Author:
Lin Chin-Wei,Tsai Ming-Hung,Li Shiou-Ting,Tsai Tsung-I,Chu Kuo-Ching,Liu Ying-Chih,Lai Meng-Yu,Wu Chia-Yu,Tseng Yung-Chieh,Shivatare Sachin S.,Wang Chia-Hung,Chao Ping,Wang Shi-Yun,Shih Hao-Wei,Zeng Yi-Fang,You Tsai-Hong,Liao Jung-Yu,Tu Yu-Chen,Lin Yih-Shyan,Chuang Hong-Yang,Chen Chia-Lin,Tsai Charng-Sheng,Huang Chiu-Chen,Lin Nan-Horng,Ma Che,Wu Chung-Yi,Wong Chi-Huey
Abstract
Antibodies have been developed as therapeutic agents for the treatment of cancer, infection, and inflammation. In addition to binding activity toward the target, antibodies also exhibit effector-mediated activities through the interaction of the Fc glycan and the Fc receptors on immune cells. To identify the optimal glycan structures for individual antibodies with desired activity, we have developed an effective method to modify the Fc-glycan structures to a homogeneous glycoform. In this study, it was found that the biantennary N-glycan structure with two terminal alpha-2,6-linked sialic acids is a common and optimized structure for the enhancement of antibody-dependent cell-mediated cytotoxicity, complement-dependent cytotoxicity, and antiinflammatory activities.
Publisher
Proceedings of the National Academy of Sciences