Giese, Sebastian Ciminski, Kevin Bolte, Hardin Moreira, Étori Aguiar Lakdawala, Seema Hu, Zehan David, Quinnlan Kolesnikova, Larissa Götz, Veronika Zhao, Yongxu Dengjel, Jörn Chin, Y. Eugene Xu, Ke Schwemmle, Martin 2017-11-02 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. application/pdf https://folia.unifr.ch/global/documents/306286 https://folia.unifr.ch/documents/306286/files/den_ria.pdf https://folia.unifr.ch/documents/306286/files/den_ria_sm.pdf eng info:eu-repo/semantics/altIdentifier/doi/10.1038/s41467-017-01112-3 info:eu-repo/semantics/openAccess License undefined Nature Communications. - 2017, vol. 8, no. 1, p. 1259 info:eu-repo/classification/udc/57 Role of influenza A virus NP acetylation on viral growth and replication http://purl.org/coar/resource_type/c_6501