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 |
| |
Authors: | Bardor Muriel Loutelier-Bourhis Corinne Paccalet Thomas Cosette Pascal Fitchette Anne-Catherine Vézina Louis-P Trépanier Sonia Dargis Michèle Lemieux Réal Lange Catherine Faye Loïc Lerouge Patrice |
| |
Affiliation: | CNRS-UMR 6037,;CNRS-UMR 6014 and;CNRS-UMR 6522, IFRMP 23, Universitéde Rouen, 76821 Mont Saint Aignan, France;;Medicago inc., 1020, Route de l'Église, Bureau 600, Sainte-Foy, Québec, Canada;;Héma-Québec, 2535, Boulevard Laurier, Sainte-Foy, Québec, Canada. |
| |
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. |
| |
Keywords: | alfalfa (Medicago sativa) glyco-engineering N-glycosylation recombinant antibodies transgenic plants |
本文献已被 PubMed 等数据库收录! |
|