ArticleScientific reports2017
Towards new cholera prophylactics and treatment: Crystal structures of bacterial enterotoxins in complex with GM1 mimics.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Kinetic Insights into Cholera Toxin B-Biomimetic Glycan Interactions.Biomacromolecules · 2026Article
- In-silico identification of anti-cholera phytochemicals from Indian medicinal plants.PloS one · 2026Article
- Orally delivered toxin-binding protein protects against diarrhoea in a murine cholera model.Nature communications · 2025Article
- Unraveling the Secrets of a Double-Life Fungus by Genomics:Journal of fungi (Basel, Switzerland) · 2023Article
- Targeting Multiple Binding Sites on Cholera Toxin B with Glycomimetic Polymers Promotes the Formation of Protein-Polymer Aggregates.Biomacromolecules · 2020Article
- Specificity ofInternational journal of molecular sciences · 2019Article
- Carbohydrate inhibitors of cholera toxin.Beilstein journal of organic chemistry · 2018Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cholera is a life-threatening disease in many countries, and new drugs are clearly needed. C-glycosidic antagonists may serve such a purpose. Here we report atomic-resolution crystal structures of three such compounds in complexes with the cholera toxin. The structures give unprecedented atomic details of the molecular interactions and show how the inhibitors efficiently block the GM1 binding site. These molecules are well suited for development into low-cost prophylactic drugs, due to their relatively easy synthesis and their resistance to glycolytic enzymes. One of the compounds links two toxin B-pentamers in the crystal structure, which may yield improved inhibition through the formation of toxin aggregates. These structures can spark the improved design of GM1 mimics, either alone or as multivalent inhibitors connecting multiple GM1-binding sites. Future developments may further include compounds that link the primary and secondary binding sites. Serving as decoys, receptor mimics may lessen symptoms while avoiding the use of antibiotics.
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Registered trials
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