Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 24909379Publication DOI: 10.1016/j.carres.2014.05.003Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: G. Widmalm <gw
organ.su.se>
Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
The structure of the O-antigen polysaccharide (PS) from Escherichia coli O42 has been investigated by NMR spectroscopy as the main method, which was complemented with sugar analysis, mass spectrometry, and analysis of biosynthetic information. The O-specific chain of the O-deacylated lipopolysaccharide (LPS-OH) consists of branched tetrasaccharide-glycerol repeating units joined by phosphodiester linkages. The lipid-free polysaccharide contains 0.8equiv of O-acetyl groups per repeating unit and has the following teichoic acid-like structure: Based on biosynthetic aspects, this should also be the biological repeating unit. This O-antigen structure is remarkably similar to that of E. coli O28ac, differing only in the presence or absence, respectively, of a glucose residue at the branching point. The structural similarity explains the serological cross-reactivity observed between strains of these two serogroups, and also their almost identical O-antigen gene cluster sequences.
NMR, O-antigen, Escherichia coli, O-acetylation
Structure type: polymer biological repeating unit
Location inside paper: p.177, fig.6, O28ac
Compound class: O-antigen
Contained glycoepitopes: IEDB_130695,IEDB_135813,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_141807,IEDB_151531,IEDB_190606
Methods: 13C NMR, 1H NMR, NMR-2D, HF solvolysis, de-O-acylation, sugar analysis, 31P NMR, ESI-MS, acid hydrolysis, GLC, NMR-1D
Comments, role: O-deacylated polysaccharide
Related record ID(s): 30057, 30236, 30238
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GTC:G68026HG
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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