1. A common glycan structure on immunoglobulin G for enhancement of effector functions
- Author
-
Ying-Chih Liu, Charng-Sheng Tsai, Hao-Wei Shih, Chi-Huey Wong, Tsai-Hong You, Yih-Shyan Lin, Sachin S. Shivatare, Shiou-Ting Li, Kuo-Ching Chu, Nan-Horng Lin, Yung-Chieh Tseng, Chung-Yi Wu, Chiu-Chen Huang, Meng-Yu Lai, Yu-Chen Tu, Hong-Yang Chuang, Chin-Wei Lin, Chia-Hung Wang, Yi-Fang Zeng, Ping Chao, Ming-Hung Tsai, Chia-Lin Chen, Shi-Yun Wang, Che Ma, Tsung-I Tsai, Jung-Yu Liao, and Chia Yu Wu
- Subjects
Glycan ,Lymphoma, B-Cell ,Streptococcus pyogenes ,Neuraminidase ,Biology ,Antibodies, Viral ,Protein Engineering ,Immunoglobulin G ,Acetylglucosamine ,Bacteroides fragilis ,Mice ,Structure-Activity Relationship ,Bacterial Proteins ,Orthomyxoviridae Infections ,Polysaccharides ,Cell Line, Tumor ,Animals ,Humans ,Structure–activity relationship ,Cytotoxicity ,Receptor ,alpha-L-Fucosidase ,Mice, Inbred BALB C ,Multidisciplinary ,Receptors, IgG ,Immunoglobulin Fc Fragments ,Antibody-Dependent Cell Cytotoxicity ,Protein engineering ,Trastuzumab ,Molecular biology ,HEK293 Cells ,Biochemistry ,Physical Sciences ,Sialic Acids ,biology.protein ,Female ,Antibody ,Rituximab - Abstract
Significance Antibodies are important therapeutic agents and have been used for the treatment of many diseases, including infectious and inflammatory diseases, and cancer. The therapeutic efficacy of an antibody is usually determined not only by the selectivity and affinity toward the target but also by the Fc-glycan structure interacting with the Fc receptors on immune cells. This study describes the preparation of various antibodies with different Fc-glycan structures as homogeneous glycoforms for the investigation of their effector activities. During this study, it was discovered that the biantennary N-glycan structure with two terminal alpha-2,6-linked sialic acids is a common and optimal structure that is able to enhance the activities of antibodies against cancer, influenza, and inflammatory diseases.
- Published
- 2015