ArticleEMBO reports2024
NS2 induces an influenza A RNA polymerase hexamer and acts as a transcription to replication switch.
Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- Live-cell single-vRNP imaging identifies viral gene expression signatures that shape influenza infection heterogeneity.Cell systems · 2026Article
- Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex.Science advances · 2026Article
- Influenza virus research in an era of emerging respiratory threats: host-virus interactions, surveillance technologies, antiviral management and resistance, and vaccine preparedness.Frontiers in microbiology · 2026Review
- The cellular activating protein-1 cFos regulates influenza A virus replication.The Journal of general virology · 2026Article
- LAIV Mutations Selectively Alter Influenza Viral RNA Polymerase Function, Favoring Transcription over Genome Synthesis.Viruses · 2025Article
- Analysis of NS2-dependent effects on influenza PB1 segment extends replication requirements beyond the canonical promoter.Nature communications · 2025Article
- Influenza A virus NS2 protein acts on vRNA-resident polymerase to drive the transcription to replication switch.Nucleic acids research · 2025Article
Corrections and comments
- Erratum issued
Authors and funding
15 authors.
Funding
Abstract
Genome transcription and replication of influenza A virus (FluA), catalyzed by viral RNA polymerase (FluAPol), are delicately controlled across the virus life cycle. A switch from transcription to replication occurring at later stage of an infection is critical for progeny virion production and viral non-structural protein NS2 has been implicated in regulating the switch. However, the underlying regulatory mechanisms and the structure of NS2 remained elusive for years. Here, we determine the cryo-EM structure of the FluAPol-NS2 complex at ~3.0 Å resolution. Surprisingly, three domain-swapped NS2 dimers arrange three symmetrical FluPol dimers into a highly ordered barrel-like hexamer. Further structural and functional analyses demonstrate that NS2 binding not only hampers the interaction between FluAPol and the Pol II CTD because of steric conflicts, but also impairs FluAPol transcriptase activity by stalling it in the replicase conformation. Moreover, this is the first visualization of the full-length NS2 structure. Our findings uncover key molecular mechanisms of the FluA transcription-replication switch and have implications for the development of antivirals.
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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.