ArticleStructure (London, England : 1993)2015
Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed.
- Divergent pathogenic mechanisms of influenza A and influenza B viruses.Archives of microbiology · 2026Review
- Structures of Nicotiana benthamiana importin-α1 complexes reveal mechanisms for plant virus NLS recognition.The Plant journal : for cell and molecular biology · 2026Article
- Structural Insights Into the Nuclear Import of Gallid Alphaherpesvirus 1 Large Tegument Protein.MicrobiologyOpen · 2026Article
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- Structural Insights Into the Nuclear Import of Marek's Disease Virus Large Tegument Protein.Advances in virology · 2026Article
- Computational Structural Analysis Predicts Host-Range Promiscuity and Antiviral Resistance in North American H5N1 Lineages.Computational and structural biotechnology journal · 2026Article
- Ran modulates allosteric crosstalk between importin β surfaces.Nature communications · 2025Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Structural Insights into the Nuclear Import of Haliotid Herpesvirus 1 Large Tegument Protein Homologue.Viruses · 2025Article
- Review
- Article
- Structural basis for nuclear import of bat adeno-associated virus capsid protein.The Journal of general virology · 2024Article
- A functional and structural comparative analysis of large tumor antigens reveals evolution of different importin α-dependent nuclear localization signals.Protein science : a publication of the Protein Society · 2024Article
- Nuclear localization signal-tagged systems: relevant nuclear import principles in the context of current therapeutic design.Chemical Society reviews · 2024Review
- Toxoplasma Gondii Importin α Shows Weak Auto-Inhibition.The protein journal · 2023Article
- Henipavirus Matrix Protein Employs a Non-Classical Nuclear Localization Signal Binding Mechanism.Viruses · 2023Article
- The ubiquitination landscape of the influenza A virus polymerase.Nature communications · 2023Article
- Article
- Recognition of the TDP-43 nuclear localization signal by importin α1/β.Cell reports · 2022Article
- G Protein Subunit β1 Facilitates Influenza A Virus Replication by Promoting the Nuclear Import of PB2.Journal of virology · 2022Article
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5 authors.
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Abstract
Influenza A virus polymerase subunit PB2 is a major virulence determinant implicated in pathogenicity and host adaptation. During cross-species virus transfer from avian to mammalian cells, PB2 switches specificity from importin α3 to α7. This specificity is not recapitulated in vitro, where PB2 binds all importin α isoforms with comparably high affinity. In this study, we investigated the structure, conformational dynamics, and autoinhibition of importin α isoforms 1, 3, and 7 in complex with PB2. Our data suggest that association of PB2 with α3 and α7 is favored by reduced autoinhibition of these isoforms and by the unique structure of the nuclear localization signal (NLS) domain of PB2. We propose that by recruiting importin α3 or α7 in the absence of importin β, PB2 reduces the complexity of adaptor-mediated import to a pseudo-bimolecular reaction, thereby acquiring a kinetic advantage over classical NLS cargos, which form an import complex only when importin α and β are simultaneously available.
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