Glycobiology, Vol 9, 365-372, Copyright © 1999 by Oxford University Press
M Cabanes-Macheteau, AC Fitchette-Laine, C Loutelier-Bourhis, C Lange, ND Vine, JK Ma, P Lerouge and L Faye
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 beta(1,
2)-xylose and alpha(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.
ORIGINAL ARTICLES
N-Glycosylation of a mouse IgG expressed in transgenic tobacco plants
Laboratoire des Transports Intracellulaires, CNRS-ESA 6037, and Spectrometrie de Masse Bio-organique, Centre Regional Universitairede Spectroscopie, IFRMP 23, Universite de Rouen, UFR des Sciences, 76821 Mont Saint Aignan Cedex, France.
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