ArticleThe Journal of biological chemistry2010
Electrostatic interactions between capsid and scaffolding proteins mediate the structural polymorphism of a double-stranded RNA virus.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Mapping Molecular Determinants of Antigenicity and Pathogenicity of Infectious Bursal Disease Virus (IBDV): A Scoping Review.Viruses · 2026Article
- Article
- Structure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.Journal of virology · 2025Article
- Development and Characterization of Monoclonal Antibodies Against VP3 Protein of Infectious Bursal Disease Virus.Transboundary and emerging diseases · 2025Article
- Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical role.PNAS nexus · 2024Article
- Oral Immunization with RecombinantVaccines · 2023Article
- Harnessing physicochemical properties of virus capsids for designing enzyme confined nanocompartments.Current opinion in virology · 2022Review
- A Single Vaccination of IBDV Subviral Particles Generated byVaccines · 2021Article
- Development of a Viral-Like Particle Candidate Vaccine Against Novel Variant Infectious Bursal Disease Virus.Vaccines · 2021Article
- Physical virology: From virus self-assembly to particle mechanics.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2020Review
- Why large icosahedral viruses need scaffolding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanics of Virus-like Particles Labeled with Green Fluorescent Protein.Biophysical journal · 2018Article
- The RNA-Binding Protein of a Double-Stranded RNA Virus Acts like a Scaffold Protein.Journal of virology · 2018Article
- Systematic analysis of biological roles of charged amino acid residues located throughout the structured inner wall of a virus capsid.Scientific reports · 2018Article
- Infectious Bursal Disease Virus Hijacks Endosomal Membranes as the Scaffolding Structure for Viral Replication.Journal of virology · 2018Article
- Assembly/disassembly of a complex icosahedral virus to incorporate heterologous nucleic acids.Journal of physics. Condensed matter : an Institute of Physics journal · 2017Article
- Voltage-Dependent Anion Channel 1 Interacts with Ribonucleoprotein Complexes To Enhance Infectious Bursal Disease Virus Polymerase Activity.Journal of virology · 2017Article
- A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability.Scientific reports · 2015Article
- Structural basis for the development of avian virus capsids that display influenza virus proteins and induce protective immunity.Journal of virology · 2015Article
- Host proteolytic activity is necessary for infectious bursal disease virus capsid protein assembly.The Journal of biological chemistry · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Capsid proteins that adopt distinct conformations constitute a paradigm of the structural polymorphism of macromolecular assemblies. We show the molecular basis of the flexibility mechanism of VP2, the capsid protein of the double-stranded RNA virus infectious bursal disease virus. The initial assembly, a procapsid-like structure, is built by the protein precursor pVP2 and requires VP3, the other infectious bursal disease virus major structural protein, which acts as a scaffold. The pVP2 C-terminal region, which is proteolyzed during virus maturation, contains an amphipathic alpha-helix that acts as a molecular switch. In the absence of VP3, efficient virus-like particle assembly occurs when the structural unit is a VP2-based chimeric protein with an N-terminal-fused His(6) tag. The His tag has a positively charged N terminus and a negatively charged C terminus, both important for virion-like structure assembly. The charge distributions of the VP3 C terminus and His tag are similar. We tested whether the His tag emulates the role of VP3 and found that the presence of a VP3 C-terminal peptide in VP2-based chimeric proteins resulted in the assembly of virus-like particles. We analyzed the electrostatic interactions between these two charged morphogenetic peptides, in which a single residue was mutated to impede the predicted interaction, followed by a compensatory double mutation to rescue electrostatic interactions. The effects of these mutations were monitored by following the virus-like and/or virus-related assemblies. Our results suggest that the basic face of the pVP2 amphipathic alpha-helix interacts with the acidic region of the VP3 C terminus and that this interaction is essential for VP2 acquisition of competent conformations for capsid assembly.
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