ArticleNucleic acids research2022
Role of NS2 specific RNA binding and phosphorylation in liquid-liquid phase separation and virus assembly.
Article in Nucleic acids research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- G-Quadruplexes: Structural Diversity and Emerging Roles in Biomolecular Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- A Molecular and Structural Perspective on Bluetongue Virus Entry and Assembly.Pathogens (Basel, Switzerland) · 2026Review
- Grass carp reovirus VP35 hijacks DHX15 into phase-separated inclusion bodies to evade host antiviral immunity.Cell communication and signaling : CCS · 2026Article
- Type II grass carp reovirus utilizes autophagosomes for viroplasm formation and subclinical persistent infection.Journal of virology · 2025Article
- Phase separation and viral factories: unveiling the physical processes supporting RNA packaging in dsRNA viruses.Biochemical Society transactions · 2024Review
- Liquid-liquid phase separation is essential for reovirus viroplasm formation and immune evasion.Journal of virology · 2024Article
- Recruitment of multi-segment genomic RNAs by Bluetongue virus requires a preformed RNA network.Nucleic acids research · 2024Article
- Crosstalk between protein post-translational modifications and phase separation.Cell communication and signaling : CCS · 2024Review
- Protein interactions: anything new?Essays in biochemistry · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Liquid-liquid phase separation (LLPS) has assumed a prominent role in biological cell systems, where it underpins the formation of subcellular compartments necessary for cell function. We investigated the underlying mechanism of LLPS in virus infected cells, where virus inclusion bodies are formed by an RNA-binding phosphoprotein (NS2) of Bluetongue virus to serve as sites for subviral particle assembly and virus maturation. We show that NS2 undergoes LLPS that is dependent on protein phosphorylation and RNA-binding and that LLPS occurrence is accompanied by a change in protein secondary structure. Site-directed mutagenesis identified two critical arginine residues in NS2 responsible for specific RNA binding and thus for NS2-RNA complex driven LLPS. Reverse genetics identified the same residues as essential for VIB assembly in infected cells and virus viability. Our findings suggest that a specific arginine-RNA interaction in the context of a phosphorylated state drives LLPS in this, and possibly other, virus infections.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.