
Technique(s) used for Glycosylation Detection | SBA (soybean agglutinin) lectin-agarose affinity chromatography |
Technique(s) used for Glycosylated Residue(s) Detection | CapLC-MS/MS (capillary liquid chromatography-tandem mass spectrometry) |
Glycan Information |
Glycan Annotation | Linkage: Bac-Asn. 1406 Da heptasaccharide composed of GalNAc-α1,4-GalNAc-α1,4-[Glcβ1,3-]GalNAc-α1,4-GalNAc-α1,4-GalNAc-α1,3-Bac-β1,N-Asn-Xaa, where Bac is bacillosamine, 2,4-diacetamido-2,4,6-trideoxyglucopyranose. |
BCSDB ID | 23625 |
GlyTouCan | G58528CE |
Technique(s) used for Glycan Identification | 1H, 13C NMR spectroscopy- one dimensional TOCSY (total correlation spectroscopy) and NOESY (nuclear Overhauser effect spectroscopy); HMBC (heteronuclear multiple bond coherence), HMQC (heteronuclear multiple quantum correlation) spectra. |
Protein Glycosylation linked (PGL) gene(s) |
OST Gene Name | PglB |
OST ProGT ID | ProGT10 |
Characterized Accessory Gene(s) | PglA, PglJ, PglH, PglI, PglC are glycosyltransferases involved in the heptasaccharide assembly. PglFED are the bacillosamine biosynthetic enzymes. PglK is a flippase. |
Accessory Gene(s)Progt ID | ProGT10.1, ProGT10.2, Pro |
Additional Comment | Sequon feature: The consensus sequence for the C jejuni PglB is D/E-X'-N-X"-S/T (where X' and X" stand for any amino acid except proline) which is glycosylated when located in flexible, exposed structural elements. Tripeptide sequence NLT too has been found to be modified in vitro. |
Literature |
Year of Identification | 2002 |
Year of Identification Month Wise | 2002.11.29 |
Year of Validation | 2002 |
Reference | Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D., 2010. Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases 2. Journal of Biological Chemistry, 285(7), pp.4941-4950. |
Corresponding Author | Daisuke Kohda |
Contact | Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan. |
Reference | Linton, D., Allan, E., Karlyshev, A.V., Cronshaw, A.D. and Wren, B.W., 2002. Identification of N‐acetylgalactosamine‐containing glycoproteins PEB3 and CgpA in Campylobacter jejuni. Molecular microbiology, 43(2), pp.497-508. |
Corresponding Author | Dennis Linton |
Contact | Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, UK. |
Reference | Olivier, N.B., Chen, M.M., Behr, J.R. and Imperiali, B., 2006. In vitro biosynthesis of UDP-N, N ‘-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry, 45(45), pp.13659-13669. |
Corresponding Author | Barbara Imperiali |
Contact | Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA. |
Reference | Young, N.M., Brisson, J.R., Kelly, J., Watson, D.C., Tessier, L., Lanthier, P.H., Jarrell, H.C., Cadotte, N., Michael, F.S., Aberg, E. and Szymanski, C.M., 2002. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. Journal of Biological Chemistry, 277(45), pp.42530-42539. |
Corresponding Author | N Martin Young |
Contact | Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada. |
Reference | Scott, N.E., Parker, B.L., Connolly, A.M., Paulech, J., Edwards, A.V., Crossett, B., Falconer, L., Kolarich, D., Djordjevic, S.P., Højrup, P. and Packer, N.H., 2011. Simultaneous glycan-peptide characterization using hydrophilic interaction chromatography and parallel fragmentation by CID, higher energy collisional dissociation, and electron transfer dissociation MS applied to the N-linked glycoproteome of Campylobacter jejuni. Molecular & cellular proteomics, 10(2), pp.S1-S18. |
Corresponding Author | Stuart J Cordwell |
Contact | School of Molecular and Microbial Biosciences, University of Sydney, Sydney, Australia |