Functional analysis of cellular membrane proteins for generation of viral envelope and transmission

我们进行了一系列的病毒学研究的细胞膜蛋白的产生HIV-1包膜和HIV-1颗粒的释放。从对抑制HIV-1颗粒从感染细胞释放的人BST 2的功能检查中发现，BST 2直接作用于HIV-1，因为人BST 2具有抑制HIV-1从多种细胞中释放的能力。其次，我们发现了HIV-1病毒蛋白U（VPU），一种人BST 2的特异性拮抗剂，人BST 2的跨膜（TM）结构域中的三个氨基酸（AA）残基（I34，L37和L41）对于与VPU的相互作用以及VPU介导的人BST 2的拮抗作用是至关重要的。此外，计算机辅助结构建模表明，这四个AA残基（I34，L37，L41和T45）在TM结构域的同一螺旋面上的对齐对于VPU介导的人BST 2的拮抗作用至关重要。这些结果有助于从分子水平了解HIV-1 VPU对人BST 2的特异性拮抗作用。另一方面，我们无法重复显示TIP 47对HIV-1 ENV掺入病毒颗粒的贡献。

We performed a series of virological investigation of cellular membrane proteins on generation of HIV-1 envelope and release of HIV-1 particles. From functional examination of human BST2 that inhibits the release of HIV-1 particles from infected cells on release of viral particles, it was suggested that BST2 acts directly to HIV-1 because human BST2 has ability to inhibit HIV-1 from variety species of cells. Next, we found HIV-1 viral protein U(VPU), a specific antagonist of human BST2, that three amino acid(AA) residues(I34, L37, and L41) in the transmembrane(TM) domain of human BST2 are critical for the interaction with VPUand VPU-mediated antagonism of human BST2. Moreover, computer-assisted structural modeling suggests that an alignment of these four AA residues(I34, L37, L41, and T45) on the same helical face in the TM domain is crucial for the VPU-mediated antagonism of human BST2. These results contribute to the molecular understanding of human BST2 specific antagonism by HIV-1 VPU. On the other hand, we are unable to repeat to show contribution of TIP47 on incorporation of HIV-1 ENV in the viral particles.