ArticleThe Journal of biological chemistry2014
The crystal structure of shiga toxin type 2 with bound disaccharide guides the design of a heterobifunctional toxin inhibitor.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 29 citations in OpenAlex.
- Role of Recent Therapeutic Applications and the Infection Strategies of Shiga Toxin-ProducingFrontiers in cellular and infection microbiology · 2021Review
- Review
- Verotoxin Receptor-Based Pathology and Therapies.Frontiers in cellular and infection microbiology · 2020Review
- Tissue Responses to Shiga Toxin in Human Intestinal Organoids.Cellular and molecular gastroenterology and hepatology · 2020Article
- Structural and Functional Characterization of Stx2k, a New Subtype of Shiga Toxin 2.Microorganisms · 2019Article
- Addition of lysophospholipids with large head groups to cells inhibits Shiga toxin binding.Scientific reports · 2016Article
- AB5 Preassembly Is Not Required for Shiga Toxin Activity.Journal of bacteriology · 2016Article
- Review
- Do the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Toxins · 2015Review
- Glycolipid binding preferences of Shiga toxin variants.PloS one · 2014Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shiga toxin type 2 (Stx2a) is clinically most closely associated with enterohemorrhagic E. coli O157:H7-mediated hemorrhagic colitis that sometimes progresses to hemolytic-uremic syndrome. The ability to express the toxin has been acquired by other Escherichia coli strains, and outbreaks of food poisoning have caused significant mortality rates as, for example, in the 2011 outbreak in northern Germany. Stx2a, an AB5 toxin, gains entry into human cells via the glycosphingolipid receptor Gb3. We have determined the first crystal structure of a disaccharide analog of Gb3 bound to the B5 pentamer of Stx2a holotoxin. In this Gb3 analog,-GalNAc replaces the terminal-Gal residue. This co-crystal structure confirms previous inferences that two of the primary binding sites identified in theB5 pentamer of Stx1 are also functional in Stx2a. This knowledge provides a rationale for the synthesis and evaluation of heterobifunctional antagonists for E. coli toxins that target Stx2a. Incorporation of GalNAc Gb3 trisaccharide in a heterobifunctional ligand with an attached pyruvate acetal, a ligand for human amyloid P component, and conjugation to poly[acrylamide-co-(3-azidopropylmethacrylamide)] produced a polymer that neutralized Stx2a in a mouse model of Shigatoxemia.
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