ArticlemAbs
O-glycosylation of glycine-serine linkers in recombinant Fc-fusion proteins: attachment of glycosaminoglycans and other intermediates with phosphorylation at the xylose sugar subunit.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Development of bicistronic plasmids and fusion proteins for clinical translation of tumor immune reprogramming.Molecular therapy. Advances · 2026Article
- Xylt2 Knockout Eliminates O-Xylosylation and Enhances Bone Morphogenetic Protein 2 Production in Chinese Hamster Ovary Cells.Biotechnology journal · 2026Article
- Bispecific antibodies targeting herpes simplex virus glycoproteins B and D.Frontiers in immunology · 2026Article
- Regulatory considerations in the design, development and quality of monoclonal antibodies and related products for the diagnosis and treatment of cancer.Frontiers in oncology · 2024Review
- O-Glycoproteomic analysis of engineered heavily glycosylated fusion proteins using nanoHILIC-MS.Analytical and bioanalytical chemistry · 2022Article
- Effect of non-repetitive linker on in vitro and in vivo properties of an anti-VEGF scFv.Scientific reports · 2022Article
- Site-Specific O-Glycosylation Analysis by Liquid Chromatography-Mass Spectrometry with Electron-Transfer/Higher-Energy Collisional Dissociation.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Reducing Hinge Flexibility of CAR-T Cells Prolongs SurvivalFrontiers in immunology · 2021Article
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- Force sensing by the vascular protein von Willebrand factor is tuned by a strong intermonomer interaction.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A xylose-based glycosaminoglycan (GAG) core was recently identified at a Ser residue in the linker sequence of a recombinant Fc fusion protein. The linker sequence, G-S-G-G-G-G, and an upstream acidic residue were serving as a substrate for O-xylosyltransferase, resulting in a major glycan composed of Xyl-Gal-Gal-GlcA and other minor intermediates. In this paper, a portion of an unrelated protein was fused to the C-terminus of an IgG Fc domain using the common (G4S) 4 linker repeat. This linker resulted in a heterogenous population of xylose-based glycans all containing at least a core Xyl. Commonly observed glycan structures include GAG-related di-, tri-, tetra-, and penta-saccharides (e.g., Xyl-Gal, Xyl-Gal-Gal, Xyl-Gal-Gal-GlcA, and Xyl-Gal-Gal-GlcA-HexNAc), as well as Xyl-Gal-Neu5Ac. Following alkaline phosphatase or sialidase treatment combined with CID fragmentation, low-level glycans with a mass addition of 79.9 Da were confirmed to be a result of phosphorylated xylose. A minute quantity of phosphorylated GAG pentasaccharides may also be sulfated (also 79.9 Da), possibly at the HexNAc moiety due to non-reactivity to alkaline phosphatase. The xylose moiety may be randomly incorporated in one of the three G-S-G sequence motifs; and the linker peptide shows evidence for multiple additions of xylose at very low levels.
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