ArticleThe Journal of biological chemistry2012
Host proteolytic activity is necessary for infectious bursal disease virus capsid protein assembly.
Article in The Journal of biological chemistry, 2012. 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, 31 citations in OpenAlex.
- Dual-expression-site fowl adenovirus 4 (FAdV-4) with high viral titer: a promising viral vector for multivalent poultry vaccines.Veterinary research · 2026Article
- Review
- Key role of TLR3 in type I IFN expression and apoptosis induction in IBDV-infected chicken fibroblast cells.Frontiers in cellular and infection microbiology · 2026Article
- Development and Application of Indirect ELISA for IBDV VP2 Antibodies Detection in Poultry.Viruses · 2025Article
- Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical role.PNAS nexus · 2024Article
- The Basic Architecture of Viruses.Sub-cellular biochemistry · 2024Review
- Review
- 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
- Cryo-electron Microscopy Structure, Assembly, and Mechanics Show Morphogenesis and Evolution of Human Picobirnavirus.Journal of virology · 2020Article
- Article
- Role of MicroRNAs in Host Defense against Infectious Bursal Disease Virus (IBDV) Infection: A Hidden Front Line.Viruses · 2020Review
- Immunogenicity and protective efficacy of orally administered recombinant Lactobacillus plantarum expressing VP2 protein against IBDV in chicken.Journal of applied microbiology · 2018Article
- The RNA-Binding Protein of a Double-Stranded RNA Virus Acts like a Scaffold Protein.Journal of virology · 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
- Infectious Bursal Disease Virus-Host Interactions: Multifunctional Viral Proteins that Perform Multiple and Differing Jobs.International journal of molecular sciences · 2017Review
- VP2 of Infectious Bursal Disease Virus Induces Apoptosis via Triggering Oral Cancer Overexpressed 1 (ORAOV1) Protein Degradation.Frontiers in microbiology · 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
- A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability.Scientific reports · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In many viruses, a precursor particle, or procapsid, is assembled and undergoes massive chemical and physical modification to produce the infectious capsid. Capsid assembly and maturation are finely tuned processes in which viral and host factors participate. We show that the precursor of the VP2 capsid protein (pVP2) of the infectious bursal disease virus (IBDV), a double-stranded RNA virus, is processed at the C-terminal domain (CTD) by a host protease, the puromycin-sensitive aminopeptidase (PurSA). The pVP2 CTD (71 residues) has an important role in determining the various conformations of VP2 (441 residues) that build the T = 13 complex capsid. pVP2 CTD activity is controlled by co- and posttranslational proteolytic modifications of different targets by the VP4 viral protease and by VP2 itself to yield the mature VP2-441 species. Puromycin-sensitive aminopeptidase is responsible for the peptidase activity that cleaves the Arg-452-Arg-453 bond to generate the intermediate pVP2-452 polypeptide. A pVP2 R453A substitution abrogates PurSA activity. We used a baculovirus-based system to express the IBDV polyprotein in insect cells and found inefficient formation of virus-like particles similar to IBDV virions, which correlates with the absence of puromycin-sensitive aminopeptidase in these cells. Virus-like particle assembly was nonetheless rescued efficiently by coexpression of chicken PurSA or pVP2-452 protein. Silencing or pharmacological inhibition of puromycin-sensitive aminopeptidase activity in cell lines permissive for IBDV replication caused a major blockade in assembly and/or maturation of infectious IBDV particles, as virus yields were reduced markedly. PurSA activity is thus essential for IBDV replication.
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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.