Specific sequences commonly found in the V3 domain of HIV-1 subtype C isolates affect the overall conformation of native Env and induce a neutralization-resistant phenotype independent of V1/V2 masking.
Specific sequences commonly found in the V3 domain of HIV-1 subtype C isolates affect the overall conformation of native Env and induce a neutralization-resistant phenotype independent of V1/V2 masking.
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HIV-1 C 亚型分离株的 V3 结构域中常见的特定序列影响天然 Env 的整体构象，并诱导独立于 V1/V2 掩蔽的中和抗性表型。
DOI：
10.1016/j.virol.2013.10.007
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发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Pinter,Abraham
中科院分区：
文献类型：
--
作者：
Salomon,Aidy;Krachmarov,Chavdar;Lai,Zhong;Honnen,William;Zingman,BarryS;Sarlo,Julie;Gorny,MiroslawK;Zolla-Pazner,Susan;Robinson,JamesE;Pinter,Abraham
Primary HIV-1 isolates are relatively resistant to neutralization by antibodies commonly induced after infection or vaccination. This is generally attributed to masking of sensitive epitopes by the V1/V2 domain and/or glycans situated at various positions in Env. Here we identified a novel masking effect mediated by subtype C-specific V3 sequences that contributes to the V1/V2-independent and glycan-independent neutralization resistance of chimeric and primary Envs to antibodies directed against multiple neutralization domains. Positions at several conserved charged and hydrophobic sites in the V3 crown and stem were also shown to affect neutralization phenotype. These results indicated that substitutions typically present in subtype C and related V3 sequences influence the overall conformation of native Env in a way that occludes multiple neutralization targets located both within and outside of the V3 domain, and may reflect an alternative mechanism for neutralization resistance that is particularly active in subtype C and related isolates.
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