The role and regulation of catalase in respiratory tract opportunistic bacterial pathogens

Microbial Pathogenesis

Volumn 74, Issue 1, 2014, Pages 50-58

  Eason, Mia M ^a   Fan, Xin ^a  

^a WEST CHESTER UNIVERSITY   (United States)

Author keywords

Catalase; Reactive oxygen species; Respiratory opportunistic pathogen

Indexed keywords

CATALASE; MANGANESE; PEROXIDASE; REACTIVE OXYGEN METABOLITE;

BACTERIAL CLEARANCE; BACTERIAL COLONIZATION; BACTERIAL SURVIVAL; CATALASE GENE; CATALYSIS; DOWN REGULATION; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME REGULATION; GENE MUTATION; HAEMOPHILUS INFLUENZAE; HUMAN; LEGIONELLA PNEUMOPHILA; LEGIONNAIRE DISEASE; LUNG TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS; NEISSERIA MENINGITIDIS; NONHUMAN; OXIDATIVE STRESS; PATHOGENESIS; PRIORITY JOURNAL; RESPIRATORY TRACT INFECTION; REVIEW; STREPTOCOCCUS PNEUMONIAE; UPREGULATION; ADAPTATION; BACTERIUM; ENZYMOLOGY; GENE EXPRESSION REGULATION; ISOLATION AND PURIFICATION; METABOLISM; MICROBIAL VIABILITY; MICROBIOLOGY;

ADAPTATION, PHYSIOLOGICAL; BACTERIA; CATALASE; GENE EXPRESSION REGULATION, BACTERIAL; MICROBIAL VIABILITY; OXIDATIVE STRESS; REACTIVE OXYGEN SPECIES; RESPIRATORY TRACT INFECTIONS;

EID: 84930356971     PISSN: 08824010     EISSN: 10961208     Source Type: Journal    
DOI: 10.1016/j.micpath.2014.07.002     Document Type: Review

References (65)

