ArticleNature communications2024
Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Article
- Genome-informed structural analysis of polymerase and glycoprotein adaptation in H5N1 clade 2.3.4.4b.Journal of veterinary science · 2026Article
- 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
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- The activation of the metabolic oxaloacetate-pyruvate axis restores influenza A virus replication during impaired glycolysis.Virology journal · 2026Article
- On the brink of emergence: an evolutionary approach to Influenza A virus H5N1 isolated from humans.Virus research · 2026Article
- Historical Pandemic and Contemporary Influenza A Viruses Reveal PB2 M631L as a Convergent Adaptation to Human ANP32.Microorganisms · 2026Article
- The emergence and molecular evolution of H5N1 influenza viruses in United States dairy cattle.bioRxiv : the preprint server for biology · 2026Article
- Human Influenza Virus Infection: A Focus on Key Host Determinants Linked to Clinical Disease Severity.Viruses · 2026Review
- Adaptation differences and mechanisms of influenza viruses to ANP32 proteins across species.Journal of virology · 2026Review
- Enhanced genome replication activity of pandemic H1N1 influenza A virus through PA mutations.Journal of virology · 2026Article
- Regulatory hotspot on the influenza A virus polymerase revealed through the structure of the NEP-polymerase complex.Science advances · 2026Article
- Polymerase mutations underlie early adaptation of H5N1 influenza virus to dairy cattle and other mammals.Nature communications · 2026Article
- Evolution, spread and impact of highly pathogenic H5 avian influenza A viruses.Nature reviews. Microbiology · 2026Review
- 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
- Emergence of mammalian-adaptive PB2 mutations enhances polymerase activity and pathogenicity of cattle-derived H5N1 influenza A virus.Nature communications · 2025Article
- Coupling of polymerase-nucleoprotein-RNA in an influenza virus mini ribonucleoprotein complex.Nature communications · 2025Article
- LAIV Mutations Selectively Alter Influenza Viral RNA Polymerase Function, Favoring Transcription over Genome Synthesis.Viruses · 2025Article
- Recent advances in avian influenza virus: Molecular pathogenesis, emerging strains, and next-generation therapeutics.World journal of virology · 2025Review
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9 authors.
Funding
Abstract
Avian influenza A viruses (IAVs) pose a public health threat, as they are capable of triggering pandemics by crossing species barriers. Replication of avian IAVs in mammalian cells is hindered by species-specific variation in acidic nuclear phosphoprotein 32 (ANP32) proteins, which are essential for viral RNA genome replication. Adaptive mutations enable the IAV RNA polymerase (FluPolA) to surmount this barrier. Here, we present cryo-electron microscopy structures of monomeric and dimeric avian H5N1 FluPolA with human ANP32B. ANP32B interacts with the PA subunit of FluPolA in the monomeric form, at the site used for its docking onto the C-terminal domain of host RNA polymerase II during viral transcription. ANP32B acts as a chaperone, guiding FluPolA towards a ribonucleoprotein-associated FluPolA to form an asymmetric dimer-the replication platform for the viral genome. These findings offer insights into the molecular mechanisms governing IAV genome replication, while enhancing our understanding of the molecular processes underpinning mammalian adaptations in avian-origin FluPolA.
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