Microbial Strategies to Prevent Oxygen-Dependent Killing by Phagocytes

References

• Sies H. Biochemistry of oxidative stress. Angewandte Chemie International Edition in English 1986; 25: 1058–1071
   Web of Science ®Google Scholar
• Bannister J.V., Bannister W.H., Rotilio G. Aspects of the structure, function, and applications of superoxide dismutase. CRC Critical Reviews in Biochemistry 1987; 22: 111–180
   PubMed Web of Science ®Google Scholar
• Fridovich I. The biology of oxygen radicals. Science 1978; 201: 875–880
   PubMed Web of Science ®Google Scholar
• Hassett D.J., Cohen M.S. Bacterial adaptation to oxidative stress: implications for pathogenesis and interaction with phagocytic cells. The FASEB Journal 1989; 3: 2574–2582
   PubMed Web of Science ®Google Scholar
• Farr S.B., Touati D., Kogoma T. Effect of oxygen stress on membrane functions in Escherichia colt: Role of HPI catalase. Journal of Bacteriology 1988; 170: 1837–1842
   Google Scholar
• Abril N., Pueyo C. Mutagenesis in Escherichia coli lacking catalase. Environmental and Molecular Mutagenesis 1990; 15: 184–189
   Google Scholar
• Imlay J.A., Linn S. Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide. Journal of Bacteriology 1987; 169: 2967–2976
   PubMed Web of Science ®Google Scholar
• Gardner P.R., Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phos-phogluconate dehydratase. The Journal of Biological Chemistry 1991; 266: 1478–1483
   PubMed Web of Science ®Google Scholar
• Fridovich I. Superoxide dismutases. Advances in Enzymology 1986; 58: 62–97
   Google Scholar
• Carlioz A., Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life?. The EMBO Journal 1986; 5: 623–630
   PubMed Web of Science ®Google Scholar
• Badwey J.A., Karnovsky M.L. Active oxygen species and the functions of phagocytic leukocytes. Annual Reviews in Biochemistry 1980; 49: 695–726
   PubMed Web of Science ®Google Scholar
• Davies B., Chattings L.S., Edwards S.W. Superoxide generation during phagocytosis by Acanthamoeba caslelanii. Similarities to the respiratory burst of immune phagocytes. Journal of General Microbiology 1991; 137: 705–710
   Google Scholar
• Babior B.M. The respiratory burst of phagocytes. Journal of Clinical Investigations 1984; 73: 599–601
   PubMed Web of Science ®Google Scholar
• Mims C.A. The pathogenesis of infectious disease. The encounter of the microbe with the phagocytic cell 3rd ed. Academic Press, London 1987; 63–91
   Google Scholar
• Hurst J.K., Barrette W.C., Jr. Leukocytic oxygen activation and microbicidal oxidative toxins. CRC Critical Reviews in Biochemistry and Molecular Biology 1989; 24: 271–328
   PubMed Web of Science ®Google Scholar
• Klebanoff S.J. Phagocytic cells: Products of oxygen metabolism. Inflammation: Basic Principles and Clinical Correlations, J.I. Gallin. Raven Press, New York 1988; 391–444
   Google Scholar
• Gabic T.G., Babior B.M. The killing of pathogens by phagocytes. Annual Reviews in Medicine 1981; 32: 313–326
   Google Scholar
• Andrews R.G.W., Orci L. A view of acidic intracellular compartments. Journal of Cell Biology 1988; 106: 539–543
   Google Scholar
• Russo M., Teixeira H.C., Marcondes M.C.G., Barbuto J.A.M. Superoxide-independent hydrogen peroxide release by activated macrophages. Brazilian Journal of Medical and Biological Research 1989; 22: 1271–1273
   PubMed Web of Science ®Google Scholar
• Godfrey R.W., Wilder M.S. Relationship between oxidative metabolism, macrophage activation, and antilisterial activity. Journal of Leukocyte Biology 1984; 36: 533–543
   Google Scholar
