title: Engineering of human-type O-glycosylation in Nicotiana benthamiana plants.
abstract: Therapeutic properties of recombinant proteins are very often affected by the composition and heterogeneity of their glycans. Conventional expression systems for recombinant pharmaceutical proteins typically do not address this problem and produce a mixture of glycoforms that are neither identical to human glycans nor optimized for enhanced efficacy. In terms of glycosylation, plants offer certain advantages over mammalian cells as the N-glycosylation pathway of plants is comparably simple and a typical mammalian O-glycosylation pathway is not present at all. During the last ten years we have developed a plant-based expression platform for the generation of recombinant glycoproteins with defined N-glycans. Now we have extended our tool-box for glyco-engineering in the tobacco related species Nicotiana benthamiana toward the production of tailored mucin-type O-glycans on recombinant proteins.
authors.affiliation: Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria. richard.strasser@boku.ac.at
authors.forename: Richard
authors.initials: R
authors.lastname: Strasser
mesh_terms: D006031:Glycosylation; D006801:Humans; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014026:Nicotiana / Q000235:genetics / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins
keywords: erythropoietin; glycoprotein; glycosylation; molecular farming; posttranslational modification; recombinant protein; sialic acid