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The Stalk and 1B Domains Are Required for Porcine Deltacoronavirus Helicase NSP13 to Separate the Double-Stranded Nucleic Acids, and the Deletion of the ZBD Impairs This Activity

文献类型： 外文期刊

作者： Wu, Chengcheng 1 ; Tao, Lihan 2 ; Zhou, Quanyong 1 ; Zhang, Fanfan 1 ; Zeng, Yanbing 1 ;

作者机构： 1.Jiangxi Acad Agr Sci, Inst Anim Husb & Vet Med, Nanchang 330200, Peoples R China

2.Jiangxi Agr Univ, Coll Anim Sci & Technol, Nanchang 330045, Peoples R China

关键词： porcine deltacoronavirus; helicase; domains; unwinding activity; ATPase activity

期刊名称：ANIMALS （ 影响因子：2.7； 五年影响因子：3.2 ）

ISSN： 2076-2615

年卷期： 2025 年 15 卷 6 期

页码：

收录情况： SCI

摘要： The nonstructural protein 13 (NSP13) of PDCoV is a highly conservative helicase and plays key roles in viral replication. NSP13 contains a zinc-binding domain (ZBD), a helical Stalk domain, a beta-barrel 1B domain, and a core helicase domain. However, the specific functions of these domains of PDCoV NSP13 remain largely unknown. Here, we expressed and purified the wild-type NSP13WT and various mutants with domain deletions, and the activities of these proteins were analyzed using multiple methods. We found that NSP13 Delta ZBD possessed the abilities to hydrolyze ATP and unwind double-stranded nucleic acids, but the unwinding efficiency was lower than that of NSP13WT. In contrast, NSP13 Delta ZBD-Stalk, NSP13 Delta 1B, and NSP13 Delta ZBD-Stalk-1B all lost their unwinding activity, but not their ATPase activity. These results revealed that the deletion of the ZBD impaired the unwinding activity of PDCoV helicase NSP13, and the Stalk and 1B domains were critical for NSP13 to separate the duplexes. The identification of the roles of each domain in this study was helpful to gain an in-depth understanding of the overall functions of helicase NSP13, providing a theoretical basis for the development of antiviral drugs targeting helicase.

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