The conformational changes of Zika virus methyltransferase upon converting SAM to SAH

Han Zhou; Fenghua Wang; Haofeng Wang; Cheng Chen; Tianqing Zhang; Xu Han; Deping Wang; Chen Chen; Chen Wu; Wei Xie; Zefang Wang; Lei Zhang; Lanfeng Wang; Haitao Yang

doi:10.18632/oncotarget.14780

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Research Papers:

The conformational changes of Zika virus methyltransferase upon converting SAM to SAH

Han Zhou, Fenghua Wang, Haofeng Wang, Cheng Chen, Tianqing Zhang, Xu Han, Deping Wang, Chen Chen, Chen Wu, Wei Xie, Zefang Wang, Lei Zhang, Lanfeng Wang and Haitao Yang _

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Oncotarget. 2017; 8:14830-14834. https://doi.org/10.18632/oncotarget.14780

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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 ^m7NGpppA^2′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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Research Papers:

The conformational changes of Zika virus methyltransferase upon converting SAM to SAH

Abstract