病毒血症
抗体
聚糖
生物
表位
病毒学
糖蛋白
V3环
中和抗体
病毒包膜
人类免疫缺陷病毒(HIV)
抗逆转录病毒疗法
免疫学
病毒载量
分子生物学
作者
Luis M. Molinos-Albert,Eduard Baquero,Mélanie Bouvin-Pley,Valérie Lorin,Caroline Charre,Cyril Planchais,Jordan D. Dimitrov,Valérie Monceaux,Matthijn Vos,Laurent Hocqueloux,Jean-Luc Berger,Michael S. Seaman,Martine Braibant,Véronique Avettand-Fènoël,Asier Sáez‐Cirión,Hugo Mouquet
标识
DOI:10.1016/j.chom.2023.06.006
摘要
HIV-1 broadly neutralizing antibodies (bNAbs) can decrease viremia but are usually unable to counteract autologous viruses escaping the antibody pressure. Nonetheless, bNAbs may contribute to natural HIV-1 control in individuals off antiretroviral therapy (ART). Here, we describe a bNAb B cell lineage elicited in a post-treatment controller (PTC) that exhibits broad seroneutralization and show that a representative antibody from this lineage, EPTC112, targets a quaternary epitope in the glycan-V3 loop supersite of the HIV-1 envelope glycoprotein. The cryo-EM structure of EPTC112 complexed with soluble BG505 SOSIP.664 envelope trimers revealed interactions with N301- and N156-branched N-glycans and the 324GDIR327 V3 loop motif. Although the sole contemporaneous virus circulating in this PTC was resistant to EPTC112, it was potently neutralized by autologous plasma IgG antibodies. Our findings illuminate how cross-neutralizing antibodies can alter the HIV-1 infection course in PTCs and may control viremia off-ART, supporting their role in functional HIV-1 cure strategies.
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