ArticleJournal of virology2007
Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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Who cites it
45 citing papers in PubMed, 80 citations in OpenAlex.
- Phosphorylation tunes strain-specific protein condensation during rotavirus replication organelle assembly.The EMBO journal · 2026Article
- Comparative analysis of NSP5/VP2-induced viroplasm-like structures in rotavirus species A to J.Journal of virology · 2025Article
- Phosphorylation enables allosteric control of a viral condensate.bioRxiv : the preprint server for biology · 2025Article
- Phase separation and viral factories: unveiling the physical processes supporting RNA packaging in dsRNA viruses.Biochemical Society transactions · 2024Review
- Characterization of viroplasm-like structures by co-expression of NSP5 and NSP2 across rotavirus species A to J.Journal of virology · 2024Article
- Iron‑sulfur clusters in viral proteins: Exploring their elusive nature, roles and new avenues for targeting infections.Biochimica et biophysica acta. Molecular cell research · 2024Review
- The Role of the Host Cytoskeleton in the Formation and Dynamics of Rotavirus Viroplasms.Viruses · 2024Review
- The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication.mBio · 2024Article
- Principles of RNA recruitment to viral ribonucleoprotein condensates in a segmented dsRNA virus.eLife · 2023Article
- Rotavirus Spike Protein VP4 Mediates Viroplasm Assembly by Association to Actin Filaments.Journal of virology · 2022Article
- Liquid-liquid phase separation underpins the formation of replication factories in rotaviruses.The EMBO journal · 2021Article
- Article
- Review
- Conserved Rotavirus NSP5 and VP2 Domains Interact and Affect Viroplasm.Journal of virology · 2020Article
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Coding-Gene Coevolution Analysis of Rotavirus Proteins: A Bioinformatics and Statistical Approach.Genes · 2019Article
- Recombinant Rotaviruses Rescued by Reverse Genetics Reveal the Role of NSP5 Hyperphosphorylation in the Assembly of Viral Factories.Journal of virology · 2019Article
- Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and Their Sequestration in Viroplasms To Promote Progeny Virus Production.Journal of virology · 2018Article
- Cytoplasmic Relocalization and Colocalization with Viroplasms of Host Cell Proteins, and Their Role in Rotavirus Infection.Journal of virology · 2018Article
- Identification of a Small Molecule That Compromises the Structural Integrity of Viroplasms and Rotavirus Double-Layered Particles.Journal of virology · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotavirus morphogenesis starts in intracellular inclusion bodies called viroplasms. RNA replication and packaging are mediated by several viral proteins, of which VP1, the RNA-dependent RNA polymerase, and VP2, the core scaffolding protein, were shown to be sufficient to provide replicase activity in vitro. In vivo, however, viral replication complexes also contain the nonstructural proteins NSP2 and NSP5, which were shown to be essential for replication, to interact with each other, and to form viroplasm-like structures (VLS) when coexpressed in uninfected cells. In order to gain a better understanding of the intermediates formed during viral replication, this work focused on the interactions of NSP5 with VP1, VP2, and NSP2. We demonstrated a strong interaction of VP1 with NSP5 but only a weak one with NSP2 in cotransfected cells in the absence of other viral proteins or viral RNA. By contrast, we failed to coimmunoprecipitate VP2 with anti-NSP5 antibodies or NSP5 with anti-VP2 antibodies. We constructed a tagged form of VP1, which was found to colocalize in viroplasms and in VLS formed by NSP5 and NSP2. The tagged VP1 was able to replace VP1 structurally by being incorporated into progeny viral particles. When applying anti-tag-VP1 or anti-NSP5 antibodies, coimmunoprecipitation of tagged VP1 with NSP5 was found. Using deletion mutants of NSP5 or different fragments of NSP5 fused to enhanced green fluorescent protein, we identified the 48 C-terminal amino acids as the region essential for interaction with VP1.
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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 OpenQuestion graph.