Zhou Jing, Huang Li, Hachey David L, Chen Chin Ho, Aiken Christopher
Department of Microbiology and Immunology and Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
J Biol Chem. 2005 Dec 23;280(51):42149-55. doi: 10.1074/jbc.M508951200. Epub 2005 Oct 25.
The small molecule 3-O-(3',3'-dimethylsuccinyl)-betulinic acid (DSB) potently inhibits human immunodeficiency virus, type 1 (HIV-1) replication by interfering with proteolytic cleavage of the viral Gag protein at a specific site. Here we have demonstrated that the antiviral mechanism involves the association of DSB with Gag at a 1:1 stoichiometry within immature HIV-1 particles. The binding was specific, as mutations in Gag that confer resistance to DSB inhibited the association, which could be competed by DSB but not by the inactive compound betulinic acid. The addition of DSB to purified immature viral cores inhibited the cleavage of Gag at the CA-SP1 junction in vitro, thus reproducing the effect of the drug when present during maturation of HIV-1 particles. Based on these findings, we propose a model in which a trimer of DSB associates with the CA-SP1 junction of adjacent subunits within the Gag polymer. The model may explain the ability of highly similar compounds to specifically target the seemingly unrelated steps of HIV-1 maturation and virus entry.
小分子3 - O -(3',3'-二甲基琥珀酰基)-桦木酸(DSB)通过干扰病毒Gag蛋白在特定位点的蛋白水解切割,有效抑制1型人类免疫缺陷病毒(HIV - 1)的复制。在此,我们证明了抗病毒机制涉及DSB在未成熟HIV - 1颗粒内以1:1化学计量比与Gag结合。这种结合具有特异性,因为赋予对DSB抗性的Gag突变抑制了这种结合,且这种结合可被DSB竞争,但不能被无活性的化合物桦木酸竞争。将DSB添加到纯化的未成熟病毒核心中,在体外抑制了Gag在CA - SP1连接处的切割,从而重现了该药物在HIV - 1颗粒成熟过程中存在时的作用效果。基于这些发现,我们提出了一个模型,其中DSB三聚体与Gag聚合物内相邻亚基的CA - SP1连接处结合。该模型可能解释了高度相似的化合物特异性靶向HIV - 1成熟和病毒进入这两个看似不相关步骤的能力。