African swine fever virus pS273R antagonizes stress granule formation by cleaving the nucleating protein G3BP1 to facilitate viral replication

文献类型： 外文期刊

第一作者： Li, Tingting

作者： Li, Tingting;Li, Xuewen;Wang, Xiao;Chen, Xin;Zhao, Gaihong;Liu, Chuanxia;Bao, Miaofei;Song, Jie;Li, Jiangnan;Huang, Li;Cai, Xuehui;Bu, Zhigao;Zheng, Jun;Weng, Changjiang;Li, Tingting;Li, Xuewen;Wang, Xiao;Chen, Xin;Zhao, Gaihong;Liu, Chuanxia;Bao, Miaofei;Song, Jie;Li, Jiangnan;Huang, Li;Zheng, Jun;Weng, Changjiang;Li, Xuewen;Rong, Jun;Tian, Kegong;Deng, Junhua;Zhu, Jianzhong

作者机构：

期刊名称：JOURNAL OF BIOLOGICAL CHEMISTRY （ 影响因子：4.8； 五年影响因子：4.8 ）

ISSN：

年卷期： 2023 年 299 卷 7 期

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收录情况： SCI

摘要： Cytoplasmic stress granules (SGs) are generally triggered by stress-induced translation arrest for storing mRNAs. Recently, it has been shown that SGs are regulated by different stimulators including viral infection, which is involved in the antiviral activity of host cells to limit viral propagation. To survive, several viruses have been reported to execute various strategies, such as modulating SG formation, to create optimal surroundings for viral replication. African swine fever virus (ASFV) is one of the most notorious pathogens in the global pig industry. However, the interplay between ASFV infection and SG formation remains largely unknown. In this study, we found that ASFV infection inhibited SG formation. Through SG inhibitory screening, we found that several ASFV-encoded proteins are involved in inhibition of SG formation. Among them, an ASFV S273R protein (pS273R), the only cysteine protease encoded by the ASFV genome, significantly affected SG formation. ASFV pS273R interacted with G3BP1 (RasGTPase-activating protein [SH3 domain] binding protein 1), a vital nucleating protein of SG formation. Furthermore, we found that ASFV pS273R cleaved G3BP1 at the G140-F141 to produce two fragments (G3BP1-N1-140 and G3BP1-C141-456). Interestingly, both the pS273R-cleaved fragments of G3BP1 lost the ability to induce SG formation and antiviral activity. Taken together, our finding reveals that the proteolytic cleavage of G3BP1 by ASFV pS273R is a novel mechanism by which ASFV counteracts host stress and innate antiviral responses.

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