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. 1983 Apr;154(1):520–523. doi: 10.1128/jb.154.1.520-523.1983

Superoxide anion production and superoxide dismutase and catalase activities in Coxiella burnetii.

E T Akporiaye, O G Baca
PMCID: PMC217490  PMID: 6300038

Abstract

Coxiella burnetii was examined for superoxide anion (O2-) production and superoxide dismutase and catalase activities. The organism generated O2- at pH 4.5 but not at pH 7.4. The rickettsia displayed superoxide dismutase activity distinguishable from that of the host cell (L-929 mouse fibroblast). Catalase activity was maximal at pH 7.0 and diminished at pH 4.5. These enzymes may account, in part, for the ability of this obligate intracellular parasite to survive within phagocytes.

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Selected References

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  1. Amin V. M., Olson N. F. Influence of catalase activity on resistance of coagulase-positive staphylococci to hydrogen peroxide. Appl Microbiol. 1968 Feb;16(2):267–270. doi: 10.1128/am.16.2.267-270.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BEERS R. F., Jr, SIZER I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133–140. [PubMed] [Google Scholar]
  3. Babior B. M., Curnutte J. T., Kipnes R. S. Biological defense mechanisms. Evidence for the participation of superoxide in bacterial killing by xanthine oxidase. J Lab Clin Med. 1975 Feb;85(2):235–244. [PubMed] [Google Scholar]
  4. Baca O. G., Akporiaye E. T., Aragon A. S., Martinez I. L., Robles M. V., Warner N. L. Fate of phase I and phase II Coxiella burnetii in several macrophage-like tumor cell lines. Infect Immun. 1981 Jul;33(1):258–266. doi: 10.1128/iai.33.1.258-266.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ballou D., Palmer G., Massey V. Direct demonstration of superoxide anion production during the oxidation of reduced flavin and of its catalytic decomposition by erythrocuprein. Biochem Biophys Res Commun. 1969 Sep 10;36(6):898–904. doi: 10.1016/0006-291x(69)90288-5. [DOI] [PubMed] [Google Scholar]
  6. Beauchamp C. O., Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochim Biophys Acta. 1973 Jul 12;317(1):50–64. doi: 10.1016/0005-2795(73)90198-0. [DOI] [PubMed] [Google Scholar]
  7. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  8. Britton L., Malinowski D. P., Fridovich I. Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms. J Bacteriol. 1978 Apr;134(1):229–236. doi: 10.1128/jb.134.1.229-236.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Burton P. R., Stueckemann J., Welsh R. M., Paretsky D. Some ultrastructural effects of persistent infections by the rickettsia Coxiella burnetii in mouse L cells and green monkey kidney (Vero) cells. Infect Immun. 1978 Aug;21(2):556–566. doi: 10.1128/iai.21.2.556-566.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. FRIDOVICH I., HANDLER P. Xanthine oxidase. IV. Participation of iron in internal electron transport. J Biol Chem. 1958 Dec;233(6):1581–1585. [PubMed] [Google Scholar]
  11. Gregory E. M., Fridovich I. Induction of superoxide dismutase by molecular oxygen. J Bacteriol. 1973 May;114(2):543–548. doi: 10.1128/jb.114.2.543-548.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gregory E. M., Fridovich I. Oxygen toxicity and the superoxide dismutase. J Bacteriol. 1973 Jun;114(3):1193–1197. doi: 10.1128/jb.114.3.1193-1197.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Gregory E. M., Yost F. J., Jr, Fridovich I. Superoxide dismutases of Escherichia coli: intracellular localization and functions. J Bacteriol. 1973 Sep;115(3):987–991. doi: 10.1128/jb.115.3.987-991.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hackstadt T., Williams J. C. Biochemical stratagem for obligate parasitism of eukaryotic cells by Coxiella burnetii. Proc Natl Acad Sci U S A. 1981 May;78(5):3240–3244. doi: 10.1073/pnas.78.5.3240. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hewitt J., Morris J. G. Superoxide dismutase in some obligately anaerobic bacteria. FEBS Lett. 1975 Feb 15;50(3):315–318. doi: 10.1016/0014-5793(75)80518-7. [DOI] [PubMed] [Google Scholar]
