ArticleImmunity2020
Human Antibodies Targeting Influenza B Virus Neuraminidase Active Site Are Broadly Protective.
Article in Immunity, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
56 citing papers in PubMed, 83 citations in OpenAlex.
- Trial
- Consensus H3N2 HA immunogens incorporating key antigenic mutations elicit broad-spectrum neutralizing responses.Emerging microbes & infections · 2026Article
- A neuraminidase-targeting nanobody as a therapeutic candidate against influenza A and B viruses.Journal of virology · 2026Article
- A neuraminidase-targeted nanobody confers broad protection against influenza B virus.Journal of virology · 2026Article
- Article
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- Review
- Coexistence of virome-encoded health-associated genes and pathogenic genes in global habitats.Applied and environmental microbiology · 2025Article
- A protective and heterosubtypic antibody lineage targeting the influenza A virus neuraminidase active site.The Journal of clinical investigation · 2025Article
- Increased dose of H1N1 pandemic influenza vaccine during pregnancy improves immunity in mothers and infants.medRxiv : the preprint server for health sciences · 2025Article
- Structure and function of a cross-neutralizing influenza neuraminidase antibody that accommodates recent N2 NA Asn245 glycosylation.Communications biology · 2025Article
- Characterization of the glycoproteins of fish and amphibian influenza B-like viruses.Science advances · 2025Article
- Functional and epitope specific monoclonal antibody discovery directly from immune sera using cryo-EM.Science advances · 2025Article
- The Persistence of Cross-Reactive Immunity to Influenza B/Yamagata Neuraminidase Despite the Disappearance of the Lineage: Structural and Serological Evidence.International journal of molecular sciences · 2025Article
- Structural basis of broad protection against influenza virus by human antibodies targeting the neuraminidase active site via a recurring motif in CDR H3.Nature communications · 2025Article
- Structural convergence and water-mediated substrate mimicry enable broad neuraminidase inhibition by human antibodies.Nature communications · 2025Article
- Identification of a seasonal influenza vaccine-induced broadly protective neuraminidase antibody.The Journal of experimental medicine · 2025Article
- Fluorescence-barcoded cell lines stably expressing membrane-anchored influenza neuraminidases.Vaccine · 2025Article
- Neuraminidase-specific antibodies drive differential cross-protection between contemporary FLUBV lineages.Science advances · 2025Article
- Antiviral strategies against influenza virus: an update on approved and innovative therapeutic approaches.Cellular and molecular life sciences : CMLS · 2025Review
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Authors and funding
17 authors at 4 institutions in 2 countries.
Funding
Abstract
Influenza B virus (IBV) infections can cause severe disease in children and the elderly. Commonly used antivirals have lower clinical effectiveness against IBV compared to influenza A viruses (IAV). Neuraminidase (NA), the second major surface protein on the influenza virus, is emerging as a target of broadly protective antibodies that recognize the NA active site of IAVs. However, similarly broadly protective antibodies against IBV NA have not been identified. Here, we isolated and characterized human monoclonal antibodies (mAbs) that target IBV NA from an IBV-infected patient. Two mAbs displayed broad and potent capacity to inhibit IBV NA enzymatic activity, neutralize the virus in vitro, and protect against lethal IBV infection in mice in prophylactic and therapeutic settings. These mAbs inserted long CDR-H3 loops into the NA active site, engaging residues highly conserved among IBV NAs. These mAbs provide a blueprint for the development of improved vaccines and therapeutics against IBVs.
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What OpenQuestion holds
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.