Towards the development of a surface plasmon resonance assay to evaluate the glycosylation pattern of monoclonal antibodies using the extracellular domains of CD16a and CD64.

We here report the production and purification of the extracellular domains of two Fcγ receptors, namely CD16a and CD64, by transient transfection in mammalian cells. The use of these two receptor ectodomains for the development of quantitative assays aiming at controlling the quality of monoclonal antibody production lots is then discussed. More specifically, the development of surface plasmon resonance-based biosensor assays for the evaluation of the glycosylation pattern and the aggregation state of monoclonal antibodies is presented. Our biosensor approach allows discriminating between antibodies harboring different galactosylation profiles as well as to detect low levels (i.e., less than 2%) of monoclonal antibody aggregates.