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About glycoengineering

Glycosylation, entailing the covalent attachment of carbohydrate moieties to specific biomolecules, is one of the most common post-translational modification mainly taking place in the endoplasmic reticulum (ER) and Golgi apparatus. About half of all proteins expressed in cells undergo this modification. Glycosylation generally has a major impact on the efficacy and stability of biopharmaceuticals. The CH2 domain of each heavy chain contains one conserved N-glycosylation site at Asn297, and approximately 1/5 of human IgGs have a second N-glycosylation motif in the variable region. Antibody glycoengineering is being developed as a method to control the composition of glycans and to enhance the pharmacological properties of therapeutic antibody, including physical stability, immunogenicity, pharmacokinetics and target recognition. For example, by removal of the core fucose residue from the Fc region of the antibody, the affinity of the antibody for receptors on immune effector cells is i

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