Differentiation between Structurally Homologous Shiga 1 and Shiga 2 Toxins by Using Synthetic Glycoconjugates

Abstract

Choose your poison: Shiga toxins 1 and 2 are the major virulence factors of E. coli O157:H7. However, Shiga 2 is more potent than Shiga 1. Biotinylated glycoconjugates have been developed that differentiate between these structurally homologous toxins (see picture; R=OH: selective for Shiga 1; R=NHAc: selective for Shiga 2). These synthetic materials efficiently capture toxins without interference from the sample matrix.

Detection of Intact Influenza Viruses using Biotinylated Biantennary S-Sialosides

“…We have observed a similar behavior with Shiga toxins where the N-acetyl group at the 2 position plays a significant role in the discriminatory binding event. 15 the NAs (N1 versus N2) could also contribute in the binding event.…”

Factors Affecting Protein–Glycan Specificity: Effect of Spacers and Incubation Time

“…By using our previously described synthetic strategy, which has been successfully used to develop ligands for the capture of toxins, [10] viruses [11] and bacteria, [12] we constructed a panel of biotinylated S-sialosides that could adopt a variety of topologies ( Figure 1). The biotinylated S-sialosides, unlike naturally occurring O-sialosides, are impervious to cleavage by viral neuraminidase (NA) and therefore, can be used to analyze HA, NA, and intact virus.…”

Chemical Synthesis of a Glycopeptide Derived from Skp1 for Probing Protein Specific Glycosylation

“…A triflic acid promoted glycosylation of 11 with benzyl protected N -α-(9-fluorenylmethyloxycarbonyl)- l - trans -4-hydroxyproline gave compound 12 in a yield of 71% mainly as the α-anomer. Reduction of the azido moiety of 12 was accomplished using thioacetic acid [22] to provide 13 which was subjected to hydrogenolysis to give 6 , which is appropriately protected for use in glycopeptide synthesis.…”