Comparative Characteristics of Antioxidative Enzymes of Yersinia pestis Strains of Different Subspecies and Yersinia pseudotuberculosis Strains
https://doi.org/10.21055/0370-1069-2008-2(96)-29-32
Abstract
Comparative electrophoretic investigation was carried out to study antioxidative enzymes (superoxide dismutase, catalase and peroxidase) in strains of Yersinia pestis, Yersinia pseudotuberculosis, Escherichia coli and Salmonella typhimurium. It was shown that Yersinia antioxidative enzymes are different from E. coli and S. typhimurium enzymes in electrophoretic motility. Their expression depends on cultivation temperature and plasmid content. Peculiarities of catalase-peroxidase expression were determined in strains of plague etiological agent of Ulegei subspecies, in strains of pseudotuberculosis etiological agent of IV serovar and in strains isolated from humans.
About the Authors
N. A. Vidyaeva
Russian Anti-Plague Research Institute “Micribe", Saratov
Russian Federation
Russian Federation
A. V. Gaeva
Russian Anti-Plague Research Institute “Micribe", Saratov
Russian Federation
Russian Federation
L. M. Koukleva
Russian Anti-Plague Research Institute “Micribe", Saratov
Russian Federation
Russian Federation
G. N. Odinokov
Russian Anti-Plague Research Institute “Micribe", Saratov
Russian Federation
Russian Federation
V. V. Kutyrev
Russian Anti-Plague Research Institute “Micribe", Saratov
Russian Federation
Russian Federation
References
1. Джапаридзе М.Н. Каталазная и пероксидазная активность чумного и псевдотуберкулезного микробов [дис. канд. мед. наук]. 1953. 205 с.
2. Куликов О.А., Дробков В.И., Дармов И.В. и др. Супероксиддисмутазы чумного микроба. Вестн. Рос. АМН. 1996; 6:45-9.
3. Куклева Л.М., Проценко О.А., Кутырев В.В. Современные представления о родстве возбудителей чумы и псевдотуберкулеза. Мол. генет., микробиол. и вирусол. 2002,1:3-7.
4. Шиманюк Н.Я., Асеева А.Е., Мишанькин Б.Н. Супероксиддисмутазная активность у иерсиний. В кн.: Иерсиниозы: микробиол., эпидемиол., клиника, патогенез, иммунол. Владивосток; 1968. С. 83-84.
5. Babior B. Oxygen-dependent microbial killing by phagocytes. New Engl. J. Med: 1978; 289: 659-68.
6. Beaman B., Black C., Doughty F., et al. Role of superoxide dismutase and catalase as determinants of pathogenicity of Nocardia asteroids: importance in resistance to microbicidal activities of human polymorphonuclear neutrophils. Infect. Immun. 1985; 47: 135-41.
7. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 1971; 44: 276-87.
8. Beyer W., Fridovich I. Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions. Anal. Biochem. 1987; 161: 559-66.
9. Brot N., Weissbach L., Werth J., et al. Enzymatic reduction of protein-bound methionine sulfoxide. Prot. Natl. Acad. Sci USA. 1981; 78:2155-58.
10. Burrows T., Farrel J., Gillett W. The catalase activity of Pasteurella pestis and other bacteria. Br. J. Exp. Pathol. 1964; 45:579-88.
11. Cohen H. The use of diaminobenzidine for spectrophotometric and acrylamide gel detection of sulfite oxidase and its applicability to hydrogen peroxide-genereting enzymes. Anal. Biochem. 1973; 53:208-22.
12. Davis B. Disc electrophoresis. II. Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 1964; 121:404-27.
13. Fridovich I. Oxygen radicals, hydrogen, peroxide and oxygen toxicity. In: W.A. Prior, editor. Free radicals in biology. New York: Academic Press; 1976. p. 239-277.
14. Fridovich I. The biology of oxygen radicals. Science. 1978; 201:875-80.
15. Carcia E., Nedialkov Y., Elliott J., et al. Molecular characterization of KatY (Antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis. J. Bacteriol. 1999; 181(10):3114-22.
16. Gregory E., Fridovich I. Visualization of catalase in acrylamide gels. Analyt. Biochem. 1974; 58:57-62.
17. Hollsstein M., Brooks P., Linn S., et al. Hydroxymethyluracil DNA glycosylase in mammalian cells. Proc. Natl. Acad. Sci. USA. 1984; 81:4003-7.
18. Mandell G. Catalase, superoxide dismutase and virulence in Staphylosossus aureus: in vitro and in vivo studies with emphasis on staphylococcal-leukocyte intraction. J. Clin. Invest. 1975; 55: 561-66.
19. Marcheva D., Nicolova S., Veljanov D. О распространении каталазной активности у бактерий рода Yersinia. Докл. Болг. АН. 1988; 41(3):57-60.
20. Mead J. Free radical mechanism of lipid damage and consequences for cellular mambranes. In: W.A. Prior, editor. Free radicals in biology. New York: Academic Press; 1976. P. 51-68.
21. Mehigh R., Brubaker R. Major stable peptides of Yersinia pestis synthesized during the low-calcium response. Infect. Immun. 1993; 61(1):13-22.
22. Raymond S. Acrylamide gel electrophoresis. Ann. N.Y. Acad. Sci. 1964; 121:350-65.
23. Rockenmacher M. Relationship of catalase activity to virulencein Pasteurella pestis. Proc. Soc. Exp. Biol. Med. 1949; 71:99-101.
24. Selander R., Caugant D., Ochman H., et al. Methods of multilocus enzyme electrophoresis for bacterial population genetics and systematics. Appl. Environ. Microbiol. 1986; 51:873-84.
25. Vassilyadi M., Archibald F. Catalase, superoxide dismutase and production of O2-sensitive mutants of Bacillus coagulans. Can. J. Microbiol. 1985; 31:994-99.
Review
For citations:
Vidyaeva N.A., Gaeva A.V., Koukleva L.M., Odinokov G.N., Kutyrev V.V. Comparative Characteristics of Antioxidative Enzymes of Yersinia pestis Strains of Different Subspecies and Yersinia pseudotuberculosis Strains. Problems of Particularly Dangerous Infections. 2008;(2(96)):29-32. (In Russ.) https://doi.org/10.21055/0370-1069-2008-2(96)-29-32
Views:
646
Email this article 