Akari H, Arold S, Fukumori T, Okazaki T, Strebel K, Adachi A
Department of Virology, The University of Tokushima School of Medicine, Tokushima, Tokushima 770-8503, Japan.
J Virol. 2000 Mar;74(6):2907-12. doi: 10.1128/jvi.74.6.2907-2912.2000.
The N-terminal alpha-helix domain of the human immunodeficiency virus type 1 (HIV-1) Nef protein plays important roles in enhancement of viral infectivity, virion incorporation of Nef, and the down-regulation of major histocompatibility complex class I (MHC-I) expression on cell surfaces. In this study, we demonstrated that Met 20 in the alpha-helix domain was indispensable for the ability of Nef to modulate MHC-I expression but not for other events. We also showed that Met 20 was unnecessary for the down-regulation of CD4. These findings indicate that the region governing MHC-I down-regulation is proximate in the alpha-helix domain but is dissociated functionally from that determining enhancement of viral infectivity, virion incorporation of Nef, and CD4 down-regulation.
人类免疫缺陷病毒1型(HIV-1)Nef蛋白的N端α-螺旋结构域在增强病毒感染性、Nef蛋白掺入病毒颗粒以及下调细胞表面主要组织相容性复合体I类(MHC-I)表达方面发挥着重要作用。在本研究中,我们证明α-螺旋结构域中的Met 20对于Nef调节MHC-I表达的能力不可或缺,但对其他事件并非如此。我们还表明,Met 20对于CD4的下调并非必需。这些发现表明,在α-螺旋结构域中,调控MHC-I下调的区域与之相邻,但在功能上与决定增强病毒感染性、Nef蛋白掺入病毒颗粒以及CD4下调的区域相分离。