A plant bunyaviral protein disrupts SERRATE phase separation to modulate microRNA biogenesis during viral pathogenesis
文献类型： 外文期刊
作者： Zou, Jing 1 ; Zhang, Shuai 1 ; Chen, Ying 1 ; He, Chun 2 ; Pan, Xin 3 ; Zhang, Yimin 1 ; Xu, Jianwei 1 ; Zheng, Lijia 4 ; Guan, Hongxin 5 ; Wu, Ming 1 ; Xie, Dongqi 2 ; Ji, Yinghua 6 ; Fang, Xianyang 3 ; Li, Yi 1 ; Ding, Shou-wei 7 ; Fang, Xiaofeng 2 ; Zhao, Shanshan 1 ; Wu, Jianguo 1 ;
作者机构： 1.Fujian Agr & Forestry Univ, Coll Plant Protect, State Key Lab Agr & Forestry Biosecur, Fuzhou, Peoples R China
2.Tsinghua Univ, Ctr Plant Biol, Sch Life Sci, Beijing, Peoples R China
3.Chinese Acad Sci, Inst Biophys, Key Lab Epigenet Regulat & Intervent, Beijing, Peoples R China
4.Higentec Co Ltd, Changsha, Hunan, Peoples R China
5.Fujian Normal Univ, Coll Life Sci, Key Lab Optoelect Sci & Technol Med, Minist Educ, Fuzhou, Peoples R China
6.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing, Peoples R China
7.Univ Calif Riverside, Inst Integrat Genome Biol, Ctr Plant Cell Biol, Dept Microbiol & Plant Pathol, Riverside, CA 92521 USA
期刊名称：NATURE COMMUNICATIONS （ 影响因子：15.7； 五年影响因子：17.2 ）
ISSN：
年卷期： 2025 年 16 卷 1 期
页码：
收录情况： SCI
摘要： Liquid-liquid phase separation (LLPS) regulates diverse biological functions by mediating the assembly of biomolecular condensates. However, it remains unclear how host LLPS is targeted by viruses during infection. Here we show that a plant bunyaviral protein, the disease-specific protein (SP) encoded by rice stripe virus (RSV), possesses phase separation potential through its N-terminal intrinsically disordered region 1 (IDR1). In vivo, however, SP does not form phase-separated biomolecular condensates independently but utilizes its phase separation properties to interfere with the phase separation of the SERRATE protein (SE), a key component of Dicing bodies essential for microRNA processing. By disrupting SE phase separation, SP inhibits D-body assembly and miRNA biogenesis. Our study demonstrates that a viral protein can modulate host microRNA processing by targeting LLPS, revealing a previously uncharacterized mechanism involved in viral infection strategies and miRNA biogenesis regulation in plants.
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