Year: 2015
Type: article
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.
Authors: Chin-Wei Lin, Ming-Hung Tsai, Shiou-Ting Li, Tsung-I Tsai, Kuo-Ching Chu, Ying-Chih Liu, Meng-Yu Lai, Chia-Yu Wu, Yung-Chieh Tseng, Sachin S. Shivatare, Chia-Hung Wang, Ping Chao, Shi-Yun Wang, Hao-Wei Shih, Yi-Fang Zeng, Tsai-Hong You, Jung-Yu Liao, Yu-Chen Tu, Yih-Shyan Lin, Hong-Yang Chuang, Chia-Lin Chen, Charng-Sheng Tsai, Chiu-Chen Huang, Nan-Horng Lin, Che Ma, Chung-Yi Wu, Chi-Huey Wong
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
OpenAlex ID: W1908224577