ArticlePloS one2020
Interaction between influenza A virus nucleoprotein and PB2 cap-binding domain is mediated by RNA.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Identifying a Marine-Derived Small-Molecule Nucleoprotein Inhibitor Against Influenza A Virus.Marine drugs · 2025Article
- Molecular basis of influenza ribonucleoprotein complex assembly and processive RNA synthesis.Science (New York, N.Y.) · 2025Article
- The ubiquitination landscape of the influenza A virus polymerase.Nature communications · 2023Article
- Interaction of Influenza A Nucleoprotein with Host hnRNP-C Is Implicated in Viral Replication.International journal of molecular sciences · 2022Article
- An overview of influenza A virus genes, protein functions, and replication cycle highlighting important updates.Virus genes · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A virus controls replication and transcription of its genome through the tight regulation of interaction between the ribonucleoprotein (RNP) complex subunits. The helical scaffold of RNP is maintained by nucleoprotein (NP). Previous studies have revealed that NP interacts with both PB2 N-terminal and C-terminal regions, with both regions sharing similar affinity to NP as revealed in co-immunoprecipitation assay. Our work here suggests that the interaction between NP and PB2 N-terminal region lies in the cap-binding domain (residue 320-483). By co-immunoprecipitation assay, the interaction was found to involve RNA. On the other hand, the cap-binding activity was not essential in the interaction. As shown by the NHS pull-down assay, a specific RNA sequence was not required. Among the cap-binding domain, residues K331 and R332 of PB2 play a role in RNP function so that polymerase activity was reduced when these residues were mutated, while K331 was found to be more crucial in the NP interaction. Collectively, our findings suggest a new binding mode between NP and PB2 which was mediated by RNA, and such interaction may provide a novel interacting site for influenza drug development.
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Registered trials
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