Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel
Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel
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DOI：
10.1016/s1097-2765(04)00183-2
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发表时间：
2004-04-23
期刊：
影响因子：
16
通讯作者：
Marbán, E
中科院分区：
文献类型：
--
作者：
Hsu, K;Seharaseyon, J;Marbán, E
序列分析预测HIV-1辅助蛋白Vpu和哺乳动物背景K+通道的ASK-1的N-末端区域之间具有显着的结构同源性。如果同源性是由于HIV-1进化过程中的分子盗版，这两种蛋白可能具有重要的功能相互作用。在这里，我们表明，在培养的细胞和艾滋病淋巴组织中的ASK和Vpu物理相互作用。功能的后果是潜在的破坏性的两个组成部分：Vpu取消了任务-1电流，而过量表达的任务导致了一个显着的损害Vpu的能力，以提高病毒颗粒的释放。此外，Task-I的前40个氨基酸（与Vpu同源的部分）能够增强HIV-1颗粒释放。这种病毒-宿主相互作用可能影响HIV-1/AIDS的进展，以及感染宿主组织中的电信号。
Sequence analysis predicted significant structural homology between the HIV-1 accessory protein Vpu and the N-terminal region of TASK-1, a mammalian background K+ channel. If the homology resulted from molecular piracy during HIV-1 evolution, these two proteins may have important functional interactions. Here we demonstrate that TASK and Vpu physically interact in cultured cells and in AIDS lymphoid tissues. The functional consequences were potentially destructive for both components: Vpu abolished TASK-1 current, while overexpressing TASK led to a marked impairment of Vpu's ability to enhance viral particle release. Further, the first 40 amino acids of TASK-1 (part of the homology to Vpu) were capable of enhancing HIV-1 particle release. This virus-host interaction may influence HIV-1/AIDS progression, as well as electrical signaling in infected host tissues.