Modification of plant N-glycans processing: the future of producing therapeutic protein by transgenic plants

Med Res Rev. 2005 May;25(3):343-60. doi: 10.1002/med.20022.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Endoplasmic Reticulum / metabolism
  • Fucose / metabolism
  • Galactose / metabolism
  • Glycosylation
  • N-Acetylneuraminic Acid / metabolism
  • Plants, Genetically Modified / genetics*
  • Polysaccharides / metabolism*
  • Recombinant Proteins / biosynthesis*
  • Recombinant Proteins / therapeutic use
  • Xylose / metabolism

Substances

  • Polysaccharides
  • Recombinant Proteins
  • Fucose
  • Xylose
  • N-Acetylneuraminic Acid
  • Galactose