ArticleJournal of virology2014
Structure of influenza virus N7: the last piece of the neuraminidase "jigsaw" puzzle.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Pre-existing and cross-reactive immunity to avian influenza H5N1 in humans: Implications for pandemic risk and vaccine strategies.The Journal of infection · 2026Review
- On the brink of emergence: an evolutionary approach to Influenza A virus H5N1 isolated from humans.Virus research · 2026Article
- Structural analysis of antigenic variation and adaptive evolution of the H5N1 neuraminidase gene.PLoS computational biology · 2026Article
- Discovery of Influenza Neuraminidase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation of Novel Chemotypes.Molecules (Basel, Switzerland) · 2025Article
- Article
- A human monoclonal antibody targeting the monomeric N6 neuraminidase confers protection against avian H5N6 influenza virus infection.Nature communications · 2024Article
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- Co-infection of the respiratory epithelium, scene of complex functional interactions between viral, bacterial, and human neuraminidases.Frontiers in microbiology · 2023Review
- Structural and inhibitor sensitivity analysis of influenza B-like viral neuraminidases derived from Asiatic toad and spiny eel.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Emerging HxNy Influenza A Viruses.Cold Spring Harbor perspectives in medicine · 2022Review
- Influenza A Virus Neuraminidase Inhibitors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Second sialic acid-binding site of influenza A virus neuraminidase: binding receptors for efficient release.The FEBS journal · 2021Article
- Influenza Neuraminidase Characteristics and Potential as a Vaccine Target.Frontiers in immunology · 2021Review
- Multiscale Simulations Examining Glycan Shield Effects on Drug Binding to Influenza Neuraminidase.Biophysical journal · 2020Article
- Article
- Drivers of recombinant soluble influenza A virus hemagglutinin and neuraminidase expression in mammalian cells.Protein science : a publication of the Protein Society · 2020Article
- Plasticity of the 340-Loop in Influenza Neuraminidase Offers New Insight for Antiviral Drug Development.International journal of molecular sciences · 2020Article
- Mutation of the second sialic acid-binding site of influenza A virus neuraminidase drives compensatory mutations in hemagglutinin.PLoS pathogens · 2020Article
- Influenza H7N9 Virus Neuraminidase-Specific Human Monoclonal Antibodies Inhibit Viral Egress and Protect from Lethal Influenza Infection in Mice.Cell host & microbe · 2019Article
- The 2nd sialic acid-binding site of influenza A virus neuraminidase is an important determinant of the hemagglutinin-neuraminidase-receptor balance.PLoS pathogens · 2019Article
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledThere are nine subtypes of influenza A virus neuraminidase (NA), N1 to N9. In addition, influenza B virus also contains NA, and there are two influenza virus NA-like molecules, N10 and N11, which were recently identified from bats. Crystal structures for all of these proteins have been solved, with the exception of N7, and there is no published report of N6, although a structure has been deposited in the Protein Data Bank. Here, we present the N7 and N6 structures at 2.1 Å and 1.8 Å, respectively. Structural comparison of all NA subtypes shows that both N7 and N6 highly resemble typical group 2 NA structures with some special characteristics, including an additional cavity adjacent to their active sites formed by novel 340-loop conformations. Comparative analysis also revealed new structural insights into the N-glycosylation, calcium binding, and second sialic acid binding site of influenza virus NA. This comprehensive study is critical for understanding the complexity of the most successful influenza drug target and for the structure-based design of novel influenza inhibitors. IMPORTANCE: Influenza viruses impose a great burden on society, by the human-adapted seasonal types as well as by variants that occasionally jump from the avian reservoir to infect humans. The surface glycoprotein neuraminidase (NA) is essential for the propagation of the virus and currently the most successfully drug-targeted molecule. Therefore, the structural and functional analysis of NA is critical for the prevention and control of influenza infections. There are nine subtypes of influenza A virus NA (N1 to N9). In addition, influenza B virus also contains NA, and there are two influenza NA-like molecules, N10 and N11, which were recently identified in bats. Crystal structures for all of these proteins have been solved and reported with the exception of N7 and N6. The structural analysis of influenza virus N7 and N6 presented in this study therefore completes the puzzle and adds to a comprehensive understanding of influenza virus NA.
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