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

Author

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  • 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)

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.

Suggested Citation

  • 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 Fa, 2025. "A plant bunyaviral protein disrupts SERRATE phase separation to modulate microRNA biogenesis during viral pathogenesis," Nature Communications, Nature, vol. 16(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-61528-0
    DOI: 10.1038/s41467-025-61528-0
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    References listed on IDEAS

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    1. Xiaofeng Fang & Liang Wang & Ryo Ishikawa & Yaoxi Li & Marc Fiedler & Fuquan Liu & Grant Calder & Beth Rowan & Detlef Weigel & Pilong Li & Caroline Dean, 2019. "Arabidopsis FLL2 promotes liquid–liquid phase separation of polyadenylation complexes," Nature, Nature, vol. 569(7755), pages 265-269, May.
    2. Qing Sang & Lusheng Fan & Tianxiang Liu & Yongjian Qiu & Juan Du & Beixin Mo & Meng Chen & Xuemei Chen, 2023. "MicroRNA156 conditions auxin sensitivity to enable growth plasticity in response to environmental changes in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
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