ArticleScientific reports2019
An Effective Neutralizing Antibody Against Influenza Virus H1N1 from Human B Cells.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Convergent evolution of the N156K mutation in A(H1N1)pdm09 hemagglutinin contributes to antigenic drift and cluster transition.Emerging microbes & infections · 2026Article
- Probing the role of membrane in neutralizing activity of antibodies against influenza virus.Structure (London, England : 1993) · 2026Article
- Article
- Neutralization of the Pandemic Influenza A/H1N1 Virus withAntibodies (Basel, Switzerland) · 2025Article
- Evaluation of a novel intramuscular prime/intranasal boost vaccination strategy against influenza in the pig model.PLoS pathogens · 2024Article
- A synergistic therapy against influenza virus A/H1N1/PR8 by a HA1 specific neutralizing single-domain VFrontiers in microbiology · 2024Article
- Adjuvant effects of combination monophosphoryl lipid A and poly I:C on antigen-specific immune responses and protective efficacy of influenza vaccines.Scientific reports · 2023Article
- New Anti-Flavivirus Fusion Loop Human Antibodies with Zika Virus-Neutralizing Potential.International journal of molecular sciences · 2022Article
- Polyclonal hyper immunoglobulin: A proven treatment and prophylaxis platform for passive immunization to address existing and emerging diseases.Human vaccines & immunotherapeutics · 2022Review
- Structural basis of polyethylene glycol recognition by antibody.Journal of biomedical science · 2020Article
- Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza is a contagious acute respiratory disease caused by the influenza virus infection. Hemagglutinin (HA) is an important target in the therapeutic treatment and diagnostic detection of the influenza virus. Influenza A virus encompasses several different HA subtypes with different strains, which are constantly changing. In this study, we identified a fully human H1N1 neutralizing antibody (32D6) via an Epstein-Barr virus-immortalized B cell-based technology. 32D6 specifically neutralizes the clinically isolated H1N1 strains after the 2009 pandemic but not the earlier strains. The epitope was identified through X-ray crystallographic analysis of the 32D6-Fab/HA1 complex structure, which revealed a unique loop conformation located on the top surface of HA. The major region is composed of two peptide segments (residues 172-177 and 206-213), which form an abreast loop conformation. The residue T262 between the two loops forms a conformational epitope for recognition by 32D6. Three water molecules were observed at the interface of HA and the heavy chain, and they may constitute a stabilizing element for the 32D6-HA association. In addition, each 32D6-Fab is likely capable of blocking one HA trimer. This study provides important information on the strain specificity of 32D6 for the therapeutic treatment and detection of viral infection.
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