A Neisseria gonorrhoeae catalase mutant is more sensitive to hydrogen peroxide and paraquat, an inducer of toxic oxygen radicals

Microbial Pathogenesis

Volumn 37, Issue 2, 2004, Pages 55-63

  Soler García, Ángel A ^a   Jerse, Ann E ^a  

^a Uniformed Services University of the Health Sciences and the Walter Reed National Military Medical Center   (United States)

Author keywords

Catalase; Hydrogen peroxide; Neisseria gonorrhoeae; Oxidative stress; Paraquat

Indexed keywords

CATALASE; FUMARIC ACID; HYDROGEN PEROXIDE; NITRATE; OXYGEN RADICAL; PARAQUAT;

ARTICLE; BACTERIAL STRAIN; BINDING SITE; CLONING VECTOR; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DELETION; MUTANT; NEISSERIA GONORRHOEAE; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; CATALASE; CLONING, MOLECULAR; DNA, RECOMBINANT; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; HERBICIDES; HYDROGEN PEROXIDE; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; MUTATION; NEISSERIA GONORRHOEAE; OXIDATIVE STRESS; PARAQUAT;

ESCHERICHIA COLI; NEISSERIA; NEISSERIA GONORRHOEAE; UNIDENTIFIED SHUTTLE VECTOR;

EID: 4143126577     PISSN: 08824010     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micpath.2004.04.007     Document Type: Article

References (42)

1. Storz G., Imlay J.A. Oxidative stress. Curr Opin Microbiol. 2:1999;188-194
2. 2-producing lactobacilli on Neisseria gonorrhoeae growth and catalase activity. J Infect Dis. 170:1994;1209-1215
3. Amant S.D.C., Valentin-Bon I.E., Jerse A.E. Inhibition of Neisseria gonorrhoeae by Lactobacillus species that are commonly isolated from the female genital tract. Infect Immun. 70:2002;7169-7171
4. Hassett D.J., Cohen M.S. Bacterial adaptation to oxidative stress: implications for pathogenesis and interaction with phagocytic cells. FASEB J. 3:1989;2574-2583
5. Parsons NJ, Kawassi AA, Turner JA, Veale, DR, Perera VY, Penn, CW, Smith H. Investigation of the determinants of the survival of Neisseria gonorrhoeae within human polymorphonuclear phagocytes. J Gen Microbiol 1981;127:103-12.
6. Archibald F.S., Duong M.N. Superoxide dismutase and oxygen toxicity defenses in the genus Neisseria. Infect Immun. 51:1986;631-641
7. Norrod P., Morse S.A. Absence of superoxide dismutase in some strains of Neisseria gonorrhoeae. Biochem Biophys Res Commun. 90:1979;1287-1294
8. Tseng H.J., Srikhanta Y., McEwan A.G., Jennings M.P. Accumulation of manganese in Neisseria gonorrhoeae correlates with resistance to oxidative killing by superoxide anion and is independent of superoxide dismutase activity. Mol Microbiol. 40:2001;1175-1186
9. Wilks K.E., Dunn K.L.R., Farranti J.L., Reddin K.M., Gorringe A.R., Langford P.R., Kroll S.J. Periplasmic superoxide dismutase in meningococcal pathogenicity. Infect Immun. 66:1998;213-217
10. 2-mediated toxicity in Neisseria gonorrhoeae. J Bacteriol. 172:1990;7293-7295
11. Zheng H.Y., Hassett D.J., Bean K., Cohen M.S. Regulation of catalase in Neisseria gonorrhoeae: effects of oxidant stress and exposure to human neutrophils. J Clin Invest. 90:1992;1000-1006
12. Johnson S.R., Steiner B.M., Cruce D.D., Perkins G.H., Arko R.J. Characterization of a catalase-deficient strain of Neisseria gonorrhoeae: evidence for the significance of catalase in the biology of N. gonorrhoeae. Infect Immun. 61:1993;1232-1238
13. Johnson S.R., Steiner B.M., Perkins G.H. Cloning and characterization of the catalase gene of Neisseria gonorrhoeae: use of the gonococcus as a host organism for recombinant DNA. Infect Immun. 64:1996;2627-2634
14. Mulvey M.R., Sorby P.A., Triggs-Raine B.L., Loewen P.C. Cloning and physcial characterization of katE and katF required for catalase HPII expression in Escherichia coli. Gene. 73:1988;337-345
15. Hassett D.J., Britigan B.E., Svendsen T., Rosen G.M., Cohen M.S. Bacteria form intracellular free radicals in response to paraquat and streptonigrin: demonstration of the potency of hydroxyl radical. J Biol Chem. 262:1987;13404-13408
16. Quinland G.J., Gutteridge J.M.C. Hydroxyl radical generation by tetracycline antibiotics with free radical damage to DNA, lipids and carbohydrate in the presence of iron and copper salts. Free Radical Biol Med. 5:1988;341-348
17. Sha S.H., Schacht J. Formation of reactive oxygen species following bioactivation of gentamicin. Free Radical Biol Med. 26:1999;41-347
18. Groves J.T. Peroxynitrite: reactive, invasive and enigmatic. Curr Opin Chem Biol. 3:1999;226-235
19. Loewen P.C. Bacterial catalases. Oxidative stress and the molecular biology of antioxidant defenses. 1997;Cold Spring Harbor Laboratory Press, New York. p. 273-308
20. Alcorn T.M., Zheng H., Gunther M.R., Hassett D.J., Cohen M.S. Variation in hydrogen peroxide sensitivity between different strains of Neisseria gonorrhoeae is dependent on factors in addition to catalase activity. Infect Immun. 62:1994;2138-2140
21. Bishai W.R., Smith H.O., Barcak G.J. A peroxide/ascorbate-inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene product. J Bacteriol. 176:1994;2914-2921
22. Rocha E.R., Smith C.J. Regulation of Bacteroides fragilis katB mRNA by oxidative stress and carbon limitation. J Bacteriol. 179:(22):1997;7033-7039
23. DeShazer D., Wood G.E., Friedman R.L. Molecular characterization of catalase from Bordetella pertussis: identification of the katA promoter in an upstream insertion sequence. Mol Microbiol. 14:1994;123-130
24. Bishai W.R., Howard N.S., Wikelstein J.A., Smith H.O. Characterization and virulence analysis of catalase mutants of Haemophilus influenzae. Infect Immun. 62:1994;4855-4860
25. Khelef N., DeShazer D., Friedman R.L., Guiso N. In vivo and in vitro analysis of Bordetella pertussis catalase and Fe-superoxide dismutase mutants. FEMS Microbiol Lett. 142:(2-3):1996;231-235
26. Turner S., Reid E., Smith H., Cole J. A novel cytochrome C peroxidase from Neisseria gonorrhoeae: a lipoprotein from a Gram-negative bacterium. Biochem J. 373:2003;865-873
27. Tseng H.J., McEwan A.G., Apicella M.A., Jennings M.P. OxyR acts as a repressor of catalase expression in Neisseria gonorrhoeae. Infect Immun. 71:2003;550-556
28. Householder T.C., Bell W.A., Lissenden S., Cole J.A., Clark V.L. cis- and trans-acting elements involved in regulation of aniA, the gene encoding the major outer membrane protein in Neisseria gonorrhoeae. J Bacteriol. 181:1999;541-551
29. Cohen M.S., Cannon J.G., Jerse A.E., Charniga L.M., Isbey S.F., Whicker L.G. Human experimentation with Neisseria gonorrhoeae: rationale, methods, and implications for the biology of infection and vaccine development. J Infect Dis. 169:1994;532-537
30. Kellogg D.S., Peacock W.L., Deacon W.E., Brown L., Pirkle C. Neisseria gonorrhoeae. I. virulence genetically linked to clonal variation. J Bacteriol. 85:1963;1274-1279
31. Menard R., Sansonetti P.J., Parsot C. Nonpolar mutagenesis of the ipa genes defines IpaB IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J Bacteriol. 175:(18):1993;5899-5906
32. Gunn J.S., Stein D.C. Use of a non-selective transformation technique to construct a multiply restriction/modification-deficient mutant of Neisseria gonorrhoeae. Mol Gen Genet. 251:1996;509-517
33. Nassiff X., Puaoi D., So M. Transposition of Tn1545-delta 3 in the pathogenic Neisseriae: a genetic tool for mutagenesis. J Bacteriol. 173:(7):1991;2147-2154
34. Stein D.C., Silver L.E., Clark V.L., Young F.E. Construction and characterization of a new shuttle vector, pLES2, capable of functioning in Escherichia coli and Neisseria gonorrhoeae. Gene. 25:1983;241-247
35. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with folin phenol reagent. J Biol Chem. 193:1951;265-275
36. Worthington V. Catalase. Worthington V. Worthington enzyme manual: enzymes and related biochemicals. 1993;77-80 Worthington Biochemical Corporation, Freehold, NJ
37. 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. 140:1984;532-537
38. Misra H.P., Fridovich I. Superoxide dismutase and peroxidase: a positive activity stain applicable to polyacrylamide gel electropherograms. Arch Biochem Biophys. 183:1977;511-515
39. Eiglmeier K., Honore N., Iuchi S., Lin E.C.C., Cole S.T. Molecular genetic analysis of FNR-dependent promoters. Mol Microbiol. 3:1989;869-878
40. Simon R., Priefer U., Puhler A. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram negative bacteria. Biotech. 1983;784-791
41. Levine M.M., Kaper J.B., Lockman H., Black R.E., Clements M.L., Falkow S. DNA recombinanat risk assessment studies in humans:efficacy of poorly mobilizable plasmids in biologic containment. J Infect Dis. 148:1983;699-709
42. Chang A.C., Cohen S.N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol. 134:(3):1978;1141-1156