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

第一作者: Luo, Dehua

作者: Luo, Dehua;Bai, Yuqing;Li, Qingling;Zheng, Yingge;Guo, Lijun;Wang, Daozhong;Chen, Xi;Wei, Dengguo;Luo, Dehua;Zheng, Yingge;Wei, Dengguo;Luo, Dehua;Zheng, Yingge;Wei, Dengguo;Luo, Dehua;Li, Qingling;Zheng, Yingge;Guo, Lijun;Wei, Dengguo;Luo, Dehua;Li, Qingling;Zheng, Yingge;Guo, Lijun;Wei, Dengguo;Wei, Dengguo;Wei, Dengguo

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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

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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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