Abstract
Infective and noninfective strains of Borrelia burgdorferi, along with Borrelia afzelii and Borrelia garinii, possessed a single iron-containing superoxide dismutase (SOD). None of the Lyme disease spirochetes tested possessed catalase or peroxidase activities. The borrelial SOD was not inducible by growth with increased oxygen concentrations and thus appeared to be produced constitutively.
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- Archibald F. S., Fridovich I. Manganese and defenses against oxygen toxicity in Lactobacillus plantarum. J Bacteriol. 1981 Jan;145(1):442–451. doi: 10.1128/jb.145.1.442-451.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Asada K., Yoshikawa K., Takahashi M., Maeda Y., Enmanji K. Superoxide dismutases from a blue-green alga, Plectonema boryanum. J Biol Chem. 1975 Apr 25;250(8):2801–2807. [PubMed] [Google Scholar]
- Austin F. E., Barbieri J. T., Corin R. E., Grigas K. E., Cox C. D. Distribution of superoxide dismutase, catalase, and peroxidase activities among Treponema pallidum and other spirochetes. Infect Immun. 1981 Aug;33(2):372–379. doi: 10.1128/iai.33.2.372-379.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Austin F. E. Maintenance of infective Borrelia burgdorferi Sh-2-82 in 4% oxygen - 5% carbon dioxide in vitro. Can J Microbiol. 1993 Dec;39(12):1103–1110. doi: 10.1139/m93-167. [DOI] [PubMed] [Google Scholar]
- 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]
- Baranton G., Postic D., Saint Girons I., Boerlin P., Piffaretti J. C., Assous M., Grimont P. A. Delineation of Borrelia burgdorferi sensu stricto, Borrelia garinii sp. nov., and group VS461 associated with Lyme borreliosis. Int J Syst Bacteriol. 1992 Jul;42(3):378–383. doi: 10.1099/00207713-42-3-378. [DOI] [PubMed] [Google Scholar]
- Barbour A. G. Isolation and cultivation of Lyme disease spirochetes. Yale J Biol Med. 1984 Jul-Aug;57(4):521–525. [PMC free article] [PubMed] [Google Scholar]
- Beaman L., Beaman B. L. Monoclonal antibodies demonstrate that superoxide dismutase contributes to protection of Nocardia asteroides within the intact host. Infect Immun. 1990 Sep;58(9):3122–3128. doi: 10.1128/iai.58.9.3122-3128.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
- Benov L. T., Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem. 1994 Oct 14;269(41):25310–25314. [PubMed] [Google Scholar]
- Burgdorfer W., Barbour A. G., Hayes S. F., Benach J. L., Grunwaldt E., Davis J. P. Lyme disease-a tick-borne spirochetosis? Science. 1982 Jun 18;216(4552):1317–1319. doi: 10.1126/science.7043737. [DOI] [PubMed] [Google Scholar]
- Canica M. M., Nato F., du Merle L., Mazie J. C., Baranton G., Postic D. Monoclonal antibodies for identification of Borrelia afzelii sp. nov. associated with late cutaneous manifestations of Lyme borreliosis. Scand J Infect Dis. 1993;25(4):441–448. doi: 10.3109/00365549309008525. [DOI] [PubMed] [Google Scholar]
- Claiborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. J Biol Chem. 1979 May 25;254(10):4245–4252. [PubMed] [Google Scholar]
- Clare D. A., Blum J., Fridovich I. A hybrid superoxide dismutase containing both functional iron and manganese. J Biol Chem. 1984 May 10;259(9):5932–5936. [PubMed] [Google Scholar]
- Clare D. A., Duong M. N., Darr D., Archibald F., Fridovich I. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem. 1984 Aug 1;140(2):532–537. doi: 10.1016/0003-2697(84)90204-5. [DOI] [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- Dougherty H. W., Sadowski S. J., Baker E. E. A new iron-containing superoxide dismutase from Escherichia coli. J Biol Chem. 1978 Jul 25;253(14):5220–5223. [PubMed] [Google Scholar]
- Franzon V. L., Arondel J., Sansonetti P. J. Contribution of superoxide dismutase and catalase activities to Shigella flexneri pathogenesis. Infect Immun. 1990 Feb;58(2):529–535. doi: 10.1128/iai.58.2.529-535.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Georgilis K., Steere A. C., Klempner M. S. Infectivity of Borrelia burgdorferi correlates with resistance to elimination by phagocytic cells. J Infect Dis. 1991 Jan;163(1):150–155. doi: 10.1093/infdis/163.1.150. [DOI] [PubMed] [Google Scholar]
