ArticleThe Journal of biological chemistry2011
Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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Who cites it
38 citing papers in PubMed, 57 citations in OpenAlex.
- Structural basis for the pore-forming activity of a complement-like toxin.Science advances · 2025Article
- Identification and Analysis of Anticancer Therapeutic Targets from the Polysaccharide Krestin (PSK) and Polysaccharopeptide (PSP) Using Inverse Docking.Molecules (Basel, Switzerland) · 2024Article
- 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
- Cholesterol-dependent cytolysins: The outstanding questions.IUBMB life · 2022Review
- Single Point Mutation and Its Role in Specific Pathogenicity to Reveal the Mechanism of Related Protein Families.Microbiology spectrum · 2022Article
- Bispecific mAbInternational journal of molecular sciences · 2022Article
- Dual functions of discoidinolysin, a cholesterol-dependent cytolysin with N-terminal discoidin domain produced fromJournal of oral microbiology · 2022Article
- Inerolysin and vaginolysin, the cytolysins implicated in vaginal dysbiosis, differently impair molecular integrity of phospholipid membranes.Scientific reports · 2019Article
- Cholesterol-Dependent Cytolysins Produced by Vaginal Bacteria: Certainties and Controversies.Frontiers in cellular and infection microbiology · 2019Review
- Complements are involved in alcoholic fatty liver disease, hepatitis and fibrosis.World journal of hepatology · 2018Review
- Cholesterol-dependent cytolysins: from water-soluble state to membrane pore.Biophysical reviews · 2018Review
- How novel structures inform understanding of complement function.Seminars in immunopathology · 2018Review
- Disentangling the roles of cholesterol and CD59 in intermedilysin pore formation.Scientific reports · 2016Article
- Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.Structure (London, England : 1993) · 2016Article
- Hijacking Complement Regulatory Proteins for Bacterial Immune Evasion.Frontiers in microbiology · 2016Review
- Crystal structure of Streptococcus pneumoniae pneumolysin provides key insights into early steps of pore formation.Scientific reports · 2015Article
- Dual modes of membrane binding direct pore formation by Streptolysin O.Molecular microbiology · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
CD59 is a glycosylphosphatidylinositol-anchored protein that inhibits the assembly of the terminal complement membrane attack complex (MAC) pore, whereas Streptococcus intermedius intermedilysin (ILY), a pore forming cholesterol-dependent cytolysin (CDC), specifically binds to human CD59 (hCD59) to initiate the formation of its pore. The identification of the residues of ILY and hCD59 that form their binding interface revealed a remarkably deep correspondence between the hCD59 binding site for ILY and that for the MAC proteins C8α and C9. ILY disengages from hCD59 during the prepore to pore transition, suggesting that loss of this interaction is necessary to accommodate specific structural changes associated with this transition. Consistent with this scenario, mutants of hCD59 or ILY that increased the affinity of this interaction decreased the cytolytic activity by slowing the transition of the prepore to pore but not the assembly of the prepore oligomer. A signature motif was also identified in the hCD59 binding CDCs that revealed a new hCD59-binding member of the CDC family. Although the binding site on hCD59 for ILY, C8α, and C9 exhibits significant homology, no similarity exists in their binding sites for hCD59. Hence, ILY and the MAC proteins interact with common amino acids of hCD59 but lack detectable conservation in their binding sites for hCD59.
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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.