• Di Mascio P., Wefers H., Do-thi H.P., Lafleur M.V.M., Sies H. Singlet molecular oxygen causes loss of biological activity in plasmid and bacteriophage DNA and induces single strand breaks. Biochimica et Biophysica Acta 1989; 1007: 151–157
   Google Scholar
• Cohen M.S., Britigan B.E., Hassett D.J., Rosen G.M. Phagocytes, 02 reduction, and hydroxyl radical. Reviews in Infectious Diseases 1988; 10: 1088–1096
   PubMedGoogle Scholar
• Buchmeier N.A., Heffron F. Induction of Salmonella stress proteins upon infection of macrophages. Science 1990; 248: 730–732
   PubMed Web of Science ®Google Scholar
• Donati Y.R.A., Slosman D.O., Polla B.S. Oxidative injury and the heat shock response. Biochemical Pharmacology 1990; 40: 2571–2577
   PubMed Web of Science ®Google Scholar
• Johnston R.B., Jr. Oxygen metabolism and the microbicidal activity of macrophages. Federation Proceedings 1978; 37: 2759–2764
   PubMedGoogle Scholar
• Beaman L., Beaman B.L. The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annual Reviews in Microbiology 1984; 38: 27–48
   PubMedGoogle Scholar
• Czuprynski C.J. Bacterial evasion of cellular defense mechanisms: an overview. Virulence mechanisms of bacterial pathogens, J.A. Roth. American Society for Microbiology. 1988; 141–160
   Google Scholar
• Horwitz M.A., Mayfield F.R. Legionella pneumophilia inhibits acidification of its phagosome in human monocytoes. Journal of Cell Biology 1984; 99: 1936–1943
   PubMed Web of Science ®Google Scholar
• Sibley L.D., Lawson R., Weidner E. Superoxide dismutase and catalase in Toxoplasma gondii. Molecular Biochemistry and Parasitology 1986; 19: 83–87
   Google Scholar
• Chakraborty T., Goebel W. Recent developments in the study of virulence in Listeria monocytogenes. Current Topics in Microbiology and Immunology 1988; 138: 41–58
   Google Scholar
• Sansonetti P.J., Ryter A., Clerc P., Maurelli A.T., Mounier J. Multiplication of Shigella flexneri within HeLa cells. Lysis of the phagocytic vacuole and plasmid-mediated contact hemolysis. Infection and Immunity 1986; 51: 461–469
   PubMed Web of Science ®Google Scholar
• Andrews N.W., Abrams C.K., Slatin S.L., Griffiths G. A T. cruzi-secreted protein immunologically related to the complement factor C9: Evidence for membrane pore-forming activity at low pH. Cell 1990; 61: 1277–1287
   PubMed Web of Science ®Google Scholar
• Sahney N.N., Lambe B.C., Summersgill J.T., Miller R.D. Inhibition of polymorphonuclear leukocyte function by Legionella pneumophila exoproducts. Microbial Pathogenesis 1990; 9: 117–125
   Google Scholar
• Glew R.H., Saha A.K., Das S., Remaley A.T. Biochemistry of the Leishmania species. Microbiological Reviews 1988; 52: 412–432
   PubMedGoogle Scholar
• Saha A.K., Dowling J.N., LaMarco K.L., Das S., Remaley A.T., Olomu N., Pope M.T., Glew R.H. Properties of an acid phosphatase from Legionella micdadei which blocks superoxide anion production by human neutrophils. Archives of Biochemistry and Biophysics 1985; 243: 150–160
   PubMedGoogle Scholar
• Wilson C.B., Tsai V., Remington J.S. Failure to trigger the oxidative metabolic burst by normal macrophages. Journal of Experimental Medicine 1980; 151: 328–346
   PubMed Web of Science ®Google Scholar
• Chang H.R., Pechere J.-C. Macrophage oxidative metabolism and intracellular Toxoplasma gondii. Microbial Pathogenesis 1989; 7: 37–44
   Google Scholar
• Tauber A.I., Pavlotsky N., Lin J.S., Rice P.A. Inhibition of human neutrophil NADPH oxidase by Chlamydia serovars E, K, and L2. Infection and Immunity 1989; 57: 1108–1112
   Google Scholar
• Hof H. Microbial strategies for intracellular survival. Infection 1991; 19: S202–S205
   Google Scholar
