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Original

Isolation and characterization of a catalase-peroxidase gene from the pathogenic fungus, Penicillium marneffei

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Pages 403-411 | Received 09 Jan 2004, Published online: 09 Jul 2009

References

  • Supparatpinyo K, Khamwan C, Baosoung V, et al. Disseminated Penicillium marneffei infection in Southeast Asia. Lancet 1994; 344: 110–113
  • Vanittanakom N, Sirisanthana T. Penicillium marneffei infection in patients infected with human immunodeficiency virus. Curr Top Med Mycol 1997; 8: 35–42
  • Cooper CR, Jr. From bamboo rats to humans: the odyssey of Penicillium marneffei. ASM News 1998; 64: 390–397
  • Duong TA. Infection due to Penicillium marneffei, an emerging pathogen: review of 155 reported cases. Clin Infect Dis 1996; 23: 125–130
  • Lo Y, Tintelnot K, Lippert U, Hoppe T. Disseminated Penicillium marneffei infection in an African AIDS patient. Trans R Soc Trop Med Hyg 2000; 94: 187
  • Mohri S, Yoshikawa K, Sagara H, Nakajima H. A case of Penicillium marneffei infection in an AIDS patient: the first case in Japan. Nippon Ishinkin Gakkai Zasshi 2000; 41: 23–26
  • Singh PN, Ranjana K, Singh YI, et al. Indigenous disseminated Penicillium marneffei infection in the state of Manipur, India: report of four autochthonous cases. J Clin Microbiol 1999; 37: 2699–2702
  • Chan YF, Chow TC. Ultrastructural observations on Penicillium marneffei in natural human infection. Ultrastruct Pathol 1990; 14: 439–452
  • Cooper CR, Jr, McGinnis MR. Pathology of Penicillium marneffei. An emerging acquired immunodeficiency syndrome-related pathogen. Arch Pathol Lab Med 1997; 121: 798–804
  • Kudeken N, Kawakami K, Saito A. Role of superoxide anion in the fungicidal activity of murine peritoneal macrophages against Penicillium marneffei. Microbiology 1999; 43: 323–330
  • Roilides E, Lyman CA, Sein T, et al. Macrophage colony-stimulating factor enhances phagocytosis and oxidative burst of mononuclear phagocytes against Penicillium marneffei conidia. FEMS Immnunol Med Microbiol 2003; 36: 19–26
  • Welinder KG. Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim Biophys Acta 1991; 1080: 215–220
  • Nadler V, Goldberg I, Hochman A. Comparative study of bacterial catalases. Biochim Biophys Acta 1986; 882: 234–241
  • Elstner EF. Oxygen activation and oxygen toxicity. Annu Rev Plant Physiol 1982; 33: 73–96
  • Long S, Salin ML. Archaeal promoter-directed expression of the Halobacterium salinarum catalase-peroxidase gene. Extremophiles 2000; 4: 351–356
  • Carpena X, Loprosert S, Mongkolsuk S, et al. Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7 A° resolution. J Mol Biol 2003; 327: 475–489
  • Yamada Y, Fujiwara T, Sato T, et al. The 2.0 A° crystal structure of catalase-peroxidase from Haloarcula marismortui. Nat Struct Biol 2002; 9: 691–695
  • Sambrook J, Russell DW. Molecular Cloning: A Laboratory Manual3rd edn. Cold Spring Harbor Laboratory Press, New York 2001
  • Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74: 5463–5467
  • Cooper CR, Jr, Breslin BJ, Dixon DM, Salkin IF. DNA typing of isolates associated with the 1988 sporotrichosis epidemic. J Clin Microbiol 1992; 30: 1631–1635
  • Vanittanakom N, Cooper CR, Jr, Chariyalertsak S, et al. Restriction endonuclease analysis of Penicillium marneffei. J Clin Microbiol 1996; 34: 1834–1836
  • Wayne LG, Diaz GA. A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Anal Biochem 1986; 157: 89–92
  • Altschul SF, Madden TL, Schaffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997; 25: 3389–3402
  • Peraza L, Hansberg W. Neurospora crassa catalases, singlet oxygen and cell differentiation. Biol Chem 2002; 383: 569–575
  • Scherer M, Wei H, Liese R, Fischer R. Aspergillus nidulans catalase-peroxidase gene (cpeA) is transcriptionally induced during sexual development through the transcription factor StuA. Eukaryot Cell 2002; 1: 725–735
  • Paris S, Wysong D, Debeaupuis JP, et al. Catalases of Aspergillus fumigatus. Infect Immun 2003; 71: 3551–3562
  • Navarro RE, Stringer MA, Hansberg W, Timberlake WE, Aguirre J. CatA, a new Aspergillus nidulans gene encoding a developmentally regulated catalase. Curr Genet 1996; 29: 352–359
  • Herruer MH, Mager WH, Rave HA, et al. Mild temperature shock affects transcription of yeast ribosomal protein genes as well as the stability of their mRNAs. Nucleic Acids Res 1988; 16: 7917–7929
  • Fraaije MW, Roubroeks HP, Hagen WR, van Berkel WJH. Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum. Eur J Biochem 1996; 235: 192–198
  • Jackett PS, Aber VR, Lowrie DB. Virulence and resistance to superoxide, low pH and hydrogen peroxide among strains of Mycobacterium tuberculosis. J Gen Microbiol 1978; 104: 37–45
  • Manca C, Paul S, Barry CE, III, et al. Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro. Infect Immun 1999; 67: 74–79
  • Ng VH, Cox JS, Sousa AO, et al. Role of KatG catalase-peroxidase in mycobacterial pathogenesis: countering the phagocyte oxidative burst. Mol Microbiol 2004; 52: 1291–1302
  • Wilson TM, de Lisle GW, Collins DM. Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Mol Microbiol 1995; 15: 1009–1015
  • Brunder W, Schmidt H, Karch H. KatP, a novel catalase-peroxidase encoded by the large plasmid of enterohaemorrhagic Escherichia coli O157:H7. Microbiology 1996; 142: 3305–3315
  • Bandyopadhyay P, Steinman HM. Legionella pneumophila catalase-peroxidases: cloning of the katB gene and studies of KatB function. J Bacteriol 1998; 180: 5369–5374
  • Garcia E, Nedialkov YA, Elliott J, et al. Molecular characterization of KatY (antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis. J Bacteriol 1999; 181: 3114–3122
  • Lefebre M, Valvano M. In vitro resistance of Burkholderia cepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production. Microbiology 2001; 147: 97–109
  • Loprasert S, Whangsuk W, Sallabhan R, Mongkolsuk S. Regulation of the KatG-dpsA operon and the importance of KatG in survival of Burkholderia pseudomallei exposed to oxidative stress. FEBS Lett 2003; 542: 17–21
  • Brown SM, Howell ML, Vasil ML, et al. Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. J Bacteriol 1995; 177: 6536–6544
  • Taramelli D, Brambilla S, Sala G, et al. Effects of iron on extracellular and intracellular growth of Penicillium marneffei. Infect Immun 2000; 68: 1724–1726

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