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The phosphorylation of the N protein could affect PRRSV virulence in vivo

Yao Chen1, Zhiqing Yu2, Heyou Yi2

  • 1School of Life Science and Engineering, Foshan University, Foshan, PR China; MOA Key Laboratory of Animal Vaccine Development, Ministry of Agriculture, College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, PR China; National and Regional Joint Engineering Laboratory for Medicament of Zoonosis Prevention and Control, PR China; South China Agricultural University/College of Veterinary and National Engineering Research Center for Breeding Swine Industry, PR China.

Veterinary Microbiology
|April 9, 2019
PubMed

Insights

Phosphorylation of the porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid protein is crucial for virus replication and virulence in piglets. Mutating these sites offers a novel strategy for PRRSV attenuation.

Area of Science:

  • Veterinary Virology
  • Molecular Pathogenesis
  • Animal Health

Background:

  • Porcine respiratory and reproductive syndrome virus (PRRSV) nucleocapsid (N) protein is multiphosphorylated.
  • N protein phosphorylation regulates PRRSV growth in Marc-145 cells.
  • The impact of N protein phosphorylation on PRRSV virulence in piglets remains unclear.

Purpose of the Study:

  • To investigate the role of N protein phosphorylation in PRRSV replication and virulence in piglets.
  • To determine if mutations affecting phosphorylation sites impact PRRSV pathogenicity.
  • To explore novel methods for PRRSV attenuation.

Main Methods:

  • Mutagenesis of PRRSV N protein phosphorylation sites.
  • Assessment of PRRSV replication in porcine primary macrophages (PAMs).
  • Animal experiments evaluating the pathogenicity of mutated PRRSV strains in piglets.

Main Results:

  • Mutations impair PRRSV replication in PAMs, similar to Marc-145 cells.
  • The mutated virus (A105-120) exhibited significantly reduced pathogenicity in piglets compared to the parent strain (XH-GD).
  • N protein phosphorylation is confirmed to contribute to PRRSV replication and virulence.

Conclusions:

  • Phosphorylation of the PRRSV N protein is a key factor in virus replication and pathogenicity.
  • Mutation of post-translational modification (PTM) sites is a promising strategy for PRRSV attenuation.
  • This study identifies a specific modification linked to PRRSV pathogenicity and suggests potential vaccine markers.
Keywords:
N proteinPRRSVPhosphorylationVirulence

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