Monoclonal antibodies

Many CDS2 antibodies have been generated including different rat isotypes (e.g. CAMPATH-1 M, rat immunoglobulin M (IgM) and CAMPATH-1 G, rat IgG2b), matched sets of chimeric human/rat IgG and a variety of mutants. These have been used to demonstrate the role of IgG isotype for complement activation and Fc receptor binding, showing that rat IgG2b and human IgGl are among the best subclasses for activating human effector systems. However, even human IgG4 (previously thought to be inert) was able to deplete human lymphocytes in vivo. CAMPATH-1 H (human IgGl) was the first fully humanized monoclonal antibody. It was created by transplantation of the complementarity-determin-ing regions of CAMPATH-1 G into human heavy and light chain genes. Initial binding affinity was diminished, but this was corrected by small modifications to framework residues. Administration of the humanized antibody to patients has greatly reduced the possible antiglobulin response, compared with the original rat antibody. Following this experience, most other therapeutic antibodies are likely to be humanized.

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