Glyco-engineering in plants to produce human-like N-glycan structures.
It is now possible to produce complex human proteins, largely correctly folded and N-glycosylated, in plants. Much effort has been invested in engineering expression technologies to develop products with superior characteristics. The results have begun to show success in controlling important posttranslational modifications such as N-glycosylation. With the emerging data increasingly indicating the significance of proper N-glycosylation for the efficacy of a drug, glyco-engineering has become an important issue not only for academia but also for the biopharmaceutical industry. Plants have demonstrated a high degree of tolerance to changes in the N-glycosylation pathway, allowing recombinant proteins to be modified into human-like structures in a specific and controlled manner. Frequently the results are a largely homogeneously glycosylated product, currently unrivalled by that of any other expression platforms. This review provides a comprehensive analysis of recent advances in plant N-glyco-engineering in the context of the expression of therapeutically relevant proteins, highlighting both the challenges and successes in the application of such powerful technologies.
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Alexandra
A
Castilho
Herta
H
Steinkellner
D001709:Biotechnology / Q000379:methods; D006023:Glycoproteins / Q000096:biosynthesis* / Q000235:genetics*; D006031:Glycosylation; D006801:Humans; D060847:Metabolic Engineering / Q000379:methods*; D010944:Plants / Q000235:genetics* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics
D006023:Glycoproteins; D011994:Recombinant Proteins