Small amino acid sequence changes within the V2 domain can affect the function of a T-cell line-tropic human immunodeficiency virus type 1 envelope gp120.
Small amino acid sequence changes within the V2 domain can affect the function of a T-cell line-tropic human immunodeficiency virus type 1 envelope gp120.
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V2 结构域内的微小氨基酸序列变化可影响 T 细胞系嗜性人类免疫缺陷病毒 1 型包膜 gp120 的功能。
DOI：
10.1006/viro.1995.1010
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Cheng-Mayer,C
中科院分区：
文献类型：
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作者：
Koito,A;Stamatatos,L;Cheng-Mayer,C
先前对体外构建的重组病毒的研究表明，囊膜gp120的V2结构域除了所需的V3结构域外，还可以提高HIV-1感染原代巨噬细胞的效率。目前利用三种针对V3环的人单抗对这些重组病毒的gp120进行的结构研究表明，V2结构域通过调节V3环的构象来影响细胞嗜性。对T细胞系嗜性病毒HIV-1SF2的V2结构域的进一步突变分析表明，单个氨基酸序列的变化，主要是那些影响潜在N-连接糖基化位点位置和该区域的正电荷的改变，也可以改变嗜性。然而，V2结构域中的这些氨基酸取代似乎并不改变V3环的构象。因此，gp120的V2结构域可以通过对V3的影响以及通过V3非依赖的机制来影响细胞的趋向性。
Prior studies with recombinant viruses constructed in vitro showed that the V2 domain of envelope gp120, in addition to the required V3 domain, enhances the efficiency of infection of primary macrophages by HIV-1. Present structural studies on the gp120s of these recombinant viruses using three human monoclonal antibodies directed to the V3 loop indicate that the V2 domain affects cell tropism by modulating the conformation of the V3 loop. Additional mutational analyses of the V2 domain of the T-cell line-tropic virus HIV-1SF2reveal that single amino acid sequence changes, mainly those affecting the location of potential N-linked glycosylation sites and the positive charge of this region, can also alter tropism. These amino acid substitutions in the V2 domain, however, do not appear to alter the conformation of the V3 loop. Thus, the V2 domain of gp120 can influence cell tropism through both an effect on V3 as well as via a V3-independent mechanism.