Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
NCBI PubMed ID: 15703289Publication DOI: 10.1073/pnas.0500044102Journal NLM ID: 7505876Publisher: National Academy of Sciences
Institutions: Institute of Microbiology, Department of Biology, Swiss Federal Institute of Technology, ETH-Hönggeberg, CH-8093 Zurich, Switzerland
Campylobacter jejuni has a general N-linked protein glycosylation system that can be functionally transferred to Escherichia coli. In this study, we engineered E. coli cells in a way that two different pathways, protein N-glycosylation and lipopolysaccharide (LPS) biosynthesis, converge at the step in which PglB, the key enzyme of the C. jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB was the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer. The relaxed specificity of the PglB oligosaccharyltransferase toward the glycan structure was exploited to create novel N-glycan structures containing two distinct E. coli or Pseudomonas aeruginosa O antigens. PglB-mediated transfer of polysaccharides might be valuable for in vivo production of O polysaccharides-protein conjugates for use as antibacterial vaccines
conjugate vaccines, glycoengineering, oligosaccharyltransferase, STT3
Structure type: oligomer
Location inside paper: p.3020
Aglycon: core oligosaccharide
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_885822,IEDB_983931,SB_192
Methods: serological methods, genetic methods, biosynthetic methods
Biological activity: serological data
Biosynthesis and genetic data: genetic adata, biosynthetic data
Comments, role: N-glycan, engineered in E. coli
Related record ID(s): 10218, 10219, 10463
NCBI Taxonomy refs (TaxIDs): 197Reference(s) to other database(s): GTC:G66397DB, GlycomeDB:
24426
Show glycosyltransferases
There is only one chemically distinct structure: