ArticleJournal of structural biology2017
Structural studies of influenza virus RNPs by electron microscopy indicate molecular contortions within NP supra-structures.
Article in Journal of structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.
What it found
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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
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- Meta-analysis of genomic characteristics for antiviral influenza defective interfering particle prioritization.NAR genomics and bioinformatics · 2025Pooled it
- Structure of the tilapia lake virus nucleoprotein bound to RNA.Nucleic acids research · 2025Article
- Analysis of polyclonal and monoclonal antibody to the influenza virus nucleoprotein in different oligomeric states.bioRxiv : the preprint server for biology · 2024Article
- Harnessing preexisting influenza virus-specific immunity increases antibody responses against SARS-CoV-2.Journal of virology · 2024Article
- Cryo-EM structure of influenza helical nucleocapsid reveals NP-NP and NP-RNA interactions as a model for the genome encapsidation.Science advances · 2023Article
- Article
- Sequential disruption of SPLASH-identified vRNA-vRNA interactions challenges their role in influenza A virus genome packaging.Nucleic acids research · 2023Article
- Article
- Inferring Protein Function in an Emerging Virus: Detection of the Nucleoprotein in Tilapia Lake Virus.Journal of virology · 2022Article
- Visualising Viruses.The Journal of general virology · 2022Review
- M2e-Based Influenza Vaccines with Nucleoprotein: A Review.Vaccines · 2021Review
- Structural insights into RNA polymerases of negative-sense RNA viruses.Nature reviews. Microbiology · 2021Review
- Modeling theBiomolecules · 2021Article
- Construction and identification of influenza plasmid pool imparting high yields to candidate vaccine viruses in Vero cell at low temperature.Journal of cellular and molecular medicine · 2020Article
- Structure and Function of the Influenza Virus Transcription and Replication Machinery.Cold Spring Harbor perspectives in medicine · 2020Review
- Selective flexible packaging pathways of the segmented genome of influenza A virus.Nature communications · 2020Article
- Structural insights into influenza A virus ribonucleoproteins reveal a processive helical track as transcription mechanism.Nature microbiology · 2020Article
- Negative-Stain Transmission Electron Microscopy of Molecular Complexes for Image Analysis by 2D Class Averaging.Current protocols in microbiology · 2019Article
- The structure of the nucleoprotein of Influenza D shows that all Orthomyxoviridae nucleoproteins have a similar NPScientific reports · 2019Article
- OVX836 a recombinant nucleoprotein vaccine inducing cellular responses and protective efficacy against multiple influenza A subtypes.NPJ vaccines · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Ribonucleoprotein (RNP) complexes of influenza viruses are composed of multiple copies of the viral nucleoprotein (NP) that can form filamentous supra-structures. RNPs package distinct viral genomic RNA segments of different lengths into pleomorphic influenza virions. RNPs also function in viral RNA transcription and replication. Different RNP segments have varying lengths, but all must be incorporated into virions during assembly and then released during viral entry for productive infection cycles. RNP structures serve varied functions in the viral replication cycle, therefore understanding their molecular organization and flexibility is essential to understanding these functions. Here, we show using electron tomography and image analyses that isolated RNP filaments are not rigid helical structures, but instead display variations in lengths, curvatures, and even tolerated kinks and local unwinding. Additionally, we observed NP rings within RNP preparations, which were commonly composed of 5, 6, or 7 NP molecules and were of similar widths to filaments, suggesting plasticity in NP-NP interactions mediate RNP structural polymorphism. To demonstrate that NP alone could generate rings of variable oligomeric state, we performed 2D single particle image analysis on recombinant NP and found that rings of 4 and 5 protomers dominated, but rings of all compositions up to 7 were directly observed with variable frequency. This structural flexibility may be needed as RNPs carry out the interactions and conformational changes required for RNP assembly and genome packaging as well as virus uncoating.
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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.