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To enhance the body’s immune ability, we developed our Fc Optimization platform, which introduces certain mutations into the Fc region of an antibody and is able to modulate antibody interaction with immune effector cells. Such interaction enhances the body’s immune ability to mediate the killing of cancer cells through antibody dependent cellular cytotoxic (ADCC).
The Fc region mediates the function of certain antibodies by binding to different activating and inhibitory IgG antibody receptors, referred to as FcγRs, on immune effector cells found within the innate immune system. By engineering Fc regions to bind with an increased affinity to the activating FcγRs and with a reduced affinity to the inhibitory FcγRs, we have been able to impart a more effective immune response, and improve effector functions, such as ADCC. This is another example in which small changes in antibody structure can confer improvements on normal immune processes.
We have established a proprietary platform to engineer, screen, identify and test antibodies’ Fc regions with customizable activity. To date, we have successfully incorporated our Fc variations in two of our clinical-stage antibody product candidates, margetuximab and enoblituzumab. We have pre-clinical data demonstrating that these Fc variants have substantially improved the therapeutic effects of these antibodies as compared to their unmodified counterparts. In addition, clinical data from our Phase 3 SOPHIA study of margetuximab demonstrated an improvement in activity over that of trastuzumab, an analog monoclonal antibody with a wild-type, non-engineered Fc domain.