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Neutralizing antibody PR8-23 targets the footprint of the sialoglycan receptor binding site of H1N1 hemagglutinin.
- Source :
-
Journal of medical virology [J Med Virol] 2021 Jun; Vol. 93 (6), pp. 3508-3515. Date of Electronic Publication: 2021 Feb 23. - Publication Year :
- 2021
-
Abstract
- 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.<br /> (© 2021 Wiley Periodicals LLC.)
- Subjects :
- Animals
Antibodies, Neutralizing metabolism
Antibodies, Viral immunology
Binding Sites
Epitopes chemistry
Epitopes metabolism
Female
Hemagglutination Inhibition Tests
Humans
Influenza A Virus, H1N1 Subtype chemistry
Influenza, Human virology
Mice
Mice, Inbred BALB C
Peptide Library
Antibodies, Neutralizing immunology
Epitopes immunology
Hemagglutinin Glycoproteins, Influenza Virus immunology
Hemagglutinin Glycoproteins, Influenza Virus metabolism
Hemagglutinins immunology
Hemagglutinins metabolism
Influenza A Virus, H1N1 Subtype immunology
Subjects
Details
- Language :
- English
- ISSN :
- 1096-9071
- Volume :
- 93
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of medical virology
- Publication Type :
- Academic Journal
- Accession number :
- 33410516
- Full Text :
- https://doi.org/10.1002/jmv.26779