Drift of the HIV-1 Envelope Glycoprotein gp120 toward Increased Neutralization Resistance over the Course of the Epidemic: a Comprehensive Study Using the Most Potent and Broadly Neutralizing Monoclonal Antibodies
Смещение оболочечного гликопротеина gp120 ВИЧ-1 в сторону повышения устойчивости к нейтрализации в ходе эпидемии: комплексное исследование с использованием наиболее мощных и широко нейтрализующих моноклональных антител
2014-09-18
SCID: 54.1/xvve6umc
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HIV-1 clade Bbroadly neutralizing antibodiesgp120 envelope glycoproteingp41 membrane-proximal external regionneutralization resistance
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Abstract (AI)
Extending our previous analyses to the most recently described monoclonal broadly neutralizing antibodies (bNAbs), we confirmed a drift of HIV-1 clade B variants over 2 decades toward higher resistance to bNAbs targeting almost all the identified gp120-neutralizing epitopes. In contrast, the sensitivity to bNAbs targeting the gp41 membrane-proximal external region remained stable, suggesting a selective pressure on gp120 preferentially. Despite this evolution, selected combinations of bNAbs remain capable of neutralizing efficiently most of the circulating variants.
Key Findings
1
Despite increased resistance, selected combinations of broadly neutralizing antibodies efficiently neutralized most circulating HIV-1 variants.
2
HIV-1 clade B variants became increasingly resistant to broadly neutralizing antibodies over two decades of the epidemic.
3
Sensitivity to antibodies targeting the gp41 membrane-proximal external region remained stable, indicating preferential selective pressure on gp120.
4
The resistance drift affected antibodies targeting nearly all identified neutralizing epitopes on the gp120 envelope glycoprotein.
Research Object
HIV-1 clade B variants and their envelope glycoprotein gp120 over the course of the epidemic
Research Subject
Temporal evolution of neutralization resistance to broadly neutralizing monoclonal antibodies, including differential changes between gp120- and gp41-targeting epitopes and the efficacy of antibody combinations
Publication Details
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2014-09-18
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