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Adv Drug Deliv Rev. 2006 Aug 7;58(5-6):640-56. Epub 2006 May 23.

Engineering of therapeutic antibodies to minimize immunogenicity and optimize function.

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  • 1Department of Protein engineering, Schering-Plough Biopharma, 901 California Avenue, Palo Alto, CA 94304, USA.


One of the first difficulties in developing monoclonal antibody therapeutics was the recognition that human anti-mouse antibody (HAMA) response limited the administration of murine antibodies. Creative science has lead to a number of ways to counter the immunogenicity of non-human antibodies, primarily through chimeric, humanized, de-immunized, and most recently, human-sequence therapeutic antibodies. Once therapeutic antibodies of low or no immunogenicity were available, the creativity then turned to engineering both the antigen-binding domains (e.g., affinity maturation, stability) and altering the effector functions (e.g. antibody-dependent cellular cytotoxicity, complement-dependent cellular cytotoxicity, and clearance rate).

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