ArticleActa crystallographica. Section F, Structural biology communications2021
Structure of an H3N2 influenza virus nucleoprotein.
Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- A Structural View of Influenza Virus Ribonucleoprotein Complex and Its Functions.Microorganisms · 2026Review
- Identification and characterization of a novel inhibitor of influenza A virus that acts by blocking nucleoprotein oligomerization.Antimicrobial agents and chemotherapy · 2026Article
- Coupling of polymerase-nucleoprotein-RNA in an influenza virus mini ribonucleoprotein complex.Nature communications · 2025Article
- Seasonal Influenza Viruses Show Distinct Adaptive Dynamics During Growth in Chicken Eggs.Molecular biology and evolution · 2025Article
- Equine influenza antigen-based particle vaccine protects mice against homologous and heterosubtypic viral challenges.Acta biomaterialia · 2025Article
- Structure of the tilapia lake virus nucleoprotein bound to RNA.Nucleic acids research · 2025Article
- The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure.Science advances · 2024Article
- Defining the minimal components of the influenza A virus replication machinery via an in vitro reconstitution system.PLoS biology · 2023Article
- Article
- Influenza and Universal Vaccine Research in China.Viruses · 2022Review
- Article
- Evolution of Swine Influenza Virus H3N2 in Vaccinated and Nonvaccinated Pigs after Previous Natural H1N1 Infection.Viruses · 2022Article
- The C-terminal LCAR of host ANP32 proteins interacts with the influenza A virus nucleoprotein to promote the replication of the viral RNA genome.Nucleic acids research · 2022Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Influenza A viruses of the H1N1 and H3N2 subtypes are responsible for seasonal epidemic events. The influenza nucleoprotein (NP) binds to the viral genomic RNA and is essential for its replication. Efforts are under way to produce therapeutics and vaccines targeting the NP. Despite this, no structure of an NP from an H3N2 virus has previously been determined. Here, the structure of the A/Northern Territory/60/1968 (H3N2) influenza virus NP is presented at 2.2 Å resolution. The structure is highly similar to those of the A/WSN/1933 (H1N1) and A/Hong Kong/483/97 (H5N1) NPs. Nonconserved amino acids are widely dispersed both at the sequence and structural levels. A movement of the 73-90 RNA-binding loop is observed to be the key difference between the structure determined here and previous structures. The data presented here increase the understanding of structural conservation amongst influenza NPs and may aid in the design of universal interventions against influenza.
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