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Relationship between Clostridium septicum alpha-toxin activity and binding to erythrocyte membranes.
Abstract: The activity of Clostridium septicum alpha-toxin was determined in erythrocytes of various animals, with sensitivities observed in the order of mouse, rat, canine, equine, rabbit, chicken, bovine, swine and ovine. Temperature and protease treatment affected the sensitivity of erythrocytes to alpha-toxin. Proteinase K treatment decreased the sensitivity of murine, canine, equine and bovine erythrocytes, but ovine erythrocytes did not change the sensitivity to alpha-toxin activity. On the other hand, the activity of alpha-toxin on swine erythrocytes increased after treatment with proteinase K, trypsin, chymotrypsin or lysyl endopeptidase. Toxin overlay assay showed that alpha-toxin bound to erythrocyte membrane proteins with a molecular mass of 30 to 45-kDa in mouse, equine, bovine, swine and chicken, whereas in rat erythrocyte membranes the toxin reacted with 100-kDa protein. The treatment of murine and swine erythrocyte membranes with phosphatidylinositol-specific phospholipase C resulted in liberation of the toxin-binding protein from the individual membranes in a native state. These results show that alpha-toxin associates with specific erythrocyte membrane proteins in any animal species, and are subsets of glycosylphosphatidylinositol-anchored proteins in various animal species. These results may reflect distinct characteristics of the hemolytic activity of alpha-toxin in response to various erythrocytes.
Publication Date: 2005-02-09 PubMed ID: 15699597DOI: 10.1292/jvms.67.69Google Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The researchers have investigated the relationship between Clostridium septicum alpha-toxin’s activity and its binding to the cell membranes of red blood cells in various animals. They found toxin’s effectiveness differs based on the animal type, temperature, protease treatment, and the type of proteins on the cell surface it binds to.
Activity and Sensitivity of Alpha-Toxin to Erythrocytes
- The research involved observing the activity of Clostridium septicum alpha-toxin in the erythrocytes (red blood cells) of several animals. The animals differed in their sensitivity to the toxin, with the order of sensitivity observed as: mouse, rat, canine, equine, rabbit, chicken, bovine, swine and ovine.
- Both the temperature and protease treatment also impacted the sensitivity of erythrocytes to the alpha-toxin. In particular, Proteinase K treatment decreased the sensitivity of murine (mouse), canine (dog), equine (horse) and bovine (cow) erythrocytes, but ovine (sheep) erythrocytes maintained their sensitivity levels to alpha-toxin activity after the treatment.
- In contrast, the alpha-toxin activity increased in swine erythrocytes following Proteinase K, trypsin, chymotrypsin or lysyl endopeptidase treatment.
Alpha-Toxin’s Binding to Erythrocyte Membrane Proteins
- The toxin overlay assay was used to determine that alpha-toxin bound to erythrocyte membrane proteins ranging between 30 to 45-kDa in mouse, horse, cow, pig and chicken. However, in rat erythrocytes, the toxin reacted with a 100-kDa protein.
- Murine and swine erythrocyte membranes were treated with phosphatidylinositol-specific phospholipase C, which resulted in the release of the toxin-binding protein from the individual membranes.
Understanding the Interaction between Alpha-Toxin and Erythrocyte Proteins
- This study reveals that alpha-toxin has an association with specific erythrocyte membrane proteins in any animal species, which are subsets of glycosylphosphatidylinositol-anchored proteins.
- The distinct characteristics of the hemolytic activity of alpha-toxin, in response to various erythrocytes, may be influenced by these results.
Cite This Article
APA
Hang'ombe MB, Kohda T, Mukamoto M, Kozaki S.
(2005).
Relationship between Clostridium septicum alpha-toxin activity and binding to erythrocyte membranes.
J Vet Med Sci, 67(1), 69-74.
https://doi.org/10.1292/jvms.67.69 Publication
Researcher Affiliations
- Laboratory of Veterinary Epidemiology, Department of Veterinary Science, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, Gakuen-cho, Sakai, Osaka, Japan.
MeSH Terms
- Animals
- Bacterial Toxins / metabolism
- Cattle
- Chickens
- Clostridium
- Dogs
- Erythrocyte Membrane / metabolism
- Erythrocytes / drug effects
- Erythrocytes / metabolism
- Hemolysin Proteins / pharmacology
- Horses
- In Vitro Techniques
- Mice
- Phosphatidylinositol Diacylglycerol-Lyase
- Phosphoinositide Phospholipase C
- Protein Binding
- Rabbits
- Rats
- Sheep
- Species Specificity
- Swine
Citations
This article has been cited 4 times.- Kennedy CL, Smith DJ, Lyras D, Chakravorty A, Rood JI. Programmed cellular necrosis mediated by the pore-forming alpha-toxin from Clostridium septicum. PLoS Pathog 2009 Jul;5(7):e1000516.
- Kennedy CL, Lyras D, Cordner LM, Melton-Witt J, Emmins JJ, Tweten RK, Rood JI. Pore-forming activity of alpha-toxin is essential for clostridium septicum-mediated myonecrosis. Infect Immun 2009 Mar;77(3):943-51.
- Forga A, Robbins K, Smith A, Coles M, Tellez-Isaias G, Vuong CN, Hargis B, Graham D. Evaluation of Clostridium septicum hemolytic activity, administration route, and dosage volume of a clostridial dermatitis (cellulitis) bacterin-toxoid on humoral immune response in commercial turkeys. Poult Sci 2023 Sep;102(9):102873.
- Nagahama M, Takehara M, Rood JI. Histotoxic Clostridial Infections. Microbiol Spectr 2019 Jul 26;7(4).
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