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- Publisher
- Oxford University Press
- Copyright
- Copyright © 2015 Oxford University Press
- ISSN
- 0959-6658
- eISSN
- 1460-2423
- DOI
- glycob;9/4/365
- Publisher site
- See Article on Publisher Site
Abstract
Since plants are emerging as an important system for the expression of recombinant glycoproteins, especially those intended for therapeutic purposes, it is important to scrutinize to what extent glycans harbored by mammalian glycoproteins produced in transgenic plants differ from their natural counterpart. We report here the first detailed analysis of the glycosylation of a functional mammalian glycoprotein expressed in a transgenic plant. The structures of the N-linked glycans attached to the heavy chains of the monoclonal antibody Guy's 13 produced in transgenic tobacco plants (plantibody Guy's 13) were identified and compared to those found in the corresponding IgG1 of murine origin. Both N-glycosylation sites located on the heavy chain of the plantibody Guy's 13 are N-glycosylated as in mouse. However, the number of Guy's 13 glycoforms is higher in the plant than in the mammalian expression system. Despite the high structural diversity of the plantibody N-glycans, glycosylation appears to be sufficient for the production of a soluble and biologically active IgG in the plant system. In addition to high-mannose-type N-glycans, 60% of the oligosaccharides N-linked to the plantibody have β(1, 2)-xylose and α(1, 3)-fucose residues linked to the core Man3GlcNAc2. These plant-specific oligosaccharide structures are not a limitation to the use of plantibody Guy's 13 for topical immunotherapy. However, their immunogenicity may raise concerns for systemic applications of plantibodies in human. Key words Key words monoclonal antibody N-glycosylation transgenic plants Abbreviations: Abbreviations HPAEC-PAD high pH anion exchange chromatography coupled to pulsed amperometric detection MAb monoclonal antibody 1 H NMR proton nuclear magnetic resonance PA pyridylamino derivative plantibody recombinant antibody produced in transgenic plants PNGase A peptide N-glycosidase A PNGase F peptide N-glycosidase F RCA Ricinus communis agglutinin © 1999 Oxford University Press « Previous | Next Article » Table of Contents This Article Glycobiology (1999) 9 (4): 365-372. » Abstract Free Full Text (HTML) Free Full Text (PDF) Free Classifications Article Services Article metrics Alert me when cited Alert me if corrected Find similar articles Similar articles in Web of Science Similar articles in PubMed Add to my archive Download citation Request Permissions Disclaimer Citing Articles Load citing article information Citing articles via CrossRef Citing articles via Scopus Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Cabanes-Macheteau, M. 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Journal
Glycobiology – Oxford University Press
Published: Apr 1, 1999