Antibody Dependant Cell Cytotoxicity (ADCC) is one of the powerful mechanisms of the immune system that can be harnessed by therapeutic monoclonal antibodies to destroy tumour cells. The effectiveness of the antibody to facilitate this activity is dependent on two factors – binding to the target protein expressed by the tumour cells and binding to the CD16a (FcγRIIIa) receptor on the effector cells. Focusing on the CD16a binding, it is widely understood that the structure of carbohydrates attached to the Fc region of the antibody are key to the binding; core fucose in particular has been shown to be very important in this respect. The result of changes to the abundance of fucose has a fundamental impact on ADCC activity. Today, many manufacturers of Biosimilars or New Biological Entities (NBEs) are interested in understanding the nature of the glycan structures on a therapeutic antibody to ensure the optimum ADCC activity is harnessed.
BioOutsource offers a Released N-Glycan Assay for the in-depth profiling of IgG glycosylation. Glycans are enzymatically removed from the antibody and then labelled before a high resolution LC separation is performed. Fluorescence detection coupled with online ESI mass spectrometry enables confident assignment and accurate quantification of the different glycan structures. These can then be grouped according to their structural classification (e.g. complex, oligomannose) and monosaccharide composition, such as fucose, galactose and sialic acid profiles.
At the heart of the biosimilar development process, lies an understanding of the link between antibody structure and function. BioOutsource offers the capabilities to understand the structural complexities of your biosimilar mAb and how this influences protein-protein interactions and consequently drives the ensuing biological activity.
To gain a deeper understanding of your biosimilar product please contact our experts today.