Glycosylation is the most abundant and diverse form of post-translational modification of proteins. It affects protein folding, stability, transport, and function, and plays important roles in both health and disease. Moreover, glycosylation influences the properties of biologic therapeutics derived from glycoproteins, such as their stability, PK/PD, antigenicity, and activity.
The biosynthesis of glycans is complex, involving approximately 200 glycosyltransferase enzymes that work in concert to produce a wide variety of glycan structures. Through collaboration with the University of Copenhagen, we have developed proprietary design matrices that enable rational and combinatorial genetic engineering of the genes encoding glycosyltransferases. This technology enable us to generate custom-designed glycans, including N-linked, O-linked, and glycosaminoglycans, in mammalian cells.
Cell-based glycanarray
The cell-based glycanarray consists of a panel of glycoengineered cell lines, each expressing homogeneous glycans in the context of proteins and lipids on the cell surface. This array provides a much broader range of glycan epitopes compared to traditional glycan arrays and allows for the identification of natural ligands.
The cell-based glycanarray has a number of applications, including:
- A sustainable resource to produce glycoproteins with defined and homogeneous glycans for therapeutic use
- A tool to interrogate binding specificities with glycan-binding proteins, such as antibodies, lectins, and microbes