Zika virus nonstructural protein 5 residue R681 is critical for dimer formation and enzymatic activity

FEBS Letters

article

Wuan-Geok Saw¹  Kitti Wing-Ki Chan²  Subhash G. Vasudevan²  Gerhard Grüber¹ 

[1] Nanyang Technological University, School of Biological Sciences;Program in Emerging Infectious Diseases, Duke-NUS Medical School;Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore

关键词: flavivirus;    methyltransferase;    nonstructural proteins;    RNAdependent RNA polymerase;    Zika;   

DOI  :  10.1002/1873-3468.13437

来源: John Wiley & Sons Ltd.

【 摘 要 】

Zika virus (ZIKV) relies on its nonstructural protein 5 (NS5) for capping and synthesis of the viral RNA. Recent small-angle X-ray scattering (SAXS) data of recombinant ZIKV NS5 protein showed that it is dimeric in solution. Here, we present insights into the critical residues responsible for its dimer formation. SAXS studies of the engineered ZIKV NS5 mutants revealed that R681A mutation on NS5 (NS5R681A) disrupts the dimer formation and affects its RNA-dependent RNA polymerase activity as well as the subcellular localization of NS5R681A in mammalian cells. The critical residues involved in the dimer arrangement of ZIKV NS5 are discussed, and the data provide further insights into the diversity of flaviviral NS5 proteins in terms of their propensity for oligomerization.

【 授权许可】

Unknown