Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern |
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Authors: | Schähs Matthias Strasser Richard Stadlmann Johannes Kunert Renate Rademacher Thomas Steinkellner Herta |
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Institution: | Institute of Applied Genetics and Cell Biology, BOKU-Wien, Austria;Department of Chemistry, BOKU-Wien, Austria;Institute of Applied Microbiology, BOKU-Wien, Austria;Rheinisch-Westfälische Technische Hochschule (RWTH), Aachen, Germany |
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Abstract: | In recent years, plants have become an attractive alternative for the production of recombinant proteins. However, their inability to perform authentic mammalian N -glycosylation may cause limitations for the production of therapeutics. A major concern is the presence of β1,2-xylose and core α1,3-fucose residues on complex N -linked glycans, as these N -glycan epitopes are immunogenic in mammals. In our attempts towards the humanization of plant N -glycans, we have generated an Arabidopsis thaliana knockout line that synthesizes complex N -glycans lacking immunogenic xylose and fucose epitopes. Here, we report the expression of a monoclonal antibody in these glycan-engineered plants that carry a homogeneous mammalian-like complex N -glycan pattern without β1,2-xylose and core α1,3-fucose. Plant and Chinese hamster ovary (CHO)-derived immunoglobulins (IgGs) exhibited no differences in electrophoretic mobility and enzyme-linked immunosorbent specificity assays. Our results demonstrate the feasibility of a knockout strategy for N -glycan engineering of plants towards mammalian-like structures, thus providing a significant improvement in the use of plants as an expression platform. |
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Keywords: | antibodies β1‚2-xylose and core α1‚3-fucose plant glycan engineering recombinant proteins |
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