ArticleThe Journal of biological chemistry2012
Modification of the Campylobacter jejuni N-linked glycan by EptC protein-mediated addition of phosphoethanolamine.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 67 citations in OpenAlex.
- The multifaceted roles of phosphoethanolamine-modified lipopolysaccharides: from stress response and virulence to cationic antimicrobial resistance.Microbiology and molecular biology reviews : MMBR · 2024Review
- Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope.Nature communications · 2024Article
- Molecular insights into phosphoethanolamine cellulose formation and secretion.bioRxiv : the preprint server for biology · 2024Article
- Phosphoethanolamine Transferases as Drug Discovery Targets for Therapeutic Treatment of Multi-Drug Resistant Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Diacylglycerol Kinase A Is Essential for Polymyxin Resistance Provided by EptA, MCR-1, and Other Lipid A Phosphoethanolamine Transferases.Journal of bacteriology · 2022Article
- The bile salt deoxycholate inducesFrontiers in microbiology · 2022Article
- Glycopeptide-Centric Approaches for the Characterization of Microbial Glycoproteomes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus.Communications biology · 2021Article
- A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-Based Glycoproteomics.Molecular & cellular proteomics : MCP · 2021Review
- Molecular Mechanisms of Campylobacter Biofilm Formation and Quorum Sensing.Current topics in microbiology and immunology · 2021Review
- Open Database Searching Enables the Identification and Comparison of Bacterial Glycoproteomes without Defining Glycan Compositions Prior to Searching.Molecular & cellular proteomics : MCP · 2020Article
- Proteomics ofMolecular & cellular proteomics : MCP · 2020Article
- TheThe Journal of biological chemistry · 2020Article
- Influence of Protein Glycosylation onFrontiers in microbiology · 2020Article
- Expanding our understanding of the role of microbial glycoproteomes through high-throughput mass spectrometry approaches.Glycoconjugate journal · 2019Article
- Definition of a Family of Nonmobile Colistin Resistance (NMCR-1) Determinants Suggests Aquatic Reservoirs for MCR-4.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Proteomics Reveals Multiple Phenotypes Associated withMolecular & cellular proteomics : MCP · 2019Article
- Update on Campylobacter vaccine development.Human vaccines & immunotherapeutics · 2019Review
- Isomeric Separation and Recognition of Anionic and Zwitterionic N-glycans from Royal Jelly Glycoproteins.Molecular & cellular proteomics : MCP · 2018Article
- NovelJournal of lipid research · 2018Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Campylobacter jejuni is the major worldwide cause of bacterial gastroenteritis. C. jejuni possesses an extensive repertoire of carbohydrate structures that decorate both protein and non-protein surface-exposed structures. An N-linked glycosylation system encoded by the pgl gene cluster mediates the synthesis of a rigidly conserved heptasaccharide that is attached to protein substrates or released as free oligosaccharide in the periplasm. Removal of N-glycosylation results in reduced virulence and impeded host cell attachment. Since the N-glycan is conserved, the N-glycosylation system is also an attractive option for glycoengineering recombinant vaccines in Escherichia coli. To determine whether non-canonical N-glycans are present in C. jejuni, we utilized high throughput glycoproteomics to characterize C. jejuni JHH1 and identified 93 glycosylation sites, including 34 not previously reported. Interrogation of these data allowed the identification of a phosphoethanolamine (pEtN)-modified variant of the N-glycan that was attached to multiple proteins. The pEtN moiety was attached to the terminal GalNAc of the canonical N-glycan. Deletion of the pEtN transferase eptC removed all evidence of the pEtN-glycan but did not globally influence protein reactivity to patient sera, whereas deletion of the pglB oligosaccharyltransferase significantly reduced reactivity. Transfer of eptC and the pgl gene cluster to E. coli confirmed the addition of the pEtN-glycan to a target C. jejuni protein. Significantly reduced, yet above background levels of pEtN-glycan were also observed in E. coli not expressing eptC, suggesting that endogenous E. coli pEtN transferases can mediate the addition of pEtN to N-glycans. The addition of pEtN must be considered in the context of glycoengineering and may alter C. jejuni glycan-mediated structure-function interactions.
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