Li Chunmei, Wang Mingshu, Cheng Anchun, Tian Bin, Huang Juan, Wu Ying, Yang Qiao, Gao Qun, Sun Di, Zhang Shaqiu, Ou Xumin, Mao Sai, Zhao Xinxin, Jia Renyong, Liu Mafeng, Chen Shun, Zhu Dekang
Avian Center of Disease Research, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang District, Chengdu City, Sichuan Povince 611130, PR China; Institute of Preventive Veterinary Medicine, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang District, Chengdu City, Sichuan Povince 611130, PR China; Key Laboratory of Animal Disease and Human Health of Sichuan Province, Wenjiang District, Chengdu City, Sichuan Povince 611130, PR China.
Institute of Preventive Veterinary Medicine, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang District, Chengdu City, Sichuan Povince 611130, PR China; Key Laboratory of Animal Disease and Human Health of Sichuan Province, Wenjiang District, Chengdu City, Sichuan Povince 611130, PR China.
Vet Microbiol. 2023 May;280:109707. doi: 10.1016/j.vetmic.2023.109707. Epub 2023 Feb 26.
Duck plague is a disease with high morbidity and mortality rates, and it causes great losses for the duck breeding industry. Duck plague virus (DPV) is the causative agent of duck plague, and DPV UL49.5 protein (pUL49.5) is homologue of glycoprotein N (gN), which is conserved in herpesviruses. UL49.5 homologues are known to be involved in processes such as immune escape, virus assembly, viral fusion, transporter associated with antigen processing (TAP) inhibition and degradation, and maturation and incorporation of glycoprotein M. However, few studies have focused on the role of gN in the early stage of virus infection cells. In this study, we determined that DPV pUL49.5 was distributed in the cytoplasm and colocalized with the endoplasmic reticulum (ER). Moreover, we found that DPV pUL49.5 was a virion component and nonglycosylated protein. To better explore its function, BAC-DPV-ΔUL49.5 was constructed, and its attachment was only approximately 25 % of the revertant virus. Additionally, the penetration ability of BAC-DPV-ΔUL49.5 has only reached 73 % of the revertant virus. The plaque sizes produced by the UL49.5-deleted virus were approximately 58 % smaller than those produced by the revertant virus. Deleting UL49.5 mainly resulted in attachment and cell-to-cell-spread defects. Taken together, these findings suggest important roles for DPV pUL49.5 in viral attachment, penetration and spread.
鸭瘟是一种发病率和死亡率都很高的疾病，给养鸭业造成了巨大损失。鸭瘟病毒（DPV）是鸭瘟的病原体，DPV UL49.5蛋白（pUL49.5）是糖蛋白N（gN）的同源物，在疱疹病毒中保守。已知UL49.5同源物参与免疫逃逸、病毒组装、病毒融合、与抗原加工相关的转运体（TAP）抑制和降解以及糖蛋白M的成熟和掺入等过程。然而，很少有研究关注gN在病毒感染细胞早期的作用。在本研究中，我们确定DPV pUL49.5分布在细胞质中，并与内质网（ER）共定位。此外，我们发现DPV pUL49.5是一种病毒体成分且为非糖基化蛋白。为了更好地探索其功能，构建了BAC-DPV-ΔUL49.5，其附着率仅约为回复病毒的25%。此外，BAC-DPV-ΔUL49.5的穿透能力仅达到回复病毒的73%。缺失UL49.5的病毒产生的蚀斑大小比回复病毒产生的蚀斑大小小约58%。删除UL49.5主要导致附着和细胞间传播缺陷。综上所述，这些发现表明DPV pUL49.5在病毒附着、穿透和传播中起重要作用。
