南美超级胎牛血清999尝鲜特惠
鉴定出UL3.5是DPV US3激酶的新型底物，其Ser64/Ser84位点的磷酸化可增强蛋白稳定性，促进病毒释放并实现细胞间传播。
Identification of UL3.5 as a novel substrate of DPV US3 kinase whose phosphorylation at Ser64/Ser84 enhances protein stability and promotes viral release, and cell-to-cell spread
Zhen Xiao, Bin Tian, Huanhuan Cao, Ran Ran, Dongjie Cai, Mingshu Wang, Ying Wu, Qiao Yang, Shaqiu Zhang, Dekang Zhu, Mafeng Liu, Xinxin Zhao, Di Sun, Juan Huang, Xumin Ou, Zhen Wu, Yu He, Yuhong Pan,
Journal：POULTRY SCIENCE
IF：4.5
DOI：10.1016/j.psj.2026.107389
PMID：
Published：2026-07-02
research field：转化医学基因治疗生物材料蛋白工程糖尿病并发症伤口愈合皮肤生物学
Abstract
Duck plague virus (DPV) is a major pathogen threatening waterfowl industry. As a conserved alphaherpesvirus kinase, DPV US3 participates in viral replication, while its functional substrates are largely uncharacterized. In this study, we verified that US3 directly binds and phosphorylates UL3.5 at Ser64 and Ser84. This post-translational modification inhibits protein degradation and prolongs the half-life of UL3.5. A phosphorylation-deficient recombinant virus was constructed, and phenotypic assays demonstrated that mutated virus had defective replication. Further tests indicated that UL3.5 phosphorylation mainly regulates viral genome replication, progeny release and cell-to-cell spread, rather than attachment and entry. Our findings expand the regulatory network of DPV US3 and uncover the biological function of UL3.5, laying a foundation for developing novel antiviral strategies against DPV.
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