• Buchmeier N.A., Heffron F. Inhibition of macrophage phagosome-lysosome fusion by Salmonella typhimurium. Infection and Immunity 1991; 59: 2232–2238
   PubMed Web of Science ®Google Scholar
• Miller S.I., Kukral A.M., Mekalanos J.J. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proceedings of the National Academy of Sciences USA 1989; 86: 5054–5058
   PubMed Web of Science ®Google Scholar
• Chan J., Fujiwara T., Brennan P., McNeil M., Turco S.J., Sibille J.-C., Snapper M., Aisen P., Bloom B.R. Microbial glycolipids: Possible virulence factors that scavenge oxygen radicals. Proceedings of the National Academy of Sciences USA 1989; 86: 2453–2457
   PubMed Web of Science ®Google Scholar
• Sample A.K., Czuprynski C.J. Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle. Infection and Immunity 1991; 59: 2239–2244
   PubMed Web of Science ®Google Scholar
• Meister A., Anderson M.E. Glutathione. Annual Reviews in Biochemistry 1983; 52: 711–760
   PubMed Web of Science ®Google Scholar
• Kelner M.J., Bagnell R. Glutathione-dependent enzymes alone can produce paraquat resistance. Free Radicals in Biology & Medicine 1990; 9: 149–153
   PubMedGoogle Scholar
• Greenberg J.R., Demple B. Glutathione in Escherichia coli is dispensable for resistance to H202 and gamma radiation. Journal of Bacteriology 1986; 168: 1026–1029
   PubMed Web of Science ®Google Scholar
• Piccolomini R., Di Ilo C., Aceto A., Allocati N., Faraone A., Cellini L., Ravagnan G., Federici G. Glutathione transferase in bacteria: subunit composition and antigenic characterization. Journal of General Microbiology 1989; 135: 3119–3125
   Google Scholar
• Hewitt J., Morris G. Superoxide dismutase in some obligately anaerobic bacteria. FEBS Letters 1975; 50: 315–318
   PubMed Web of Science ®Google Scholar
• Steinman H.M., Ely B. Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing, and mapping of the gene and periplasmic location of the enzyme. Journal of Bacteriology 1990; 172: 2901–2910
   PubMed Web of Science ®Google Scholar
• Touati D. Molecular genetics of superoxide dismutases. Free Radical Biology & Medicine 1988; 5: 393–402
   PubMed Web of Science ®Google Scholar
• Hassan H.M. Biosynthesis and regulation of superoxide dismutases. Free Radical Biology & Medicine 1988; 5: 377–385
   PubMed Web of Science ®Google Scholar
• Goldberg I., Hochman A. Purification and characterization of a novel type of catalase from the bacterium Klebsiella pneumoniae. Biochimica el Biophysica Acta 1989; 991: 330–336
   PubMedGoogle Scholar
• Nadler V., Goldberg I., Hochman A. Comparative study of bacterial catalases. Biochimica el Biophysica Ada 1986; 882: 234–241
   Google Scholar
• Haas A., Brehm K., Kreft J., Goebel W. Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases. Journal of Bacteriology 1991; 173: 5159–5167
   Google Scholar
• Loewen P.C., Stauffer G.V. Nucleotide sequence of katG of Salmonella typhimurium and characterization of its product, hydroperoxidase I. Molecular and General Genetics 1991; 224: 147–151
   Google Scholar
• Wayne L.G., Diaz G.A. A double staining method for differentiation between two classes of mycobacterial catalases in polyacrylamide gel electrophoresis gels. Analytical Biochemistry 1986; 157: 89–92
   PubMed Web of Science ®Google Scholar
• Goerlich O., Quillardet P., Hofnung M. Induction of the SOS response by hydrogen peroxide in various Escherichia coli mutants with altered protection against oxidative DNA damage. Journal of Bacteriology 1989; 171: 6141–6147
   PubMed Web of Science ®Google Scholar
• Carlsson J., Carpenter V.S. The recA* gene product is more important than catalase and superoxide dismutase in protecting Escherichia coli against hydrogen peroxide toxicity. Journal of Bacteriology 1980; 142: 319–321
