Журнал микробиологии, эпидемиологии и иммунобиологии. 2021; 98: 91-103
Современные представления об этиопатогенетических и генетических особенностях токсинов Clostridium perfringens
https://doi.org/10.36233/0372-9311-37Аннотация
Список литературы
1. Kiu R., Hall L.J. An update on the human and animal enteric pathogen Clostridium perfringens. Emerg. Microb. Infect. 2018; 7(1): 141. https://doi.org/10.1038/s41426-018-0144-8
2. Hobbs B.C., Smith M.T., Oakley C.L., Warrack G.H., Cruickshank J.C. Clostridium welchii food poisoning. J. Hyg. 1953;51:75–101. dоi: 10.1017/S0022172400015515
3. McClane B.A., Uzal F.A., Miyakawa M.F., Lyerly D., Wilkins T.D. The enterotoxic clostridia. In: Dworkin M., Falkow S., Rosenburg E., Schleifer H., Stackebrandt E., eds. The Prokaryotes. New York: Springer NY Press; 2006: 688–752.
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12. Rossjohn J., Polekhina G., Feil S.C., Morton C.J., Tweten R.K., Parker M.W. Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins. J. Mol. Biol. 2007; 367(5): 1227–36. https://doi.org/10.1016/j.jmb.2007.01.042
13. Ma M., Li J., McClane B.A. Genotypic and phenotypic characterization of Clostridium perfringens isolates from Darmbrand cases in post-World War II Germany. Infect. Immun. 2012; 80(12): 4354–63. https://doi.org/10.1128/iai.00818-12
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18. Shatursky O., Bayles R., Rogers M., Jost B.H., Songer J.G., Tweten R.K. Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers. Infect. Immun. 2000; 68(10): 5546–51. https://doi.org/10.1128/iai.68.10.5546-5551.2000
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20. Popoff M.R. Epsilon toxin: a fascinating pore-forming toxin. FEBS J. 2011; 278(23): 4602–15. https://doi.org/10.1111/j.1742-4658.2011.08145.x
21. Bokori-Brown M., Savva C.G., Fernandes da Costa S.P., Naylor C.E., Basak A.K., Titball R.W. Molecular basis of toxicity of Clostridium perfringens epsilon toxin. FEBS J. 2011; 278(23): 4589–601. https://doi.org/10.1111/j.1742-4658.2011.08140.x
22. Minami J., Katayama S., Matsushita O., Matsushita C., Okabe A. Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides. Microbiol. Immunol. 1997; 41(7): 527–35. https://doi.org/10.1111/j.1348-0421.1997.tb01888.x
23. Miyata S., Matsushita O., Minami J., Katayama S., Shimamoto S., Okabe A. Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane. J. Biol. Chem. 2001; 276(17): 13778–83. https://doi.org/10.1074/jbc.m011527200
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25. Nestorovich E.M., Karginov V.A., Bezrukov S.M. Polymer partitioning and ion selectivity suggest asymmetrical shape for the membrane pore formed by epsilon toxin. Biophys. J. 2010; 99(3): 782–9. https://doi.org/10.1016/j.bpj.2010.05.014
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Journal of microbiology, epidemiology and immunobiology. 2021; 98: 91-103
Current notions about etiopathogenic and genetics specific features of Сlostridium perfringens toxins
https://doi.org/10.36233/0372-9311-37Abstract
References
1. Kiu R., Hall L.J. An update on the human and animal enteric pathogen Clostridium perfringens. Emerg. Microb. Infect. 2018; 7(1): 141. https://doi.org/10.1038/s41426-018-0144-8
2. Hobbs B.C., Smith M.T., Oakley C.L., Warrack G.H., Cruickshank J.C. Clostridium welchii food poisoning. J. Hyg. 1953;51:75–101. doi: 10.1017/S0022172400015515
3. McClane B.A., Uzal F.A., Miyakawa M.F., Lyerly D., Wilkins T.D. The enterotoxic clostridia. In: Dworkin M., Falkow S., Rosenburg E., Schleifer H., Stackebrandt E., eds. The Prokaryotes. New York: Springer NY Press; 2006: 688–752.
4. Freedman J.C., Shrestha A. Clostridium perfringens enterotoxin: action, genetics, and translational application. Toxins (Basel). 2016; 8(3): 73. https://doi.org/10.3390/toxins8030073
5. Glotova T.I., Terent'eva T.E., Glotov A.G. Vozbuditeli i vozrastnaya vospriimchivost' krupnogo rogatogo skota k klostridiozam. Sibirskii vestnik sel'skokhozyaistvennoi nauki. 2017; 47(1): 90–6.
