Journal
PLANT BIOTECHNOLOGY JOURNAL
Volume 5, Issue 5, Pages 657-663Publisher
WILEY
DOI: 10.1111/j.1467-7652.2007.00273.x
Keywords
antibodies; beta 1,2-xylose and core alpha 1,3-fucose; plant glycan; engineering; recombinant proteins
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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 beta 1,2-xylose and core alpha 1,3-fucose residues on complex Winked 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 beta 1,2-xylose and core alpha 1,3-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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