Modification of plant N-glycans processing: the future of producing therapeutic protein by transgenic plants.
Transgenic plants are regarded as one of the most promising systems for the production of human therapeutic proteins. The number of therapeutic proteins successfully produced in plants is steadily arising. However, the glycoproteins normally produced from plants are not the same as native therapeutic proteins produced from mammals or humans. In addition to in vitro enzymatic modeling glycoproteins, there are two gene manipulation strategies to humanize plant N-glycans connected to the glycoproteins. One is retaining the recombinant glycoproteins in endoplasmic reticulum (ER), the site where few specific modifications of N-glycans occurs. The other is inhibiting the plant endogenous Golgi glycosyltransferase and/or adding new glycosyltransferase from mammalians. In this review, the biosynthesis of N-glycans in plants, the modification of the plant N-glycans processing will be discussed.
Chen
Min
M
The State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong 250100, P.R. China.
Liu
Xianwei
X
Wang
Zhankun
Z
Song
Jing
J
Qi
Qingsheng
Q
Wang
Peng George
PG
D004721:Endoplasmic Reticulum / Q000378:metabolism; D005643:Fucose / Q000378:metabolism; D005690:Galactose / Q000378:metabolism; D006031:Glycosylation; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D030821:Plants, Genetically Modified / Q000235:genetics*; D011134:Polysaccharides / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000627:therapeutic use; D014994:Xylose / Q000378:metabolism
D011134:Polysaccharides; D011994:Recombinant Proteins; D005643:Fucose; D014994:Xylose; D019158:N-Acetylneuraminic Acid; D005690:Galactose