ArticleScientific reports2017
Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin α isoforms.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 21 citations in OpenAlex.
- Divergent pathogenic mechanisms of influenza A and influenza B viruses.Archives of microbiology · 2026Review
- Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.Current opinion in structural biology · 2026Review
- Highly efficient expression of DNA-peptide conjugates in growth-arrested cells.Nature communications · 2026Article
- Isothermal Titration Calorimetry for Investigating Thermodynamics of Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Natural mutations in key NLS amino acids regulate nucleoplasmic shuttling and replication efficiency in PRRSV.Frontiers in microbiology · 2025Article
- Review
- Article
- Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism.Viruses · 2023Article
- Nuclear localisation sequences of chloride intracellular channels 1 and 4 facilitate nuclear import via interactions with import mediator importin-α: An empirical and theoretical perspective.Journal of molecular recognition : JMR · 2023Article
- Workshop on RanBP2/Nup358 and acute necrotizing encephalopathy.Nucleus (Austin, Tex.) · 2022Article
- Interaction of Influenza A Nucleoprotein with Host hnRNP-C Is Implicated in Viral Replication.International journal of molecular sciences · 2022Article
- Article
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- Differential recognition of canonical NF-κB dimers by Importin α3.Nature communications · 2022Article
- Differential Behaviours and Preferential Bindings of Influenza Nucleoproteins on Importins-α.Viruses · 2020Article
- High-Throughput MicroRNA Profiles of Permissive Madin-Darby Canine Kidney Cell Line Infected with Influenza B Viruses.Viruses · 2019Article
- The Extended C-Terminal Region of Influenza C Virus Nucleoprotein Is Important for Nuclear Import and Ribonucleoprotein Activity.Journal of virology · 2019Article
- The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NPScientific reports · 2019Article
- Review
- Correlation of CRM1-NES affinity with nuclear export activity.Molecular biology of the cell · 2018Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The influenza A virus nucleoprotein (NP) is an essential multifunctional protein that encapsidates the viral genome and functions as an adapter between the virus and the host cell machinery. NPs from all strains of influenza A viruses contain two nuclear localization signals (NLSs): a well-studied monopartite NLS1 and a less-characterized NLS2, thought to be bipartite. Through site-directed mutagenesis and functional analysis, we found that NLS2 is also monopartite and is indispensable for viral infection. Atomic structures of importin α bound to two variants of NLS2 revealed NLS2 primarily binds the major-NLS binding site of importin α, unlike NLS1 that associates with the minor NLS-pocket. Though peptides corresponding to NLS1 and NLS2 bind weakly to importin α, the two NLSs synergize in the context of the full length NP to confer high avidity for importin α7, explaining why the virus efficiently replicates in the respiratory tract that exhibits high levels of this isoform. This study, the first to functionally characterize NLS2, demonstrates NLS2 plays an important and unexpected role in influenza A virus infection. We propose NLS1 and NLS2 form a bipartite NLS in trans, which ensures high avidity for importin α7 while preventing non-specific binding to viral RNA.
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