New Mutants of Epsilon Toxin from Clostridium perfringens with an Altered Receptor-Binding Site and Cell-Type Specificity
| Autor: | Jonatan Dorca-Arévalo, Inmaculada Gómez de Aranda, Juan Blasi |
|---|---|
| Rok vydání: | 2022 |
| Předmět: |
Kidney diseases
Bacterial toxins Lectines Lectins epsilon toxin Clostridium perfringens pulpy kidney disease lectin pronase E N-glycosidase F β-elimination proximal tubules MDCK cells enterotoxemia Health Toxicology and Mutagenesis Toxines bacterianes Mutació (Biologia) Malalties del ronyó Mutation (Biology) Toxicology |
| Zdroj: | Toxins; Volume 14; Issue 4; Pages: 288 Dipòsit Digital de la UB Universidad de Barcelona |
| ISSN: | 2072-6651 |
| Popis: | Epsilon toxin (Etx) from Clostridium perfringens is the third most potent toxin after the botulinum and tetanus toxins. Etx is the main agent of enterotoxemia in ruminants and is produced by Clostridium perfringens toxinotypes B and D, causing great economic losses. Etx selectively binds to target cells, oligomerizes and inserts into the plasma membrane, and forms pores. A series of mutants have been previously generated to understand the cellular and molecular mechanisms of the toxin and to obtain valid molecular tools for effective vaccination protocols. Here, two new non-toxic Etx mutants were generated by selective deletions in the binding (Etx-ΔS188-F196) or insertion (Etx-ΔV108-F135) domains of the toxin. As expected, our results showed that Etx-ΔS188-F196 did not exhibit the usual Etx binding pattern but surprisingly recognized specifically an O-glycoprotein present in the proximal tubules of the kidneys in a wide range of animals, including ruminants. Although diminished, Etx-ΔV108-F135 maintained the capacity for binding and even oligomerization, indicating that the mutation particularly affected the pore-forming ability of the toxin. |
| Databáze: | OpenAIRE |
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