Broadly neutralizing anti-HIV-1 antibodies tether viral particles at the surface of infected cells.
Broadly neutralizing anti-HIV-1 antibodies tether viral particles at the surface of infected cells.
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DOI：
10.1038/s41467-022-28307-7
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发表时间：
2022-02-02
影响因子：
16.6
通讯作者：
Bruel T
中科院分区：
文献类型：
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作者：
Dufloo J;Planchais C;Frémont S;Lorin V;Guivel-Benhassine F;Stefic K;Casartelli N;Echard A;Roingeard P;Mouquet H;Schwartz O;Bruel T
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. Broadly neutralizing antibodies (bNAbs) neutralize HIV-1 and exert Fc-dependent activities against infected cells. Here, Dufloo et al. show that bNAbs also block HIV-1 release by trapping viral particles at the surface of infected cells.
