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Immunological and catalytic features of InfA‐15 mAb and the light chain raised against hemagglutinin molecule for Influenza virus A type
Author(s) -
Hifumi Emi,
Fujimoto Naoko,
Yahiro Takaaki,
Uda Taizo
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.928.2
Subject(s) - monoclonal antibody , immunoglobulin light chain , hemagglutinin (influenza) , protein subunit , microbiology and biotechnology , virus , chemistry , antibody , antigen , virology , cleavage (geology) , biology , biochemistry , gene , genetics , paleontology , fracture (geology)
Through we have been exploring the catalytic antibody (antigenase) in this decade, we have produced a unique monoclonal antibody (InfA‐15) raised against a conserved region of HA2 subunit of the hemagglutinin molecule of influenza virus A type (1). The InfA‐15 monoclonal antibody could recognize all important hemagglutinin molecules such as H1, H3 and H5‐subtype of the virus. Based on the structural analysis, the InfA‐15 monoclonal antibody possesses a catalytic triad‐like structure which is considered to work as the active center of the enzymatic function of the antibody. Thus, we investigated the some features such as amidase activity for synthetic peptide and cleavage activity for the antigen. Moreover the light chain of InfA‐15 monoclonal antibody was genetically synthesized to investigate the detail enzymatic function. It was interesting that the light chain prepared from mouse antibody and the recombinant light chain expressed in E.coli showed the different characteristics for the cleavage reaction of the substrate (antigen). The catalytic function of the antibody or its subunit will be discussed on the molecular basis.