ArticleInfection and immunity2000
Clostridium perfringens iota-toxin requires activation of both binding and enzymatic components for cytopathic activity.
Article in Infection and immunity, 2000. 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, 71 citations in OpenAlex.
- Processing ofToxins · 2025Article
- Clostridial Myonecrosis: A Comprehensive Review of Toxin Pathophysiology and Management Strategies.Microorganisms · 2024Review
- Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile.Nature communications · 2022Article
- Pathogenicity and virulence ofVirulence · 2021Article
- Mechanism of Cell Penetration by Permeabilization of Late Endosomes: Interplay between a Multivalent TAT Peptide and Bis(monoacylglycero)phosphate.Cell chemical biology · 2020Article
- Structural elucidation of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Virulence Plasmids of the Pathogenic Clostridia.Microbiology spectrum · 2019Article
- TwoToxins · 2019Article
- Mechanisms of Action and Cell Death Associated withToxins · 2018Review
- The role of toxins in Clostridium difficile infection.FEMS microbiology reviews · 2017Review
- Cellular Entry of Clostridium perfringens Iota-Toxin and Clostridium botulinum C2 Toxin.Toxins · 2017Review
- Article
- Review
- Characterization of Clostridium perfringens TpeL toxin gene carriage, production, cytotoxic contributions, and trypsin sensitivity.Infection and immunity · 2015Article
- Clostridium perfringens type A-E toxin plasmids.Research in microbiology · 2015Review
- Identification and Characterization of a New Enterotoxin Produced by Clostridium perfringens Isolated from Food Poisoning Outbreaks.PloS one · 2015Article
- Clostridium and bacillus binary enterotoxins: bad for the bowels, and eukaryotic being.Toxins · 2014Review
- Clostridial binary toxins: iota and C2 family portraits.Frontiers in cellular and infection microbiology · 2011Review
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Iota-toxin is produced by Clostridium perfringens type E strains and consists of two independent components, the enzymatic and binding components, referred to as Ia and Ib, respectively. A recombinant C. perfringens strain, strain 667/pMRP147, produced processed Ia and partially processed Ib, while a recombinant C. perfringens type A strain, strain TS133/pMRP147, in which the VirR-VirS two-component system is inactivated, produced only precursor forms of Ia and Ib. This suggests that iota-toxin is processed by a VirR-VirS-responsive protease, although not completely in the recombinant type A strain. The precursor forms of Ia and Ib were purified from cultures of the latter strain, and their proteolytic activation was examined. Treatment with proteases cleaved off small peptides (9 to 13 amino acid residues) and a 20-kDa peptide from the N termini of the Ia and Ib precursors, respectively, leading to their active forms. They were activated efficiently by alpha-chymotrypsin, pepsin, proteinase K, subtilisin, and thermolysin but only weakly by trypsin, as demonstrated by the cell-rounding assay. lambda-Protease from the C. perfringens type E strain, which was found to be a zinc-dependent protease related to thermolysin, activated iota-toxin as efficiently as did alpha-chymotrypsin. These results suggest that lambda-protease is most responsible for the activation of iota-toxin in type E strains.
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