GlcNAc transferases and glycoengineering in Chinese hamster ovary cells

Abstract

Glycosylation constitutes one of the most important post-translational modifications of proteins, with over 60% of proteins known to be glycosylated. GlcNAc transferases (GnTs) belong to a large subfamily of glycosyltransferases residing in the Golgi apparatus and play a key role in the synthesis of mature A-linked glycan structures attached to proteins. In forming multi-antennary A-glycan structures in Chinese hamster ovary cells (CHO), GlcNAc residues may be added to the trimannosyl core by four different GlcNAc transferases (I, II, IV and V).