ArticleVeterinary microbiology2019
The phosphorylation of the N protein could affect PRRSV virulence in vivo.
Article in Veterinary microbiology, 2019. 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, 27 citations in OpenAlex.
- Multi-Proteomic Insights into Lysine Propionylation and Malonylation Remodeling in PRRSV-Infected Porcine Lungs.Veterinary sciences · 2026Article
- Immune Protection Gap Between Porcine Reproductive and Respiratory Syndrome Subunit Vaccine (N Protein) and Live Vaccine.Vaccines · 2025Article
- Understanding Post-Translational Modifications in Porcine Reproductive and Respiratory Syndrome Virus Infection.Veterinary sciences · 2024Review
- Research progress on the N protein of porcine reproductive and respiratory syndrome virus.Frontiers in microbiology · 2024Review
- Protein kinase Cdc7 supports viral replication by phosphorylatingJournal of virology · 2023Article
- Research Progress of Porcine Reproductive and Respiratory Syndrome Virus NSP2 Protein.Viruses · 2023Review
- Glycyrrhiza polysaccharides inhibits PRRSV replication.Virology journal · 2023Article
- p38MAPK- and GSK3-Mediated Phosphorylation of Snakehead Vesiculovirus Phosphoprotein at Threonine 160 Facilitates Viral Replication.Journal of virology · 2023Article
- A novel amino acid site of N protein could affect the PRRSV-2 replication by regulating the viral RNA transcription.BMC veterinary research · 2022Article
- Canine Adenovirus 1 Isolation Bioinformatics Analysis of the Fiber.Frontiers in cellular and infection microbiology · 2022Article
- Hyper-phosphorylation of nsp2-related proteins of porcine reproductive and respiratory syndrome virus.Virology · 2020Article
- Article
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid (N) protein is a multiphosphorylated protein.It has been proved that the phosphorylation of N protein could regulate the growth ability of PRRSV in Marc-145 cells. However, further investigation is needed to determine whether phosphorylation of the N protein could affect PRRSV virulence in piglets. In this study, we confirmed that the mutations could impair PRRSV replication ability in porcine primary macrophages (PAMs) as they did in Marc-145 cells. The animal experiments suggested that the pathogenicity of the mutated virus (A105-120) was significantly reduced compared with parent strain (XH-GD). Our results suggested that the phosphorylation of the N protein contributes to virus replication and virulence. This study is the first to identify a specific modification involved in PRRSV pathogenicity. Mutation of PTMs sites is also a novel way to attenuate PRRSV virulence. The mutations could be a marker in a vaccine. In conclusion, our study will improve our understanding of the molecular mechanisms of PRRSV pathogenicity.
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