Open AccessEstablishment and Characterization of Mouse‐Human Chimeric Monoclonal Antibody to erbB ‐2 Product
Author(s) -
Ishida Tadao,
Tsujisaki Masayuki,
Hinoda Yuji,
Imai Kohzoh,
Yachi Akira
Publication year - 1994
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.1994.tb02079.x
Subject(s) - monoclonal antibody , microbiology and biotechnology , antibody , immunoglobulin light chain , biology , transfection , mutant , monoclonal , expression vector , cell culture , chemistry , virology , gene , recombinant dna , biochemistry , immunology , genetics
A mouse‐human chimeric antibody for erbB ‐2 product was established by a new procedure using heavy chain loss mouse mutant hybridoma and human immunoglobulin expression vector. The E401 hybridoma secreted anti‐ erbB ‐2 product monoclonal antibody (MoAb) (IgG1, k ). The gene of the mouse variable regions of heavy chain was amplified and cloned by the polymerase chain reaction technique directly from the E401 hybridoma RNA. The variable region of heavy chain was joined with the expression vector, which contains human γ1 constant gene. The expression vector was transfected into heavy chain loss mutant cells E401‐12, which produced only murine immunoglobulin light chains. A chimeric monoclonal antibody CH401 retained full binding reactivity to erbB ‐2 product, compared with murine E401 parental antibody. Furthermore, the chimeric MoAb CH401 was much more efficient in supporting antibody dependent cell‐mediated cytotoxicity activity against erbB ‐2‐bearing human adenocarcinoma cells than murine MoAb E401. These suggest that a chimeric monoclonal antibody CH401 may be a potent reagent for therapy of human adenocarcinomas.