Engineering of Sialylated Mucin-type O-Glycosylation in Plants

• Published in: The Journal of biological chemistry Vol. 287; no. 43; pp. 36518 - 36526
• Main Authors: Castilho, Alexandra, Neumann, Laura, Daskalova, Sasha, Mason, Hugh S., Steinkellner, Herta, Altmann, Friedrich, Strasser, Richard
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 19.10.2012; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Caenorhabditis elegans - genetics; Caenorhabditis elegans Proteins - biosynthesis; Caenorhabditis elegans Proteins - genetics; Drosophila melanogaster; Drosophila Proteins - biosynthesis; Drosophila Proteins - genetics; Erythropoietin; Erythropoietin - biosynthesis; Erythropoietin - genetics; Genetic Engineering; Glycobiology and Extracellular Matrices; Glycosylation; Humans; Immunoglobulin G - biosynthesis; Immunoglobulin G - genetics; Mice; Mucins; Nicotiana - genetics; Nicotiana - metabolism; Plant; Plants, Genetically Modified - genetics; Plants, Genetically Modified - metabolism; Post Translational Modification; Recombinant Fusion Proteins - biosynthesis; Recombinant Fusion Proteins - genetics; Recombinant Protein Expression; Sialic Acid; Sialyltransferases - biosynthesis; Sialyltransferases - genetics; Post Translational Modification; Sialic Acid; Recombinant Protein Expression; Plant; Glycosylation; Erythropoietin

Proper N- and O-glycosylation of recombinant proteins is important for their biological function. Although the N-glycan processing pathway of different expression hosts has been successfully modified in the past, comparatively little attention has been paid to the generation of customized O-linked g...