Comparison of binding platforms yields insights into receptor binding differences between shiga toxins 1 and 2.

ABSTRACT: Protein-glycan interactions are typically very weak, and avid binding is achieved when proteins express multiple glycan binding sites. Shiga toxin (Stx) uses glycan receptors to enter cells. Stx has five identical binding subunits, each with three nonidentical glycan binding sites. Previous studies examined binding to biantennary glycans expressing Pk trisaccharide mimics immobilized on streptavidin, resulting in display of four trisaccharides per streptavidin face. Stx1 preferred the Pk trisaccharide of its native receptor, globotriaosylceramide (Gb3), while the more potent and clinically relevant variant, Stx2, preferred the Pk trisaccharide with the terminal galactose replaced with N-acetylgalactosamine (NHAc-Pk). In the present study, binding of Stxs to Pk analogues was examined using

SUBMITTER: Flagler MJ 

PROVIDER: S-EPMC2857392 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature