A triple-arginine motif in the amino-terminal domain and oligomerization are required for HIV-1 inhibition by human MX2.
A triple-arginine motif in the amino-terminal domain and oligomerization are required for HIV-1 inhibition by human MX2.
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DOI：
10.1128/jvi.00169-15
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发表时间：
2015-04
影响因子：
5.4
通讯作者：
Malim MH
中科院分区：
文献类型：
--
作者：
Goujon C;Greenbury RA;Papaioannou S;Doyle T;Malim MH
我们采用分子遗传学方法来了解HIV-1耐药因子黏液病毒耐药2 （MX2）的结构域组织。首先，我们描述了一个重要的三精氨酸基序在氨基末端区域。其次，我们证明了这个91-残基结构域在附加到异源蛋白上时介导抗病毒活性，并且我们提供了遗传证据，证明蛋白质寡聚化是MX2功能所必需的。这些见解将有助于未来旨在阐明MX2作用机制的工作。
We have employed molecular genetic approaches to understand the domain organization of the HIV-1 resistance factor myxovirus resistance 2 (MX2). First, we describe an essential triple-arginine motif in the amino-terminal domain. Second, we demonstrate that this 91-residue domain mediates antiviral activity when appended to heterologous proteins, and we provide genetic evidence that protein oligomerization is required for MX2 function. These insights will facilitate future work aiming to elucidate MX2's mechanism of action.