对HIV-2 Vpx的突变分析表明，多聚脯氨酸基序中的脯氨酸残基109调节SAMHD1的降解。
Mutational analysis of HIV-2 Vpx shows that proline residue 109 in the poly-proline motif regulates degradation of SAMHD1.
作者信息
Ciftci Halil Ibrahim, Fujino Haruna, Koga Ryoko, Yamamoto Minami, Kawamura Sogo, Tateishi Hiroshi, Iwatani Yasumasa, Otsuka Masami, Fujita Mikako
机构信息
Department of Bioorganic Medicinal Chemistry, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
Clinical Research Center, National Hospital Organization, Nagoya Medical Center, Nagoya, Japan.
出版信息
FEBS Lett. 2015 Jun 4;589(13):1505-14. doi: 10.1016/j.febslet.2015.04.038. Epub 2015 Apr 30.
In this study, we performed a mutational analysis to determine whether the mechanism by which HIV-2 Vpx confers the capacity for infectivity and viral replication in macrophages is solely dependent on its ability to degrade the host antiviral factor SAMHD1. Contrary to expectations, we demonstrated that P(109) in the C-terminal poly-proline motif of HIV-2 Vpx has two unique roles: to facilitate the specific degradation of SAMHD1 in macrophages, and to facilitate multimerization of Vpx, therefore preventing SAMHD1 degradation in the presence of high levels of Vpx.
在本研究中，我们进行了一项突变分析，以确定HIV-2 Vpx赋予巨噬细胞感染性和病毒复制能力的机制是否仅取决于其降解宿主抗病毒因子SAMHD1的能力。与预期相反，我们证明HIV-2 Vpx C末端多脯氨酸基序中的P(109)具有两个独特作用：促进巨噬细胞中SAMHD1的特异性降解，以及促进Vpx的多聚化，从而在高水平Vpx存在时防止SAMHD1降解。
Zotero 插件