ReviewToxins2015
Membrane-Binding Mechanism of Clostridium perfringens Alpha-Toxin.
Review in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 76 citations in OpenAlex.
- Innovative Approaches Against Planktonic and Biofilm-ProducingVeterinary sciences · 2026Review
- Epidemiological and Metabolic Characteristics ofAnimals : an open access journal from MDPI · 2026Article
- Biochemistry of Human Gut Microbiota: Related Diseases and Dietary Interactions.Molecules (Basel, Switzerland) · 2026Review
- Article
- Review
- Unveiling the pathogenic mechanisms ofEmerging microbes & infections · 2024Review
- Molecular identification of hyaluronate lyase, not hyaluronidase, as an intrinsic hyaluronan-degrading enzyme in Clostridium perfringens strain ATCC 13124.Scientific reports · 2024Article
- Review of advances in molecular structure and biological function ofCanadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2024Review
- Preparation and Application ofVeterinary sciences · 2024Article
- Clostridial Myonecrosis: A Comprehensive Review of Toxin Pathophysiology and Management Strategies.Microorganisms · 2024Review
- Isolation of a VirulentCurrent issues in molecular biology · 2024Article
- The Barrier Disruption and Pyroptosis of Intestinal Epithelial Cells Caused by Perfringolysin O (PFO) fromCells · 2024Article
- Purinergic Receptor Antagonists Inhibit Hemolysis Induced byPathogens (Basel, Switzerland) · 2024Article
- The Effects ofAnimals : an open access journal from MDPI · 2024Article
- Exploring the Genomic Landscape ofCurrent issues in molecular biology · 2024Article
- Exploring the predictive power of jejunal microbiome composition in clinical and subclinical necrotic enteritis caused by Clostridium perfringens: insights from a broiler chicken model.Journal of translational medicine · 2024Article
- Article
- Comparative Phylogenetic Analysis and Protein Prediction Reveal the Taxonomy and Diverse Distribution of Virulence Factors in FoodborneEvolutionary bioinformatics online · 2024Article
- Antimicrobial potential of myricetin-coated zinc oxide nanocomposite against drug-resistant Clostridium perfringens.BMC microbiology · 2023Article
- Necrotic Enteritis in Broiler Chickens: A Review on the Pathogen, Pathogenesis, and Prevention.Microorganisms · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium perfringens alpha-toxin is a key mediator of gas gangrene, which is a life-threatening infection that manifests as fever, pain, edema, myonecrosis, and gas production. Alpha-toxin possesses phospholipase C and sphingomyelinase activities. The toxin is composed of an N-terminal domain (1-250 aa, N-domain), which is the catalytic site, and a C-terminal domain (251-370 aa, C-domain), which is the membrane-binding site. Immunization of mice with the C-domain of alpha-toxin prevents the gas gangrene caused by C. perfringens, whereas immunization with the N-domain has no effect. The central loop domain (55-93 aa), especially H….SW(84)Y(85)….G, plays an important role in the interaction with ganglioside GM1a. The toxin binds to lipid rafts in the presence of a GM1a/TrkA complex, and metabolites from phosphatidylcholine to diacylglycerol through the enzymatic activity of alpha-toxin itself. These membrane dynamics leads to the activation of endogenous PLCγ-1 via TrkA. In addition, treatment with alpha-toxin leads to the formation of diacylglycerol at membrane rafts in ganglioside-deficient DonQ cells; this in turn triggers endocytosis and cell death. This article summarizes the current the membrane-binding mechanism of alpha-toxin in detail.
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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.