Premium
Chimerization of mu‐9
Author(s) -
Krishnan Indira S.,
Hansen Hans J.,
Losman Michele J.,
Goldenberg David M.,
Leung Shuion
Publication year - 1997
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/(sici)1097-0142(19971215)80:12+<2667::aid-cncr44>3.0.co;2-7
Subject(s) - immunogenicity , antigen , antibody , monoclonal antibody , microbiology and biotechnology , complementary dna , cloning (programming) , medicine , immunology , biology , biochemistry , gene , computer science , programming language
BACKGROUND Mu‐9 is a murine monoclonal antibody that is directed against affinity‐purified colon‐specific antigen‐p (CSAp). CSAp is a tumor‐associated antigen that is present in 60% of colorectal carcinomas. Preclinical and clinical studies have shown Mu‐9 to have excellent targeting abilities. However, as administration of the murine immunoglobulin G (IgG) provoked a human anti‐mouse antibody response, chimerization of Mu‐9 is warranted for decreasing immunogenicity. METHODS Polymerase chain reaction and cDNA library screening methods were used for the cloning of Mu‐9 heavy and light chain variable regions for the construction of chimeric Mu‐9. RESULTS The functional chimeric Mu‐9 antibody binds to the CSAp antigen in the GW‐39 extracts. It has immunochemical properties similar to that of murine Mu‐9. CONCLUSIONS The V‐region sequence information will be used for design of humanized Mu‐9, which will be evaluated for targeting gastrointestinal carcinomas. Cancer 1997; 80:2667‐74. © 1997 American Cancer Society.