N-Glycosylation of Plant-produced Recombinant Proteins

H.J. Bosch, A. Castilho, A. Loos, A. Schots, H. Steinkeller

Research output: Contribution to journalArticleAcademicpeer-review

101 Citations (Scopus)


Plants are gaining increasingly acceptance as a production platform for recombinant proteins. One reason for this is their ability to carry out posttranslational protein modifications in a similar if not identical way as mammalian cells. The capability of plants to carry out human-like complex glycosylation is well known. Moreover, the targeted manipulation of the plant N-glycosylation pathway allows the production of proteins carrying largely homogeneous, human-type oligosaccharides. These outstanding results have placed plants in a favourable position compared to other eukaryotic expression systems. This review provides a comprehensive summary of the N-glycosylation of plant-produced recombinant proteins, the possible impact of plant-specific N-glycans on the human immune system, and recent advances in engineering the plant N-glycosylation pathway towards the synthesis of (complex) human-type glycan structures, highlighting challenges and achievements in the application of these powerful technologies
Original languageEnglish
Pages (from-to)5503-5512
JournalCurrent Pharmaceutical Design
Issue number31
Publication statusPublished - 2013


  • reactive carbohydrate determinants
  • human monoclonal-antibody
  • sialic acid transporter
  • arabidopsis-thaliana
  • transgenic plants
  • storage vacuoles
  • endoplasmic-reticulum
  • high-level
  • beta-1,4-n-acetylglucosaminyltransferase iii
  • human beta-1,4-galactosyltr


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