ArticleJournal of virology2023
Flexibility of the Rotavirus NSP2 C-Terminal Region Supports Factory Formation via Liquid-Liquid Phase Separation.
Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Phosphorylation tunes strain-specific protein condensation during rotavirus replication organelle assembly.The EMBO journal · 2026Article
- K294E change in the rotavirus factory forming protein NSP2 stabilizes a rare C-terminal conformation.Journal of biomolecular structure & dynamics · 2026Article
- Article
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Metabolic Reprogramming in Respiratory Viral Infections: A Focus on SARS-CoV-2, Influenza, and Respiratory Syncytial Virus.Biomolecules · 2025Review
- 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
- Influenza A virus RNA localisation and the interceding trafficking pathways of the host cell.PLoS pathogens · 2025Review
- Characterization of viroplasm-like structures by co-expression of NSP5 and NSP2 across rotavirus species A to J.Journal of virology · 2024Article
- Isolation, Genomic Characterization and Evolution of Six Porcine Rotavirus A Strains in a Pig Farming Group.Veterinary sciences · 2024Article
- Recruitment of multi-segment genomic RNAs by Bluetongue virus requires a preformed RNA network.Nucleic acids research · 2024Article
- Review
- The Role of the Host Cytoskeleton in the Formation and Dynamics of Rotavirus Viroplasms.Viruses · 2024Review
- The Formation and Function ofInternational journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Many viruses sequester the materials needed for their replication into discrete subcellular factories. For rotaviruses (RVs), these factories are called viroplasms, and they are formed in the host cell cytosol via the process of liquid-liquid phase separation (LLPS). The nonstructural protein 2 (NSP2) and its binding partner, nonstructural protein 5 (NSP5), are critical for viroplasm biogenesis. Yet it is not fully understood how NSP2 and NSP5 cooperate to form factories. The C-terminal region (CTR) of NSP2 (residues 291 to 317) is flexible, allowing it to participate in domain-swapping interactions that promote interoctamer interactions and, presumably, viroplasm formation. Molecular dynamics simulations showed that a lysine-to-glutamic acid change at position 294 (K294E) reduces NSP2 CTR flexibility
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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 OpenQuestion graph.