期刊
EMBO JOURNAL
卷 36, 期 7, 页码 919-933出版社
WILEY
DOI: 10.15252/embj.201696241
关键词
crystal structure; methyltransferase; polymerase; RNA capping; Zika virus
资金
- Emergency Task-Force Project of the National Natural Science Foundation of China (NSFC) [81641001]
- China Ministry of Science and Technology National 973 Project [2014CB542503]
- Task-Force of ZIKV Research from the Chinese Academy of Sciences (CAS)
- National Key Plan for Scientific Research and Development of China [2016YFD0500300, 2016YFC1200305]
- Zika Special Project of the Ministry of Science and Technology Reform and Development Project
- Strategic Priority Research Program of CAS [XDB08020100]
- External Cooperation Program of CAS [153211KYSB20160001]
- Excellent Young Scientist Program from NSFC [81622031]
- Excellent Young Scientist Program of CAS
- Youth Innovation Promotion Association CAS [2015078, 2017117]
- NSFC Innovative Research Group Grant [81621091]
Zika virus (ZIKV) has emerged as major health concern, as ZIKV infection has been shown to be associated with microcephaly, severe neurological disease and possibly male sterility. As the largest protein component within the ZIKV replication complex, NS5 plays key roles in the life cycle and survival of the virus through its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains. Here, we present the crystal structures of ZIKV NS5 MTase in complex with an RNA cap analogue (m7GpppA) and the free NS5 RdRp. We have identified the conserved features of ZIKV NS5 MTase and RdRp structures that could lead to development of current antiviral inhibitors being used against flaviviruses, including dengue virus and West Nile virus, to treat ZIKV infection. These results should inform and accelerate the structure-based design of antiviral compounds against ZIKV.
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