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9. Yonogi S., Matsuda S., Kawai T., Yoda T., Harada T., Kumeda Y., et al. BEC, a novel enterotoxin of Clostridium perfringens found in human clinical isolates from acute gastroenteritis outbreaks. Infect. Immun. 2014; 82(6): 2390–9. https://doi.org/10.1128/iai.01759-14
10. Titball R.W., Naylor C.E., Basak A.K. The Clostridium perfringens alpha-toxin. Anaerobe. 1999; 5(2): 51–64. https://doi.org/10.1006/anae.1999.0191
11. Sakurai J., Nagahama M., Oda M. Clostridium perfringens alpha-toxin: characterization and mode of action. J. Biochem. (Tokyo). 2004; 136(5): 569–74. https://doi.org/10.1093/jb/mvh161
12. Rossjohn J., Polekhina G., Feil S.C., Morton C.J., Tweten R.K., Parker M.W. Structures of perfringolysin O suggest a pathway for activation of cholesterol-dependent cytolysins. J. Mol. Biol. 2007; 367(5): 1227–36. https://doi.org/10.1016/j.jmb.2007.01.042
13. Ma M., Li J., McClane B.A. Genotypic and phenotypic characterization of Clostridium perfringens isolates from Darmbrand cases in post-World War II Germany. Infect. Immun. 2012; 80(12): 4354–63. https://doi.org/10.1128/iai.00818-12
14. Bryant A.E., Chen R.Y., Nagata Y., Wang Y., Lee C.H., Finegold S., et al. Clostridial gas gangrene. I. Cellular and molecular mechanisms of microvascular dysfunction induced by exotoxins of Clostridium perfringens. J. Infect. Dis. 2000; 182(3): 799–807. https://doi.org/10.1086/315756
15. Hunter S.E.C., Brown J.E., Oynston P.C.F., Sakurai J., Titball R.W. Molecular genetic analysis of beta-toxin of Clostridium perfringens reveals sequence homology with alpha-toxin, gamma-toxin, and leukocidin of Staphylococcus aureus. Infect. Immun. 1993; 61: 3958–65. https://doi.org/10.1128/iai.61.9.3958-3965.1993
16. Macias Rioseco M., Beingesser J., Uzal F.A. Freezing or adding trypsin inhibitor to equine intestinal contents extends the lifespan of Clostridium perfringens beta-toxin for diagnostic purposes. Anaerobe. 2012; 18(3): 357–60. https://doi.org/10.1016/j.anaerobe.2012.03.003
17. Sakurai J., Duncan C.L. Some properties of the beta-toxin produced by Clostridium perfringens type C. Infect. Immun. 1978; 21(2): 678–80. https://doi.org/10.1128/iai.21.2.678-680.1978
18. Shatursky O., Bayles R., Rogers M., Jost B.H., Songer J.G., Tweten R.K. Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers. Infect. Immun. 2000; 68(10): 5546–51. https://doi.org/10.1128/iai.68.10.5546-5551.2000
19. Gibert M., Jolivet-Reynaud C., Popoff M.R. Beta2 toxin, a novel toxin produced by Clostridium perfringens. Gene. 1997; 203(1): 65–73. https://doi.org/10.1016/s0378-1119(97)00493-9
20. Popoff M.R. Epsilon toxin: a fascinating pore-forming toxin. FEBS J. 2011; 278(23): 4602–15. https://doi.org/10.1111/j.1742-4658.2011.08145.x
21. Bokori-Brown M., Savva C.G., Fernandes da Costa S.P., Naylor C.E., Basak A.K., Titball R.W. Molecular basis of toxicity of Clostridium perfringens epsilon toxin. FEBS J. 2011; 278(23): 4589–601. https://doi.org/10.1111/j.1742-4658.2011.08140.x
22. Minami J., Katayama S., Matsushita O., Matsushita C., Okabe A. Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides. Microbiol. Immunol. 1997; 41(7): 527–35. https://doi.org/10.1111/j.1348-0421.1997.tb01888.x
23. Miyata S., Matsushita O., Minami J., Katayama S., Shimamoto S., Okabe A. Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane. J. Biol. Chem. 2001; 276(17): 13778–83. https://doi.org/10.1074/jbc.m011527200
24. Robertson S.L., Li J., Uzal F.A., McClane B.A. Evidence for a prepore stage in the action of Clostridium perfringens epsilon toxin. PLoS One. 2011; 6(7): e22053. https://doi.org/10.1371/journal.pone.0022053
25. Nestorovich E.M., Karginov V.A., Bezrukov S.M. Polymer partitioning and ion selectivity suggest asymmetrical shape for the membrane pore formed by epsilon toxin. Biophys. J. 2010; 99(3): 782–9. https://doi.org/10.1016/j.bpj.2010.05.014
26. Sakurai J., Nagahama M., Oda M., Tsuge H., Kobayashi K. Clostridium perfringens iota-toxin: structure and function. Toxins (Basel). 2009; 1(2): 208–28. https://doi.org/10.3390/toxins1020208
27. Stiles B.G., Wigelsworth D.J., Popoff M.R., Barth H. Clostridial binary toxins: iota and C2 family portraits. Front. Cell. Infect. Microbiol. 2011; 1: 11. https://doi.org/10.3389/fcimb.2011.00011
28. Barth H., Stiles B.G. Binary actin-ADP-ribosylating toxins and their use as molecular Trojan horses for drug delivery into eukaryotic cells. Curr. Med. Chem. 2008; 15(5): 459–69. https://doi.org/10.2174/092986708783503195
29. Manich M., Knapp O., Gibert M., Maier E., Jolivet-Reynaud C., Geny B. Clostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences. PLoS One. 2008; 3(11): e3764. https://doi.org/10.1371/journal.pone.0003764
30. Abildgaard L., Sondergaard T.E., Engberg R.M., Schramm A., Hojberg O. In vitro production of necrotic enteritis toxin B, NetB, by netB-positive and netB-negative Clostridium perfringens originating from healthy and diseased broiler chickens. Vet. Microbiol. 2010; 144(1-2): 231–5. https://doi.org/10.1016/j.vetmic.2009.12.036
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