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영어

Antibody IgG has been evolved in natural immune system against a variety of pathogens and widely used for therapeutics, diagnostics, and research reagents due to its high evolvability which adopts new functions at ease with tolerating destabilizing mutations. In IgG molecules, removal of the invariant glycan at Asn297 abolishes binding to FcγRs (Fc gamma receptors) expressed on the surface of various immune cells. Therefore, aglycosylated antibodies produced in bacteria have not been used for therapeutic antibodies requiring effector functions such as clearance of tumor cells. In this lecture, I will present a set of Fc (fragment crystallizable) engineered versions of aglycosylated antibody with various FcγRs selectivities and unique therapeutic effector functions that clinical grade glycosylated antibodies do not display. Additionally, cytochrome P450 enzyme, a biocatalyst transforming a broad scope of substrates, has been evolved for a novel diagnostic tool. Strategies to increase sensitivity of the biomedical agent have been developed and will be discussed.