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Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis

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  • Wei Xu

    (Washington University School of Medicine
    Present address: State Key Lab of Respiratory Disease, Guangzhou Eighth People’s Hospital, Guangzhou Medical University, Guangzhou 510060, China)

  • Priya Luthra

    (Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University)

  • Chao Wu

    (Washington University School of Medicine)

  • Jyoti Batra

    (Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University)

  • Daisy W. Leung

    (Washington University School of Medicine)

  • Christopher F. Basler

    (Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University)

  • Gaya K. Amarasinghe

    (Washington University School of Medicine)

Abstract

Ebola virus (EBOV) is an enveloped negative-sense RNA virus that causes sporadic outbreaks with high case fatality rates. Ebola viral protein 30 (eVP30) plays a critical role in EBOV transcription initiation at the nucleoprotein (eNP) gene, with additional roles in the replication cycle such as viral assembly. However, the mechanistic basis for how eVP30 functions during the virus replication cycle is currently unclear. Here we define a key interaction between eVP30 and a peptide derived from eNP that is important to facilitate interactions leading to the recognition of the RNA template. We present crystal structures of the eVP30 C-terminus in complex with this eNP peptide. Functional analyses of the eVP30–eNP interface identify residues that are critical for viral RNA synthesis. Altogether, these results support a model where the eVP30–eNP interaction plays a critical role in transcription initiation and provides a novel target for the development of antiviral therapy.

Suggested Citation

  • Wei Xu & Priya Luthra & Chao Wu & Jyoti Batra & Daisy W. Leung & Christopher F. Basler & Gaya K. Amarasinghe, 2017. "Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis," Nature Communications, Nature, vol. 8(1), pages 1-11, August.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15576
    DOI: 10.1038/ncomms15576
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    Cited by:

    1. Filip Mihalič & Caroline Benz & Eszter Kassa & Richard Lindqvist & Leandro Simonetti & Raviteja Inturi & Hanna Aronsson & Eva Andersson & Celestine N. Chi & Norman E. Davey & Anna K. Överby & Per Jemt, 2023. "Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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