Abstract
The glycosylation of biomolecules is essential for cell recognition and immune regulation. Intermolecular carbohydrate-carbohydrate interactions between the antibody Fc fragment and Fc receptor (FcR) are required for immune-cell activation. Further, antibody Fc glycans can be glycoengineered to enhance these interactions for applications in cancer immunotherapy: e.g. the removal of core fucose in the antibody Fc glycan enhances binding of the Fc fragment to the FcR and, thereby, immune-cell activity.
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