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Infectious Bursal Disease Virus Capsid Protein VP3 Interacts both with VP1, the RNA-Dependent RNA Polymerase, and with Viral Double-Stranded RNA

19 Oct 2002

Abstract excerpt

Infectious bursal disease virus (IBDV) is a double-stranded RNA (dsRNA) virus of the Birnaviridae family. Its two genome segments are encapsidated together with multiple copies of the viral RNA-dependent RNA polymerase, VP1, in a single-shell capsid that is composed of VP2 and VP3. In this study we identified the domains responsible for the interaction between VP3 and VP1. Using the yeast two-hybrid system we...

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PMID: 12388690
DOI: 10.1128/jvi.76.22.11301-11311.2002

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Infectious Bursal Disease Virus Capsid Protein VP3 Interacts both with VP1, the RNA-Dependent RNA Polymerase, and with Viral Double-Stranded RNAPMID 12388690Read ↗

Identification and Molecular Characterization of the RNA Polymerase-Binding Motif of Infectious Bursal Disease Virus Inner Capsid Protein VP3Semantic proximity Read ↗

Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical roleSemantic proximity Read ↗

Infectious Bursal Disease Virus VP3 Upregulates VP1-Mediated RNA-Dependent RNA ReplicationSemantic proximity Read ↗

VP1 and VP3 Are Required and Sufficient for Translation Initiation of Uncapped Infectious Bursal Disease Virus Genomic Double-Stranded RNASemantic proximity Read ↗

Infectious Bursal Disease Virus Hijacks Endosomal Membranes as the Scaffolding Structure for Viral ReplicationSemantic proximity Read ↗

VP1, the Putative RNA-Dependent RNA Polymerase of Infectious Bursal Disease Virus, Forms Complexes with the Capsid Protein VP3, Leading to Efficient Encapsidation into Virus-Like ParticlesSemantic proximity Read ↗

The VP3 Factor from Viruses of Birnaviridae Family Suppresses RNA Silencing by Binding Both Long and Small RNA DuplexesSemantic proximity Read ↗

The Infectious Bursal Disease Virus RNA-Binding VP3 Polypeptide Inhibits PKR-Mediated ApoptosisSemantic proximity Read ↗

The Endosomal Pathway and the Golgi Complex Are Involved in the Infectious Bursal Disease Virus Life CycleSemantic proximity Read ↗

The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virusSemantic proximity Read ↗

Inhibition of Antiviral Innate Immunity by Birnavirus VP3 Protein via Blockage of Viral Double-Stranded RNA Binding to the Host Cytoplasmic RNA Detector MDA5Semantic proximity Read ↗

C Terminus of Infectious Bursal Disease Virus Major Capsid Protein VP2 Is Involved in Definition of the T Number for Capsid AssemblySemantic proximity Read ↗

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