ArticleNature communications2025
A plant bunyaviral protein disrupts SERRATE phase separation to modulate microRNA biogenesis during viral pathogenesis.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- Nanoclustering of a plant transcription factor enables strong yet specific DNA binding.Science advances · 2026Article
- The multidimensional significance of virus-host protein interactions and their implications in the antiviral defense of plants.Stress biology · 2026Review
- Liquid-liquid phase separation at the frontline of plant-pathogen battles.Plant communications · 2026Review
- Natural genetic variation of a single amino acid in beet necrotic yellow vein virus P31 protein modulates evasion of plant ubiquitination-mediated antiviral immunity.PLoS pathogens · 2026Article
- Diverse RNA viral effectors converge on facilitation of AGO4 degradation to promote infection.Nucleic acids research · 2025Article
- Antiviral RNA interference in plants: Increasing complexity and integration with other biological processes.Plant communications · 2025Review
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Authors and funding
18 authors.
Funding
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.
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