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[BK21 Plus Seminar]
▶Subject: Engineered Fc variants to modulate Fc-mediated functions
▶Speaker: Chang-Han Lee, Ph.D. (University of Texas at Austin)
▶Date: 11:10AM/Nov. 25(Mon.)/2019
▶Place: Conference room(#179), Postech Biotech Center
Monoclonal antibody such as immunoglobulin G (IgG) is a good biomolecule for clinical purpose. Therapeutic IgG has two functional domains; 1) Fab domain which recognize pathogenic target and 2) Fc domain which triggers numerous cellular phenotypes via Fc-binding proteins, collectively referred to as “effector functions”. Antibody effector functions constitute a critical link between adaptive and innate immunity and are of paramount significance for the clearance of pathogenic cells and for immune homeostasis. Fc effector functions are central to the mechanism of action of numerous therapeutic antibodies, especially for the treatment of cancer and for infectious diseases. Fc domain of IgG binds to neonatal Fc receptor (FcRn), complement C1q and six Fcγ receptors (FcγRs). C1q and FcγRs are responsible in IgG-mediated effector functions which are critical for the development of improved therapeutics, but the role of C1q or each FcγR is not clear because most immune cells express several FcγRs and complement receptors (CRs). In order to study the role of C1q or each FcγR, I developed C1q-specific Fc variant, FcγRIIIa-specific Fc variant, and FcγRIIa-selective Fc variant using bacterial display techniques such as E.coli-display and yeast surface display. First, using engineered C1q-specific Fc domain, I demonstrate that for therapeutic antibodies, complement-dependent cellular cytotoxicity (CDCC) and complement-dependent cellular phagocytosis (CDCP) by immunological effector molecules mediated the clearance of target cells. Second, using each FcγR-specific Fc variant, I study the contribution of particular FcγRs in effector functions.
▶Inquiry: Prof. Jie-Oh Lee (279-2323)
* This seminar will be given in English.
Please refrain from taking photos during seminars. *