Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 10574995Publication DOI: 10.1074/jbc.274.49.35129Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: mvalvano
julian.uwo.ca
Institutions: Instituto de Investigaciones Bioquimicas Fundacion Campomar, Buenos Aires, Argentina, Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada, Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada
During O antigen lipopolysaccharide (LPS) synthesis in bacteria, transmembrane migration of undecaprenylpyrophosphate (Und-P-P)-bound O antigen subunits occurs before their polymerization and ligation to the rest of the LPS molecule. Despite the general nature of the translocation process, putative O-antigen translocases display a low level of amino acid sequence similarity. In this work, we investigated whether complete O antigen subunits are required for translocation. We demonstrate that a single sugar, GlcNAc, can be incorporated to LPS of Escherichia coli K-12. This incorporation required the functions of two O antigen synthesis genes, wecA (UDP-GlcNAc:Und-P GlcNAc-1-P transferase) and wzx (O-antigen translocase). Complementation experiments with putative O-antigen translocases from E. coli O7 and Salmonella enterica indicated that translocation of O antigen subunits is independent of the chemical structure of the saccharide moiety. Furthermore, complementation with putative translocases involved in synthesis of exopolysaccharides demonstrated that these proteins could not participate in O antigen assembly. Our data indicate that recognition of a complete Und-P-P-bound O antigen subunit is not required for translocation and suggest a model for O antigen synthesis involving recognition of Und-P-P-linked sugars by a putative complex made of Wzx translocase and other proteins involved in the processing of O antigen
biosynthesis, antigen, structure, O-antigen, O antigen, Escherichia, Escherichia coli, activity, assembly, chemical, chemical structure, putative, sugar
Structure type: suggested polymer biological repeating unit
Location inside paper: Fig. 3
The structure in this paper was incorrect:
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
Biosynthesis and genetic data: biosynthetic data
Comments, role: anomeric configurations seem to be incorrectly copied from the original publication
Related record ID(s): 2061, 2163, 2164, 2165, 10463, 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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