- 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]
- Gregory E. M., Fridovich I. Visualization of catalase on acrylamide gels. Anal Biochem. 1974 Mar;58(1):57–62. doi: 10.1016/0003-2697(74)90440-0. [DOI] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli. J Bacteriol. 1977 Mar;129(3):1574–1583. doi: 10.1128/jb.129.3.1574-1583.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Regulation of the synthesis of catalase and peroxidase in Escherichia coli. J Biol Chem. 1978 Sep 25;253(18):6445–6420. [PubMed] [Google Scholar]
- Hassett D. J., Charniga L., Bean K., Ohman D. E., Cohen M. S. Response of Pseudomonas aeruginosa to pyocyanin: mechanisms of resistance, antioxidant defenses, and demonstration of a manganese-cofactored superoxide dismutase. Infect Immun. 1992 Feb;60(2):328–336. doi: 10.1128/iai.60.2.328-336.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Johnson R. C., Hyde F. W., Rumpel C. M. Taxonomy of the Lyme disease spirochetes. Yale J Biol Med. 1984 Jul-Aug;57(4):529–537. [PMC free article] [PubMed] [Google Scholar]
- Johnson R. C., Marek N., Kodner C. Infection of Syrian hamsters with Lyme disease spirochetes. J Clin Microbiol. 1984 Dec;20(6):1099–1101. doi: 10.1128/jcm.20.6.1099-1101.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kikuchi H. E., Suzuki T. An electrophoretic analysis of superoxide dismutase in Campylobacter spp. J Gen Microbiol. 1984 Nov;130(11):2791–2796. doi: 10.1099/00221287-130-11-2791. [DOI] [PubMed] [Google Scholar]
- Kornblatt A. N., Steere A. C., Brownstein D. G. Experimental Lyme disease in rabbits: spirochetes found in erythema migrans and blood. Infect Immun. 1984 Oct;46(1):220–223. doi: 10.1128/iai.46.1.220-223.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- 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]
- Moody K. D., Barthold S. W., Terwilliger G. A. Lyme borreliosis in laboratory animals: effect of host species and in vitro passage of Borrelia burgdorferi. Am J Trop Med Hyg. 1990 Jul;43(1):87–92. doi: 10.4269/ajtmh.1990.43.87. [DOI] [PubMed] [Google Scholar]
- Padgett P. J., Cover W. H., Krieg N. R. The Microaerophile SPirillum volutans: Cultivation on Complex Liquid and Solid Media. Appl Environ Microbiol. 1982 Feb;43(2):469–477. doi: 10.1128/aem.43.2.469-477.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Robinson J., Cooper J. M. Method of determining oxygen concentrations in biological media, suitable for calibration of the oxygen electrode. Anal Biochem. 1970 Feb;33(2):390–399. doi: 10.1016/0003-2697(70)90310-6. [DOI] [PubMed] [Google Scholar]
- Rorth M., Jensen P. K. Determination of catalase activity by means of the Clark oxygen electrode. Biochim Biophys Acta. 1967 May 16;139(1):171–173. doi: 10.1016/0005-2744(67)90124-6. [DOI] [PubMed] [Google Scholar]
- Rotilio G., Bray R. C., Fielden E. M. A pulse radiolysis study of superoxide dismutase. Biochim Biophys Acta. 1972 May 12;268(2):605–609. doi: 10.1016/0005-2744(72)90359-2. [DOI] [PubMed] [Google Scholar]
- Sambri V., Cevenini R., La Placa M. Susceptibility of iron-loaded Borrelia burgdorferi to killing by hydrogen peroxide and human polymorphonuclear leucocytes. FEMS Microbiol Lett. 1991 Jun 1;65(1):67–71. doi: 10.1016/0378-1097(91)90473-n. [DOI] [PubMed] [Google Scholar]
- Schwan T. G., Burgdorfer W., Garon C. F. Changes in infectivity and plasmid profile of the Lyme disease spirochete, Borrelia burgdorferi, as a result of in vitro cultivation. Infect Immun. 1988 Aug;56(8):1831–1836. doi: 10.1128/iai.56.8.1831-1836.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spiegelhalder C., Gerstenecker B., Kersten A., Schiltz E., Kist M. Purification of Helicobacter pylori superoxide dismutase and cloning and sequencing of the gene. Infect Immun. 1993 Dec;61(12):5315–5325. doi: 10.1128/iai.61.12.5315-5325.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Welch D. F., Sword C. P., Brehm S., Dusanic D. Relationship between superoxide dismutase and pathogenic mechanisms of Listeria monocytogenes. Infect Immun. 1979 Mar;23(3):863–872. doi: 10.1128/iai.23.3.863-872.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]