2. Academic Validation
  3. SRPK1 facilitates IBDV replication by phosphorylating VP1 at S48

SRPK1 facilitates IBDV replication by phosphorylating VP1 at S48

  • Int J Biol Macromol. 2024 Dec 21:291:139002. doi: 10.1016/j.ijbiomac.2024.139002.
Qinghua Zeng 1,  Zheng Chen 1,  Yu Huang 2,  Qiuling Fu 2,  Zhen Chen 2,  Huansheng Wu 3
Affiliations

Affiliations

  • 1 Department of Veterinary Preventive Medicine, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China; Jiangxi Provincial Key Laboratory for Animal Health, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China.
  • 2 Institute of Animal Husbandry and Veterinary Medicine of Fujian Academy of Agricultural Sciences, Fuzhou 350013, PR China.
  • 3 Department of Veterinary Preventive Medicine, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China; Jiangxi Provincial Key Laboratory for Animal Health, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China. Electronic address: huanswu@jxau.edu.cn.
PMID: 39716705 DOI: 10.1016/j.ijbiomac.2024.139002
Abstract

Infectious Bursal Disease Virus (IBDV), a double-stranded RNA virus of the Avibirnavirus genus, causes significant vaccine failures in immunocompromised young poultry. The VP1 protein of IBDV undergoes post-translational modifications that are critical for viral RNA transcription, genome replication, and overall viral proliferation. Phosphorylation enhances the ability of the IBDV polymerase VP1 and facilitates viral replication, while the specific mechanisms underlying VP1 phosphorylation and its role in the IBDV life cycle remain largely unexplored. This study shows that SRPK1 phosphorylates VP1 at the serine 48 (S48) residue in the N-terminal 46SPSR49 motif, enhancing polymerase activity and promoting replication. During IBDV Infection, VP1 recruits SRPK1 and co-localizes with it. Inhibiting or deleting SRPK1 greatly reduced VP1 polymerase activity, a leading to a decrease in viral replication. Mutant strains S48A and S48E displayed impaired replication, highlighting the crucial role of SRPK1-mediated phosphorylation in VP1 function. These findings emphasize the key role of SRPK1-mediated VP1 phosphorylation in IBDV replication, providing new insights into viral-host interactions and potential therapeutic targets.

Keywords

IBDV VP1; S48 phosphorylation; SRPK1.

Figures
Products