ArticleNature communications2022
Structure-based design of stabilized recombinant influenza neuraminidase tetramers.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 72 citations in OpenAlex.
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- Target-Based Antiviral Drug Development Against Human Respiratory Viruses.Pathogens (Basel, Switzerland) · 2026Review
- ELISA-based quantification of neuraminidase in commercial influenza vaccines using virus-derived reference antigens.Microbiology spectrum · 2026Article
- INAAC: An affinity chromatography strategy enabling characterization and quantification of influenza neuraminidase antigens in vaccines.The Journal of biological chemistry · 2026Article
- T-cell-mediated immunity to influenza A (H2N3): implications for caccine efficacy and cross-subtype protection.Archives of microbiology · 2026Review
- Oseltamivir aziridines are potent influenza neuraminidase inhibitors and imaging agents.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Improved cross-protection and immunity against influenza A virus in mice using a novel mRNA vaccine with optimized design of RNA sequence.Molecular therapy. Nucleic acids · 2026Article
- Spermine: A Hemoglobin Modifier That Reduces Autoxidation and Regulates Oxygen Delivery.International journal of molecular sciences · 2026Article
- Cross-protective efficacy of NA-based mRNA vaccine candidates against seasonal and avian influenza viruses.Frontiers in microbiology · 2026Article
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- Computational design of bifaceted protein nanomaterials.Nature materials · 2025Article
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- Broad neuraminidase antibodies confer protection against seasonal and avian influenza viruses.Nature communications · 2025Article
- Elucidating the characteristics and clonal evolutionary trajectory of influenza neuraminidase broadly reactive B cell.Science advances · 2025Article
Corrections and comments
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Authors and funding
22 authors at 4 institutions in 1 country.
Funding
Abstract
Influenza virus neuraminidase (NA) is a major antiviral drug target and has recently reemerged as a key target of antibody-mediated protective immunity. Here we show that recombinant NAs across non-bat subtypes adopt various tetrameric conformations, including an "open" state that may help explain poorly understood variations in NA stability across viral strains and subtypes. We use homology-directed protein design to uncover the structural principles underlying these distinct tetrameric conformations and stabilize multiple recombinant NAs in the "closed" state, yielding two near-atomic resolution structures of NA by cryo-EM. In addition to enhancing thermal stability, conformational stabilization improves affinity to protective antibodies elicited by viral infection, including antibodies targeting a quaternary epitope and the broadly conserved catalytic site. Stabilized NAs can also be integrated into viruses without affecting fitness. Our findings provide a deeper understanding of NA structure, stability, and antigenicity, and establish design strategies for reinforcing the conformational integrity of recombinant NA proteins.
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