Research Papers:
The conformational changes of Zika virus methyltransferase upon converting SAM to SAH
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Abstract
Han Zhou1,2,*, Fenghua Wang1,*, Haofeng Wang1,*, Cheng Chen1, Tianqing Zhang1, Xu Han1, Deping Wang1, Chen Chen1, Chen Wu1, Wei Xie1, Zefang Wang1, Lei Zhang1, Lanfeng Wang3, Haitao Yang1,2
1School of Life Sciences, Tianjin University, Tianjin 300072, China
2Tianjin International Joint Academy of Biotechnology and Medicine, Tianjin 300457, China
3Key Laboratory of Molecular Virology and Immunology, Institute Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai 200031, China
*These authors contributed equally to this work
Correspondence to:
Haitao Yang, email: [email protected]
Lanfeng Wang, email: [email protected]
Keywords: Zika virus, methyltransferase, crystal structure, SAH, antiviral drug development
Received: November 16, 2016 Accepted: January 11, 2017 Published: January 21, 2017
ABSTRACT
An outbreak of Zika virus (ZIKV) infection has been reported in South and Central America and the Caribbean. Neonatal microcephaly potentially associated with ZIKV infection has already caused a public health emergency of international concern. Currently, there are no clinically effective vaccines or antiviral drugs available to treat ZIKV infection. The methyltransferase domain (MTase) of ZIKV nonstructural protein 5 (NS5) can sequentially methylate guanine N-7 and ribose 2′-O to form m7NGpppA2′Om cap structure in the new RNA transcripts. This methylation step is crucial for ZIKV replication cycle and evading the host immune system, making it a target for drug design. Here, we present the 1.76 Å crystal structure of ZIKV MTase in complex with the byproduct SAH, providing insight into the elegant methylation process, which will benefit the following antiviral drug development.
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