IgG-Fc glycoengineering in non-mammalian expression hosts.
The remarkable success of therapeutic applications of immunoglobulin G (IgG) in form of monoclonal antibodies and pooled immunoglobulin G preparations has directed attention to this class of glycoproteins. It is commonly appreciated that oligosaccharides attached to the Fc-region play a critical role in the biological activity of IgGs. Thus, glycosylation has been a focus of interest for many scientists and the biopharmaceutical industry and expression hosts have been engineered in order to optimize antibody products. In this review we focus on efforts towards a targeted manipulation of IgG-Fc N-glycans using non-mammalian expression hosts, i.e. yeast, insect cells and plants. Current achievements in generating human-like N-glycan structures will be presented and recent data on the molecular mechanisms that might explain how these potent drugs mediate in vivo activities will be discussed.
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. andreas.loos@boku.ac.at
Andreas
A
Loos
Herta
H
Steinkellner
D000818:Animals; D000911:Antibodies, Monoclonal / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular / Q000379:methods; D015870:Gene Expression; D006031:Glycosylation; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000235:genetics* / Q000378:metabolism; D007074:Immunoglobulin G / Q000235:genetics* / Q000378:metabolism; D010944:Plants / Q000235:genetics; D011134:Polysaccharides / Q000235:genetics* / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D015003:Yeasts / Q000235:genetics
D000911:Antibodies, Monoclonal; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D011134:Polysaccharides