O-glycoprotein-based Cell Surface Glycoengineering Service

O-glycoprotein-based Cell Surface Glycoengineering Service

What Is O-glycosylation?

Protein glycosylation is a vital post-translational modification (PTM), containing O-linked glycosylation, which is the attachment of glycan units to the protein backbone through the side chains of Thr or Ser residues, without a consensus sequence. Different kinds of sugars may add to O-glycosylation, including the addition of N-acetylglucosamine (GlcNAc), N-acetylgalactosamine (GalNAc), mannose (Man), galactose (Gal), fucose (Fuc), glucose (Glc) or xylose (Xyl). Different types of O-glycosylation start at different sites, resulting in heterogeneity in the attached oligosaccharide structure. O-glycosylation arises in the endoplasmic reticulum or the Golgi apparatus, as well as before or after protein folding. Glycosylation facilitates protein folding, thereby altering the structure and physical features of the protein to which it is attached.

Three O-linked monomannose residues at Thr1, Ser3, and Ser14 sites.Fig.1 Three O-linked monomannose residues at Thr1, Ser3, and Ser14 sites. (Chaffey, et al., 2017)

O-glycoprotein-based Cell Surface Glycoengineering Services at CD BioGlyco

  • O-glycoprotein modification

CD BioGlyco provides diverse modifications of O-glycoproteins based on the cell surface, such as modifications at specific positions, sugar units, or structures.

  • O-glycoprotein modification regulation

CD BioGlyco regulates the expression level of specific O-glycoprotein modification-related enzymes (such as GalNAc-T family members) through gene editing or RNA interference technology, to control the level and type of cell surface O-glycoprotein modification.

  • O-glycosyltransferase engineering

CD BioGlyco introduces or regulates the gene expression of specific O-glycosyltransferases, such as GalT, ST6Gal, or FucT, so as to control the O-sugar decoration type, structure, and quantity of the target protein.

  • O-glycoprotein expression and positioning

CD BioGlyco introduces the target O-glycoprotein gene into cells through genetic engineering technology, enabling them to synthesize inside the cells and correctly set on the surface of the cells.

  • Sugar protein analysis and detection

CD BioGlyco provides O-glycoprotein analysis and detection services, including mass spectrometer analysis and immune chromatography.

O-glycoprotein-based cell surface glycoengineering services.Fig.2 O-glycoprotein-based cell surface glycoengineering services. (CD BioGlyco)

Applications

  • Cell adhesion signal conduction research: By regulating the surface of the cell surface O-sugar modification, is used to study its impact on cell adhesion, external matrix interaction, and related signal pathways.
  • Biomedicine: Regulating O-sugar modification on antibodies changes their activity, stability, and immunogenicity, thereby meeting specific biomedical application needs, such as antibody therapy and diagnostic reagent development.
  • Establishment of the disease model: By changing the O-sugar modification of the cell surface, cell models related to specific diseases (such as cancer cell models) are constructed, and these models are used for drug screening, effect assessment, and mechanism research.

Advantages

  • CD BioGlyco has extensive experience and provides customized O-glycoprotein glycoengineering services.
  • Our scientists have professional cell engineering skills and perform precise O-glycoprotein glycoengineering services on the cell surface.
  • CD BioGlyco provides diverse modifications based on cell surface O-glycoproteins and adopts a strict quality control system to ensure the provision of high-efficiency and high-yield products.

CD BioGlyco provides professional O-glycoprotein-based cell surface glycoengineering services. Moreover, a variety of glycoengineering-related services are also provided by CD BioGlyco, including Cell Surface N-glycan Glycoengineering Service and Cell Surface O-glycan Glycoengineering Service. Please feel free to contact us if you would like to consult about specific cell surface glycoengineering services.

References

  1. Okamoto, R.; et al. Decoration of proteins with sugar chains: recent advances in glycoprotein synthesis. Current Opinion in Chemical Biology. 2014, 22, 92-99.
  2. Chaffey, P.K.; et al. Quantitative effects of O-linked glycans on protein folding. Biochemistry. 2017, 56(34): 4539-4548.
This service is for Research Use Only, not intended for any clinical use.

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