Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
- PMID: 12186869
- DOI: 10.1074/jbc.M206114200
Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
Abstract
Mass spectrometry investigations of partially purified Campylobacter jejuni protein PEB3 showed it to be partially modified with an Asn-linked glycan with a mass of 1406 Da and composed of one hexose, five N-acetylhexosamines and a species of mass 228 Da, consistent with a trideoxydiacetamidohexose. By means of soybean lectin affinity chromatography, a mixture of glycoproteins was obtained from a glycine extract, and two-dimensional gel proteomics analysis led to the identification of at least 22 glycoproteins, predominantly annotated as periplasmic proteins. Glycopeptides were prepared from the glycoprotein mixture by Pronase digestion and gel filtration. The structure of the glycan was determined by using nano-NMR techniques to be GalNAc-alpha1,4-GalNAc-alpha1,4-[Glcbeta1,3-]GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-Bac-beta1,N-Asn-Xaa, where Bac is bacillosamine, 2,4-diacetamido-2,4,6-trideoxyglucopyranose. Protein glycosylation was abolished when the pglB gene was mutated, providing further evidence that the enzyme encoded by this gene is responsible for formation of the glycopeptide N-linkage. Comparison of the pgl locus with that of Neisseria meningitidis suggested that most of the homologous genes are probably involved in the biosynthesis of bacillosamine.
Similar articles
-
Synthesis of asparagine-linked bacillosamine.Carbohydr Res. 2006 Aug 14;341(11):1922-9. doi: 10.1016/j.carres.2006.04.031. Epub 2006 May 15. Carbohydr Res. 2006. PMID: 16697990
-
Detection of conserved N-linked glycans and phase-variable lipooligosaccharides and capsules from campylobacter cells by mass spectrometry and high resolution magic angle spinning NMR spectroscopy.J Biol Chem. 2003 Jul 4;278(27):24509-20. doi: 10.1074/jbc.M301273200. Epub 2003 Apr 25. J Biol Chem. 2003. PMID: 12716884
-
Direct biochemical evidence for the utilization of UDP-bacillosamine by PglC, an essential glycosyl-1-phosphate transferase in the Campylobacter jejuni N-linked glycosylation pathway.Biochemistry. 2006 Apr 25;45(16):5343-50. doi: 10.1021/bi0602056. Biochemistry. 2006. PMID: 16618123
-
Structure of the O-glycopeptides isolated from bovine milk component PP3.Glycoconj J. 1998 Apr;15(4):371-8. doi: 10.1023/a:1006973802139. Glycoconj J. 1998. PMID: 9613824
-
Identifying the targets and functions of N-linked protein glycosylation in Campylobacter jejuni.Mol Omics. 2020 Aug 10;16(4):287-304. doi: 10.1039/d0mo00032a. Mol Omics. 2020. PMID: 32347268 Review.
Cited by
-
Characterization of PglJ, a Glycosyltransferase in the Campylobacter concisus N-Linked Protein Glycosylation Pathway that Expands Glycan Diversity.Biochemistry. 2024 Jan 2;63(1):141-151. doi: 10.1021/acs.biochem.3c00564. Epub 2023 Dec 18. Biochemistry. 2024. PMID: 38110367 Free PMC article.
-
Ligand Recognition by the Macrophage Galactose-Type C-Type Lectin: Self or Non-Self?-A Way to Trick the Host's Immune System.Int J Mol Sci. 2023 Dec 3;24(23):17078. doi: 10.3390/ijms242317078. Int J Mol Sci. 2023. PMID: 38069400 Free PMC article. Review.
-
De Novo Synthetic Approach to 2,4-Diamino-2,4,6-trideoxyhexoses (DATDH): Bacterial and Rare Deoxy-Amino Sugars.Org Lett. 2023 Nov 3;25(43):7873-7877. doi: 10.1021/acs.orglett.3c03106. Epub 2023 Oct 20. Org Lett. 2023. PMID: 37862141
-
Glycosylation Circuit Enables Improved Catalytic Properties for Recombinant Alkaline Phosphatase.ACS Omega. 2023 Aug 31;8(39):36218-36227. doi: 10.1021/acsomega.3c04669. eCollection 2023 Oct 3. ACS Omega. 2023. PMID: 37810695 Free PMC article.
-
Thioglycosides Act as Metabolic Inhibitors of Bacterial Glycan Biosynthesis.ACS Infect Dis. 2023 Oct 13;9(10):2025-2035. doi: 10.1021/acsinfecdis.3c00324. Epub 2023 Sep 12. ACS Infect Dis. 2023. PMID: 37698279 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases