Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
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DOI：
10.1016/j.virol.2005.08.001
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发表时间：
2005-11-25
期刊：
影响因子：
3.7
通讯作者：
Thali, M
中科院分区：
文献类型：
--
作者：
Batonick, M;Favre, M;Thali, M
HIV-1的包膜糖蛋白（Env）在病毒复制周期的晚期与网格蛋白相关的衔接子复合物AP-2相互作用。因此，在其合成时，Env从细胞表面回收，除非内化被病毒Gag抑制。在这里，我们证明了不仅Env，而且HIV-1 Gag也特异性结合AP-2。Gag-AP-2协会被发现依赖于酪氨酸残基132和缬氨酸残基135在基质衣壳连接的Gag多蛋白。对表达显性阴性AP-2的细胞中病毒逸出的形态学分析结果表明，AP-2参与将HIV-1逸出限制在不同的微域中。此外，与从野生型细胞的释放相比，从AP-2突变细胞的颗粒释放增强，但从这些细胞释放的病毒的感染性适度降低。这些数据一起归因于AP-2复合物在调节HIV-1组装/释放中的作用。(c)2005年爱思唯尔公司All rights reserved.
The envelope glycoprotein (Env) of HIV-1 interacts with the clathrin-associated adaptor complex AP-2 during the late phase of the viral replication cycle. Upon its synthesis, Env, therefore, is retrieved from the cellular surface unless internalization is inhibited by viral Gag. Here we demonstrate that not only Env, but also HIV-1 Gag, specifically binds to AP-2. Gag-AP-2 association was found to depend on tyrosine residue 132 and valine residue 135 at the matrix-capsid junction in the Gag polyprotein. Results of a morphological analysis of viral egress from cells expressing dominant-negative AP-2 suggest an involvement of AP-2 in confining HIV-1 exit to distinct microdomains. Further, particle release from AP-2-mutant cells was enhanced compared to release from wild-type cells but the infectivity of virus released from these cells was moderately reduced. Together these data attribute a role to the AP-2 complex in the regulation of HIV-1 assembly/release. (c) 2005 Elsevier Inc. All rights reserved.