Post-translational modifications of protein biopharmaceuticals

The GalNAc-type O-Glycoproteome of CHO Cells Characterized by the SimpleCell Strategy

“…The CHO cell is the major production platform for recombinant therapeutics and most of these are glycoproteins (27). The major focus on glycosylation capacity in CHO cells has been devoted to the N-glycosylation pathway primarily with respect to sialylation and core fucosylation as these parameters serve important functions for circulatory half-life of therapeutics and effector functions of IgGs, respectively (28,29).…”

Vinyl Sulfone: A Multi-Purpose Function in Proteomics

“…Artificial covalent modification of proteins is an arduous but fruitful task of major interest for the biophysics and biochemistry communities that normally pursue as goals the detection or purification of the protein itself in order to have a more thorough understanding of molecular mechanisms and the expansion of the applicability of such biomolecules. Despite the intrinsic difficulties associated to perform those chemical modifications of proteins, the attachment of analytical or engineered probes for protein tracking (labelling) (Giepmans et al, 2006;Waggoner, 2006;Wu & Goody, 2010) or protein profiling (chemical proteomics) (Evans & Cravatt, 2006;Cravatt et al, 2008), the introduction of affinity tags for separation-isolation of proteins (affinity chromatography) (Azarkan et al, 2007;Fang & Zhang, 2008) or for mass spectroscopy-based protein identification and characterization (chemical tagging) (Leitner & Lindner, 2006), the immobilization onto solid supports (microarray technologies) (Wong et al, 2009) and the conjugation with other biomolecules (post-translational modifications) (Gamblin et al, 2008b;Walsh, 2009;Heal & Tate, 2010) are among some of the most useful and frontier techniques and methodologies used in Proteomics. For the chemical modification of proteins, a large number of strategies are nowadays available (Hermanson, 2008).…”

Long-lasting recombinant factor VIII proteins for hemophilia A

“…28,37,38 rFVIIIFc is produced from human embryonic kidney (HEK) 293 cells via recombinant DNA technology. HEK cells ensure fully human, posttranslational modifications, [39][40][41][42] including glycosylation, with theoretical functional relevance compared with nonhuman mammalian expression systems such as CHO cells, which insert nonhuman glycosylations. Glycosylation modulates yield, bioactivity, solubility, stability against proteolysis, immunogenicity, and clearance rate from circulation.…”