Journal
NUCLEIC ACIDS RESEARCH
Volume 47, Issue 11, Pages 5837-5851Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkz340
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Funding
- Strategic Priority Research Program of Chinese Academy of Sciences [XDPB0301]
- National Science and Technology Major Project [2018ZX10101004]
- National Natural Science Foundation of China [31761130075, 31670161]
- Newton Advanced Fellowship from the Academy of Medical Sciences, UK [NAF005\1002]
- Science and Technology Bureau of Wuhan [2018060401011309]
- Advanced Customer Cultivation Project of Wuhan National Biosafety Laboratory [2018ACCP-MS11]
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Ebola virus (EBOV) is a non-segmented, negative-sense RNA virus (NNSV) in the family Filoviridae, and is recognized as one of the most lethal pathogens in the planet. For RNA viruses, cellular or virus-encoded RNA helicases play pivotal roles in viral life cycles by remodelling viral RNA structures and/or unwinding viral dsRNA produced during replication. However, no helicase or helicase-like activity has ever been found to associate with any NNSV-encoded proteins, and it is unknown whether the replication of NNSVs requires the participation of any viral or cellular helicase. Here, we show that despite of containing no conserved NTPase/helicase motifs, EBOV VP35 possesses the NTPase and helicase-like activities that can hydrolyse all types of NTPs and unwind RNA helices in an NTP-dependent manner, respectively. Moreover, guanidine hydrochloride, an FDA-approved compound and inhibitor of certain viral helicases, inhibited the NTPase and helicase-like activities of VP35 as well as the replication/transcription of an EBOV minigenome replicon in cells, highlighting the importance of VP35 helicase-like activity during EBOV life cycle. Together, our findings provide the first demonstration of the NTPase/helicase-like activity encoded by EBOV, and would foster our understanding of EBOV and NNSVs.
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