ArticleJournal of virology2002
The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 84 citations in OpenAlex.
- Review
- Structure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.Journal of virology · 2025Article
- Article
- A Single Mutation of VP2 is Responsible for the Lethality and Antigenicity Differences between Novel Variant and Very Virulent IBDV Strains.Transboundary and emerging diseases · 2023Article
- Identification and Pathogenicity Evaluation of a Novel Reassortant Infectious Bursal Disease Virus (Genotype A2dB3).Viruses · 2021Article
- Development of a Viral-Like Particle Candidate Vaccine Against Novel Variant Infectious Bursal Disease Virus.Vaccines · 2021Article
- Cryo-electron Microscopy Structure, Assembly, and Mechanics Show Morphogenesis and Evolution of Human Picobirnavirus.Journal of virology · 2020Article
- Article
- Chicken eEF1α is a Critical Factor for the Polymerase Complex Activity of Very Virulent Infectious Bursal Disease Virus.Viruses · 2020Article
- Discovery of nonnucleoside inhibitors of polymerase from infectious pancreatic necrosis virus (IPNV).Drug design, development and therapy · 2018Article
- Molecular characterization of infectious pancreatic necrosis virus strains isolated from the three types of salmonids farmed in Chile.Virology journal · 2017Article
- Efficient self-assembly and protective efficacy of infectious bursal disease virus-like particles by a recombinant baculovirus co-expressing precursor polyprotein and VP4.Virology journal · 2015Article
- Article
- Binding of the pathogen receptor HSP90AA1 to avibirnavirus VP2 induces autophagy by inactivating the AKT-MTOR pathway.Autophagy · 2015Article
- Inhibition of antiviral innate immunity by birnavirus VP3 protein via blockage of viral double-stranded RNA binding to the host cytoplasmic RNA detector MDA5.Journal of virology · 2014Article
- Conformational dynamics inside amino-terminal disease hotspot of ryanodine receptor.Structure (London, England : 1993) · 2013Article
- Host proteolytic activity is necessary for infectious bursal disease virus capsid protein assembly.The Journal of biological chemistry · 2012Article
- Crystal structure of an Aquabirnavirus particle: insights into antigenic diversity and virulence determinism.Journal of virology · 2010Article
- Autoproteolytic activity derived from the infectious bursal disease virus capsid protein.The Journal of biological chemistry · 2009Article
- Infectious Bursal disease virus: ribonucleoprotein complexes of a double-stranded RNA virus.Journal of molecular biology · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infectious bursal disease virus (IBDV) is a nonenveloped avian virus with a two-segment double-stranded RNA genome. Its T=13 icosahedral capsid is most probably assembled with 780 subunits of VP2 and 600 copies of VP3 and has a diameter of about 60 nm. VP1, the RNA-dependent RNA polymerase, resides inside the viral particle. Using a baculovirus expression system, we first observed that expression of the pVP2-VP4-VP3 polyprotein encoded by the genomic segment IBDA results mainly in the formation of tubules with a diameter of about 50 nm and composed of pVP2, the precursor of VP2. Very few virus-like particles (VLPs) and VP4 tubules with a diameter of about 25 nm were also identified. The inefficiency of VLP assembly was further investigated by expression of additional IBDA-derived constructs. Expression of pVP2 without any other polyprotein components results in the formation of isometric particles with a diameter of about 30 nm. VLPs were observed mainly when a large exogeneous polypeptide sequence (the green fluorescent protein sequence) was fused to the VP3 C-terminal domain. Large numbers of VLPs were visualized by electron microscopy, and single particles were shown to be fluorescent by standard and confocal microscopy analysis. Moreover, the final maturation process converting pVP2 into the VP2 mature form was observed on generated VLPs. We therefore conclude that the correct scaffolding of the VP3 can be artificially induced to promote the formation of VLPs and that the final processing of pVP2 to VP2 is controlled by this particular assembly. To our knowledge, this is the first report of the engineering of a morphogenesis switch to control a particular type of capsid protein assembly.
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