1. Andisi V., Hinojosa C., de Jong A., Kuipers O., Orihuela C., Bijlsma J. Pneumococcal gene complex involved in resistance to extracellular oxidative stress. Infect Immun 2012, 80(3):1037-1049.
2. Anjum M., Stevanin T., Read R., Moir J. Nitric oxide metabolism in Neisseria meningitidis. JBacteriol 2002, 184(11):2987-2993.
3. Antelmann H., Helmann J. Thiol-based redox switches and gene regulation. Antioxid Redox Signal 2011, 14(6):1049-1063.
4. Bandyopadhyay P., Byrne B., Chan Y., Swanson M., Steinman H. Legionella pneumophila catalase-peroxidases are required for proper trafficking and growth in primary macrophages. Infect Immun 2003, 71:4526-4535.
5. Bishai W.R., Howard N.S., Winkelstein J.A., Smith H.O. Characterization and virulence analysis of catalase mutants of Haemophilus influenzae. Infect Immun 1994, 62(11):4855-4860.
6. Bishai W.R., Smith H.O., Barcak G.J. Aperoxide/ascorbate- inducible catalase from Haemophilus influenzae is homologous to the Escherichia coli katE gene Product. JBacteriol 1994, 176(10):2914-2921.
7. Bogaert D., de Groot R., Hermans P. Streptococcus pneumoniae colonization: the key to pneumococcal disease. Infect Dis 2004, 4:144-152.
8. Bortoni M., Terra V., Hinds J., Andrew P., Yesilkaya H. The pneumococcal response to oxidative stress includes a role for Rgg. Microbiology 2009, 155:4123-4134.
9. Centers for Disease Control (CDC) Legionella (legionnaires' disease and pontiac fever) 2012, Available from:. http://www.cdc.gov/legionella/about/causes-transmission.html.
10. Chelikani P., Fita I., Loewen P. Diversity of structures and properties among catalases. Cell Mol Life Sci 2004, 61:192-208.
11. Chelikani P., Ramana T., Radhakrishnan T. Catalase: a repertoire of unusual features. Indian J Clin Biochem 2005, 20(2):131-135.
12. 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.
13. Christman M.F., Storz G., Ames B.N. OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci U S A 1989, 86:3484-3488.
14. Cole S., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393:537-543.
15. Domínguez L., Sosa-Peinado A., Hansberg W. Catalase evolved to concentrate H2O2 at its active site. Arch Biochem Biophys 2010, 500:82-91.
16. Eady N., Jesmin N., Servos S., Cass A., Nagy J., Brown K. Probing the function of Mycobacterium tuberculosis catalase-peroxidase by site-directed mutagenesis. Dalt Trans 2005, 21:3495-3500.
17. Faraci F.M. Hydrogen peroxide: watery fuel for change in vascular biology. Arterioscler Thromb Vasc Biol 2006, 26:1931-1933.
18. Foxwell R., Kyd J.M., Cripps A.W. Nontypeable Haemophilus influenzae: pathogenesis and prevention. Microbiol Mol Biol Rev 1998, 62(2):294-308.
19. Freudenberg M.A., Galanos C. Bacterial lipopolysaccharides: structure, metabolism and mechanisms of action. Int Rev Immunol 1990, 6:207-221.
20. Hajaj B., Yesilkaya H., Benisty R., David M., Andrew P., Porat N. Thiol peroxidase is an important component of Streptococcus pneumoniae in oxygenated environments. Infect Immun 2012, 80(12):4333-4343.
21. Harrison A., Bakaletz L., Munson R. Haemophilus influenzae and oxidative stress. Front Cell Infect Microbiol 2012, 2(40). Available from:. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3417577/.
22. Harrison A., Ray W.C., Baker B.D., Armbruster D.W., Bakaletz L.O., Munson R.S. The OxyR regulon in nontypeable Haemophilus influenzae. JBacteriol 2007, 189(3):1004-1012.
23. Heck D., Shakarjian M., Kim D., Laskin J., Vetrano A. Mechanisms of oxidant generation by catalase. Ann N Y Acad Sci 2010, 1203:120-125.
24. Held P. An introduction to reactive oxygen species 2010, Available from:. http://www.biotek.com/resources/articles/reactive-oxygen-species.html.
25. Hoban D., Doern G., Fluit A., Roussel-Delvallez M., Jones R. Worldwide prevalence of antimicrobial resistance in Streptococcus pneumoniae, Haemophilus influenzae, and Moraxella catarrhalis in the SENTRY antimicrobial surveillance program, 1997-1999. Clin Infect Dis 2001, 32(Suppl.2):S81-S93.
26. Ieva R., Roncarati D., Metruccio M., Seib K., Scarlato V., Delany I. OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms. Mol Microbiol 2008, 70(5):1152-1165.
27. Imlay J. Pathways of oxidative damage. Annu Rev Microbiol 2003, 57:395-418.
28. Jagielski T., Bakuła Z., Roeske K., Kamiński M., Napiórkowska A., Augustynowicz-Kopeć E., et al. Detection of mutations associated with isoniazid resistance in multidrug-resistant Mycobacterium tuberculosis clinical isolates. JAntimicrob Chemother 2014, 69(9):2369-2375.
29. Ju J., Jiang S., Liu Q.Y., Ma S., Li Y., Li C.P. Analysis of mutational characteristics of the drug-resistant gene katG in multi-drug resistant Mycobacterium tuberculosis L-form among patients with pneumoconiosis complicated with tuberculosis. Mol Med Reports 2014, 9(5):2031-2035.
30. Kirkman H., Gaetani G. Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH. Proc Natl Acad Sci U S A 1984, 81:4343-4347.
31. Klotz M.G., Klassen G.R., Loewen P.C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol Biol Evol 1997, 14(9):951-958.
32. Knapp G., Tsai J., Hu J. The oligomerization of OxyR in Escherichia coli. Protein Sci 2008, 18:101-107.
33. Kullik I., Toledano M.B., Tartaglia L.A., Storz G. Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. JBacteriol 1995, 177(5):1275-1284.
