A plant bunyaviral protein disrupts SERRATE phase separation to modulate microRNA biogenesis during viral pathogenesis

Jing Zou, Shuai Zhang, Ying Chen, Chun He, Xin Pan, Yimin Zhang, Jianwei Xu, Lijia Zheng, Hongxin Guan, Ming Wu, Dongqi Xie, Yinghua Ji, Xianyang Fang, Yi Li, Shou-wei Ding (), Xiaofeng Fang (), Shanshan Zhao () and Jianguo Wu ()
Additional contact information
Jing Zou: Fujian Agriculture and Forestry University
Shuai Zhang: Fujian Agriculture and Forestry University
Ying Chen: Fujian Agriculture and Forestry University
Chun He: Tsinghua University
Xin Pan: Chinese Academy of Sciences
Yimin Zhang: Fujian Agriculture and Forestry University
Jianwei Xu: Fujian Agriculture and Forestry University
Lijia Zheng: Ltd
Hongxin Guan: Fujian Normal University
Ming Wu: Fujian Agriculture and Forestry University
Dongqi Xie: Tsinghua University
Yinghua Ji: Jiangsu Academy of Agricultural Sciences
Xianyang Fang: Chinese Academy of Sciences
Yi Li: Fujian Agriculture and Forestry University
Shou-wei Ding: University of California
Xiaofeng Fang: Tsinghua University
Shanshan Zhao: Fujian Agriculture and Forestry University
Jianguo Wu: Fujian Agriculture and Forestry University

Nature Communications, 2025, vol. 16, issue 1, 1-16

Abstract: Abstract 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.

Date: 2025
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DOI: 10.1038/s41467-025-61528-0

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