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Glycobiology Advance Access originally published online on January 18, 2008
Glycobiology 2008 18(3):235-241; doi:10.1093/glycob/cwm137
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

A plant-derived human monoclonal antibody induces an anti-carbohydrate immune response in rabbits

Chunsheng Jin3, Friedrich Altmann3, Richard Strasser2, Lukas Mach2, Matthias Schähs2, Renate Kunert4, Thomas Rademacher5, Josef Glössl2 and Herta Steinkellner1,2

2 Institute of Applied Genetics and Cell Biology
3 Department of Chemistry
4 Institute of Applied Microbiology, University of Natural Resources and Applied Life Sciences, Muthgasse 18, 1190 Vienna, Austria
5 Rheinisch-Westfälische Technische Hochschule, Worringerweg 1, 52074, Aachen, Germany

1 To whom correspondence should be addressed: Tel: +43-1-36006-6700; Fax: +43-1-36006-6392; e-mail: herta.steinkellner{at}boku.ac.at

Received on July 26, 2007; revised on November 15, 2007; accepted on December 21, 2007

A common argument against using plants as a production system for therapeutic proteins is their inability to perform authentic N-glycosylation. A major concern is the presence of beta 1,2-xylose and core alpha 1,3-fucose residues on complex N-glycans as these nonmammalian N-glycan residues may provoke unwanted side effects in humans. In this study we have investigated the potential antigenicity of plant-type N-glycans attached to a human monoclonal antibody (2G12). Using glyco-engineered plant lines as expression hosts, four 2G12 glycoforms differing in the presence/absence of beta 1,2-xylose and core alpha 1,3-fucose were generated. Systemic immunization of rabbits with a xylose and fucose carrying 2G12 glycoform resulted in a humoral immune response to both N-glycan epitopes. Furthermore, IgE immunoblotting with sera derived from allergic patients revealed binding to plant-produced 2G12 carrying core alpha 1,3 fucosylated N-glycan structures. Our results provide evidence for the adverse potential of nonmammalian N-glycan modifications present on monoclonal antibodies produced in plants. This emphasizes the need for the use of glyco-engineered plants lacking any potentially antigenic N-glycan structures for the production of plant-derived recombinant proteins intended for parenteral human application.

Key words: anti-carbohydrate immune response / beta 1,2 xylose / core alpha 1,3 fucose / glyco-engineered plants / recombinant antibodies / N-glycosylation


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