ArticleBiochemistry2012
Identification of amino acids important for binding of Clostridium perfringens epsilon toxin to host cells and to HAVCR1.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
- Cytotoxic effects of epsilon toxin fromToxicology research · 2025Article
- Confinement energy landscape classification reveals membrane receptor nano-organization mechanisms.Biophysical journal · 2024Article
- The Molecular Architecture and Mode of Action ofToxins · 2024Review
- Comparative Phylogenetic Analysis and Protein Prediction Reveal the Taxonomy and Diverse Distribution of Virulence Factors in FoodborneEvolutionary bioinformatics online · 2024Article
- Membrane Dynamics and Remodelling in Response to the Action of the Membrane-Damaging Pore-Forming Toxins.The Journal of membrane biology · 2022Review
- New Mutants of Epsilon Toxin fromToxins · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- Article
- New Insights Into Biomphalysin Gene Family Diversification in the Vector SnailFrontiers in immunology · 2021Article
- Article
- Glabralysins, Potential New β-Pore-Forming Toxin Family Members from the Schistosomiasis Vector SnailGenes · 2020Article
- The pore structure of Clostridium perfringens epsilon toxin.Nature communications · 2019Article
- Article
- A Novel Panel of Rabbit Monoclonal Antibodies and Their Diverse Applications Including Inhibition ofAntibodies (Basel, Switzerland) · 2018Article
- F199E substitution reduced toxicity of Clostridium perfringens epsilon toxin by depriving the receptor binding capability.Human vaccines & immunotherapeutics · 2017Article
- Review
- Immunization with a novel Clostridium perfringens epsilon toxin mutant rETX(Y196E)-C confers strong protection in mice.Scientific reports · 2016Article
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- The Myelin and Lymphocyte Protein MAL Is Required for Binding and Activity of Clostridium perfringens ε-Toxin.PLoS pathogens · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Clostridium perfringens epsilon toxin belongs to the aerolysin-like family of pore-forming toxins and is one of the most potent bacterial toxins known. The epsilon toxin causes fatal enterotoxemia in sheep, goats, and possibly humans. Evidence indicates that the toxin binds to protein receptors including hepatitis A virus cellular receptor 1 (HAVCR1), but the region of the toxin responsible for cell binding has not been identified. In the present study, we identify amino acids within the epsilon toxin important for this cell interaction. Site-specific mutagenesis was used to investigate the role of a surface-accessible cluster of aromatic amino acids, and purified mutant proteins were tested in a series of cell-culture assays to assess cytotoxic activity and cell binding. When added to cells, four mutant proteins (Etx-Y29E, Etx-Y30E, Etx-Y36E and Etx-Y196E) were severely impaired in their ability to not only kill host cells, but also in their ability to permeabilize the plasma membrane. Circular dichroism spectroscopy and thermal stability studies revealed that the wild-type and mutant proteins were similarly folded. Additional experiments revealed that these mutant proteins were defective in binding to host cells and to HAVCR1. These data indicate that an amino acid motif including Y29, Y30, Y36, and Y196 is important for the ability of epsilon toxin to interact with cells and HAVCR1.
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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.