Host helicase DHX36 inhibits pseudorabies virus proliferation by unwinding the G-quadruplex in the 3'UTR of IE180
文献类型： 外文期刊
作者： Luo, Dehua 1 ; Bai, Yuqing 1 ; Li, Qingling 1 ; Zheng, Yingge 1 ; Guo, Lijun 1 ; Wang, Daozhong 1 ; Chen, Xi 1 ; Wei, Dengguo 1 ;
作者机构： 1.Huazhong Agr Univ, Coll Vet Med, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
2.Huazhong Agr Univ, Hubei Hongshan Lab, Wuhan 430070, Peoples R China
3.Huazhong Agr Univ, Interdisciplinary Sci Inst, Wuhan 430070, Peoples R China
4.Huazhong Agr Univ, Natl Reference Lab Vet Drug Residues HZAU, Coll Vet Med, Wuhan 430070, Peoples R China
5.Huazhong Agr Univ, MAO Key Lab Detect Vet Drug Residues, Hubei Hongshan Lab, Wuhan 430070, Peoples R China
6.Huazhong Agr Univ, Shenzhen Inst Nutr & Hlth, Shenzhen 518000, Peoples R China
7.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Guangdong Lab Lingnan Modern Agr, Shenzhen Branch,Genome Anal Lab,Minist Agr, Shenzhen 518000, Peoples R China
关键词： Pseudorabies virus; G-quadruplex; DHX36; IE180; Viral proliferation
期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：2.7； 五年影响因子：2.9 ）
ISSN： 0378-1135
年卷期： 2025 年 306 卷
页码：
收录情况： SCI
摘要： The balance between proliferation and persistence of pseudorabies virus (PRV) in the host is crucial for its longterm survival. Understanding the mechanisms that regulate viral survival may offer new strategies for disease prevention and control. The immediate-early gene 180 (IE180) is essential for PRV replication, and we previously identified a G-quadruplex (PQS18-1) located in the 3' untranslated region (3'UTR) of IE180 that enhances its expression and promotes viral replication. However, the mechanisms by which this G-quadruplex is unwound and contributes to immune evasion remain unclear. In this study, we identified the host helicase DHX36 as a binding partner of PQS18-1 through RNA pull-down assays. Both in vitro and cellular experiments demonstrated that DHX36 destabilizes the G-quadruplex, thereby suppressing gene expression and regulating PRV replication. Our findings reveal a novel host-virus interaction mechanism involving G-quadruplex structures and helicase activity, which may offer new targets for therapeutic intervention.
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