title: Using glyco-engineering to produce therapeutic proteins.
abstract: BACKGROUND
  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.
  
  
  METHODS
  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.
  
  
  CONCLUSIONS
  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.affiliation: a 1 University of Natural Resources and Life Sciences , Department of Applied Genetics and Cell Biology , Muthgasse 18, Vienna, Austria.
authors.forename: Martina
authors.initials: M
authors.lastname: Dicker
authors.affiliation: b 2 University of Natural Resources and Life Sciences, Department of Applied Genetics and Cell Biology , Muthgasse 18, Vienna, Austria +43 1 47654 6705 ; +43 1 47654 6392 ; richard.strasser@boku.ac.at.
authors.forename: Richard
authors.initials: R
authors.lastname: Strasser
mesh_terms: D000911:Antibodies, Monoclonal / Q000235:genetics / Q000378:metabolism / Q000493:pharmacokinetics; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism* / Q000493:pharmacokinetics; D006031:Glycosylation; D006207:Half-Life; D006801:Humans; D011134:Polysaccharides / Q000378:metabolism*; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000493:pharmacokinetics
chemical_list: D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D011134:Polysaccharides; D011994:Recombinant Proteins
keywords: N-glycosylation; O-glycosylation; biopharmaceuticals; glycosyltransferases; recombinant glycoprotein