The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
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DOI：
10.1016/j.virol.2008.04.017
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发表时间：
2008-07-20
期刊：
影响因子：
3.7
通讯作者：
D'Aquila, Richard T.
中科院分区：
文献类型：
--
作者：
Donahue, John P.;Vetter, Michael L.;D'Aquila, Richard T.
HIV-1病毒粒子感染因子（Vif）在病毒复制过程中是必需的，以抑制宿主细胞抗病毒因子APOBEC 3G（A3 G）。Vif结合A3 G和Cullin 5-ElonginBC E3泛素连接酶复合物，其导致A3 G的蛋白酶体降解。Vif PPLP基序（氨基酸161-164）对于正常Vif功能是必需的，因为该基序中的突变降低了T细胞中产生的病毒粒子的感染性。在这份报告中，我们证明了Vif PPLP基序的突变降低了Vif与A3 G的结合，而不影响其与ElonginC和Cullin 5的相互作用。我们证明了Vif突变体结合A3 G的失败导致A3 G掺入装配病毒体中，丧失病毒感染性。(c)2008年爱思唯尔公司All rights reserved.
The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acids 161-164) is essential for normal Vif function because mutations in this motif reduce the infectivity of virions produced in T-cells. In this report, we demonstrate that mutation of the Vif PPLP motif reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5. We demonstrate that the failure of the Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity. (c) 2008 Elsevier Inc. All rights reserved.