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2020 ; 35
(3
): 321-329
Nephropedia Template TP
gab.com Text
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English Wikipedia
SARS-Coronavirus-2 Nsp13 Possesses NTPase and RNA Helicase Activities That Can Be
Inhibited by Bismuth Salts
#MMPMID32500504
Shu T
; Huang M
; Wu D
; Ren Y
; Zhang X
; Han Y
; Mu J
; Wang R
; Qiu Y
; Zhang DY
; Zhou X
Virol Sin
2020[Jun]; 35
(3
): 321-329
PMID32500504
show ga
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.