ArticleNature microbiology2020
Structural insights into influenza A virus ribonucleoproteins reveal a processive helical track as transcription mechanism.
Article in Nature microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 67 citations in OpenAlex.
- Nucleocapsid-like cryo-EM structure of influenza B virus.PLoS pathogens · 2026Article
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026Article
- Coupling of polymerase-nucleoprotein-RNA in an influenza virus mini ribonucleoprotein complex.Nature communications · 2025Article
- Visualizing influenza A virus assembly by in situ cryo-electron tomography.Nature communications · 2025Article
- High-throughput single-virion DNA-PAINT reveals structural diversity, cooperativity, and flexibility during selective packaging in influenza.Nucleic acids research · 2025Article
- Implications of morphological variation in influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025Review
- Viral polymerase-host interaction analysis reveals that the association between avian NUP93 and PB1 promotes H5N6 avian influenza virus replication.Microbiology spectrum · 2025Article
- Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.Science (New York, N.Y.) · 2025Article
- Structure of the tilapia lake virus nucleoprotein bound to RNA.Nucleic acids research · 2025Article
- Influenza a virus antiparallel helical nucleocapsid-like pseudo-atomic structure.Nucleic acids research · 2025Article
- Purification and Ultramicroscopic Observation of the Influenza A Virus Ribonucleoprotein Complex.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Dominant HPAIV H5N1 genotypes of Germany 2021/2022 are linked to high virulence in Pekin ducklings.Npj viruses · 2024Article
- Analysis of polyclonal and monoclonal antibody to the influenza virus nucleoprotein in different oligomeric states.bioRxiv : the preprint server for biology · 2024Article
- A Fluorogenic Pseudoinfection Assay to Probe Transfer and Distribution of Influenza Viral Contents to Target Vesicles.Analytical chemistry · 2024Article
- Conformational Dynamics of Influenza A Virus Ribonucleoprotein Complexes during RNA Synthesis.ACS nano · 2024Article
- Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.Nature communications · 2024Article
- Structural Impact of the Interaction of the Influenza A Virus Nucleoprotein with Genomic RNA Segments.Viruses · 2024Article
- Review
- Semantic segmentation-based detection algorithm for challenging cryo-electron microscopy RNP samples.Frontiers in molecular biosciences · 2024Article
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Authors and funding
9 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The influenza virus genome consists of eight viral ribonucleoproteins (vRNPs), each consisting of a copy of the polymerase, one of the genomic RNA segments and multiple copies of the nucleoprotein arranged in a double helical conformation. vRNPs are macromolecular machines responsible for messenger RNA synthesis and genome replication, that is, the formation of progeny vRNPs. Here, we describe the structural basis of the transcription process. The mechanism, which we call the 'processive helical track', is based on the extreme flexibility of the helical part of the vRNP that permits a sliding movement between both antiparallel nucleoprotein-RNA strands, thereby allowing the polymerase to move over the genome while bound to both RNA ends. Accordingly, we demonstrate that blocking this movement leads to inhibition of vRNP transcriptional activity. This mechanism also reveals a critical role of the nucleoprotein in maintaining the double helical structure throughout the copying process to make the RNA template accessible to the polymerase.
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