Role of influenza A virus NP acetylation on viral growth and replication
Post-translational modifications of influenza A virus proteins can regulate virus replication, but the effect of nucleoprotein (NP) acetylation is not known. Here, Giese et al. identify four NP lysine residues that are acetylated in infected cells and study their role in polymerase activity and viri...
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2017-11-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-01112-3 |
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doaj-6ed0845914b74bd29b55b944319e93732021-05-11T07:43:34ZengNature Publishing GroupNature Communications2041-17232017-11-018111110.1038/s41467-017-01112-3Role of influenza A virus NP acetylation on viral growth and replicationSebastian Giese0Kevin Ciminski1Hardin Bolte2Étori Aguiar Moreira3Seema Lakdawala4Zehan Hu5Quinnlan David6Larissa Kolesnikova7Veronika Götz8Yongxu Zhao9Jörn Dengjel10Y. Eugene Chin11Ke Xu12Martin Schwemmle13Institute of Virology, Medical Center University of FreiburgInstitute of Virology, Medical Center University of FreiburgInstitute of Virology, Medical Center University of FreiburgInstitute of Virology, Medical Center University of FreiburgDepartment of Microbiology and Molecular Genetics, University of Pittsburgh School of MedicineDepartment of Dermatology, Medical Center, University of FreiburgInstitute of Virology, Medical Center University of FreiburgInstitute of Virology, Philipps-Universität MarburgInstitute of Virology, Medical Center University of FreiburgInstitute of Health Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of SciencesDepartment of Dermatology, Medical Center, University of FreiburgInstitute of Health Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of SciencesKey Laboratory of Molecular Virology & Immunology, Institut Pasteur of Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of SciencesInstitute of Virology, Medical Center University of FreiburgPost-translational modifications of influenza A virus proteins can regulate virus replication, but the effect of nucleoprotein (NP) acetylation is not known. Here, Giese et al. identify four NP lysine residues that are acetylated in infected cells and study their role in polymerase activity and virion release.https://doi.org/10.1038/s41467-017-01112-3 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
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 Martin Schwemmle |
spellingShingle |
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 Martin Schwemmle Role of influenza A virus NP acetylation on viral growth and replication Nature Communications |
author_facet |
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 Martin Schwemmle |
author_sort |
Sebastian Giese |
title |
Role of influenza A virus NP acetylation on viral growth and replication |
title_short |
Role of influenza A virus NP acetylation on viral growth and replication |
title_full |
Role of influenza A virus NP acetylation on viral growth and replication |
title_fullStr |
Role of influenza A virus NP acetylation on viral growth and replication |
title_full_unstemmed |
Role of influenza A virus NP acetylation on viral growth and replication |
title_sort |
role of influenza a virus np acetylation on viral growth and replication |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2017-11-01 |
description |
Post-translational modifications of influenza A virus proteins can regulate virus replication, but the effect of nucleoprotein (NP) acetylation is not known. Here, Giese et al. identify four NP lysine residues that are acetylated in infected cells and study their role in polymerase activity and virion release. |
url |
https://doi.org/10.1038/s41467-017-01112-3 |
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