ArticleNature communications2020
Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Structures of Nicotiana benthamiana importin-α1 complexes reveal mechanisms for plant virus NLS recognition.The Plant journal : for cell and molecular biology · 2026Article
- 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
- Molecular Characterization of Highly Pathogenic Avian Influenza H5N1 Viruses Circulating in Bulgaria During 2024-2025: Evidence for Hidden Circulation and Zoonotic Risk Markers.International journal of molecular sciences · 2026Article
- Polymerase mutations underlie early adaptation of H5N1 influenza virus to dairy cattle and other mammals.Nature communications · 2026Article
- Identification and characterization of PB2 mutations associated with mammalian adaptation of highly pathogenic H5N1 avian influenza viruses.Frontiers in microbiology · 2026Article
- Identification of amino acid residues in polymerase PB2 responsible for differential replication and pathogenicity of avian influenza virus H5N1 isolated from human and cattle in Texas, US.Emerging microbes & infections · 2025Article
- An emerging PB2-627 polymorphism increases the zoonotic risk of avian influenza virus by overcoming ANP32 host restriction in mammalian and avian hosts.Journal of virology · 2025Article
- Avian Influenza Virus: Comparative Evolution as the Key for Predicting Host Tropism Expansion.Pathogens (Basel, Switzerland) · 2025Article
- E627V mutation in PB2 protein promotes the mammalian adaptation of novel H10N3 avian influenza virus.Veterinary research · 2025Article
- Evolutionary Pro-To-Thr Mutation in the Intrinsically Disordered Domain of ANP32 Family Members Modulates Their Target Binding Modes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.Nature communications · 2024Article
- Functional Analysis of GRSF1 in the Nuclear Export and Translation of Influenza A Virus mRNAs.Viruses · 2024Article
- Unravelling the interaction between Influenza virus and the nuclear pore complex: insights into viral replication and host immune response.Virusdisease · 2024Review
- PB2 residue 473 contributes to the mammalian virulence of H7N9 avian influenza virus by modulating viral polymerase activity via ANP32A.Journal of virology · 2024Article
- BAG6 inhibits influenza A virus replication by inducing viral polymerase subunit PB2 degradation and perturbing RdRp complex assembly.PLoS pathogens · 2024Article
- Review
- The host RNA polymerase II C-terminal domain is the anchor for replication of the influenza virus genome.Nature communications · 2024Article
- Editorial: Exploring genetic characteristics and molecular mechanisms of host adaptation of viruses with artificial intelligence (AI) or (and) biological (BIO) approaches.Frontiers in cellular and infection microbiology · 2024Article
- Pathogenicity and virulence of influenza.Virulence · 2023Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Adaptive mutants are localised on the C-terminal (627-NLS) domains of the PB2 subunit. In particular, mutation of PB2 residue 627 from E to K rescues polymerase activity in mammalian cells. A host transcription regulator ANP32A, comprising a long C-terminal intrinsically disordered domain (IDD), is responsible for this adaptation. Human ANP32A IDD lacks a 33 residue insertion compared to avian ANP32A, and this deletion restricts avian influenza polymerase activity. We used NMR to determine conformational ensembles of E627 and K627 forms of 627-NLS of PB2 in complex with avian and human ANP32A. Human ANP32A IDD transiently binds to the 627 domain, exploiting multivalency to maximise affinity. E627 interrupts the polyvalency of the interaction, an effect compensated by an avian-unique motif in the IDD. The observed binding mode is maintained in the context of heterotrimeric influenza polymerase, placing ANP32A in the immediate vicinity of known host-adaptive PB2 mutants.
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