ArticleJournal of virology2010
An antibody against a novel and conserved epitope in the hemagglutinin 1 subunit neutralizes numerous H5N1 influenza viruses.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 69 citations in OpenAlex.
- Mapping hemagglutinin residues driving antigenic diversity in H5Nx avian influenza viruses.Journal of virology · 2026Article
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- Designing Sandwich ELISA with Broadly Reactive Anti-Nucleocapsid Monoclonal Antibodies to Detect Bat-Borne Merbecoviruses.Viruses · 2025Article
- Antiviral Activity of Angelica Tenuissima Nakai against Influenza A Virus.Pathogens (Basel, Switzerland) · 2024Article
- Vaccination with recombinant Lactococcus lactis expressing HA1-IgY Fc fusion protein provides protective mucosal immunity against H9N2 avian influenza virus in chickens.Virology journal · 2023Article
- Analysis of the conserved protective epitopes of hemagglutinin on influenza A viruses.Frontiers in immunology · 2023Review
- The protective effect of a combination of human intracellular and extracellular antibodies against the highly pathogenic avian influenza H5N1 virus.Human vaccines & immunotherapeutics · 2022Article
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- A comprehensive influenza reporter virus panel for high-throughput deep profiling of neutralizing antibodies.Nature communications · 2021Article
- Matrix Protein 2 Extracellular Domain-Specific Monoclonal Antibodies Are an Effective and Potentially Universal Treatment for Influenza A.Journal of virology · 2021Article
- Development of a colloidal gold-based immunochromatographic strip test using two monoclonal antibodies to detect H7N9 avian influenza virus.Virus genes · 2020Article
- Generation of neutralizing and non-neutralizing monoclonal antibodies against H7N9 influenza virus.Emerging microbes & infections · 2020Article
- Contribution of Fc-dependent cell-mediated activity of a vestigial esterase-targeting antibody against H5N6 virus infection.Emerging microbes & infections · 2020Article
- A NS1-binding monoclonal antibody interacts with two residues that are highly conserved in seasonal as well as newly emerged influenza A virus.Pathogens and disease · 2019Article
- The Quest for a Truly Universal Influenza Vaccine.Frontiers in cellular and infection microbiology · 2019Review
- Overexpression of the nucleocapsid protein of Middle East respiratory syndrome coronavirus up-regulates CXCL10.Bioscience reports · 2018Article
- The Vestigial Esterase Domain of Haemagglutinin of H5N1 Avian Influenza A Virus: Antigenicity and Contribution to Viral Pathogenesis.Vaccines · 2018Review
- Asymmetric antiviral effects of ebolavirus antibodies targeting glycoprotein stem and glycan cap.PLoS pathogens · 2018Article
- Generation and testing anti-influenza human monoclonal antibodies in a new humanized mouse model (DRAGA: HLA-A2. HLA-DR4. Rag1 KO. IL-2Rγc KO. NOD).Human vaccines & immunotherapeutics · 2018Article
- Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spread of the recently emerged, highly pathogenic H5N1 avian influenza virus has raised concern. Preclinical studies suggest that passive immunotherapy could be a new form of treatment for H5N1 virus infection. Here, a neutralizing monoclonal antibody (MAb) against the hemagglutinin (HA) of the influenza A/chicken/Hatay/2004 H5N1 virus, MAb 9F4, was generated and characterized. MAb 9F4 binds both the denatured and native forms of HA. It was shown to recognize the HA proteins of three heterologous strains of H5N1 viruses belonging to clades 1, 2.1, and 2.2, respectively. By use of lentiviral pseudotyped particles carrying HA on the surface, MAb 9F4 was shown to effectively neutralize the homologous strain, Hatay04, and another clade 1 strain, VN04, at a neutralization titer of 8 ng/ml. Furthermore, MAb 9F4 also neutralized two clade 2 viruses at a neutralizing titer of 40 ng/ml. The broad cross-neutralizing activity of MAb 9F4 was confirmed by its ability to neutralize live H5N1 viruses of clade 2.2.2. Epitope-mapping analysis revealed that MAb 9F4 binds a previously uncharacterized epitope below the globular head of the HA1 subunit. Consistently, this epitope is well conserved among the different clades of H5N1 viruses. MAb 9F4 does not block the interaction between HA and its receptor but prevents the pH-mediated conformational change of HA. MAb 9F4 was also found to be protective, both prophylactically and therapeutically, against a lethal viral challenge of mice. Taken together, our results showed that MAb 9F4 is a neutralizing MAb that binds a novel and well-conserved epitope in the HA1 subunit of H5N1 viruses.
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