Glycobiology Advance Access published online on December 17, 2002
Glycobiology, doi:10.1093/glycob/cwg024
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© 2002 Oxford University Press
ORIGINAL ARTICLES
1 CNRS-UMR 6037, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan cédex, France The presence of non-mammalian core-
Revised on October 22, 2002
Accepted on October 24, 2002
Immunoreactivity in mammals of two typical plant glyco-epitopes, core-
(1,3)-fucose- and core-xylose
2 INSERM U547, Institut Pasteur de Lille, 59019 Lille, France
3 INSERM U519, Université de Rouen, 76821 Mont Saint Aignan cédex, France
4 INSERM U413, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan cédex, France
(1,3)-fucose and core-xylose glyco-epitopes onto glycans N-linked to therapeutic glycoproteins produced in plants has raised the question of their immunogenicity in human therapy. We addressed this question by studying the distribution of these N-glycans in pea, rice and maize, which are the crops intended for the production of therapeutic proteins and by reinvestigating their immunogenicity in rodents. We found that immunization with a model glycoprotein, horseradish peroxidase, elicits in C57BL/6 mice and rats the production of antibodies (Abs) specific for core-
(1,3)-fucose and core-xylose epitopes. Furthermore, we demonstrated that about 50% of non-allergic blood donors contains in their sera Abs specific for core-xylose whereas 25% have Abs against core-
(1,3)-fucose. These Abs probably result from sensitisation to environmental antigens. While the immunological significance of these data is too speculative at the moment, the presence of such Abs might introduce some limitations to the use of plant-derived biopharmaceutical glycoproteins such as an accelerated clearance during human therapy.
Keywords: Transgenic plants, N-glycans, Immunogenicity, Recombinant proteins
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