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Importance of tyrosine in the RNA-binding domain of human parainfluenza virus type 2 nucleoprotein for polymerase activity

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Abstract

The RNA genome of human parainfluenza virus type 2 (hPIV2) is encapsidated by nucleoprotein (NP) to act as a template for RNA synthesis. We examined the importance of individual amino acids in the RNA-binding domain of hPIV2 NP for polymerase activity using a mini-replicon assay. We showed that substitution of tyrosine at amino acid position 260, located in the RNA-binding pocket of NP, severely reduced polymerase activity. The aromatic side-chain of Y260 may be required for the formation of stable contacts between nucleotides and basic amino acids, thereby affecting promoter recognition by the viral polymerase.

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Acknowledgements

We acknowledge proofreading and editing by Benjamin Phillis, Clinical Study Support Center, Wakayama Medical University.

Funding

This work was supported by JSPS KAKENHI grant number 16K19143.

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Authors and Affiliations

  1. Department of Microbiology, School of Medicine, Wakayama Medical University, 811-1 Kimiidera, Wakayama, 641-8509, Japan

    Yusuke Matsumoto, Keisuke Ohta & Machiko Nishio

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  1. Yusuke Matsumoto
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  2. Keisuke Ohta
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  3. Machiko Nishio
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Correspondence to Machiko Nishio.

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Matsumoto, Y., Ohta, K. & Nishio, M. Importance of tyrosine in the RNA-binding domain of human parainfluenza virus type 2 nucleoprotein for polymerase activity. Arch Virol 164, 1851–1855 (2019). https://doi.org/10.1007/s00705-019-04240-x

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  • DOI: https://doi.org/10.1007/s00705-019-04240-x

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