Abstract
Antibody dynamics on membranes, such as endocytosis and clustering, are vital in determining antibody functions. In this study, we demonstrated that glycan conjugation can modulate antibody dynamics through the glycan-lectin interaction to regulate its potency. The anti-HER2 antibody, an anti-breast cancer antibody, was conjugated with galactose-containing N-glycan, and its internalization was suppressed by interaction with galectin-3, leading to enhanced complement-dependent cytotoxic (CDC) activity. This glycan-antibody conjugate is proposed as a new approach to modulate antibody activity and may provide an alternative strategy for redeveloping antibody drugs that do not exhibit sufficient activity.
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