ArticleBMC molecular biology2007
Bluetongue virus RNA binding protein NS2 is a modulator of viral replication and assembly.
Article in BMC molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 103 citations in OpenAlex.
- Mapping of three novel linear B-cell epitopes on the VP7 protein of epizootic hemorrhagic disease virus with monoclonal antibodies.Veterinary research · 2026Article
- Article
- Visualization and tracking of tubule-derived, fluorescent-labeled NS1 as a marker of bluetongue virus in living cells.Journal of virology · 2025Article
- Type II grass carp reovirus utilizes autophagosomes for viroplasm formation and subclinical persistent infection.Journal of virology · 2025Article
- Monoclonal antibody and B-cell epitope mapping of the VP7 protein in bluetongue virus.Virology journal · 2025Article
- Inhibition of early EHDV2-Ibaraki infection steps in bovine cells by endosome alkalinization or ikarugamycin, but not by blockage of individual endocytic pathways.Frontiers in cellular and infection microbiology · 2025Article
- Increased Virulence ofViruses · 2024Article
- Article
- Grass carp reovirus VP56 and VP35 induce formation of viral inclusion bodies for replication.iScience · 2024Article
- Identification of Orbivirus Non-Structural Protein 5 (NS5), Its Role and Interaction with RNA/DNA in Infected Cells.International journal of molecular sciences · 2023Article
- Interferon-stimulated gene 15 facilitates BTV replication through interacting with the NS1 protein.Frontiers in microbiology · 2023Article
- Role of NS2 specific RNA binding and phosphorylation in liquid-liquid phase separation and virus assembly.Nucleic acids research · 2022Article
- Investigating the Role of African Horse Sickness Virus VP7 Protein Crystalline Particles on Virus Replication and Release.Viruses · 2022Article
- Generation of a Soluble African Horse Sickness Virus VP7 Protein Capable of Forming Core-like Particles.Viruses · 2022Article
- Comparative Virus-Host Protein Interactions of the Bluetongue Virus NS4 Virulence Factor.Viruses · 2022Article
- Vaccination as a Strategy to Prevent Bluetongue Virus Vertical Transmission.Pathogens (Basel, Switzerland) · 2021Review
- Review
- In Vitro Reassortment between Endemic Bluetongue Viruses Features Global Shifts in Segment Frequencies and Preferred Segment Combinations.Microorganisms · 2021Article
- Inhibition of the IFN Response by Bluetongue Virus: The Story So Far.Frontiers in microbiology · 2021Review
- Differential Localization of Structural and Non-Structural Proteins during the Bluetongue Virus Replication Cycle.Viruses · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundBluetongue virus (BTV) particles consist of seven structural proteins that are organized into two capsids. In addition, BTV also encodes three non-structural (NS) proteins of which protein 2 (NS2) is the RNA binding protein and is also the major component of virus encoded inclusion bodies (VIBs), which are believed to be virus assembly sites. To investigate the contribution of NS2 in virus replication and assembly we have constructed inducible mammalian cell lines expressing full-length NS2. In addition, truncated NS2 fragments were also generated in an attempt to create dominant negative mutants for NS2 function.
resultsOur data revealed that expression of full-length NS2 was sufficient for the formation of inclusion bodies (IBs) that were morphologically similar to the VIBs formed during BTV infection. By using either, individual BTV proteins or infectious virions, we found that while the VP3 of the inner capsid (termed as "core") that surrounds the transcription complex was closely associated with both NS2 IBs and BTV VIBs, the surface core protein VP7 co-localized with NS2 IBs only in the presence of VP3. In contrast to the inner core proteins, the outer capsid protein VP2 was not associated with either IBs or VIBs. Like the core proteins, newly synthesized BTV RNAs also accumulated in VIBs. Unlike full-length NS2, neither the amino-, nor carboxyl-terminal fragments formed complete IB structures and each appeared to interfere in overall virus replication when similarly expressed.
conclusionTogether, these data demonstrate that NS2 is sufficient and necessary for IB formation and a key player in virus replication and core assembly. Perturbation of NS2 IB formation resulted in reduced virus synthesis and both the N terminal (NS2-1) and C terminal (NS2-2) fragments act as dominant negative mutants of NS2 function.
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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.