ArticlePloS one2013
Isolation of recombinant phage antibodies targeting the hemagglutinin cleavage site of highly pathogenic avian influenza virus.
Article in PloS one, 2013. 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, 16 citations in OpenAlex.
- Overcoming Challenges in Avian Influenza Diagnosis: The Role of Surface-Enhanced Raman Spectroscopy in Poultry Health Monitoring.Veterinary sciences · 2025Review
- H5N1 Avian Influenza: A Narrative Review of Scientific Advances and Global Policy Challenges.Viruses · 2025Review
- Advances in Detection Techniques for the H5N1 Avian Influenza Virus.International journal of molecular sciences · 2023Review
- Antibody Phage Display Technology for Sensor-Based Virus Detection: Current Status and Future Prospects.Biosensors · 2023Review
- Recent Advances in Quenchbody, a Fluorescent Immunosensor.Sensors (Basel, Switzerland) · 2021Review
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- Generation of a recombinant chickenized monoclonal antibody against the neuraminidase of H9N2 avian influenza virus.AMB Express · 2020Article
- Single-Step Detection of the Influenza Virus Hemagglutinin Using Bacterially-Produced Quenchbodies.Sensors (Basel, Switzerland) · 2018Article
- Recombinant antibodies for diagnostics and therapy against pathogens and toxins generated by phage display.Proteomics. Clinical applications · 2016Review
- Generating Recombinant Antibodies to Membrane Proteins through Phage Display.Antibodies (Basel, Switzerland) · 2016Review
- Diagnostic Potential of Recombinant scFv Antibodies Generated Against Hemagglutinin Protein of Influenza A Virus.Frontiers in immunology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Highly pathogenic avian influenza (HPAI) H5N1 viruses, which have emerged in poultry and other wildlife worldwide, contain a characteristic multi-basic cleavage site (CS) in the hemagglutinin protein (HA). Because this arginine-rich CS is unique among influenza virus subtypes, antibodies against this site have the potential to specifically diagnose pathogenic H5N1. By immunizing mice with the CS peptide and screening a phage display library, we isolated four antibody Fab fragment clones that specifically bind the antigen peptide and several HPAI H5N1 HA proteins in different clades. The soluble Fab fragments expressed in Escherichia coli bound the CS peptide and the H5N1 HA protein with nanomolar affinity. In an immunofluorescence assay, these Fab fragments stained cells infected with HPAI H5N1 but not those infected with a less virulent strain. Lastly, all the Fab clones could detect the CS peptide and H5N1 HA protein by open sandwich ELISA. Thus, these recombinant Fab fragments will be useful novel reagents for the rapid and specific detection of HPAI H5N1 virus.
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