   PubMed Web of Science ®Google Scholar
• Yost F.J., Fridovich I. Superoxide radical and phagocytosis. Archives of Biochemistry and Biophysics 1974; 161: 395–401
   Google Scholar
• Braun V., Hantke K. Genetics of siderophore biosynthesis and transport. Handbook of microbial iron chelates (siderophores), G. Winkelmann. CRC Press, Boca Raton, FL 1991, in press
   Google Scholar
• Hoepelman I.M., Bezemer W.A., Vandenbroucke-Grauls C.M.J.E., Marx J.J.M., Verhoef J. Bacterial iron enhances oxygen radical-mediated killing of Staphylococcus aureus by phagocytes. Infection and Immunity 1990; 58: 26–31
   PubMed Web of Science ®Google Scholar
• Repine J.E., Fox R.B., Berger E.M. Hydrogen peroxide kills Staphylococcus aureus by reacting with staphylococcal iron to form hydroxyl radical. The Journal of Biological Chemistry 1981; 256: 7094–7096
   PubMed Web of Science ®Google Scholar
• Mandell G.L. Catalase, superoxide dismutase, and virulence of Staphylococcus aureus. The Journal of Clinical Investigations 1975; 55: 561–566
   PubMed Web of Science ®Google Scholar
• Bloch C.A., Thome G.M., Ausubel F.M. General method for site-directed mutagenesis in Escherchia coli OI8ac:K1:H7: Deletion of the inducible superoxide dismutase gene, sodA, does not diminish bacteremia in neonatal rats. Infection and Immunity 1989; 57: 2141–2148
   Google Scholar
• Smith M.W., Neidhardt F.C. Proteins induced by aerobiosis in Escherichia coli. Journal of Bacteriology 1983; 154: 344–350
   PubMed Web of Science ®Google Scholar
• Schwartz C.E., Krall J., Norton L., McKay K., Kay D., Lynch R.E. Catalase and superoxide dismutase in Escherichia coli. Roles in resistance to killing by neutrophils. The Journal of Biological Chemistry 1983; 258: 6277–6281
   PubMed Web of Science ®Google Scholar
• Johnston R.B., Keele B., Misra H.P., Lehmeyer J.E., Webb L.S., Bashner R.L., Rajagopalan K.V. The role of superoxide anion generation in phagocytic bactericidal activity. Journal of Clinical Investigation 1975; 55: 1357–1372
   PubMed Web of Science ®Google Scholar
• Franzon V.L., Arondel J., Sansonetti P.J. Contribution of superoxide dismutase and catalase activities to Shigella flexneri pathogenesis. Infection and Immunity 1990; 58: 529–535
   Google Scholar
• Fields P.I., Swanson R.V., Haidaris C.G., Heffron F. Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent. Proceedings of the National Academy of Sciences USA 1986; 83: 5189–5193
   PubMed Web of Science ®Google Scholar
• Britton L., Fridovich I. Intracellular location of the superoxide dismutases of Escherichia coli: a reevaluation. Journal of Bacteriology 1977; 131: 815–820
   PubMed Web of Science ®Google Scholar
• Beaman B.L., Scates S.M., Moring S.E., Deem R., Misra H.P. Purification and properties of a unique superoxide dismutase from Nocardia asteroides. The Journal of Biological Chemistry 1983; 258: 91–96
   PubMed Web of Science ®Google Scholar
• Beaman L., Beaman B.L. Monoclonal antibodies demonstrate that superoxide dismutase contributes to protection of Nocardia asteroides within the intact host. Infection and Immunity 1990; 58: 3122–3128
   PubMed Web of Science ®Google Scholar
• Jackett P.S., Aber V.R., Lowrie D.B. Virulence and resistance to superoxide, low pH and hydrogen peroxide among strains of Mycobacterium tuberculosis. Journal of General Microbiology 1978; 104: 37–45
   PubMedGoogle Scholar
• Yamada Y., Saito H., Tomioka H., Jidoi J. Susceptibility of micro-organisms to active oxygen species: sensitivity to the xanthine-oxidase-mediated antimicrobial system. Journal of General Microbiology 1987; 133: 2007–2014
