Post-translational modification of plant-made foreign proteins; glycosylation and beyond

Diane Webster, Merlin C Thomas

Research output: Contribution to journalArticleResearchpeer-review

58 Citations (Scopus)

Abstract

The complex and diverse nature of the post-translational modification (PTM) of proteins represents an efficient and cost-effective mechanismfor the exponential diversification of the genome. PTMs have been shown to affect almost every aspect of protein activity, including function, localisation, stability, and dynamic interactions with other molecules. Although many PTMs are evolutionarily conserved there are also important kingdom-specific modifications which should be considered when expressing recombinant proteins. Plants are gaining increasing acceptance as an expression system for recombinant proteins, particularly where eukaryotic-like PTMs are required.Glycosylation is themost extensively studied PTMof plant-made recombinant proteins.However, other types of protein processing and modification also occur which are important for the production of high quality recombinant protein, such as hydroxylation and lipidation. Plant and/or protein engineering approaches offer many opportunities to exploit PTM pathways allowing the molecular farmer to produce a humanised product withmodifications functionally similar or identical to the native protein. Indeed, plants have demonstrated a high degree of tolerance to changes in PTM pathways allowing recombinant proteins to be modified in a specific and controlled manner, frequently resulting in a homogeneity of product which is currently unrivalled by alternative expression platforms. Whether a recombinant protein is intended for use as a scientific reagent, a cosmetic additive or as a pharmaceutical, PTMs through their presence and complexity, offer an extensive range of options for the rational design of humanised (biosimilar), enhanced (biobetter) or novel products.
Original languageEnglish
Pages (from-to)410 - 418
Number of pages9
JournalBiotechnology Advances
Volume30
DOIs
Publication statusPublished - 2012

Cite this