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Coronavirus S protein alters dsRNA accumulation and stress granule formation through regulation of ADAR1-p150 expression

文献类型： 外文期刊

作者： Fan, Baochao 1 ; Li, Yupeng 1 ; Wang, Yi 1 ; Yang, Shanshan 1 ; Peng, Qi 1 ; Qian, Jiali 1 ; Wang, Chuanhong 1 ; Zhang, Xue 1 ; Xu, Hong 1 ; Liu, Shiyu 1 ; He, Wenlong 1 ; Zhang, Gege 1 ; Zhu, Xuejiao 1 ; Li, Yunchuan 1 ; Zhao, Yongxiang 1 ; Hu, Mi 1 ; Wang, Wei 1 ; Zhou, Jinzhu 1 ; Guo, Rongli 1 ; He, Kongwang 1 ; Li, Bin 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Vet Med, Key Lab Vet Biol Engn & Technol, Minist Agr, 50 Zhongling St, Nanjing 210014, Peoples R China

2.Minist Sci & Technol, State Key Lab Cultivat Base, Jiangsu Key Lab Food Qual & Safety, 50 Zhongling St, Nanjing 210014, Peoples R China

3.Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, 88 South Daxue Rd, Yangzhou 225009, Peoples R China

4.Nanjing Agr Univ, Coll Vet Med, 1 Weigang,Xiaolingwei St, Nanjing 210095, Peoples R China

5.Jiangsu Univ, Sch Life Sci, 301 Xuefu Rd,Xiangshan St, Zhenjiang 212013, Peoples R China

6.GuoTai Taizhou Ctr Technol Innovat Vet Biol, 28 Xinglin Rd, Taizhou 225300, Peoples R China

7.Jiangsu Univ, Sch Food & Biol Engn, 301 Xuefu Rd,Xiangshan St, Zhenjiang 212013, Peoples R China

期刊名称：NUCLEIC ACIDS RESEARCH （ 影响因子：13.1； 五年影响因子：16.8 ）

ISSN： 0305-1048

年卷期： 2024 年 52 卷 21 期

页码：

收录情况： SCI

摘要： The precise role of the highly variable coronavirus S protein in modulating innate immune responses remains unclear. In this study, we demonstrated that the mutant strain of swine coronavirus porcine enteric diarrhea virus induced significantly lower levels of double-stranded RNA (dsRNA) accumulation, inhibited protein kinase R (PKR) activation and suppressed stress granule (SG) formation compared with the classical strain. The 29th amino acid at N-terminus of S was identified as the key functional site for regulation of SG formation, and found that mutant S inhibited PKR phosphorylation and SG formation by upregulating adenosine deaminase acting on RNA 1 (ADAR1)-p150. Notably, the Z alpha domain of ADAR1-p150 was essential for inhibiting SG formation. Upregulation of ADAR1-p150 also reduced accumulation of dsRNA depending on its RNA editing function. Virus rescue confirmed that the mutant carrying a substitution at amino acid 29 failed to induce ADAR1-p150, leading to dsRNA accumulation, PKR activation and SG formation. Interestingly, the latest severe acute respiratory syndrome coronavirus-2 strains exhibit a novel 25PPA27 deletion at N-terminus of S that was also shown to lead to altered ADAR1-p150 expression and SG inhibition. The transcription factor TCF7L2 was identified as a player in S-mediated transcriptional enhancement of ADAR1-p150. This study is the first to clarify the crucial role of N-terminus of S in immune regulation of coronaviruses. [GRAPHICS]

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