Cheng Weijia, Chen Shiyou, Li Ruiling, Chen Yu, Wang Min, Guo Deyin
School of Basic Medical Sciences, Wuhan University, Wuhan, 430072, China.
Virol Sin. 2015 Apr;30(2):153-61. doi: 10.1007/s12250-015-3581-8. Epub 2015 Apr 17.
Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes eight accessory proteins, the functions of which are not yet fully understood. SARS-CoV protein 6 (P6) is one of the previously studied accessory proteins that have been documented to enhance viral replication and suppress host interferon (IFN) signaling pathways. Through yeast two-hybrid screening, we identified eight potential cellular P6-interacting proteins from a human spleen cDNA library. For further investigation, we targeted the IFN signaling pathway-mediating protein, N-Myc (and STAT) interactor (Nmi). Its interaction with P6 was confirmed within cells. The results showed that P6 can promote the ubiquitin-dependent proteosomal degradation of Nmi. This study revealed a new mechanism of SARS-CoV P6 in limiting the IFN signaling to promote SARS-CoV survival in host cells.
严重急性呼吸综合征冠状病毒（SARS-CoV）编码8种辅助蛋白，其功能尚未完全明确。SARS-CoV蛋白6（P6）是之前研究过的辅助蛋白之一，已证明它能增强病毒复制并抑制宿主干扰素（IFN）信号通路。通过酵母双杂交筛选，我们从人脾脏cDNA文库中鉴定出8种潜在的与P6相互作用的细胞蛋白。为进一步研究，我们将目标锁定在IFN信号通路介导蛋白，即N-Myc（和STAT）相互作用分子（Nmi）。其与P6在细胞内的相互作用得到了证实。结果表明，P6可促进Nmi依赖泛素的蛋白酶体降解。本研究揭示了SARS-CoV P6在限制IFN信号以促进SARS-CoV在宿主细胞中存活方面的新机制。
