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

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 (), Ke Xu () and Martin Schwemmle ()
Additional contact information
Sebastian Giese: Medical Center University of Freiburg
Kevin Ciminski: Medical Center University of Freiburg
Hardin Bolte: Medical Center University of Freiburg
Étori Aguiar Moreira: Medical Center University of Freiburg
Seema Lakdawala: University of Pittsburgh School of Medicine
Zehan Hu: University of Freiburg
Quinnlan David: Medical Center University of Freiburg
Larissa Kolesnikova: Philipps-Universität Marburg
Veronika Götz: Medical Center University of Freiburg
Yongxu Zhao: Institute of Health Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences
Jörn Dengjel: University of Freiburg
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

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-017-01112-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01112-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-01112-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().