Schwartz O, Maréchal V, Friguet B, Arenzana-Seisdedos F, Heard J M
Laboratoire Rétrovirus et Transfert Génétique, URA CNRS 1157, Institut Pasteur, Paris, France.
J Virol. 1998 May;72(5):3845-50. doi: 10.1128/JVI.72.5.3845-3850.1998.
Following cell surface receptor binding and membrane fusion, human immunodeficiency virus (HIV) virion cores are released in the cytoplasm. Incoming viral proteins represent potential targets for cytosolic proteases. We show that treatment of target cells with the proteasome inhibitors MG132 and lactacystin increased the efficiency of HIV infection. Proteasome inhibitors were active at the early steps of the viral cycle. Incoming p24Gag proteins accumulated in the cytosol, and larger amounts of proviral DNA were synthesized. In vitro, purified 20S proteasome degraded HIV virion components. Thus, degradation of incoming viral proteins by the proteasome represents an early intracellular defense against infection.
在细胞表面受体结合和膜融合之后，人类免疫缺陷病毒（HIV）病毒粒子核心被释放到细胞质中。进入细胞的病毒蛋白是胞质蛋白酶的潜在作用靶点。我们发现，用蛋白酶体抑制剂MG132和乳胞素处理靶细胞可提高HIV感染效率。蛋白酶体抑制剂在病毒周期的早期阶段具有活性。进入细胞的p24Gag蛋白在细胞质中积累，并且合成了大量的前病毒DNA。在体外，纯化的20S蛋白酶体可降解HIV病毒粒子成分。因此，蛋白酶体对进入细胞的病毒蛋白的降解代表了细胞内对感染的早期防御。
