Rhesus monkey TRIM5 alpha protein SPRY domain contributes to AP-1 activation

文献类型： 外文期刊

第一作者： Na, Lei

作者： Na, Lei;Tang, Yan-Dong;Wang, Cuihui;Liu, Cong;Wang, Xiaojun

作者机构：

期刊名称：JOURNAL OF BIOLOGICAL CHEMISTRY （ 影响因子：5.157； 五年影响因子：5.041 ）

ISSN： 0021-9258

年卷期： 2018 年 293 卷 8 期

页码：

收录情况： SCI

摘要： TRIM5 alpha is an important host restriction factor that could potently block retrovirus infection. The SPRY domain of TRIM5 alpha mediates post-entry restriction by recognition of and binding to the retroviral capsid. Human TRIM5 alpha also functions as an innate immune sensor to activate AP-1 and NF-kappa B signaling, which subsequently restrict virus replication. Previous studies have shown that the AP-1 and NF-kappa B signaling activation relies on the RING motif of TRIM5 alpha. In this study, we have demonstrated that the SPRY domain is essential for rhesus macaque TRIM5 alpha to activate AP-1 but not NF-kappa B signaling. The AP-1 activation mainly depends on all of the beta-sheet barrel on SPRY structure of TRIM5 alpha. Furthermore, the SPRY-mediated auto-ubiquitination of TRIM5 alpha is required for AP-1 activation. This study reports that rhesus macaque TRIM5 alpha mainly undergoes Lys27-linked and Met1-linked auto-polyubiquitination. Finally, we found that the TRIM5 alpha signaling function was positively correlated with its retroviral restriction activity. This study discovered an important role of the SPRY domain in immune signaling and antiviral activity and further expanded our knowledge of the antiviral mechanism of TRIM5 alpha.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序