The production of recombinant glycoproteins with special reference to simple eukaryotes including Dictyostelium discoideum.
Because many recombinantly produced proteins require post-translational modification to be properly folded and active, there is a new emphasis on eukaryotic expression systems. Dictyostelium discoideum is a well studied eukaryotic model organism for the investigation of key questions in molecular and cell biology. More recently D. discoideum was successfully used as a system for recombinant glycoprotein production. The vegetative amoebae are easy and inexpensive to grow either in axenic culture or on Gram-negative bacteria. Reliable and uncomplicated transformation systems are also well established. This organism harbours the machinery to perform post-translational modifications such as phosphorylation, acylation, formation of glycosylphosphatidylinositol anchors and more importantly N- and O-linked glycosylation. This review provides an overview of glycosylation in different expression systems and focuses on glycosylation in D. discoideum.
Jung
E
E
MUCAB (Macquarie University Center for Analytical Biotechnology), Macquarie University, Sydney, NSW, Australia.
Williams
K L
KL
D000818:Animals; D002240:Carbohydrate Sequence; D003001:Cloning, Molecular; D004023:Dictyostelium / Q000235:genetics*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics*; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics*; D006031:Glycosylation; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D005656:Fungal Proteins; D006023:Glycoproteins; D011994:Recombinant Proteins