ArticleCell2016
Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes.
Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 292 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
292 citing papers in PubMed.
- A Randomized, Placebo-Controlled Trial to Evaluate the Safety and Efficacy of VIR-2482 in Healthy Adults for Prevention of Influenza A Illness (PENINSULA).Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2024Trial
- A phase 1 study in healthy volunteers to investigate the safety, tolerability, and pharmacokinetics of VIR-2482: a monoclonal antibody for the prevention of severe influenza A illness.Antimicrobial agents and chemotherapy · 2024Trial
- Anti-idiotypic antibodies as molecular mimics of conserved influenza hemagglutinin epitopes.Protein science : a publication of the Protein Society · 2026Article
- Diminished sialoside binding in novel H5N1 influenza hemagglutinin variants identified in a human patient.Nature communications · 2026Article
- Article
- What Antibody Repertoires See: Structural and Immunogenetic Insights Into Influenza A Virus Hemagglutinin Recognition.Immunological reviews · 2026Review
- Article
- Single-component self-assembling protein nanoparticles displaying stabilized prefusion-closed hemagglutinin trimers for influenza vaccine development.Nature communications · 2026Article
- The Influenza-Specific Immunoglobulin Repertoire - Nimble Yet Steeped in Tradition.Immunological reviews · 2026Review
- Counteracting Influenza Virus Evolution Through the Full Spectrum of Broadly Protective Antibodies.Immunological reviews · 2026Review
- Computational Design and Expression of Headless Influenza Hemagglutinin Antigens Toward a Modular Universal Nanoparticle Vaccine.Antibodies (Basel, Switzerland) · 2026Article
- A neutralizing nanobody targeting a conserved lateral patch on HA1 confers protection against multiple H7 avian influenza viruses.Journal of virology · 2026Article
- Elicitation of stem-directed antibodies in rhesus macaques by a conventional hemagglutinin immunogen.bioRxiv : the preprint server for biology · 2026Article
- Sialic acid-anchored haemagglutinin stalk neutralizing antibody M-SiaB enhances protection against highly pathogenic influenza H5N1/Texas/2024.Nature communications · 2026Article
- Structural basis for distinct protective mechanisms of IGHV3-23 antibodies targeting influenza hemagglutinin stem.Nature communications · 2026Article
- A bivalent mRNA-LNP vaccine confers broad-spectrum protection against both homologous and heterologous H5/H7 highly pathogenic avian influenza viruses in SPF chickens.Veterinary research · 2026Article
- Development of a recombinant single-cycle influenza viral vector as an intranasal vaccine against SARS-CoV-2.Scientific reports · 2026Article
- Egyptian rousette bat humoral immunity to H9 influenza hemagglutinin.bioRxiv : the preprint server for biology · 2026Article
- A C-type single-domain antibody with protective efficacy against H1N1 via respiratory administration.Virologica Sinica · 2026Article
- Review
232 more citing papers are in PubMed but not listed here.
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Authors and funding
29 authors.
Funding
Abstract
Influenza virus remains a threat because of its ability to evade vaccine-induced immune responses due to antigenic drift. Here, we describe the isolation, evolution, and structure of a broad-spectrum human monoclonal antibody (mAb), MEDI8852, effectively reacting with all influenza A hemagglutinin (HA) subtypes. MEDI8852 uses the heavy-chain VH6-1 gene and has higher potency and breadth when compared to other anti-stem antibodies. MEDI8852 is effective in mice and ferrets with a therapeutic window superior to that of oseltamivir. Crystallographic analysis of Fab alone or in complex with H5 or H7 HA proteins reveals that MEDI8852 binds through a coordinated movement of CDRs to a highly conserved epitope encompassing a hydrophobic groove in the fusion domain and a large portion of the fusion peptide, distinguishing it from other structurally characterized cross-reactive antibodies. The unprecedented breadth and potency of neutralization by MEDI8852 support its development as immunotherapy for influenza virus-infected humans.
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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.