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
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
Methods: 13C NMR, 1H NMR, TLC, chemical synthesis
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