Custom Glycosylation of Bacteria Membranes

Custom Glycosylation of Bacteria Membranes

CD BioGlyco has been committed to glycosylation research for many years. We provide glycosylation modification and characterization of bacteria membranes for our global customers.

Glycosylation in Bacteria

Glycosylation is the most abundant polypeptide chain modification in nature. The N-glycosylation pathway was first demonstrated in Campylobacter jejuni in 2002. After that, bacterial glycoproteins from Campylobacter coli, Pseudomonas aeruginosa, Helicobacter pylori, and Aeromonas caviae were identified. Studies have shown that glycosylation of proteins in bacteria plays an important role in adhesion, immune escape, and host colonization. The protein glycosylation pathway in bacteria mainly includes lipid carrier-mediated en bloc glycosylation and stepwise protein glycosylation. En bloc glycosylation refers to the overall transfer of oligosaccharides from lipid-linked oligosaccharides (LLOs) to target proteins in the periplasm by oligosaccharyltransferases (OST). Stepwise protein glycosylation is the stepwise addition of sugars to asparagine (Asn) and serine or threonine (Ser/Thr) residues of the target protein by glycosyltransferases (GTs).

General Glycosylation Pathway of Campylobacter Jejuni

The protein N-glycosylation pathway in Campylobacter jejuni is considered to study the origin of glycosylation in host-microbe interactions. Its heptasaccharide is constructed on the cytoplasmic side of the inner membrane on the lipid-linked precursor, undecadiene phosphate (Und-P). Then, under the action of the ATP-dependent flippase PglK, LLO is transported to the periplasmic space and transferred to the Asn residue of the target protein by the oligosaccharyltransferase (OTase) PglB. The N-glycosylation pathway of Campylobacter jejuni has been reported to modify many proteins. Disruption of this pathway reduced human and animal serum protein immunoreactivity and the ability to adhere and invade epithelial cells in vitro.

The glycosylation pathway of Campylobacter jejuni.Fig.1 The glycosylation pathway of Campylobacter jejuni. (Nothaft, 2010)

Glycosylation Services of Bacteria Membranes

  • Modification of bacteria membranes glycosylation

We use a variety of glycosylation modification strategies to provide customers with custom glycosylation of bacteria membranes. For example, we glycosylate bacterial membranes with oligosaccharides-cyclic carbamates. We can also use N-glycosyltransferases to glycosylate bacterial membrane proteins in vitro.

  • Characterization of bacteria membrane glycosylation

We also provide glycosylation characterization of bacteria membranes. Our methods include capillary electrophoresis (CE), high-performance liquid chromatography (HPLC), liquid chromatography-MS/MS (LC-MS/MS), electrospray ionization MS (ESI-MS), and Fourier ion cyclotron resonance MS (FT-ICR-MS), etc.

CD BioGlyco provides our customers with high-quality, cost-effective, and hassle-free bacteria membranes glycosylation services. If you are interested in our services, please feel free to contact us, we are looking forward to being your indispensable assistant in the glycosylation field.


  1. Nothaft, H.; Szymanski, C.M. Protein glycosylation in bacteria: sweeter than ever. Nature Reviews Microbiology. 2010, 8(11): 765-778.
  2. Whitehead, M.W.; et al. Custom glycosylation of cells and proteins using cyclic carbamate-derivatized oligosaccharides. Cell chemical biology. 2017, 24(11): 1336-1346.
  3. Ahangama Liyanage, L.; et al. In vitro glycosylation of membrane proteins using N-glycosyltransferase. ACS omega. 2021, 6(18): 12133-12142.
This service is for Research Use Only, not intended for any clinical use.

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