ArticleCell reports2013
Structural basis for recognition of the pore-forming toxin intermedilysin by human complement receptor CD59.
Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
35 citing papers in PubMed, 63 citations in OpenAlex.
- Advances in cryo-EM that have shaped mechanistic models of membrane-attack-complex assembly and regulation.IUCrJ · 2026Review
- Introduction to Special Issue on Role of Membranes in the Pore-Formation Mechanism of Pore-Forming Proteins and Toxins.The Journal of membrane biology · 2025Article
- 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
- Genetic Engineering of Donor Pig for the First Human Cardiac Xenotransplantation: Combatting Rejection, Coagulopathy, Inflammation, and Excessive Growth.Current cardiology reports · 2023Review
- 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
- 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
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- New Insights Into Biomphalysin Gene Family Diversification in the Vector SnailFrontiers in immunology · 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
- Structural insights into loss of function of a pore forming toxin and its role in pneumococcal adaptation to an intracellular lifestyle.PLoS pathogens · 2020Article
- Versatile cell ablation tools and their applications to study loss of cell functions.Cellular and molecular life sciences : CMLS · 2019Review
- Justification of specific genetic modifications in pigs for clinical organ xenotransplantation.Xenotransplantation · 2019Review
- The complex functioning of the complement system in xenotransplantation.Xenotransplantation · 2019Review
- Pharmacological Targeting of Pore-Forming Toxins as Adjunctive Therapy for Invasive Bacterial Infection.Toxins · 2018Review
- CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers.Nature communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Pore-forming proteins containing the structurally conserved membrane attack complex/perforin fold play an important role in immunity and host-pathogen interactions. Intermedilysin (ILY) is an archetypal member of a cholesterol-dependent cytolysin subclass that hijacks the complement receptor CD59 to make cytotoxic pores in human cells. ILY directly competes for the membrane attack complex binding site on CD59, rendering cells susceptible to complement lysis. To understand how these bacterial pores form in lipid bilayers and the role CD59 plays in complement regulation, we determined the crystal structure of human CD59 bound to ILY. Here, we show the ILY-CD59 complex at 3.5 Å resolution and identify two interfaces mediating this host-pathogen interaction. An ILY-derived peptide based on the binding site inhibits pore formation in a CD59-containing liposome model system. These data provide insight into how CD59 coordinates ILY monomers, nucleating an early prepore state, and suggest a potential mechanism of inhibition for the complement terminal pathway.
Indexed as
Identifiers
What OpenQuestion holds
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.