ArticleNature communications2025
Broad neuraminidase antibodies confer protection against seasonal and avian influenza viruses.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Pre-existing and cross-reactive immunity to avian influenza H5N1 in humans: Implications for pandemic risk and vaccine strategies.The Journal of infection · 2026Review
- A neuraminidase-targeted nanobody confers broad protection against influenza B virus.Journal of virology · 2026Article
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- From Global Insights to Local Action: Bridging Vaccine Design and Manufacturing Gaps in H5N1 Pandemic Readiness.Vaccines · 2026Article
- A semi-replicating VSV (srVSV)-based platform for developing broad-spectrum mucosal vaccines against influenza A viruses.Virologica Sinica · 2026Article
- A nanoemulsion-adjuvanted trivalent neuraminidase vaccine confers cross-protection against divergent influenza viruses.Frontiers in cellular and infection microbiology · 2026Article
- Recombinant expression and functional characterization of influenza A virus neuraminidase in a mammalian cell system.Frontiers in microbiology · 2025Article
Corrections and comments
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Authors and funding
26 authors.
Funding
Abstract
Neuraminidase (NA) is a critical target for universal influenza vaccines and therapeutic antibodies, yet its antigenic landscape remains incompletely understood. Here we identify two broadly cross-protective monoclonal antibodies, CAV-F6 and CAV-F34, from influenza-infected individuals. These antibodies inhibit NA enzymatic activity across multiple subtypes and confer protection against seasonal influenza in female mouse models. Importantly, the two antibodies also neutralize emerging avian strains, including recent bovine H5N1 and H7N9 strains, both with pandemic potential. Structural studies reveal that both antibodies target conserved regions of the NA active site via HCDR3, blocking sialic acid interaction. Furthermore, we observe distinct occupancy for the two antibodies on N2 tetramer, which is likely due to differences in binding affinity. Our findings provide molecular insights into NA-targeted immunity and offer a foundation for developing broadly protective influenza vaccines and therapeutics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.