ArticleNucleic acids research2025
Influenza a virus antiparallel helical nucleocapsid-like pseudo-atomic structure.
Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- LncRNA ckATP1A1-AS1 inhibits influenza A virus replication by mediating innate immune responses and suppressing viral nuclear import.Journal of virology · 2026Article
- 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
- Differences in RNA Binding Between Segmented and Non-Segmented Negative-Strand Virus Nucleocapsids.Microorganisms · 2026Article
- Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes.Science advances · 2026Article
- Assembly of the Linear Viral Nucleocapsid.Microorganisms · 2026Article
- 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
- Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.Science (New York, N.Y.) · 2025Article
- Influenza virus antagonizes self sensing by RIG-I to enhance viral replication.bioRxiv : the preprint server for biology · 2025Article
- Structure of the tilapia lake virus nucleoprotein bound to RNA.Nucleic acids research · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Influenza A viruses are responsible for human seasonal epidemics and severe animal pandemics with a risk of zoonotic transmission to humans. The viral segmented RNA genome is encapsidated by nucleoproteins (NP) and attached to the heterotrimeric polymerase, forming the viral ribonucleoproteins (vRNPs). Flexible helical vRNPs are central for viral transcription and replication. In this study, we present an advanced biological tool, the antiparallel helical RNP-like complex, assembled from recombinant N-terminally truncated NP and short synthetic RNA. The 3.0 Å cryo-electron microscopy structure details for the first time the whole RNA pathway across NP as well as NP-NP interactions that drive the antiparallel helical assembly accommodating major and minor grooves. Our findings show that the surface of the protein can harbour several conformations of the RNA, confirming that the number of nucleobases that binds to NP is not fixed, but ranges probably between 20 and 24. Taking all together, our data provide details to further understand the genome encapsidation and explain the inherent flexibility of influenza A virus vRNPs.
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Registered trials
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