Open AccessProduction of a monoclonal antibody in plants with a humanized N ‐glycosylation pattern
Author(s) -
Schähs Matthias,
Strasser Richard,
Stadlmann Johannes,
Kunert Renate,
Rademacher Thomas,
Steinkellner Herta
Publication year - 2007
Publication title -
plant biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.525
H-Index - 115
eISSN - 1467-7652
pISSN - 1467-7644
DOI - 10.1111/j.1467-7652.2007.00273.x
Subject(s) - glycan , biology , epitope , glycosylation , fucose , monoclonal antibody , chinese hamster ovary cell , arabidopsis thaliana , biochemistry , xylose , recombinant dna , antibody dependent cell mediated cytotoxicity , antibody , mutant , galactose , glycoprotein , gene , genetics , receptor , fermentation
Summary 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.