Currently, recombinant IgG’s are the major biotherapeutics that are being used to treat many human diseases. These IgG’s are glycosylated in the Fc region and glycans play important roles in the antibody effector functions. However, these glycans are highly heterogeneous and the heterogeneity arises from the presence or the absence of different terminal sugars, including sialic acid, galactose and N-acetylglucosamine, core fucose along with bisecting N-acetylglucosamine. To understand the influence of individual terminal sugar residues on serum half-life and antibody effector functions, it is necessary to prepare homogeneous IgG glycoforms. This presentation describes glycoengineering strategies to prepare IgG molecules containing homogeneous glycan chains in the Fc region and their significance in assessing IgG functions.

 During conventional primary screening, monoclonal antibodies are characterized and grouped into different bins based on their binding affinity, specificity, species cross-reactivity, and cell based functional activity. However, identifying antibodies binding to distinct, non-overlapping epitopes would complement conventional screening and thus guide the selection of lead therapeutic monoclonal antibodies with broader diversity