Journal
GLYCOBIOLOGY
Volume 30, Issue 4, Pages 214-225Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwz068
Keywords
antibody; Fc gamma receptor; immunoglobulin G; N-glycosylation
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Funding
- National Institutes of Health [R01 GM115489]
- Japan Society for the Promotion of Science Kakenhi [JP16H04758, JP19H03362]
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Therapeutic monoclonal antibodies (mAbs) are the fastest growing group of drugs with 11 new antibodies or antibody-drug conjugates approved by the Food and Drug Administration in 2018. Many mAbs require effector function for efficacy, including antibody-dependent cell-mediated cytotoxicity triggered following contact of an immunoglobulin G (IgG)-coated particle with activating crystallizable fragment (Fc) gamma receptors (Fc gamma Rs) expressed by leukocytes. Interactions between IgG1 and the Fc gamma Rs require post-translational modification of the Fc with an asparagine-linked carbohydrate (N-glycan). Though the structure of IgG1 Fc and the role of Fc N-glycan composition on disease were known for decades, the underlying mechanism of how the N-glycan affected Fc gamma R binding was not defined until recently. This review will describe the current understanding of how N-glycosylation impacts the structure and function of the IgG1 Fc and describe new techniques that are poised to provide the next critical breakthroughs.
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