Earticle

초록

영어

The N-linked glycan on the Fc (fragment crystallizable) domain of IgG antibody is indispensable for binding to effector Fc gamma receptors (FcγRs) expressed on various immune cells and hence for the clearance of abnormal target cells. In IgG molecules, removal of the invariant glycan at Asn297 abolishes binding to FcγRs and effector functions. Recently, we have engineered aglycosylated IgG Fc variants that showed binding to FcγRI with affinity nearly identical to that of glycosylated antibodies. Interestingly, the engineered aglycosylated antibodies were able to potentiate tumor cell killing with dendritic cells (DCs) as effectors, while the glycosylated antibodies did not induce the DC-mediated ADCC (antibody dependent cell-mediated cytotoxicity). Additionally, we have isolated an aglycosylated antibody with selectivity towards activating FcγRIIa over inhibitory FcγRIIb and with superior macrophage-mediated ADCP (antibody dependent cell-mediated phagocytosis) when compared with a clinical grade glycosylated antibody. A set of Fc engineered versions of aglycosylated antibody with various receptor selectivities and unique effector functions have been generated and will be discussed.

키워드

저자

• Sang Taek JUNG [ Dept. of Chemical Engineering, The University of Texas at Austin, Austin, TX 78712. ]
• Tae Hyun KANG [ Dept. of Biomedical Engineering, The University of Texas at Austin, Austin, TX 78712. ]
• William KELTON [ Dept. of Chemical Engineering, The University of Texas at Austin, Austin, TX 78712. ]
• George GEORGIOU [ Dept. of Chemical Engineering, The University of Texas at Austin, Austin, TX 78712. ]

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576