ArticleInfection and immunity2001
Cellular uptake of the Clostridium perfringens binary iota-toxin.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 81 citations in OpenAlex.
- The Pore-Forming Subunit C2IIa of the BinaryFrontiers in pharmacology · 2022Article
- CRISPA: A Non-viral, Transient Cas9 Delivery System Based on Reengineered Anthrax Toxin.Frontiers in pharmacology · 2021Article
- Structural elucidation of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.Nature structural & molecular biology · 2020Article
- The role of toxins in Clostridium difficile infection.FEMS microbiology reviews · 2017Review
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- Article
- Inhibiting bacterial toxins by channel blockage.Pathogens and disease · 2016Review
- A novel Hsp70 inhibitor prevents cell intoxication with the actin ADP-ribosylating Clostridium perfringens iota toxin.Scientific reports · 2016Article
- Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin.PloS one · 2015Article
- Clostridium and bacillus binary enterotoxins: bad for the bowels, and eukaryotic being.Toxins · 2014Review
- Tailored cyclodextrin pore blocker protects mammalian cells from clostridium difficile binary toxin CDT.Toxins · 2014Article
- Clostridium difficile virulence factors: Insights into an anaerobic spore-forming pathogen.Gut microbes · 2014Review
- Article
- Designed azolopyridinium salts block protective antigen pores in vitro and protect cells from anthrax toxin.PloS one · 2013Article
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
- Intracellular trafficking of Clostridium perfringens iota-toxin b.Infection and immunity · 2012Article
- Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins.Biophysical journal · 2012Article
- Identification of the cellular receptor of Clostridium spiroforme toxin.Infection and immunity · 2012Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binary iota-toxin is produced by Clostridium perfringens type E strains and consists of two separate proteins, the binding component iota b (98 kDa) and an actin-ADP-ribosylating enzyme component iota a (47 kDa). Iota b binds to the cell surface receptor and mediates the translocation of iota a into the cytosol. Here we studied the cellular uptake of iota-toxin into Vero cells. Bafilomycin A1, but not brefeldin A or nocodazole, inhibited the cytotoxic effects of iota-toxin, indicating that toxin is translocated from an endosomal compartment into the cytoplasm. Acidification (pH < or = 5.0) of the extracellular medium enabled iota a to directly enter the cytosol in the presence of iota b. Activation by chymotrypsin induced oligomerization of iota b in solution. An average mass of 530 +/- 28 kDa for oligomers was determined by analytical ultracentrifugation, indicating heptamer formation. The entry of iota-toxin into polarized CaCo-2 cells was studied by measuring the decrease in transepithelial resistance after toxin treatment. Iota-toxin led to a significant decrease in resistance when it was applied to the basolateral surface of the cells but not following application to the apical surface, indicating a polarized localization of the iota-toxin receptor.
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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.