ArticleJournal of virology2010
Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 95 citations in OpenAlex.
- The genetic driver of Acute Necrotizing Encephalopathy, RANBP2, regulates the inflammatory response to Influenza A virus infection.Nature communications · 2026Article
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Filament formation and NAD processing by noncanonical human FAM118 sirtuins.Nature structural & molecular biology · 2025Article
- Design, synthesis and biological evaluation of a novel class of indazole-containing compounds with potent anti-influenza activities targeting the PA-PB1 interface.Acta pharmaceutica Sinica. B · 2025Article
- The PB2 I714S mutation influenced mammalian adaptation of the H3N2 canine influenza virus by interfering with nuclear import efficiency and RNP complex assembly.Emerging microbes & infections · 2024Article
- Antiviral activity of intracellular nanobodies targeting the influenza virus RNA-polymerase core.PLoS pathogens · 2024Article
- G Protein Subunit β1 Facilitates Influenza A Virus Replication by Promoting the Nuclear Import of PB2.Journal of virology · 2022Article
- Article
- Strategies for fighting pandemic virus infections: Integration of virology and drug delivery.Journal of controlled release : official journal of the Controlled Release Society · 2022Review
- Nucleoporin 85 interacts with influenza A virus PB1 and PB2 to promote its replication by facilitating nuclear import of ribonucleoprotein.Frontiers in microbiology · 2022Article
- Host Cell Factors That Interact with Influenza Virus Ribonucleoproteins.Cold Spring Harbor perspectives in medicine · 2021Review
- Multicolor fluorescence fluctuation spectroscopy in living cells via spectral detection.eLife · 2021Article
- Light modulates important physiological features of Ralstonia pseudosolanacearum during the colonization of tomato plants.Scientific reports · 2021Article
- Number and Brightness Analysis: Visualization of Protein Oligomeric State in Living Cells.Advances in experimental medicine and biology · 2021Article
- Eukaryotic Translation Elongation Factor 1 Delta Inhibits the Nuclear Import of the Nucleoprotein and PA-PB1 Heterodimer of Influenza A Virus.Journal of virology · 2020Article
- A PB1-K577E Mutation in H9N2 Influenza Virus Increases Polymerase Activity and Pathogenicity in Mice.Viruses · 2018Article
- Quantifying membrane protein oligomerization with fluorescence cross-correlation spectroscopy.Methods (San Diego, Calif.) · 2018Article
- Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement.Frontiers in immunology · 2018Review
- Role of the PB2 627 Domain in Influenza A Virus Polymerase Function.Journal of virology · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular transport and assembly of the subunits of the heterotrimeric RNA-dependent RNA polymerase constitute a key component of the replication cycle of influenza virus. Recent results suggest that efficient polymerase assembly is a limiting factor in the viability of reassortant viruses. The mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, is still controversial, yet it is clearly of great significance in understanding the emergence of new strains with pandemic potential. In this study, we systematically investigated the interactions between the polymerase subunits and their localization in living cells by fluorescence cross-correlation spectroscopy (FCCS) and quantitative confocal microscopy. We could show that PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus separately from PB2. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase. Photon-counting histogram analysis revealed that trimeric polymerase complexes can form higher-order oligomers in the nucleus. We furthermore demonstrate that impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm. Taken together, our results demonstrate which of the previously discussed influenza virus polymerase transport models operates in live cells. Our study sheds light on the interplay between the nuclear import of the subunits and the assembly of the influenza virus polymerase and provides a methodological framework to analyze the effects of different host range mutations in the future.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.