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A fijiviral nonstructural protein triggers cell death in plant and bacterial cells via its transmembrane domain

文献类型： 外文期刊

作者： Yuan, Zhengjie 1 ; Geng, Yanfei 1 ; Dai, Yuanxing 1 ; Li, Jing 1 ; Lv, Mingfang 1 ; Liao, Qiansheng 3 ; Xie, Li 4 ; Zhang, Heng-Mu 1 ;

作者机构： 1.Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, Lab Virol, Hangzhou 310021, Peoples R China

2.Zhejiang Normal Univ, Coll Chem & Life Sci, Jinhua, Zhejiang, Peoples R China

3.Zhejiang Sci Tech Univ, Coll Life Sci, Hangzhou, Peoples R China

4.Zhejiang Univ, Anal Ctr Agrobiol & Environm Sci, Hangzhou, Peoples R China

关键词： cell death; fijivirus; transmembrane domain; viral nonstructural protein

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：4.9； 五年影响因子：5.9 ）

ISSN： 1464-6722

年卷期： 2023 年 24 卷 1 期

页码：

收录情况： SCI

摘要： Southern rice black-streaked dwarf virus (SRBSDV; Fijivirus, Reoviridae) has become a threat to cereal production in East Asia in recent years. Our previous cytopathologic studies have suggested that SRBSDV induces a process resembling programmed cell death in infected tissues that results in distinctive growth abnormalities. The viral product responsible for the cell death, however, remains unknown. Here P9-2 protein, but not its RNA, was shown to induce cell death in Escherichia coli and plant cells when expressed either locally with a transient expression vector or systemically using a heterologous virus. Both computer prediction and fluorescent assays indicated that the viral nonstructural protein was targeted to the plasma membrane (PM) and further modification of its subcellular localization abolished its ability to induce cell death, indicating that its PM localization was required for the cell death induction. P9-2 was predicted to harbour two transmembrane helices within its central hydrophobic domain. A series of mutation assays further showed that its central transmembrane hydrophobic domain was crucial for cell death induction and that its conserved F90, Y101, and L103 amino acid residues could play synergistic roles in maintaining its ability to induce cell death. Its homologues in other fijiviruses also induced cell death in plant and bacterial cells, implying that the fijiviral nonstructural protein may trigger cell death by targeting conserved cellular factors or via a highly conserved mechanism.

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