   Google Scholar
• Zhang Y., Lathigra R., Garbe T., Catty D., Young D. Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis. Molecular Microbiology 1991; 5: 381–391
   Google Scholar
• Thangaraj H.S., Lamb F.I., Davis E.O., Jenner PJ., Jeyakumar L.H., Colston M.J. Identification, sequencing, and expression of Mycobacterium leprae superoxide dismutase, a major antigen. Infection and Immunity 1990; 58: 1937–1942
   Google Scholar
• Bricker B.J., Tabatabai L.B., Judge B.A., Deyoe B.L., Mayfield J.E. Cloning, expression, and occurrence of the Brucella Cu-Zn superoxide dismutase. Infection and Immunity. 1990; 58: 2935–2939
   Google Scholar
• Kusunose E., Ichihara K., Noda Y., Kusunose M. Superoxide dismutase from Mycobacterium tuberculosis. Journal of Biochemistry 1976; 80: 1343–1352
   Google Scholar
• Welch D.F., Sword C.P., Brehm S., Dusanic D. Relationship between superoxide dismutase and pathogenic mechanisms of Listeria monocytogenes. Infection and Immunity 1980; 23: 863–872
   Google Scholar
• Brehm K., Haas A., Kreft J., Goebel W. A gene encoding a superoxide dismutase of the facultative intracellular bacterium Listeria monocytogenes. Manuscript 1992, submitted
   Google Scholar
• Welch D.F. Role of catalase and superoxide dismutase in the virulence of Listeria monocytogenes. Annales Microbiologie (Institut Pasteur) 1987; 138: 265–268
   Google Scholar
• Bortolussi R., Vandenbroucke-Grauls C.M.J.E., van Asbeck B.S., Verhoef J. Relationship of bacterial growth phase to killing of Listeria monocytogenes by oxidative agents generated by neutrophils and enzyme systems. Infection and Immunity 1987; 55: 3197–3203
   Google Scholar
• Leblond-Francillard M., Gaillard J.-L., Berche P. Loss of catalase activity in Tn1545-induced mutants does not reduce growth of Listeria monocytogenes in vivo. Infection and Immunity 1989; 57: 2569–2573
   Google Scholar
• DiGuiseppi J., Fridovich I. Oxygen toxicity in Streptococcus sanguis. The Journal of Biological Chemistry 1982; 257: 4046–4051
   PubMed Web of Science ®Google Scholar
• Archibald F.S., Duong M.N. Superoxide dismutase and oxygen toxicity defenses in the genus. Neisseria. Infection and Immunity 1986; 51: 631–641
   PubMedGoogle Scholar
• Haas A., Goebel W. Cloning of a superoxide dismutase gene from Listeria ivanovii by functional complementation in Escherichia coli and characterization of the gene product. Molecular and General Genetics 1992, in press
   Google Scholar
• Dallmier A.W., Martin S.E. Catalase, superoxide dismutase, and hemolysin activities and heat susceptibility of Listeria monocytogenes after growth in media containing sodium chloride. Applied and Environmental Microbiology 1990; 56: 2807–2810
   Google Scholar
• Hassett D.J., Charniga L., Cohen M.S. recA and catalase in H2o2 mediated toxicity in Neisseria gonorrhoeae. Journal of Bacteriology 1990; 172: 7293–7295
   Google Scholar
• Schiavone J.R., Hassan H.M. Biosynthesis of superoxide dismutase in eight prokaryotes: effects of oxygen, paraquat and an iron chelator. FEMS Microbiology Letters 1987; 42: 33–38
   Google Scholar
• Davies W.A. Kinetics of killing Listeria monocytogenes by macrophages: rapid killing accompanying phagocytosis. RES: Journal of the Reticuloendothelial Society 1983; 34: 131–141
   Google Scholar
• Peck R. Gamma interferon induces monocyte killing of Listeria monocytogenes by an oxygen-dependent pathway; alpha- or beta-interferons by oxygen-independent pathways. Journal of Leukocyte Biology 1989; 46: 434–440
   PubMedGoogle Scholar
