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IgG-Fc glycoengineering in non-mammalian expression hosts.

ABSTRACT: 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.

SUBMITTER: Loos A

PROVIDER: S-EPMC3442181 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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IgG-Fc glycoengineering in non-mammalian expression hosts.

Loos Andreas A Steinkellner Herta H

Archives of biochemistry and biophysics 20120523 2

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 opti ...[more]

PMID: 22634260

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