文献类型： 外文期刊
作者： Zeng, Qinghua 1 ; Chen, Zheng 1 ; Huang, Yu 3 ; Fu, Qiuling 3 ; Chen, Zhen 3 ; Wu, Huansheng 1 ;
作者机构： 1.Jiangxi Agr Univ, Coll Anim Sci & Technol, Dept Vet Prevent Med, Nanchang 330045, Peoples R China
2.Jiangxi Agr Univ, Coll Anim Sci & Technol, Jiangxi Prov Key Lab Anim Hlth, Nanchang 330045, Peoples R China
3.Fujian Acad Agr Sci, Inst Anim Husb & Vet Med, Fuzhou 350013, Peoples R China
关键词： IBDV VP1; SRPK1; S48 phosphorylation
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）
ISSN： 0141-8130
年卷期： 2025 年 291 卷
页码：
收录情况： SCI
摘要： 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 posttranslational 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.
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