ArticleInfection and immunity2004
Binding and internalization of Clostridium perfringens iota-toxin in lipid rafts.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 70 citations in OpenAlex.
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- LSR antibody promotes apoptosis and disrupts epithelial barriers via signal pathways in endometrial cancer.Tissue barriers · 2023Article
- Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile.Nature communications · 2022Article
- Modulating the Blood-Brain Barrier: A Comprehensive Review.Pharmaceutics · 2021Review
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- Brain endothelial tricellular junctions as novel sites for T cell diapedesis across the blood-brain barrier.Journal of cell science · 2021Article
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- The Importance of Therapeutically Targeting the Binary Toxin fromInternational journal of molecular sciences · 2021Review
- A Method to Prepare a Bioprobe for Regulatory Science of the Drug Delivery System to the Brain: An Angulin Binder to Modulate Tricellular Tight Junction-Seal.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Tight Junction Modulating Bioprobes for Drug Delivery System to the Brain: A Review.Pharmaceutics · 2020Review
- Structure of the cell-binding component of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Epithelial barrier dysfunction and cell migration induction via JNK/cofilin/actin by angubindin-1.Tissue barriers · 2020Article
- Potential for Tight Junction Protein-Directed Drug Development Using Claudin Binders and Angubindin-1.International journal of molecular sciences · 2019Review
- Interaction ofToxins · 2018Article
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- 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
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium perfringens iota-toxin is a binary toxin composed of an enzymatic component (Ia) and a binding component (Ib). The oligomer of Ib formed in membranes induces endocytosis. We examined the binding and internalization of Ib by using Cy3-labeled Ib. Labeled Ib was retained at the membranes of MDCK cells for 60 min of incubation at 37 degrees C, and later it was detected in cytoplasmic vesicles. To determine whether Ib associates with lipid rafts, we incubated MDCK cells with Ib at 4 or 37 degrees C and fractionated the Triton-insoluble membranes. An Ib complex of 500 kDa was localized at 37 degrees C to the insoluble fractions that fulfilled the criteria of lipid rafts, but it did not form at 4 degrees C. The amount of complex in the raft fraction reached a maximum after 60 min of incubation at 37 degrees C. When the cells that were preincubated with Ib at 4 degrees C were incubated at 37 degrees C, the complex was detected in the raft fraction. The treatment of MDCK cells with methyl-beta-cyclodextrin reduced the localization of the Ib complex to the rafts and the rounding of the cells induced by Ia plus Ib. When 125I-labeled Ia was incubated with the cells in the presence of Ib at 37 degrees C, it was localized in the raft fraction. Surface plasmon resonance analysis revealed that Ia binds to the oligomer of Ib. We conclude that Ib binds to a receptor in membranes and then moves to rafts and that Ia bound to the oligomer of Ib formed in the rafts is internalized.
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