Cosson P
Basel Institute for Immunology, Switzerland.
EMBO J. 1996 Nov 1;15(21):5783-8.
The incorporation of the envelope (env) glycoprotein of the human immunodeficiency virus type 1 (HIV-1) into budding virions has been proposed to be mediated by an interaction between its cytoplasmic domain and the matrix protein of HIV-1. However, this interaction was never directly demonstrated and its role in the biogenesis of HIV-1 virions is still debated. Here, a direct interaction is reported between the matrix protein of HIV-1 and the cytoplasmic domain of the env protein of HIV-1. No interaction was seen with the env cytoplasmic domain of other retroviruses. The region of the HIV-1 env involved in the interaction was delineated by mutagenesis and is comprised of the C-terminal 67 amino acid residues of env. These results, as well as the analysis of mutants of the matrix protein, suggest that the interaction between the HIV-1 env and matrix proteins accounts for the specific incorporation of the env glycoprotein into HIV-1 virions.
有人提出，人类免疫缺陷病毒1型（HIV-1）包膜（env）糖蛋白纳入出芽病毒粒子的过程是由其胞质结构域与HIV-1基质蛋白之间的相互作用介导的。然而，这种相互作用从未得到直接证实，其在HIV-1病毒粒子生物发生中的作用仍存在争议。在此，报告了HIV-1基质蛋白与HIV-1 env蛋白胞质结构域之间的直接相互作用。未观察到与其他逆转录病毒的env胞质结构域有相互作用。通过诱变确定了参与该相互作用的HIV-1 env区域，该区域由env的C末端67个氨基酸残基组成。这些结果以及对基质蛋白突变体的分析表明，HIV-1 env与基质蛋白之间的相互作用解释了env糖蛋白特异性纳入HIV-1病毒粒子的现象。
