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Neutralizing antibody PR8‐23 targets the footprint of the sialoglycan receptor binding site of H1N1 hemagglutinin
Author(s) -
Yan Liting,
Sun Lijun,
Guo Chunyan,
Li Lanlan,
Sun Jingying,
Huang Xiaoyan,
Zhao Penghua,
Xie Xin,
Hu Jun
Publication year - 2021
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.26779
Subject(s) - virology , epitope , hemagglutinin (influenza) , antibody , monoclonal antibody , sialic acid , neutralizing antibody , biology , antigenic drift , virus , phage display , receptor , peptide library , influenza a virus , hemagglutination assay , microbiology and biotechnology , peptide sequence , biochemistry , immunology , gene , titer
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.