Koito A, Harrowe G, Levy J A, Cheng-Mayer C
Department of Medicine, University of California, San Francisco 94143-0128.
J Virol. 1994 Apr;68(4):2253-9. doi: 10.1128/JVI.68.4.2253-2259.1994.
We have examined the influence of the V1/V2 region of the human immunodeficiency virus type 1 (HIV-1) gp120 on certain biologic properties of the virus. We observed that on the genomic background of the T-cell-line-tropic strain, HIV-1SF2mc, both the V1 and V2 domains of the macrophage-tropic strain, HIV-1SF162mc, in addition to the required V3 domain, are necessary to attain full macrophage tropism. Furthermore, the V2 domain modulates the sensitivity of HIV-1 to soluble CD4 neutralization. Structural studies of recombinant and mutant envelope glycoproteins suggest that the function of the V1/V2 region is to interact with the V3 domain and confer on the envelope gp120 of HIV-1SF2mc a conformation more similar to that of the macrophage-tropic strain HIV-1SF162mc. The conformation of the envelope gp120 appears to be strain specific and plays an important role in determining HIV-1 tissue tropism and sensitivity to soluble CD4 neutralization.
我们研究了人类免疫缺陷病毒1型(HIV-1)gp120的V1/V2区域对该病毒某些生物学特性的影响。我们观察到,在T细胞系嗜性毒株HIV-1SF2mc的基因组背景下,除了所需的V3结构域外,巨噬细胞嗜性毒株HIV-1SF162mc的V1和V2结构域对于实现完全的巨噬细胞嗜性也是必需的。此外,V2结构域可调节HIV-1对可溶性CD4中和作用的敏感性。重组和突变包膜糖蛋白的结构研究表明,V1/V2区域的功能是与V3结构域相互作用,并使HIV-1SF2mc的包膜gp120具有与巨噬细胞嗜性毒株HIV-1SF162mc更相似的构象。包膜gp120的构象似乎具有毒株特异性,并且在决定HIV-1组织嗜性和对可溶性CD4中和作用的敏感性方面起着重要作用。