由包膜V3环内的单个氨基酸决定的趋化因子受体作为1型人类免疫缺陷病毒共受体的选择性应用。
Selective employment of chemokine receptors as human immunodeficiency virus type 1 coreceptors determined by individual amino acids within the envelope V3 loop.
作者信息
Speck R F, Wehrly K, Platt E J, Atchison R E, Charo I F, Kabat D, Chesebro B, Goldsmith M A
机构信息
Gladstone Institute of Virology and Immunology, San Francisco, California, USA.
出版信息
J Virol. 1997 Sep;71(9):7136-9. doi: 10.1128/JVI.71.9.7136-7139.1997.
Abstract
The chemokine receptor CCR5 acts as an essential cofactor for cell entry by macrophage-tropic human immunodeficiency virus type 1 (HIV-1) strains, whereas CXCR4 acts as an essential cofactor for T-cell-line-adapted strains. We demonstrated that the specific amino acids in the V3 loop of the HIV-1 envelope protein that determine cellular tropism also regulate chemokine coreceptor preference for cell entry by the virus. Further, a strong correlation was found between HIV-1 strains classified as syncytium inducing in standard assays and those using CXCR4 as a coreceptor. These data support the hypothesis that progressive adaptation to additional coreceptors is a key molecular basis for HIV-1 phenotypic evolution in vivo.
摘要
趋化因子受体CCR5是嗜巨噬细胞性1型人类免疫缺陷病毒（HIV-1）毒株进入细胞所必需的辅助因子，而CXCR4则是T细胞系适应性毒株进入细胞所必需的辅助因子。我们证明，HIV-1包膜蛋白V3环中决定细胞嗜性的特定氨基酸也调节病毒进入细胞时对趋化因子共受体的偏好。此外，在标准检测中被分类为合胞体诱导型的HIV-1毒株与那些使用CXCR4作为共受体的毒株之间发现了很强的相关性。这些数据支持了这样一种假说，即对额外共受体的逐步适应是HIV-1在体内表型进化的关键分子基础。
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