Surface plasmon resonance analysis of the glycosylation of monoclonal antibody therapeutics using lectins


Amit K Dutta1,2, Alexander Peterson1, Hua-Jun He1, Rebecca Zangmeister1, Peter Schuck2, and Michael J. Tarlov1


1 Biochemical Science Division, Material Measurements Laboratory,

National Institute of Standards and Technology


2 Laboratory of Cellular Imaging and Macromolecular Biophysics, National Institute of Health



Monoclonal antibody (mAb) therapeutics will soon be the largest class of drugs for treating human disease. Most mAbs are of the IgG class and are glycoproteins with oligosaccharides or glycans attached in the Fc region. These glycans play a key role in the mechanism of action of mAb therapeutics, and antibody efficacy can vary greatly with changes in composition or structure of glycans. Precise control and complete characterization of glycosylation is therefore essential in the production of mAb-based therapeutics. Current analytical methods for characterizing glycosylation such as high performance liquid chromatography and mass spectrometry are capable of rigorously determining composition, sequence, linkage, and stereoisomerism of glycans. Although powerful techniques, they are time consuming and require considerable expertise. There is a need for more rapid, sensitive, and lower cost methods to analyze oligosaccharides of mAb therapeutics. We are developing a surface plasmon resonance based method using lectins, proteins that selectively bind glycans to rapidly assess the structure and composition of mAb glycans.