MUC16 Protein and the Role of Glycosylation in Developing Antibody Therapies for Ovarian Cancer

Andrew Manion, Seerat Aujla, Dr. Cory Brooks

Vol. 8, Jan-Dec 2022

Page Number: 104-108

Abstract:

To test the competitiveness of our panel of antibodies and determine whether glycosylation affects antibody binding affinity, we examine the aberrant functioning of the MUC16 protein in cancer cells. After identifying the MUC16 protein contains the CA125 biomarker and determining its role in ovarian tumor growth and metastasis, the goal is to determine the impact glycosylation has on the binding affinity on certain antibodies, such as mAR9.6. Due to cleaving and shedding of the extracellular domain of the MUC16 protein, it has been difficult to find a promising region for target therapies; most antibodies cannot detect the remaining MUC16 fragment on the surface of the cell after it has been cleaved off. Additionally, MUC16 can act as a barrier to Natural Killer (NK) cells and monocytes, inhibiting its ability to attack tumor cells (Aithal et. al 6). Therefore, antibodies that target non-tandem repeat domains, such as the SEA5 domain, were used to understand how glycosylation plays a role in antibody binding and analyze the number of epitopes they will bind in the MUC16 protein.

Back Download