Engineering Asymmetrically Glycosylated IgG Antibodies

Application

A novel method to develop asymmetrically glycosylated therapeutic monoclonal IgG antibodies for preventing and treating diseases like cancer, infectious diseases, and autoimmune disorders.

Key Benefits

Different IgG antibody glycoforms can be produced, each with its unique effector functions and biological and therapeutic effects.
Potential to produce a new class of therapeutic monoclonal antibodies for treating a wide range of human diseases.

Market Summary

Monoclonal antibodies are essential therapeutic modalities for treating a plethora of different diseases, ranging from cancer, autoimmune disorders, degenerative diseases, and inflammation. The FDA approved the first antibody over three decades ago, and since then more than 570 have been studied in clinical trials, over 80 have been FDA-approved. Although antibodies have changed how many diseases are treated, they still have several limitations, including intracellular targeting, undruggable targets, protein-protein interactions, etc. One of the primary indicators of an antibody's effectiveness is the glycosylation or the arrangement of sugar molecules within the drug. For instance, the glycan attached to Asn297 of immunoglobulin G (IgG) antibodies is a major molecular determinant in a drug’s activity. However, current antibodies lack the optimal glycosylation patterns for maximum efficacy.

Technical Summary

Emory researchers have developed a new method for producing asymmetrically glycosylated IgG antibodies with Asn297-linked glycan structures. The process uses protein engineering and state-of-the-art glycosylation techniques to achieve asymmetric glycosylation on IgG antibodies. These antibodies have differentiated Asn297-linked glycan structures on either IgG heavy chain protomer, which can improve antibody efficacy.