Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: hemolytic-uremic syndrome (HUS) [ICD11:
3A21.2 
];
infection due to Escherichia coli [ICD11:
XN6P4 ]
NCBI PubMed ID: 23768952Publication DOI: 10.1016/j.carres.2013.05.010Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: dave.bundle
ualberta.ca (D.R. Bundle)
Institutions: Alberta Glycomics Centre, Department of Chemistry, University of Alberta, Edmonton, AB, Canada
Hemolytic uremic syndrome is a potentially fatal complication of food poisoning caused by Escherichia coli O157:H7, especially those strains that produce the Stx2 Shiga toxin. Multivalent inhibitors based on the Pk trisaccharide are most effective against Stx1 the less dangerous of the two Shiga toxins. Inhibitors containing a terminal 2-acetamido-2-deoxy-α-D-galactopyranosyl residue in place of the terminal α-D-galactopyranosyl residue of Pk trisaccharide have been shown to exhibit preferential binding to Stx2. A multivalent heterobifunctional Pk analog containing 2-acetamido-2-deoxy-α-D-galactopyranose has been synthesized in a format that facilitates the ablation of toxin activity via supramolecular complex formation between Stx and the endogenous protein, Human serum amyloid P component (HuSAP).
Escherichia coli O157:H7, Glycomics, Shiga Toxin 2, Pk trisaccharide, Toxin inhibitors, Trisaccharide synthesis, Heterobifunctional ligand
Structure type: oligomer
Location inside paper: p.5, fig.1
Contained glycoepitopes: IEDB_130648,IEDB_136044,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_153215,IEDB_190606,IEDB_885822,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88
Methods: 13C NMR, 1H NMR, TLC, chemical synthesis
Synthetic data: chemical
Comments, role: a modified Pk trisaccharide part of nature ligand for Shiga toxin 2 (Stx2).
Related record ID(s): 29209
NCBI Taxonomy refs (TaxIDs): 83334Reference(s) to other database(s): GTC:G89090WX
Show glycosyltransferases
There is only one chemically distinct structure:
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