ArticlePloS one2015
Avibirnavirus VP4 Protein Is a Phosphoprotein and Partially Contributes to the Cleavage of Intermediate Precursor VP4-VP3 Polyprotein.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- IBDV-SSA, a novel molecular approach for the recovery of infectious bursal disease virus whole genomes from FTA cards.Microbiology spectrum · 2025Article
- Protein kinase Cdc7 supports viral replication by phosphorylatingJournal of virology · 2023Article
- Article
- PRMT5 Facilitates Infectious Bursal Disease Virus Replication through Arginine Methylation of VP1.Journal of virology · 2023Article
- Phosphorylation of VP1 Mediated by CDK1-Cyclin B1 Facilitates Infectious Bursal Disease Virus Replication.Journal of virology · 2023Article
- TRAF6 autophagic degradation byAutophagy · 2022Article
- Full-length genome sequencing of a very virulent infectious bursal disease virus isolated in Tunisia.Poultry science · 2021Article
- Article
- Binding ofAutophagy · 2020Article
- SUMO1 Modification Facilitates Avibirnavirus Replication by Stabilizing Polymerase VP1.Journal of virology · 2019Article
- Ubiquitination Is Essential for Avibirnavirus Replication by Supporting VP1 Polymerase Activity.Journal of virology · 2019Article
- The C-terminal amyloidogenic peptide contributes to self-assembly of Avibirnavirus viral protease.Scientific reports · 2015Article
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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
Birnavirus-encoded viral protein 4 (VP4) utilizes a Ser/Lys catalytic dyad mechanism to process polyprotein. Here three phosphorylated amino acid residues Ser538, Tyr611 and Thr674 within the VP4 protein of the infectious bursal disease virus (IBDV), a member of the genus Avibirnavirus of the family Birnaviridae, were identified by mass spectrometry. Anti-VP4 monoclonal antibodies finely mapping to phosphorylated (p)Ser538 and the epitope motif 530PVVDGIL536 were generated and verified. Proteomic analysis showed that in IBDV-infected cells the VP4 was distributed mainly in the cytoskeletal fraction and existed with different isoelectric points and several phosphorylation modifications. Phosphorylation of VP4 did not influence the aggregation of VP4 molecules. The proteolytic activity analysis verified that the pTyr611 and pThr674 sites within VP4 are involved in the cleavage of viral intermediate precursor VP4-VP3. This study demonstrates that IBDV-encoded VP4 protein is a unique phosphoprotein and that phosphorylation of Tyr611 and Thr674 of VP4 affects its serine-protease activity.
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