A method to detect the binding of hyper-glycosylated fragment crystallizable (Fc) region of human IgG1 to glycan receptors

Abstract

Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines. Such Fc-effector functions are largely controlled by posttranslational modifications (PTMs) within the Fc, including the addition of glycans that introduce structural and functional heterogeneity to this class of therapeutic. Here, we describe a detailed method to allow the detection of hyper-sialylated Fcs to glycan receptors that will facilitate the future development of new mAbs and Fc-fragment therapies and vaccines.