Journal
EXPERT OPINION ON BIOLOGICAL THERAPY
Volume 15, Issue 10, Pages 1501-1516Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1517/14712598.2015.1069271
Keywords
biopharmaceuticals; glycosyltransferases; N-glycosylation; O-glycosylation; recombinant glycoprotein
Funding
- Austrian Federal Ministry of Transport, Innovation, and Technology (bmvit)
- Austrian Science Fund (FWF) [TRP 242-B20]
- Austrian Science Fund (FWF) [TRP 242] Funding Source: researchfish
- Austrian Science Fund (FWF) [TRP242] Funding Source: Austrian Science Fund (FWF)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available