Paulus C, Hellebrand S, Tessmer U, Wolf H, Kräusslich H G, Wagner R
Institut für Medizinische Mikrobiologie und Hygiene, Universität Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany.
J Biol Chem. 1999 Jul 30;274(31):21539-43. doi: 10.1074/jbc.274.31.21539.
The human immunodeficiency virus type-1 (HIV-1) transframe protein p6* is located between the structural and enzymatic domains of the Gag-Pol polyprotein, flanked by the nucleocapsid (NC) and the protease (PR) domain at its amino and carboxyl termini, respectively. Here, we report that recombinant highly purified HIV-1 p6* specifically inhibits mature HIV-1 PR activity. Kinetic analyses and cross-linking experiments revealed a competitive mechanism for PR inhibition by p6*. We further demonstrate that the four carboxyl-terminal residues of p6* are essential but not sufficient for p6*-mediated inhibition of PR activity. Based on these results, we suggest a role of the transframe protein p6* in regulating HIV-1 PR activity during viral replication.
人类免疫缺陷病毒1型（HIV-1）的移码蛋白p6位于Gag-Pol多聚蛋白的结构域和酶结构域之间，其氨基端和羧基端分别由核衣壳（NC）结构域和蛋白酶（PR）结构域侧翼包围。在此，我们报告重组的高度纯化HIV-1 p6可特异性抑制成熟HIV-1 PR的活性。动力学分析和交联实验揭示了p6抑制PR的竞争机制。我们进一步证明，p6的四个羧基端残基对于p6介导的PR活性抑制是必不可少的，但并不充分。基于这些结果，我们认为移码蛋白p6在病毒复制过程中对HIV-1 PR活性具有调节作用。
