Department of Oncology, University of Torino, Candiolo, Italy.
FEBS Lett. 2013 Sep 17;587(18):2943-51. doi: 10.1016/j.febslet.2013.07.039. Epub 2013 Jul 31.
Preventing cell entry of human immunodeficiency virus 1 (HIV-1) is of interest for the development of innovative therapies. We previously reported a specific interaction between HIV-1 envelope glycoprotein 120 (gp120) and Tat at the cell surface, which enhances virus attachment and entry. We also identified a gp120-mimicking peptide, CT319, that competes with gp120 for Tat binding, thus inhibiting HIV-1 infection. Here we report a molecular dissection of gp120 regions involved in this mechanism. Our findings identify the V1/V2 loop of gp120 as involved in Tat binding, and define this interaction as functionally relevant for HIV-1 entry into host cells.
预防人类免疫缺陷病毒 1（HIV-1）进入细胞对于开发创新疗法具有重要意义。我们之前曾报道过 HIV-1 包膜糖蛋白 120（gp120）与细胞表面 Tat 之间的特异性相互作用，这种相互作用增强了病毒的附着和进入。我们还鉴定出一种 gp120 模拟肽 CT319，它与 Tat 竞争结合 gp120，从而抑制 HIV-1 感染。在这里，我们报告了对参与该机制的 gp120 区域进行分子剖析的结果。我们的发现确定了 gp120 的 V1/V2 环参与 Tat 结合，并将这种相互作用定义为 HIV-1 进入宿主细胞的功能相关。
