Research Article
Shilei Wang, Quanyong He, Jinl
Abstract
Protein glycosylation is a site-specific enzymatic process to attach oligosaccharides or carbohydrates to proteins. N-linked glycosylation (N-glycosylation) is the major type of glycosylation for the post-translational and co-translational modification of proteins in eukaryotic cells. N-linked glycosylation is to link saccharide molecules to proteins via covalently coupling oligosaccharides or glycans to the amino acid residue asparagine (Asn, N) of proteins, mostly with the requirement of a Asn–X–Ser/Thr (N-X-S/T) consensus sequence. N-linked protein glycosylation is of significance and plays critical roles in biological and pathological processes, and also applied for modern drug development. Particularly, the strategy to engineer N-linked glycosylation site(s) can stabilize the recombinant fusion proteins. This technology has been widely applied for drug discovery, especially for the peptide drugs such as rabies viral glycoprotein (RVG), cardiac-targeting peptide (CTP), bovine adrenal medulla (BAM).