ATPase and helicase activities of porcine epidemic diarrhea virus nsp13.
ATPase and helicase activities of porcine epidemic diarrhea virus nsp13.
复制标题
猪流行性腹泻病毒nsp 13的ATP酶和解旋酶活性。
DOI：
10.1016/j.vetmic.2021.109074
复制
发表时间：
2021-06
影响因子：
3.3
通讯作者：
Fang L
中科院分区：
文献类型：
--
作者：
Ren J;Ding Z;Fang P;Xiao S;Fang L
Porcine epidemic diarrhea virus (PEDV) is a reemerging Alphacoronavirus that causes lethal diarrhea in piglets. Coronavirus nonstructural protein 13 (nsp13) encodes helicase, which plays pivotal roles during viral replication by unwinding viral RNA. However, the biochemical characterization of PEDV nsp13 remains largely unknown. In this study, PEDV nsp13 was expressed in Escherichia coli and purified. The recombinant nsp13 possessed ATPase and helicase activities for binding and unwinding dsDNA/RNA substrates with 5′-overhangs, and Mg2+ and Mn2+ were critical for its ATPase and helicase activities. PEDV nsp13 also unwound dsDNA into ssDNA in the pH from 6.0–9.0, and used energy from all nucleoside triphosphates and deoxynucleoside triphosphates. Site-directed mutagenesis demonstrated that Lys289 (K289) of PEDV nsp13 was essential for its ATPase and helicase activities. These results provide new insights into the biochemical properties of PEDV nsp13, which is a potential target for developing antiviral drugs.
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