ArticleThe EMBO journal2021
Liquid-liquid phase separation underpins the formation of replication factories in rotaviruses.
Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 129 citations in OpenAlex.
- Article
- Phosphorylation tunes strain-specific protein condensation during rotavirus replication organelle assembly.The EMBO journal · 2026Article
- A global database of West Nile virus host prevalence and competence.Scientific data · 2026Article
- K294E change in the rotavirus factory forming protein NSP2 stabilizes a rare C-terminal conformation.Journal of biomolecular structure & dynamics · 2026Article
- Review
- Liquid-liquid phase separation in the viral replication cycle: new paradigms and therapeutic opportunities.Archives of virology · 2026Review
- Liquid-liquid phase separation mediated immune evasion of respiratory syncytial virus against oligoadenylate synthetase-RNase L pathway.PLoS pathogens · 2026Article
- Article
- Grass carp reovirus VP35 hijacks DHX15 into phase-separated inclusion bodies to evade host antiviral immunity.Cell communication and signaling : CCS · 2026Article
- Extrachromosomal DNA associates with nuclear condensates and reorganizes chromatin structures to enhance oncogenic transcription.Cancer cell · 2025Article
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Poxvirus H5 mediates the formation of liquid-liquid phase separation condensates which promote virus factory assembly.PLoS pathogens · 2025Article
- High-throughput single-virion DNA-PAINT reveals structural diversity, cooperativity, and flexibility during selective packaging in influenza.Nucleic acids research · 2025Article
- Spatiotemporal coordination of reovirus peripheral core replication to perinuclear whole virus assembly.PLoS pathogens · 2025Article
- Computer Simulations Show That Liquid-Liquid Phase Separation Enhances Self-Assembly.ACS nano · 2025Article
- Plant negative-strand RNA virus phosphoprotein condensates exploit host trafficking and lipid synthesis for viral factory assembly.Science advances · 2025Article
- A plant bunyaviral protein disrupts SERRATE phase separation to modulate microRNA biogenesis during viral pathogenesis.Nature communications · 2025Article
- Uncovering protein conformational dynamics within two-component viral biomolecular condensates.Protein science : a publication of the Protein Society · 2025Article
- Phosphorylation enables allosteric control of a viral condensate.bioRxiv : the preprint server for biology · 2025Article
- Type II grass carp reovirus utilizes autophagosomes for viroplasm formation and subclinical persistent infection.Journal of virology · 2025Article
18 more citing papers are in PubMed but not listed here.
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16 authors at 6 institutions in 5 countries.
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Abstract
RNA viruses induce the formation of subcellular organelles that provide microenvironments conducive to their replication. Here we show that replication factories of rotaviruses represent protein-RNA condensates that are formed via liquid-liquid phase separation of the viroplasm-forming proteins NSP5 and rotavirus RNA chaperone NSP2. Upon mixing, these proteins readily form condensates at physiologically relevant low micromolar concentrations achieved in the cytoplasm of virus-infected cells. Early infection stage condensates could be reversibly dissolved by 1,6-hexanediol, as well as propylene glycol that released rotavirus transcripts from these condensates. During the early stages of infection, propylene glycol treatments reduced viral replication and phosphorylation of the condensate-forming protein NSP5. During late infection, these condensates exhibited altered material properties and became resistant to propylene glycol, coinciding with hyperphosphorylation of NSP5. Some aspects of the assembly of cytoplasmic rotavirus replication factories mirror the formation of other ribonucleoprotein granules. Such viral RNA-rich condensates that support replication of multi-segmented genomes represent an attractive target for developing novel therapeutic approaches.
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