Yang Linjiang, Hu Xixia, Cheng Anchun, Wang Mingshu, Jia Renyong, Yang Qiao, Wu Ying, Chen Shun, Liu Mafeng, Zhu Dekang, Ou Xumin, Wen XingJian, Mao Sai, Sun Di, Zhang Shaqiu, Zhao Xinxin, Huang Juan, Gao Qun, Liu Yunya, Yu Yanling, Zhang Ling, Tian Bin, Pan Leichang, Chen Xiaoyue
Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, PR China; Key Laboratory of Animal Disease and Human Health of Sichuan Province, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, PR China; Avian Disease Research Center, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, PR China.
Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, PR China; Key Laboratory of Animal Disease and Human Health of Sichuan Province, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, PR China; Avian Disease Research Center, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, PR China.
Poult Sci. 2021 Jan;100(1):26-38. doi: 10.1016/j.psj.2020.09.069. Epub 2020 Oct 8.
Duck enteritis virus (DEV) multifunctional tegument protein UL13 is predicted to be a conserved herpesvirus protein kinase; however, little is known about its subcellular localization signal. In this study, through transfection of 2 predicted nuclear signals of DEV UL13 fused to enhanced green fluorescent protein, 2 bipartite nuclear localization signals (NLS) were identified. We found that ivermectin blocked the NLS-mediated nuclear import of DEV UL13, showing that the nuclear localization signal of DEV UL13 is a classical importin α- and β-dependent process. We constructed a DEV UL13 mutant strain in which the NLS of DEV UL13 was deleted to explore whether deletion of the NLS affects viral replication. Amino acids 4 to 7 and 90 to 96 were predicted to be NLSs, further proving that nuclear import occurs via a classical importin α- and β-dependent process. We also found that the NLS of pUL13 had no effect on DEV replication in cell culture. Our study enhances the understanding of DEV pUL13. Taken together, these results provide significant information regarding the biological function of pUL13 during DEV infection.
鸭肠炎病毒（DEV）的多功能被膜蛋白UL13被预测为一种保守的疱疹病毒蛋白激酶；然而，对其亚细胞定位信号却知之甚少。在本研究中，通过转染与增强型绿色荧光蛋白融合的DEV UL13的2个预测核信号，鉴定出2个双分型核定位信号（NLS）。我们发现伊维菌素阻断了NLS介导的DEV UL13的核输入，表明DEV UL13的核定位信号是一个经典的依赖输入蛋白α和β的过程。我们构建了一个缺失DEV UL13的NLS的DEV UL13突变株，以探究NLS的缺失是否影响病毒复制。第4至7位氨基酸和第90至96位氨基酸被预测为NLS，进一步证明核输入是通过一个经典的依赖输入蛋白α和β的过程发生的。我们还发现pUL13的NLS对DEV在细胞培养中的复制没有影响。我们的研究增进了对DEV pUL13的理解。综上所述，这些结果提供了关于pUL13在DEV感染期间生物学功能的重要信息。
