Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern Export

@article{citeulike:1526858, abstract = {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 beta1,2-xylose and core alpha1,3-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 beta1,2-xylose and core alpha1,3-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.}, author = {Schahs, Matthias and Strasser, Richard and Stadlmann, Johannes and Kunert, Renate and Rademacher, Thomas and Steinkellner, Herta}, citeulike-article-id = {1526858}, citeulike-linkout-0 = {http://www.blackwell-synergy.com/doi/abs/10.1111/j.1467-7652.2007.00273.x}, citeulike-linkout-1 = {http://dx.doi.org/10.1111/j.1467-7652.2007.00273.x}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17678502}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17678502}, doi = {10.1111/j.1467-7652.2007.00273.x}, journal = {Plant Biotechnology Journal}, keywords = {arabidopsis, glycosylation, hiv}, number = {5}, pages = {657--663}, posted-at = {2008-09-01 21:38:24}, priority = {2}, title = {Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern}, url = {http://dx.doi.org/10.1111/j.1467-7652.2007.00273.x}, volume = {5}, year = {2007} }

TY - JOUR ID - citeulike:1526858 L3 - citeulike-article-id:1526858 N2 - 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 beta1,2-xylose and core alpha1,3-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 beta1,2-xylose and core alpha1,3-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. IS - 5 JF - Plant Biotechnology Journal EP - 663 TI - Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern VL - 5 SP - 657 KW - arabidopsis KW - glycosylation KW - hiv AU - Schahs, Matthias AU - Strasser, Richard AU - Stadlmann, Johannes AU - Kunert, Renate AU - Rademacher, Thomas AU - Steinkellner, Herta PY - 2007/// UR - http://dx.doi.org/10.1111/j.1467-7652.2007.00273.x ER -