Lentiviral Vif Degrades the APOBEC3Z3/APOBEC3H Protein of Its Mammalian Host and Is Capable of Cross-Species Activity
Lentiviral Vif Degrades the APOBEC3Z3/APOBEC3H Protein of Its Mammalian Host and Is Capable of Cross-Species Activity
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DOI：
10.1128/jvi.00685-10
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发表时间：
2010-08-15
影响因子：
5.4
通讯作者：
Harris, Reuben S.
中科院分区：
文献类型：
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作者：
LaRue, Rebecca S.;Lengyel, Joy;Harris, Reuben S.
除马传染性贫血病毒（EIAV）外，所有慢病毒都使用小辅蛋白Vif来抵消宿主物种相关APOBEC3 （A3）蛋白的限制性活性。先前的研究表明，Vif-A3相互作用是物种特异性的。在这里，使用来自五种不同哺乳动物的APOBEC3H （Z3）型蛋白，我们报告了这种情况通常不是这样的：一些慢病毒Vif蛋白能够触发其正常宿主物种和其他几种哺乳动物的a3z3型蛋白的降解。例如，SIVmac Vif可以介导人、猕猴和牛的a3z3型蛋白的降解，但不能介导羊或猫的a3z3型蛋白的降解。maedii -visna病毒（MVV） Vif同样是混杂的，不仅降解羊的A3Z3，还降解人、猕猴、牛和猫的A3Z3型蛋白。与这些Vif蛋白的中和能力相反，人类免疫缺陷病毒（HIV）、牛免疫缺陷病毒（BIV）和猫免疫缺陷病毒（FIV） Vif似乎对其宿主的a3z3型蛋白具有特异性。我们得出结论，首先，Vif-A3Z3相互作用可能是混杂的，其次，尽管有这种倾向，每个慢病毒Vif蛋白都被优化以降解其哺乳动物宿主的A3Z3蛋白。因此，我们的结果表明，Vif-A3Z3相互作用与慢病毒生物学有关。
All lentiviruses except equine infectious anemia virus (EIAV) use the small accessory protein Vif to counteract the restriction activity of the relevant APOBEC3 (A3) proteins of their host species. Prior studies have suggested that the Vif-A3 interaction is species specific. Here, using the APOBEC3H (Z3)-type proteins from five distinct mammals, we report that this is generally not the case: some lentiviral Vif proteins are capable of triggering the degradation of both the A3Z3-type protein of their normal host species and those of several other mammals. For instance, SIVmac Vif can mediate the degradation of the human, macaque, and cow A3Z3-type proteins but not of the sheep or cat A3Z3-type proteins. Maedi-visna virus (MVV) Vif is similarly promiscuous, degrading not only sheep A3Z3 but also the A3Z3-type proteins of humans, macaques, cows, and cats. In contrast to the neutralization capacity of these Vif proteins, human immunodeficiency virus (HIV), bovine immunodeficiency virus (BIV), and feline immunodeficiency virus (FIV) Vif appear specific to the A3Z3-type protein of their hosts. We conclude, first, that the Vif-A3Z3 interaction can be promiscuous and, second, despite this tendency, that each lentiviral Vif protein is optimized to degrade the A3Z3 protein of its mammalian host. Our results thereby suggest that the Vif-A3Z3 interaction is relevant to lentivirus biology.