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SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be Inhibited by Bismuth Salts
Shu,Ting1,2; Huang,Muhan2; Wu,Di2; Ren,Yujie2,3; Zhang,Xueyi2; Han,Yang1,2; Mu,Jingfang2; Wang,Ruibing4; Qiu,Yang1,2,5; Zhang,Ding Yu1; Zhou,Xi1,2,5
2020-06-01
Source PublicationVirologica Sinica
ISSN1674-0769
Volume35Issue:3Pages:321-329
Abstract

The ongoing outbreak of Coronavirus Disease 2019 (COVID-19) has become a global public health emergency. SARS-coronavirus-2 (SARS-CoV-2), the causative pathogen of COVID-19, is a positive-sense single-stranded RNA virus belonging to the family Coronaviridae. For RNA viruses, virus-encoded RNA helicases have long been recognized to play pivotal roles during viral life cycles by facilitating the correct folding and replication of viral RNAs. Here, our studies show that SARS-CoV-2-encoded nonstructural protein 13 (nsp13) possesses the nucleoside triphosphate hydrolase (NTPase) and RNA helicase activities that can hydrolyze all types of NTPs and unwind RNA helices dependently of the presence of NTP, and further characterize the biochemical characteristics of these two enzymatic activities associated with SARS-CoV-2 nsp13. Moreover, we found that some bismuth salts could effectively inhibit both the NTPase and RNA helicase activities of SARS-CoV-2 nsp13 in a dose-dependent manner. Thus, our findings demonstrate the NTPase and helicase activities of SARS-CoV-2 nsp13, which may play an important role in SARS-CoV-2 replication and serve as a target for antivirals.

KeywordAntiviral Target Helicase Nsp13 Ntpase Sars-coronavirus-2 (Sars-cov-2)
DOI10.1007/s12250-020-00242-1
URLView the original
Indexed BySCIE
WOS Research AreaVirology
WOS SubjectVirology
WOS IDWOS:000537953600001
Scopus ID2-s2.0-85085988704
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Cited Times [WOS]:48   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionUniversity of Macau
Corresponding AuthorZhang,Ding Yu; Zhou,Xi
Affiliation1.Center for Translational Medicine,Wuhan Jinyintan Hospital,Wuhan,430023,China
2.State Key Laboratory of Virology,Wuhan Institute of Virology,Center for Biosafety Mega-Science,Chinese Academy of Sciences,Wuhan,430071,China
3.Center for Precision Translational Medicine of Wuhan Institute of Virology and Guangzhou Women and Children’s Medical Center,Guangzhou Women and Children’s Medical Center,Guangzhou,510120,China
4.State Key Laboratory of Quality Research in Chinese Medicine,Institute of Chinese Medical Sciences,University of Macau,Macau SAR,999078,China
5.University of Chinese Academy of Sciences,Beijing,100049,China
Recommended Citation
GB/T 7714
Shu,Ting,Huang,Muhan,Wu,Di,et al. SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be Inhibited by Bismuth Salts[J]. Virologica Sinica,2020,35(3):321-329.
APA Shu,Ting,Huang,Muhan,Wu,Di,Ren,Yujie,Zhang,Xueyi,Han,Yang,Mu,Jingfang,Wang,Ruibing,Qiu,Yang,Zhang,Ding Yu,&Zhou,Xi.(2020).SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be Inhibited by Bismuth Salts.Virologica Sinica,35(3),321-329.
MLA Shu,Ting,et al."SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be Inhibited by Bismuth Salts".Virologica Sinica 35.3(2020):321-329.
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