Protein glycosylation in diverse cell systems: implications for modification and analysis of recombinant proteins.
A major challenge for the biotechnology industry is to engineer the glycosylation pathways of expression systems to synthesize recombinant proteins with human glycosylation. Inappropriate glycosylation can result in reduced activity, limited half-life in circulation and unwanted immunogenicity. In this review, the complexities of glycosylation in human cells are explained and compared with glycosylation in bacteria, yeasts, fungi, insects, plants and nonhuman mammalian species. Key advances in the engineering of the glycosylation of expression systems are highlighted. Advances in the challenging and technically complex field of glycan analysis are also described. The emergence of a new generation of expression systems with sophisticated engineering for humanized glycosylation of glycoproteins appears to be on the horizon.
Brooks
Susan A
SA
Oxford Brookes University, School of Biological & Molecular Sciences, Gipsy Lane, Headington, Oxford, OX3 0BP, UK. sbrooks@brookes.ac.uk
D002478:Cells, Cultured; D006023:Glycoproteins / Q000138:chemical synthesis* / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D015202:Protein Engineering / Q000379:methods*; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000032:analysis / Q000138:chemical synthesis / Q000378:metabolism
D006023:Glycoproteins; D011994:Recombinant Proteins