• Czuprynski C.J., Campbell P. A., Henson P.M. Killing of Listeria monocytogenes by human neutrophils and monocytes, but not by monocyte-derived macrophages. RES: Journal of the Reticuloendothelial Society 1983; 34: 29–44
   PubMedGoogle Scholar
• Kossack R.E., Guerrant R.I., Densen P., Schadelin J., Mandell G.I. Diminished neutrophil oxidative metabolism after phagocytosis of virulent Salmonella typhi. Infection and Immunity 1981; 31: 674–678
   PubMedGoogle Scholar
• Johnston K., Charles I., Dougan D., Pickard D., O'Gaora P., Costa G., AH T., Miller I., Hormaecke C. The role of a stress-response protein in Salmonella typhimurium virulence. Molecular Microbiology 1991; 5: 401–407
   Google Scholar
• Camilli A., Paynton C.R., Portnoy D.A. Intracellular methicillin selection of Listeria monocytogenes mutants unable to replicate in a mouse macrophage cell line. Proceedings of the National Academy of Sciences USA 1989; 86: 5522–5526
   Google Scholar
• Godfrey R.W., Wilder M.S. Generation of oxygen species and virulence of Listeria monocytogenes. Infection and Immunity 1985; 47: 837–839
   Google Scholar
• Storz G., Tartaglia L.A., Farr S.B., Ames B.N. Bacterial defenses against oxidative stress. Trends in Genetics. 1990; 6: 363–368
   PubMed Web of Science ®Google Scholar
• Storz G., Tartaglia L.A., Ames B.N. Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation. Science 1990; 248: 189–194
   PubMed Web of Science ®Google Scholar
• Tsaneva L.R., Weiss B. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. Journal of Bacteriology 1990; 172: 4197–4205
   PubMed Web of Science ®Google Scholar
• Amabile-Cuevas C.F., Demple B. Molecular characterization of the soxRS genes of Escherichia coli: two genes control a superoxide stress regulon,. Nucleic Acids Research 1991; 19: 4479–4484
   PubMed Web of Science ®Google Scholar
• Spiro S., Guest J.R. Adaptive responses to oxygen limitation in Escherichia coli. Trends in Biochemical Sciences 1991; 16: 310–314
   PubMed Web of Science ®Google Scholar
• Tardat B., Touati D. Two global regulators repress the anaerobic expression of MnSOD in Escherichia coli: Fur (ferric uptake regulation) and Arc (aerobic respiration control). Molecular Microbiology 1991; 5: 455–465
   PubMed Web of Science ®Google Scholar
• Niederhoffer E.C., Naranjo CM., Bradley K.L., Fee J.A. Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulon (fur) locus. Journal of Bacteriology 1990; 172: 1930–1938
   PubMed Web of Science ®Google Scholar
• Bowen S.W., Hassan H.M. Induction of the manganese-containing superoxide dismutase in Escherichia coli is independent of the oxidative stress (oxyR-controlled) regulon. The Journal of Biological Chemistry 1988; 263: 14808–14811
   PubMedGoogle Scholar
• Touati D. Transcriptional and posttranscriptional regulation of manganese superoxide dismutase biosynthesis in Escherichia coli, studied with operon and protein fusions. Journal of Bacteriology 1988; 170: 2511–2520
   PubMed Web of Science ®Google Scholar
• Storz G., Christman M.F., Sies H., Ames B.N. Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium. Proceedings of the National Academy of Sciences USA 1987; 84: 8917–8921
   PubMed Web of Science ®Google Scholar
• Tao K., Makino K., Yonei S., Nakata A., Shinagawa H. Molecular cloning and nucleotide sequencing of oxyR, the positive regulatory gene of a regulon for adaptive response to oxidative stress in Escherichia coli: homologies between OxyR protein and a family of bacterial activator proteins. Molecular and General Genetics 1989; 218: 371–376
   PubMedGoogle Scholar
