鸭瘟病毒pUL15在体外通过其C末端核酸酶结构域发挥非特异性切割活性。

Duck plague virus pUL15 performs a nonspecial cleavage activity through its C terminal nuclease domain in vitro.

作者信息

Yang Qiao, Liu Yiheng, Wang Mingshu, Wu Ying, Bin Tian, Ou Xumin, Mao Sai, Huang Juan, Sun Di, Gao Qun, Zhao Xinxin, Zhang Shaqiu, Chen Shun, Liu Mafeng, Zhu Dekang, Jia Renyong, Cheng Anchun

机构信息

Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, China; Key Laboratory of Animal Disease and Human Health of Sichuan Province, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, China; Avian Disease Research Center, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, Chengdu City, Sichuan 611130, China.

出版信息

Vet Microbiol. 2023 Apr;279:109671. doi: 10.1016/j.vetmic.2023.109671. Epub 2023 Jan 29.

DOI:10.1016/j.vetmic.2023.109671

PMID:36731190

Abstract

Duck plague virus (DPV), also known as anatid herpesvirus, is a double-stranded DNA virus and a member of α herpesvirus. DPV pUL15 is a homolog of herpes simplex virus 1 (HSV-1) pUL15, a terminase large subunit, and plays a key role in the cleavage and packaging of the viral concatemeric genome. However, the sequence similarity between DPV pUL15 and its homologs is low, and it is not sure if DPV pUL15 has the potential to cleave the concatemeric genome as same as its homologs. Here, we expressed the C terminal domain of DPV pUL15 to explore the nuclease function of DPV pUL15. The main results showed that (Ⅰ) DPV pUL15 C-terminal domain possesses nonspecific nuclease activity and lacks the DNA binding ability. (Ⅱ) DPV pUL15 nuclease activity needs to coordinate with divalent metal ions and tends to be more active at high temperatures. (Ⅲ) Even though the structure of DPV pUL15 nuclease domain is relatively conserved, the mutations of conserved amino acids on the nuclease domain do not significantly inhibit the nuclease activity.

摘要

鸭瘟病毒（DPV），也称为鸭疱疹病毒，是一种双链DNA病毒，属于α疱疹病毒属。DPV pUL15是单纯疱疹病毒1型（HSV-1）pUL15的同源物，pUL15是一种末端酶大亚基，在病毒串联基因组的切割和包装中起关键作用。然而，DPV pUL15与其同源物之间的序列相似性较低，尚不确定DPV pUL15是否具有与其同源物相同的切割串联基因组的潜力。在此，我们表达了DPV pUL15的C末端结构域，以探索DPV pUL15的核酸酶功能。主要结果表明：（Ⅰ）DPV pUL15 C末端结构域具有非特异性核酸酶活性，且缺乏DNA结合能力。（Ⅱ）DPV pUL15核酸酶活性需要与二价金属离子协同作用，并且在高温下更具活性。（Ⅲ）尽管DPV pUL15核酸酶结构域的结构相对保守，但核酸酶结构域上保守氨基酸的突变并未显著抑制核酸酶活性。