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.
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