| Literature DB >> 26253764 |
Chin-Wei Lin1, Ming-Hung Tsai2, Shiou-Ting Li3, Tsung-I Tsai3, Kuo-Ching Chu2, Ying-Chih Liu2, Meng-Yu Lai4, Chia-Yu Wu3, Yung-Chieh Tseng5, Sachin S Shivatare2, Chia-Hung Wang2, Ping Chao2, Shi-Yun Wang2, Hao-Wei Shih2, Yi-Fang Zeng2, Tsai-Hong You2, Jung-Yu Liao2, Yu-Chen Tu2, Yih-Shyan Lin2, Hong-Yang Chuang2, Chia-Lin Chen6, Charng-Sheng Tsai2, Chiu-Chen Huang2, Nan-Horng Lin2, Che Ma3, Chung-Yi Wu7, Chi-Huey Wong8.
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.Entities:
Keywords: Fc glycosylation; endoglycosidase; glycoengineered antibodies; homogeneous antibodies; sugar oxazoline
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Year: 2015 PMID： 26253764 PMCID： PMC4553773 DOI： 10.1073/pnas.1513456112
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205