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Role of influenza A virus NP acetylation on viral growth and replication

Author

Listed:
  • Sebastian Giese

    (Medical Center University of Freiburg
    University of Freiburg)

  • Kevin Ciminski

    (Medical Center University of Freiburg
    University of Freiburg)

  • Hardin Bolte

    (Medical Center University of Freiburg
    University of Freiburg
    University of Freiburg
    University of Freiburg)

  • Étori Aguiar Moreira

    (Medical Center University of Freiburg
    University of Freiburg
    University of Freiburg
    University of Freiburg)

  • Seema Lakdawala

    (University of Pittsburgh School of Medicine)

  • Zehan Hu

    (University of Freiburg
    University of Fribourg)

  • Quinnlan David

    (Medical Center University of Freiburg
    University of Freiburg)

  • Larissa Kolesnikova

    (Philipps-Universität Marburg)

  • Veronika Götz

    (Medical Center University of Freiburg
    University of Freiburg)

  • Yongxu Zhao

    (Institute of Health Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

  • Jörn Dengjel

    (University of Freiburg
    University of Fribourg)

  • Y. Eugene Chin

    (Institute of Health Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

  • Ke Xu

    (Key Laboratory of Molecular Virology & Immunology, Institut Pasteur of Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences)

  • Martin Schwemmle

    (Medical Center University of Freiburg
    University of Freiburg)

Abstract

Lysine acetylation is a post-translational modification known to regulate protein functions. Here we identify several acetylation sites of the influenza A virus nucleoprotein (NP), including the lysine residues K77, K113 and K229. Viral growth of mutant virus encoding K229R, mimicking a non-acetylated NP lysine residue, is severely impaired compared to wildtype or the mutant viruses encoding K77R or K113R. This attenuation is not the result of decreased polymerase activity, altered protein expression or disordered vRNP co-segregation but rather caused by impaired particle release. Interestingly, release deficiency is also observed mimicking constant acetylation at this site (K229Q), whereas virus encoding NP-K113Q could not be generated. However, mimicking NP hyper-acetylation at K77 and K229 severely diminishes viral polymerase activity, while mimicking NP hypo-acetylation at these sites has no effect on viral replication. These results suggest that NP acetylation at K77, K113 and K229 impacts multiple steps in viral replication of influenza A viruses.

Suggested Citation

  • Sebastian Giese & Kevin Ciminski & Hardin Bolte & Étori Aguiar Moreira & Seema Lakdawala & Zehan Hu & Quinnlan David & Larissa Kolesnikova & Veronika Götz & Yongxu Zhao & Jörn Dengjel & Y. Eugene Chin, 2017. "Role of influenza A virus NP acetylation on viral growth and replication," Nature Communications, Nature, vol. 8(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01112-3
    DOI: 10.1038/s41467-017-01112-3
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