In Vitro Glycoengineering Of IgG1 And Its Effect On Fc Receptor Binding And ADCC Activity

By Marco Thomann, Tilman Schlothauer, Tetyana Dashivets, Sebastian Malik, Cecile Avenal, Patrick Bulau, Petra Rüger, Dietmar Reusch

The glycosylation profile of therapeutic antibodies is a critical quality attribute that can impact their efficacy and is often subject to batch-to-batch variability. This variation makes it challenging to study the precise effect of individual glycan species. This paper overcomes that challenge by using in vitro glycoengineering (IVGE) to create five distinct glycovariants from a single IgG1 batch. The samples included hypo- and hyper-galactosylated variants and variants with increasing levels of sialylation.

Using surface plasmon resonance, affinity chromatography, and cell-based ADCC assays, researchers found that increased galactosylation positively impacts FcγRIIIa receptor binding and ADCC activity. In contrast, sialylation had no significant negative effect.

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