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Theproduction of recombinant glycoproteins with special reference to simple eukaryotesincluding Dictyostelium discoideum
Author(s) -
Jung Eva,
Williams Keith L.
Publication year - 1997
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1997.tb00407.x
Subject(s) - dictyostelium discoideum , glycosylation , glycoprotein , axenic , biology , recombinant dna , mycetozoa , organism , model organism , microbiology and biotechnology , slime mold , dictyostelium , biochemistry , bacteria , gene , genetics
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 .