  16. Ismail G., Sawyer W. D., Wegener W. S. Effect of hydrogen peroxidase and superoxide radical on viability of Neisseria gonorrhoeae and related bacteria. Proc Soc Exp Biol Med. 1977 Jun;155(2):264–269. doi: 10.3181/00379727-155-39786. [DOI] [PubMed] [Google Scholar]
  17. Jackett P. S., Aber V. R., Lowrie D. B. Virulence and resistance to superoxide, low pH and hydrogen peroxide among strains of Mycobacterium tuberculosis. J Gen Microbiol. 1978 Jan;104(1):37–45. doi: 10.1099/00221287-104-1-37. [DOI] [PubMed] [Google Scholar]
  18. Johnston R. B., Jr, Keele B. B., Jr, Misra H. P., Lehmeyer J. E., Webb L. S., Baehner R. L., RaJagopalan K. V. The role of superoxide anion generation in phagocytic bactericidal activity. Studies with normal and chronic granulomatous disease leukocytes. J Clin Invest. 1975 Jun;55(6):1357–1372. doi: 10.1172/JCI108055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Keele B. B., Jr, McCord J. M., Fridovich I. Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. J Biol Chem. 1970 Nov 25;245(22):6176–6181. [PubMed] [Google Scholar]
  20. Klebanoff S. J. Antimicrobial mechanisms in neutrophilic polymorphonuclear leukocytes. Semin Hematol. 1975 Apr;12(2):117–142. [PubMed] [Google Scholar]
  21. Klug D., Rabani J., Fridovich I. A direct demonstration of the catalytic action of superoxide dismutase through the use of pulse radiolysis. J Biol Chem. 1972 Aug 10;247(15):4839–4842. [PubMed] [Google Scholar]
  22. Massey V., Strickland S., Mayhew S. G., Howell L. G., Engel P. C., Matthews R. G., Schuman M., Sullivan P. A. The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen. Biochem Biophys Res Commun. 1969 Sep 10;36(6):891–897. doi: 10.1016/0006-291x(69)90287-3. [DOI] [PubMed] [Google Scholar]
  23. McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
  24. McCord J. M., Keele B. B., Jr, Fridovich I. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc Natl Acad Sci U S A. 1971 May;68(5):1024–1027. doi: 10.1073/pnas.68.5.1024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Murray H. W., Cohn Z. A. Macrophage oxygen-dependent antimicrobial activity. I. Susceptibility of Toxoplasma gondii to oxygen intermediates. J Exp Med. 1979 Oct 1;150(4):938–949. doi: 10.1084/jem.150.4.938. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Myers W. F., Warfel L. E., Wisseman C. L., Jr Absence of hydrogen peroxide production by or catalase action in Rickettsia prowazeki. J Bacteriol. 1978 Oct;136(1):452–454. doi: 10.1128/jb.136.1.452-454.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. ORMSBEE R. A., PEACOCK M. G. METABOLIC ACTIVITY IN COXIELLA BURNETII. J Bacteriol. 1964 Nov;88:1205–1210. doi: 10.1128/jb.88.5.1205-1210.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. PARETSKY D., DOWNS C. M., CONSIGLI R. A., JOYCE B. K. Studies on the physiology of rickettsiae. I. Some enzyme systems of Coxiella burnetii. J Infect Dis. 1958 Jul-Aug;103(1):6–11. doi: 10.1093/infdis/103.1.6. [DOI] [PubMed] [Google Scholar]
  29. Salin M. L., McCord J. M. Superoxide dismutases in polymorphonuclear leukocytes. J Clin Invest. 1974 Oct;54(4):1005–1009. doi: 10.1172/JCI107816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Silberman R., Fiset P. Method for counting Rickettsiae and Chlamydiae in purified suspensions. J Bacteriol. 1968 Jan;95(1):259–261. doi: 10.1128/jb.95.1.259-261.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Weisiger R. A., Fridovich I. Superoxide dismutase. Organelle specificity. J Biol Chem. 1973 May 25;248(10):3582–3592. [PubMed] [Google Scholar]

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