The pharmacology of monoclonal antibodies is discussed by Peakeil.99.3.).. Murine antibodies

Kohler and Millstein first described the production of monoclonal-antibody-secreting cell lines in 1975. Immortal non-antibody-secreting murine myeloma cells were fused with antibody-secreting splenocytes from mice immunized with a particular antigen. Following the isolation of hybrid cells, the preferred hybridoma producing the desired antibody was identified and cloned. The technique yielded a perpetually reproducing cell line secreting unlimited quantities of murine monoclonal antibody of a single immunoglobulin class and subclass with identical structure, affinity, and specificity for the antigenic determinant.

Human antibodies

In 1977, the potential immunogenicity of murine antibodies stimulated the production of human antibodies from human myeloma cells and B lymphocytes. However, human antibody production has numerous technical limitations. To overcome these problems, heteromyeloma monoclonal antibodies such as HA-1A (Centocor) have been produced by fusing murine myeloma and human B cells to form non-secreting human-mouse fusion partners which are then fused with human B lymphocytes.

Humanized antibodies

Molecular biology techniques have permitted the development of humanized murine monoclonal antibodies which reduce the immunogenicity of murine antibodies and overcome the limitations of human hybridoma technology. Chimeric human-mouse antibodies are produced by inserting the genetic sequence encoding the mouse variable region of the immunoglobulin next to the human constant region (the most immunogenic portion). The recombinant DNA is then transfected into the murine myeloma cell line and the humanized antibody (approximately 66 per cent human DNA) is secreted. CDR-grafted antibodies (approximately 90 per cent human DNA) can also be produced by inserting only the mouse CDR DNA sequence into the human variable and constant regions.

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