Plant Biotechnol J. 2003 Nov;1(6):451-62. doi: 10.1046/j.1467-7652.2003.00041.x.

Monoclonal C5-1 antibody produced in transgenic alfalfa plants exhibits a N-glycosylation that is homogenous and suitable for glyco-engineering into human-compatible structures.

Plant biotechnology journal

Muriel Bardor, Corinne Loutelier-Bourhis, Thomas Paccalet, Pascal Cosette, Anne-Catherine Fitchette, Louis-P Vézina, Sonia Trépanier, Michèle Dargis, Réal Lemieux, Catherine Lange, Loïc Faye, Patrice Lerouge

PMID: 17134403 DOI: 10.1046/j.1467-7652.2003.00041.x

Abstract

Structural analysis of the N-glycosylation of alfalfa proteins was investigated in order to evaluate the capacity of this plant to perform this biologically important post-translational modification. We show that, in alfalfa, N-linked glycans are processed into a large variety of mature oligosaccharides having core-xylose and core alpha(1,3)-fucose, as well as terminal Lewis(a) epitopes. In contrast, expression of the C5-1 monoclonal antibody in alfalfa plants results in the production of plant-derived IgG1 which is N-glycosylated by a predominant glycan having a alpha(1,3)-fucose and a beta(1,2)-xylose attached to a GlcNAc2Man3GlcNAc2 core. Since this core is common to plant and mammal N-linked glycans, it therefore appears that alfalfa plants have the ability to produce recombinant IgG1 having a N-glycosylation that is suitable for in vitro or in vivo glycan remodelling into a human-compatible plantibody. For instance, as proof of concept, in vitro galactosylation of the alfalfa-derived C5-1 mAb resulted in a homogenous plantibody harbouring terminal beta(1,4)-galactose residues as observed in the mammalian IgG.

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• Journal Article