ArticleMolecular cell2016
Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains.
Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.
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Who cites it
96 citing papers in PubMed, 150 citations in OpenAlex.
- Mapping in-cell protein contact sites reveals hijacking of paraspeckles during influenza A virus infection.Nature microbiology · 2026Article
- Divergent pathogenic mechanisms of influenza A and influenza B viruses.Archives of microbiology · 2026Review
- Hybrid Approach to Protein-Protein Complex Affinity Prediction Based on Language Models and Molecular Dynamics.International journal of molecular sciences · 2026Article
- Anti-influenza drugs targeting trimeric RNA polymerase complex: From development to clinics.Acta pharmaceutica Sinica. B · 2026Review
- From neuraminidase inhibitors to novel mechanisms: expanding therapeutic strategies against influenza.Frontiers in cellular and infection microbiology · 2026Review
- Cryo-EM structure of influenza polymerase bound to the cRNA promoter provides insights into the mechanism of viral replication.Communications biology · 2025Article
- A two-step mechanism for RIG-I activation by influenza virus mvRNAs.Science advances · 2025Article
- Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.Science (New York, N.Y.) · 2025Article
- Structural insights into the RNA-dependent RNA polymerase complexes from highly pathogenic Marburg and Ebola viruses.Nature communications · 2025Article
- Influenza A virus NS2 protein acts on vRNA-resident polymerase to drive the transcription to replication switch.Nucleic acids research · 2025Article
- Understanding Influenza.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.Nature communications · 2024Article
- Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.Nature communications · 2024Article
- Review
- The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome.Nature communications · 2024Article
- Twenty natural amino acid substitution screening at the last residue 121 of influenza A virus NS2 protein reveals the critical role of NS2 in promoting virus genome replication by coordinating with viral polymerase.Journal of virology · 2024Article
- Structural and functional analysis of the minimal orthomyxovirus-like polymerase of Tilapia Lake Virus from the highly diverged Amnoonviridae family.Nature communications · 2023Article
- Multivalent Dynamic Colocalization of Avian Influenza Polymerase and Nucleoprotein by Intrinsically Disordered ANP32A Reveals the Molecular Basis of Human Adaptation.Journal of the American Chemical Society · 2023Article
- An intermediate state allows influenza polymerase to switch smoothly between transcription and replication cycles.Nature structural & molecular biology · 2023Article
- Phosphorylation of the PA subunit of influenza polymerase at Y393 prevents binding of the 5'-termini of RNA and polymerase function.Scientific reports · 2023Article
36 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)-containing domain translocates ∼90 Å to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.
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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.