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Fc-galactosylation modulates antibody-dependent cellular cytotoxicity of therapeutic antibodies
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文摘

Exploratory statistical analysis of data from 54 manufactured batches of an IgG1 therapeutic antibody (mAb1) suggests that ADCC activity is not only modulated by afucose but also by galactose.

We enzymatically modulate the galactose levels of four different batches of mAb1 and confirm that the presence of terminal galactose enhances ADCC activity.

The ADCC enhancing effect of galactose is observed in 4 additional monoclonal antibodies derived using standard CHO-based manufacturing processes.

In contrast, the ADCC activity of IgG1 monoclonal antibody glycoengineered to contain a high degree of afucosylation remains unchanged by the addition of galactose, suggesting that while the levels of galactose have some influence on ADCC activity, the impact of afucose is still predominant.

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