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Structural modulations of the envelope gp120 glycoprotein of human immunodeficiency virus type 1 upon oligomerization and differential V3 loop epitope exposure of isolates displaying distinct tropism upon virion-soluble receptor binding.

We investigated the binding of conformation-dependent anti-V2, anti-V3, and anti-CD4-binding site monoclonal antibodies to monomeric and virion-associated gp120 from human immunodeficiency virus type 1 isolates displaying marked differences in cell tropism. For all viruses examined, we found that th...

詳細記述

保存先:
書誌詳細
出版年:J Virol
主要な著者: Stamatatos, L, Cheng-Mayer, C
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Microbiology (ASM) 1995
主題:
オンライン・アクセス:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC189516/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7545244/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.69.10.6191-6198.1995
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