34. Klotz M.G., Loewen P.C. The molecular evolution of catalatic hydroperoxidases: evidence for multiple lateral transfer of genes between prokaryota and from bacteria into eukaryota. Mol Biol Evol 2003, 20:1098-1112.
35. Loew O. Anew enzyme of general occurrence in organismis. Science 1900, 11:701-702.
36. Loewen P. Probing the structure of catalase HPII of Escherichia coli - a review. Gene 1996, 179:39-44.
37. Loots du T. An altered Mycobacterium tuberculosis metabolome induced by katG mutations resulting in isoniazid resistance. Antimicrobial Agents Chemother 2014, 58(4):2144-2149.
38. Male D. Immunology: an illustrated guide 2004, Mosby, Philadelphia, PA. 4th ed.
39. Manca C., Paul S., Barry C., Freedman V., Kaplan G. Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes invitro. Infect Immun 1999, 67(1):74-79.
40. Missouri Department of Health and Senior Services (MDHSS) Haemophilus influenzae invasive disease including meningitis. Section 4.0 diseases and conditions. Subsection: Haemophilus influenzae, Invasive 2005, P1-P22.
41. Murphy T., Parameswaran G. Moraxella catarrhalis, a human respiratory tract pathogen. Clin Pract 2009, 49:124-130.
42. Palmieri B., Sblendorio V. Oxidative stress detection: what for? part II. Eur Rev Med Pharmacol Sci 2011, 11:27-54.
43. Park S., You X., Imlay J. Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli. Proc Natl Acad Sci U S A 2005, 12(26):9317-9322.
44. Pauwels F., Veragauwen B., Van Beeumen J. Physiological characterization of Haemophilus influenzae Rd deficient in its glutathione- dependent peroxidase PGdx. JBiol Chem 2004, 279(3):12163-12170.
45. Pericone C., Park S., Imlay J., Weiser J. Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction. JBacteriol 2003, 185(23):6815-6825.
46. Prescott L., Harley J., Klein D. Microbiology 2005, McGraw Hill, Boston, MA. 6th ed.
47. Rodriguez C., Mayo J., Sainz R., Antoín I., Herrera F., Martín V., et al. Regulation of antioxidant enzymes: a significant role for melatonin. JPineal Res 2004, 36:1-9.
48. Sak B., Eisenstark A., Touati D. Exonuclease III and the catalase hydroperoxidase II Escherichia coli are both regulated by the katF gene product. Proc Natl Acad Sci U S A 1989, 86:3271-3275.
49. Song X.M., Janson H. Differences in genetic and transcriptional organization of the glpTQ operons between Haemophilus influenzae type b and nontypeable strains. JBacteriol 2003, 185(24):7285-7290.
50. Spooner R., Yilmaz O. The role of reactive-oxygen-species in microbial persistence and inflammation. Int J Mol Sci 2011, 12:334-352.
51. Storz G., Tartaglia L.A., Ames B.N. OxyR, a transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 1990, 248:189-194.
52. Suarez J., Ranguelova K., Schelvis J., Magliozzo R. Antibiotic resistance in Mycobacterium tuberculosis: peroxidase intermediate bypass causes poor isoniazid activation by the S315G mutant of M.tuberculosis catalase-peroxidase (KatG). JBiol Chem 2009, 284(24):16146-16155.
53. Sumner J., Gralén N. The molecular weight of crystalline catalase. JBiol Chem 1938, 125:33-36.
54. Switala J., Triggs-Raine B., Loewen P. Homology among bacterial catalase genes. Can J Microbiol 1990, 36:728-731.
55. Vergauwen B., Herbert M., Van Beeumen J.J. Hydrogen peroxide scavenging is not a virulence determinant in the pathogenesis of Haemophilus influenzae type b strain Eagan. BMC Microbiol 2006, 6(3).
56. Vergauwen B., Pauwels F., Van Beeumen J.J. Gluatathione and catalase provide overlapping defenses for protection against respiration-generated hydrogen peroxide in Haemophilus influenzae. JBacteriol 2003, 185(18):5555-5562.
57. Vlasits J., Jakopitsch C., Bernroitner M., Zamocky M., Furtmüller P., Obinger C. Mechanisms of catalase activity of heme peroxidases. Arch Biochem Biophys 2010, 500:74-81.
58. Wald E.R., Pang D., Milmoe G.J., Schramm V.L. Sinusitis and its complications in the pediatric patient. Pediatr Clin North Am 1981, 28:777-796.
59. Whitby P., Morton D., VanWagoner T., Seale T., Cole B., Huda M., et al. Haemophilus influenzae OxyR: characterization of its regulation, regulon, and role in fitness. Public Libr Sci ONE 2012, 7(11). Available from:. http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050588.
60. World Health Organization (WHO) Acute respiratory infections 2012, Available from:. http://www.who.int/vaccine_research/diseases/ari/en/.
61. World Health Organization (WHO) Immunization, vaccines, and biologicals 2012, Available from:. http://www.who.int/immunization/topics/meningitis/en/.
62. World Health Organization (WHO) Tuberculosis 2012, Available from:. http://www.who.int/mediacentre/factsheets/fs104/en/index.html.
63. Yesilkaya H., Kadioglu A., Gingles N., Alexander J., Mitchell T., Andrew P. Role of manganese-containing superoxide dismutase in oxidative stress and virulence of Streptococcus pneumoniae. Infect Immun 2000, 68(5):2819-2826.
64. Zamocky M., Koller F. Understanding the structure and function of catalases: clues from molecular evolution and invitro mutagenesis. Prog Biophys Mol Biol 1999, 72:19-66.
65. Zamocky M., Furtmüller P., Obinger C. Evolution of catalases from bacteria to humans. Antioxid Redox Signal 2008, 10(9):1527-1548.