Neutralizing antibody PR8‐23 targets the footprint of the sialoglycan receptor binding site of H1N1 hemagglutinin
- Resource Type
- Authors
- Xin Xie; Li-Ting Yan; Xiaoyan Huang; Chunyan Guo; Lanlan Li; Lijun Sun; Jun Hu; Jingying Sun; Penghua Zhao
- Source
- Journal of Medical Virology. 93:3508-3515
- Subject
- Phage display
medicine.drug_class
viruses
Hemagglutinin (influenza)
Hemagglutinin Glycoproteins, Influenza Virus
Antibodies, Viral
Monoclonal antibody
Epitope
Epitopes
Mice
03 medical and health sciences
chemistry.chemical_compound
Influenza A Virus, H1N1 Subtype
0302 clinical medicine
Peptide Library
Virology
Influenza, Human
medicine
Animals
Humans
030212 general & internal medicine
Neutralizing antibody
Mice, Inbred BALB C
Binding Sites
Hemagglutination assay
biology
virus diseases
Hemagglutination Inhibition Tests
Antibodies, Neutralizing
Sialic acid
Hemagglutinins
Infectious Diseases
chemistry
biology.protein
Female
030211 gastroenterology & hepatology
Antibody
- Language
- ISSN
- 1096-9071
0146-6615
Influenza virus cause seasonal influenza epidemic and seriously sporadic influenza pandemic outbreaks. Hemagglutinin (HA) is an important target in the therapeutic treatment and diagnostic detection of the influenza virus. Variation in the sialic acid receptor binding site leads to strain-specific binding and results in different binding modes to the host receptors. Here, we evaluated the neutralizing activity and hemagglutination inhibition activity of a prepared murine anti-H1N1 monoclonal antibody PR8-23. Then we identified the epitope peptide of antibody PR8-23 by phage display technique from phage display peptide libraries. The identified epitope, 63-IAPLQLGKCNIA-74, containing two α-helix and two β-fold located at the footprint of the sialoglycan receptor on the RBS in the globular head domain of HA. It broads the growing arsenal of motifs for the amino acids on the globular head domain of HA in sialic acid receptor binding site and neutralizing antibody production.