ArticleEmerging microbes & infections2021
Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus.
Article in Emerging microbes & infections, 2021. 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, 12 citations in OpenAlex.
- Genetic and biological characterization of H9N2 avian influenza viruses isolated from swine in China.BMC veterinary research · 2026Article
- Genetic Evolution of H9N2 Avian Influenza Virus in Guangxi, China.Microorganisms · 2025Article
- Genetic evolution and molecular characteristics of avian influenza viruses in Jining from 2018 to 2023.Frontiers in microbiology · 2025Article
- Engineering an Optimal Y280-Lineage H9N2 Vaccine Strain by Tuning PB2 Activity.International journal of molecular sciences · 2023Article
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- Identification of a Novel Insertion Site HVT-005/006 for the Generation of Recombinant Turkey Herpesvirus Vector.Frontiers in microbiology · 2022Article
- Identification of Hemagglutinin Mutations Caused by Neuraminidase Antibody Pressure.Microbiology spectrum · 2021Article
- A Cross-Reactive Monoclonal Antibody Against Neuraminidases of Both H9N2 and H3N2 Influenza Viruses Shows Protection in Mice Challenging Models.Frontiers in microbiology · 2021Article
- Anti-neuraminidase immunity in the combat against influenza.Expert review of vaccinesReview
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza A H9N2 virus causes economic loss to the poultry industry and has likely contributed to the genesis of H5N1 and H7N9 viruses. The neuraminidase (NA) of H9N2 virus, like haemagglutinin, is under antibody selective pressure and may undergo antigenic change; however, its antigenic structure remains to be elucidated. In this study, we used monoclonal antibodies (mAbs) to probe the H9N2 viral NA residues that are key for antibody binding/inhibition. These mAbs fell into three groups based on their binding/inhibition of the NA of H9N2 viruses isolated during 1999-2019: group I only bounded the NA of the early 2000 H9N2 viruses but possessed no neutralizing ability, group II bounded and inhibited the NA of H9N2 viruses isolated before 2012, and group III reacted with most or all tested H9N2 viruses. We showed that NA residue 356 is key for the recognition by group I mAbs, residues 344, 368, 369, and 400 are key for the binding/inhibition of NA by group II antibodies, whereas residues 248, 253, and the 125/296 combination are key for neutralizing antibodies in group III. Our findings highlighted NA antigenic change of the circulating H9N2 viruses, and provided data for a more complete picture of the antigenic structure of H9N2 viral NA.
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