ArticlePloS one2014
Correlation between in vitro cytotoxicity and in vivo lethal activity in mice of epsilon toxin mutants from Clostridium perfringens.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Epsilon Toxin fromToxins · 2024Article
- The Molecular Architecture and Mode of Action ofToxins · 2024Review
- New Mutants of Epsilon Toxin fromToxins · 2022Article
- Article
- Recombinant unpurified rETXThe Journal of veterinary medical science · 2021Article
- Lung endothelial cells are sensitive to epsilon toxin from Clostridium perfringens.Veterinary research · 2020Article
- Clostridium perfringens epsilon toxin induces blood brain barrier permeability via caveolae-dependent transcytosis and requires expression of MAL.PLoS pathogens · 2019Article
- Review
- Does the Gut Microbiota Influence Immunity and Inflammation in Multiple Sclerosis Pathophysiology?Journal of immunology research · 2017Review
- Targeting and alteration of tight junctions by bacteria and their virulence factors such as Clostridium perfringens enterotoxin.Pflugers Archiv : European journal of physiology · 2017Review
- Review
- Animal models to study the pathogenesis of human and animal Clostridium perfringens infections.Veterinary microbiology · 2015Review
- Clostridium Perfringens Epsilon Toxin Binds to Membrane Lipids and Its Cytotoxic Action Depends on Sulfatide.PloS one · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Epsilon toxin (Etx) from Clostridium perfringens is a pore-forming protein with a lethal effect on livestock, producing severe enterotoxemia characterized by general edema and neurological alterations. Site-specific mutations of the toxin are valuable tools to study the cellular and molecular mechanism of the toxin activity. In particular, mutants with paired cysteine substitutions that affect the membrane insertion domain behaved as dominant-negative inhibitors of toxin activity in MDCK cells. We produced similar mutants, together with a well-known non-toxic mutant (Etx-H106P), as green fluorescent protein (GFP) fusion proteins to perform in vivo studies in an acutely intoxicated mouse model. The mutant (GFP-Etx-I51C/A114C) had a lethal effect with generalized edema, and accumulated in the brain parenchyma due to its ability to cross the blood-brain barrier (BBB). In the renal system, this mutant had a cytotoxic effect on distal tubule epithelial cells. The other mutants studied (GFP-Etx-V56C/F118C and GFP-Etx-H106P) did not have a lethal effect or cross the BBB, and failed to induce a cytotoxic effect on renal epithelial cells. These data suggest a direct correlation between the lethal effect of the toxin, with its cytotoxic effect on the kidney distal tubule cells, and the ability to cross the BBB.
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