ArticleProtein science : a publication of the Protein Society2013
Clostridium perfringens epsilon toxin H149A mutant as a platform for receptor binding studies.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 47 citations in OpenAlex.
- Development and evaluation of recombinant epsilon antigen based indirect-ELISA for sero-monitoring of enterotoxaemia specific antibodies in small ruminants.Veterinary research communications · 2026Article
- Cytotoxic effects of epsilon toxin fromToxicology research · 2025Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- The Molecular Architecture and Mode of Action ofToxins · 2024Review
- Statins as Potential Preventative Treatment of ETX and Multiple Pore-Forming Toxin-Induced Diseases.International journal of molecular sciences · 2023Article
- Interaction ofToxins · 2022Article
- The crystal structure of Cry78Aa from Bacillus thuringiensis provides insights into its insecticidal activity.Communications biology · 2022Article
- New Mutants of Epsilon Toxin fromToxins · 2022Article
- Safety assessment of Mpp75Aa1.1, a new ETX_MTX2 protein from Brevibacillus laterosporus that controls western corn rootworm.PloS one · 2022Article
- Cell death analysis of recombinant mature epsilon toxin on the kidney cell line.Iranian journal of microbiology · 2021Article
- Review
- Article
- Lung endothelial cells are sensitive to epsilon toxin from Clostridium perfringens.Veterinary research · 2020Article
- 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
- Clostridium perfringens Epsilon Toxin Compromises the Blood-Brain Barrier in a Humanized Zebrafish Model.iScience · 2019Article
- Article
- Pharmacological Targeting of Pore-Forming Toxins as Adjunctive Therapy for Invasive Bacterial Infection.Toxins · 2018Review
- A Novel Panel of Rabbit Monoclonal Antibodies and Their Diverse Applications Including Inhibition ofAntibodies (Basel, Switzerland) · 2018Article
- Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Clostridium perfringens epsilon toxin (Etx) is a pore-forming toxin responsible for a severe and rapidly fatal enterotoxemia of ruminants. The toxin is classified as a category B bioterrorism agent by the U.S. Government Centres for Disease Control and Prevention (CDC), making work with recombinant toxin difficult. To reduce the hazard posed by work with recombinant Etx, we have used a variant of Etx that contains a H149A mutation (Etx-H149A), previously reported to have reduced, but not abolished, toxicity. The three-dimensional structure of H149A prototoxin shows that the H149A mutation in domain III does not affect organisation of the putative receptor binding loops in domain I of the toxin. Surface exposed tyrosine residues in domain I of Etx-H149A (Y16, Y20, Y29, Y30, Y36 and Y196) were mutated to alanine and mutants Y30A and Y196A showed significantly reduced binding to MDCK.2 cells relative to Etx-H149A that correlated with their reduced cytotoxic activity. Thus, our study confirms the role of surface exposed tyrosine residues in domain I of Etx in binding to MDCK cells and the suitability of Etx-H149A for further receptor binding studies. In contrast, binding of all of the tyrosine mutants to ACHN cells was similar to that of Etx-H149A, suggesting that Etx can recognise different cell surface receptors. In support of this, the crystal structure of Etx-H149A identified a glycan (β-octyl-glucoside) binding site in domain III of Etx-H149A, which may be a second receptor binding site. These findings have important implications for developing strategies designed to neutralise toxin activity.
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.