Fackler O T, Kremmer E, Mueller-Lantzsch N
Universitätskliniken des Saarlandes, Abt. Virologie, Homburg/Saar, Germany.
Virus Res. 1996 Dec;46(1-2):105-10. doi: 10.1016/s0168-1702(96)01389-5.
HIV-Nef protein supports viral infectivity prior to proviral integration. This requires Nef to be present before the expression of viral genes and suggests its delivery as part of the virion. We report here that the Nef proteins of HIV-2-HOM and HIV-2-ROD are associated with the virion. After the separation of pelleted virus in a 20-60% sucrose density gradient, both proteins cosedimented with the virion-associated reverse transcriptase (RT) activity at a density characteristic of retroviral particles. Whereas Nef-2-ROD was present in the virion only as the full-length protein, HIV-2-HOM appeared as 32 and 35 kDa isoforms. The smaller isoform is identical in molecular weight to the protein expected from proteolytic cleavage of full-length Nef-2-HOM by the virion-based protease. Virion-association of Nef helps to explain the recently redefined biological function of this regulatory protein.
在原病毒整合之前,HIV-Nef蛋白支持病毒的感染性。这要求Nef在病毒基因表达之前就已存在,并表明它作为病毒粒子的一部分被传递。我们在此报告,HIV-2-HOM和HIV-2-ROD的Nef蛋白与病毒粒子相关。在20%-60%的蔗糖密度梯度中对沉淀的病毒进行分离后,这两种蛋白都与病毒粒子相关的逆转录酶(RT)活性一起以逆转录病毒颗粒的密度特征共同沉降。虽然Nef-2-ROD仅以全长蛋白的形式存在于病毒粒子中,但HIV-2-HOM表现为32 kDa和35 kDa的同工型。较小的同工型在分子量上与基于病毒粒子的蛋白酶对全长Nef-2-HOM进行蛋白水解切割所预期的蛋白相同。Nef与病毒粒子的关联有助于解释这种调节蛋白最近重新定义的生物学功能。