About the Report: The majority of clinically approved protein drugs bear some form of post-translational modification, most commonly glycosylation. Glycosylation is the attachment of a carbohydrate group to a protein, catalyzed by enzymes called glycosyl transferases. It is either N-linked, in which a carbohydrate is attached to the side chain of a specific asparagine, or O-linked, in which it is attached to the hydroxyl oxygen of a serine or threonine, the former being most prominent. While N-linked glycosylation occurs largely in the endoplasmic reticulum (ER) of mammalian cells, O-linked glycosylation initiates in either the ER or Golgi apparatus. Glycosylation is important because it can influence the therapeutic efficacy, immunogenicity, solubility, and in-vivo half life of the glycoprotein. A major obstacle in the pharmaceutical application of glycoproteins is the inherent heterogeneity of their glycan structures. Mammalian cell culture systems, especially Chinese hamster ovary (CHO) cells, are the preferred method for the production of therapeutic glycoproteins. Other systems such as E.coli, filamentous fungi, yeast, insects, plants and transgenic animals are also being engineered to produce proteins with optimal glycosylation pattern. Optimizing production methods to obtain a glycoform profile as similar to that in humans is the current goal in glycoengineering research. Some of the bestsellers among therapeutic proteins will soon lose patent protection. Therefore ...
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