ArticleFrontiers in microbiology2022
Nucleoporin 85 interacts with influenza A virus PB1 and PB2 to promote its replication by facilitating nuclear import of ribonucleoprotein.
Article in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- HVIface: sequence-based deep learning for decoding human-virus protein-protein interfaces.Frontiers in bioinformatics · 2026Article
- PB1 mutations as key drivers of influenza A virus evolution.Frontiers in microbiology · 2026Review
- Lycorine Inhibits Influenza Virus Replication by Affecting Nascent Nucleoporin Nup93 Synthesis.International journal of molecular sciences · 2025Article
- Quantitative analysis of proteomic changes in two monoclonal suspension MDCK cell lines infected with human influenza A virus (H1N1).PloS one · 2025Article
- Unravelling the interaction between Influenza virus and the nuclear pore complex: insights into viral replication and host immune response.Virusdisease · 2024Review
- Predicting Functional Consequences of Recent Natural Selection in Britain.Molecular biology and evolution · 2024Article
- Article
- Predicting functional consequences of recent natural selection in Britain.bioRxiv : the preprint server for biology · 2023Article
- Avian Influenza Virus Tropism in Humans.Viruses · 2023Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription and replication of the influenza A virus (IAV) genome take place in the nucleus of infected cells, which rely on host factors to aid viral ribonucleoprotein (vRNP) to cross the nuclear pore complex (NPC) and complete the bidirectional nucleocytoplasmic trafficking. Here, we showed that nucleoporin 85 (NUP85), a component of NPC, interacted with RNP subunits polymerase basic 1 (PB1) and polymerase basic 2 (PB2) in an RNA-dependent manner during IAV infection. Knockdown of NUP85 delayed the nuclear import of vRNP, PB1 and PB2, inhibiting polymerase activity and ultimately suppressing viral replication. Further analysis revealed that NUP85 assisted the binding of PB1 to nuclear transport factor Ran-binding protein 5 (RanBP5) and the binding of PB2 to nuclear transport factor importin α1 and importin α7. We also found that NUP85 expression was downregulated upon IAV infection. Together, our study demonstrated that NUP85 positively regulated IAV infection by interacting with viral PB1 and PB2, which may provide new insight into the process of vRNP nuclear import and a novel target for effective antivirals.
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