ArticleStructure (London, England : 1993)2016
Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Strain-level heterogeneity in Gardnerella urinary tract persistence and pathogenesis in an in vivo model is consistent with comparative phylogenomic analyses.BMC microbiology · 2026Article
- Macrocyclic Peptide Probes for Immunomodulatory Protein CD59: Potent Modulators of Bacterial Toxin Activity and Antibody-Dependent Cytotoxicity.Angewandte Chemie (International ed. in English) · 2025Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Characterization of tigurilysin, a novel human CD59-specific cholesterol-dependent cytolysin, reveals a role for host specificity in augmenting toxin activity.Microbiology (Reading, England) · 2023Article
- Gaining New Insights into Fundamental Biological Pathways by Bacterial Toxin-Based Genetic Screens.Bioengineering (Basel, Switzerland) · 2023Review
- Characterization of Tigurilysin, a Novel Human CD59-Specific Cholesterol-Dependent Cytolysin, Reveals a Role for Host Specificity in Augmenting Toxin Activity.bioRxiv : the preprint server for biology · 2023Article
- Article
- Structural basis for membrane attack complex inhibition by CD59.Nature communications · 2023Article
- Cholesterol-dependent cytolysins: The outstanding questions.IUBMB life · 2022Review
- Article
- Gardnerella vaginalis alters cervicovaginal epithelial cell function through microbe-specific immune responses.Microbiome · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- Intermedilysin cytolytic activity depends on heparan sulfates and membrane composition.PLoS genetics · 2021Article
- Sequence Comparison of Vaginolysin from DifferentPathogens (Basel, Switzerland) · 2021Article
- How Structures of Complement Complexes Guide Therapeutic Design.Sub-cellular biochemistry · 2021Review
- Structural basis for tuning activity and membrane specificity of bacterial cytolysins.Nature communications · 2020Article
- Article
- All major cholesterol-dependent cytolysins use glycans as cellular receptors.Science advances · 2020Article
- Nanopore Fabrication and Application as Biosensors in Neurodegenerative Diseases.Critical reviews in biomedical engineering · 2020Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Cholesterol-dependent cytolysins (CDCs) are a family of pore-forming toxins that punch holes in the outer membrane of eukaryotic cells. Cholesterol serves as the receptor, but a subclass of CDCs first binds to human CD59. Here we describe the crystal structures of vaginolysin and intermedilysin complexed to CD59. These studies, together with small-angle X-ray scattering, reveal that CD59 binds to each at different, though overlapping, sites, consistent with molecular dynamics simulations and binding studies. The CDC consensus undecapeptide motif, which for the CD59-responsive CDCs has a proline instead of a tryptophan in the motif, adopts a strikingly different conformation between the structures; our data suggest that the proline acts as a selectivity switch to ensure CD59-dependent CDCs bind their protein receptor first in preference to cholesterol. The structural data suggest a detailed model of how these water-soluble toxins assemble as prepores on the cell surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.