Introduction: Glycans are increasingly important in the development of new biopharmaceuticals with optimized efficacy, half-life, and antigenicity. Current expression platforms for recombinant glycoprotein therapeutics typically do not produce homogeneous glycans and frequently display non-human glycans which may cause unwanted side effects. To circumvent these issues, glyco-engineering has been applied to different expression systems including mammalian cells, insect cells, yeast, and plants.
Areas covered: This review summarizes recent developments in glyco-engineering focusing mainly on in vivo expression systems for recombinant proteins. The highlighted strategies aim at producing glycoproteins with homogeneous N- and O-linked glycans of defined composition.
Expert opinion: Glyco-engineering of expression platforms is increasingly recognized as an important strategy to improve biopharmaceuticals. A better understanding and control of the factors leading to glycan heterogeneity will allow simplified production of recombinant glycoprotein therapeutics with less variation in terms of glycosylation. Further technological advances will have a major impact on manufacturing processes and may provide a completely new class of glycoprotein therapeutics with customized functions.
Keywords: N-glycosylation; O-glycosylation; biopharmaceuticals; glycosyltransferases; recombinant glycoprotein.