Glyco-engineering of biotherapeutic proteins in plants

• Published in: Molecules and cells Vol. 25; no. 4; pp. 494 - 503
• Main Authors: Ko, K.S. (Wonkwang University, Iksan, Republic of Korea), E-mail: ksko@wku.ac.kr, Ahn, M.H. (Wonkwang University, Iksan, Republic of Korea), Song, M.R. (Wonkwang University, Iksan, Republic of Korea), Choo, Y.K. (Wonkwang University, Iksan, Republic of Korea), Kim, H.S. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea), Ko, Kinarm (Max Planck Institute for Molecular Biomedicine, Department of Cell and Developmental Biology, Munster, Germany), Joung, H. (Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea)
• Format: Journal Article
• Language: English
• Published: United States 한국분자세포생물학회 30.06.2008
• Subjects: Biopharmaceutics - methods; Endoplasmic Reticulum - metabolism; GLICOPROTEINAS; GLYCOPROTEINE; GLYCOPROTEINS; Glycoproteins - biosynthesis; Glycoproteins - genetics; Glycosylation; Golgi Apparatus - metabolism; Humans; molecular biopharming; monoclonal antibody; PLANTAS TRANSGENICAS; PLANTE TRANSGENIQUE; Plants, Genetically Modified - cytology; Plants, Genetically Modified - enzymology; Plants, Genetically Modified - genetics; Protein Engineering; Protein Transport - genetics; PROTEINAS RECOMBINANTES; PROTEINE RECOMBINANTE; RECOMBINANT PROTEINS; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Recombinant Proteins - therapeutic use; TRANSGENIC PLANTS; 생물학
• ISSN: 1016-8478; 0219-1032
• DOI: 10.1016/s1016-8478(23)17610-2

Many therapeutic glycoproteins have been successfully generated in plants. Plants have advantages regarding practical and economic concerns, and safety of protein production over other existing systems. However, plants are not ideal expression systems for the production of biopharmaceutical proteins, due to the fact that they are incapable of the authentic human N-glycosylation process. The majority of therapeutic proteins are glycoproteins which harbor N-glycans, which are often essential for their stability, folding, and biological activity. Thus, several glyco-engineering strategies have emerged for the tailor-making of N-glycosylation in plants, including glycoprotein subcellular targeting, the inhibition of plant specific glycosyltranferases, or the addition of human specific glycosyltransferases. This article focuses on plant N-glycosylation structure, glycosylation variation in plant cell, plant expression system of glycoproteins, and impact of glycosylation on immunological function. Furthermore, plant glyco-engineering techniques currently being developed to overcome the limitations of plant expression systems in the production of therapeutic glycoproteins will be discussed in this review.