activity correlates with the capacity of bNAbs to bind to Env at the cell surface and to neutralize cell-free viral particles. We further show that antibody bivalency is required for viral retention, and that aggregated virions are neutralized. We have thus identified an additional antiviral activity of bNAbs, which block HIV-1 release by tethering viral particles at the surface of infected cells.

Date: 2022
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DOI: 10.1038/s41467-022-28307-7

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