Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
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: suggested polymer biological repeating unit
Location inside paper: Fig. 4
Compound class: O-polysaccharide, core oligosaccharide, O-antigen
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_150899,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_137,SB_165,SB_166,SB_187,SB_195,SB_29,SB_44,SB_67,SB_7,SB_72,SB_88
Methods: serological methods, genetic methods, biosynthetic methods
Biological activity: serological data
Biosynthesis and genetic data: genetic data, biosynthetic data
Comments, role: Quip4NAc = VioNAc = N-acetylviosamin
Related record ID(s): 2162, 10033, 10218, 10219, 11786, 20641, 23054, 23640, 29648, 30268, 108701, 114155, 116994
NCBI Taxonomy refs (TaxIDs): 2162916Reference(s) to other database(s): GTC:G47971KQ, GlycomeDB:
27141
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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