• Dowds B.C.A., Hoch J.A. Regulation of the oxidative stress response by the hpr gene in Bacillus subtilis. Journal of General Microbiology 1991; 137: 1121–1125
   Google Scholar
• Keller R., Kerst R., Erb P., Aebischer T., de Libero G., Balzer M., Groscurth P., Keller H.U. Expression of cellular effector functions and production of reactive nitrogen intermediates: a comparative study including T-lymphocytes, T-like cells, neutrophil granulocytes, and mononuclear phagocytes. Cellular Immunology 1990; 131: 398–403
   PubMedGoogle Scholar
• Keller R., Gehrl R., Keist R., Huf E., Kayser F.H. The interaction of macrophages and bacteria: a comparative study of the induction of tumoricidal activity and of reactive nitrogen intermediates. Cellular Immunology 1991; 134: 249–256
   Google Scholar
• Granger D.L., Hibbs J.B., Jr., Perfect J.R., Durack D.T. Specific amino acid (L-arginine) requirement for the microbiostatic activity of murine macrophages. Journal of Clinical Investigations 1988; 81: 1129–1136
   PubMed Web of Science ®Google Scholar
• Alspaugh J.A., Granger D.L. Inhibition of Cryptococcus neoformans by nitrogen oxides supports the role of these molecules as effectors of macrophage-mediated cytostasis. Infection and Immunity 1991; 59: 2291–2296
   PubMedGoogle Scholar
• Buchmeier N.A., Heffron F. Intracellular survival of wild-type Salmonella typhimurium and macrophage-sensitive mutants in diverse populations of macrophages. Infection and Immunity 1989; 57: 1–7
   PubMed Web of Science ®Google Scholar
• Christman M.F., Morgan R.W., Jacobson F.S., Ames B.N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 1985; 41: 753–762
   PubMed Web of Science ®Google Scholar
• Clark R.A. Oxidative inactivation of pneumolysin by the myeloperoxidase system and stimulated human neutrophils. The Journal of Immunology 1986; 136: 4617–4622
   Google Scholar
• Nakayama K. The superoxide dismutase-encoding gene of the obligately anaerobic bacterium Bacteroides gingivalis. Gene 1990; 96: 149–150
   Google Scholar
• Choi J.-I., Takahashi N., Kato T., Kuramitsu H.K. Isolation, expression, and nucleotide sequence of the sod gene from Porphyromonas gingivalis. Infection and Immunity 1991; 59: 1564–1566
   Google Scholar
• Heinzen R.A., Frazier ME., Mallavia LP. Nucleotide sequence of Coxiella burnetti superoxide dismutase. Nucleic Acids Research 1990; 18: 6437
   Google Scholar
• Nettleton C.J., Bull C., Baldwin TO., Fee J.A. Isolation of the Escherichia coli iron superoxide dismutase gene: evidence that intracellular superoxide concentration does not regulate oxygen-dependent synthesis of the manganese superoxide dismutase. Proceedings of the National Academy of Sciences USA 1984; 81: 4970–4973
   PubMed Web of Science ®Google Scholar
• Carlioz A., Ludwig M.L., Stalling W.L., Fee J.A., Steinman H.M., Touati D. Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. The Journal of Biological Chemistry 1988; 263: 1555–1562
   PubMedGoogle Scholar
• Touati D. Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12. Journal of Bacteriology 1983; 155: 1078–1085
   PubMed Web of Science ®Google Scholar
• Takeda Y., Avila H. Structure and gene expression of the E. coli Mn superoxide dismutase gene. Nucleic Acids Research 1986; II: 4577–4589
   Google Scholar
• Triggs-Raine B.L., Doble B.W., Mulvey M.R., Sorby P.A., Loewen P.C. Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli. Journal of Bacteriology 1988; 170: 4415–4419
   PubMedGoogle Scholar
• von Ossowski I., Mulvey M.R., Leco P.A., Borys A., Loewen P.C. Nucleotide sequence of Escherichia coli katE, which encodes catalase HPI. Journal of Bacteriology 1991; 173: 514–520
   PubMed Web of Science ®Google Scholar