Open AccessMonoclonal C5‐1 antibody produced in transgenic alfalfa plants exhibits a N‐glycosylation that is homogenous and suitable for glyco‐engineering into human‐compatible structures
Author(s) -
Bardor Muriel,
LoutelierBourhis Corinne,
Paccalet Thomas,
Cosette Pascal,
Fitchette AnneCatherine,
Vézina LouisP.,
Trépanier Sonia,
Dargis Michèle,
Lemieux Réal,
Lange Catherine,
Faye Loïc,
Lerouge Patrice
Publication year - 2003
Publication title -
plant biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.525
H-Index - 115
eISSN - 1467-7652
pISSN - 1467-7644
DOI - 10.1046/j.1467-7652.2003.00041.x
Subject(s) - glycosylation , fucose , glycan , biology , monoclonal antibody , epitope , biochemistry , xylose , recombinant dna , n linked glycosylation , galactose , glycoprotein , antibody , gene , immunology , fermentation
Summary 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 α(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 IgG 1 which is N‐glycosylated by a predominant glycan having a α(1,3)‐fucose and a β(1,2)‐xylose attached to a GlcNAc 2 Man 3 GlcNAc 2 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 IgG 1 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 β(1,4)‐galactose residues as observed in the mammalian IgG.