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Volumn 188, Issue 11, 2006, Pages 3837-3848

The superoxide dismutases of Bacillus anthracis do not cooperatively protect against endogenous superoxide stress

Author keywords

[No Author keywords available]

Indexed keywords

SUPEROXIDE; SUPEROXIDE DISMUTASE;

EID: 33744764304     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00239-06     Document Type: Article
Times cited : (46)

References (59)
  • 2
    • 0348049821 scopus 로고    scopus 로고
    • Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis
    • Battistoni, A. 2003. Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis. Biochem. Soc. Trans. 31:1326-1329.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1326-1329
    • Battistoni, A.1
  • 5
    • 0037673252 scopus 로고    scopus 로고
    • SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis
    • Braunstein, M., B. J. Espinosa, J. Chan, J. T. Belisle, and W. R. Jacobs, Jr. 2003. SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol. Microbiol. 48:453-464.
    • (2003) Mol. Microbiol. , vol.48 , pp. 453-464
    • Braunstein, M.1    Espinosa, B.J.2    Chan, J.3    Belisle, J.T.4    Jacobs Jr., W.R.5
  • 6
    • 10044234054 scopus 로고    scopus 로고
    • Catalase and superoxide dismutase: Distribution, properties, and physiological role in cells of strict anaerobes
    • Brioukhanov, A. L., and A. I. Netrusov. 2004. Catalase and superoxide dismutase: distribution, properties, and physiological role in cells of strict anaerobes. Biochemistry 69:949-962.
    • (2004) Biochemistry , vol.69 , pp. 949-962
    • Brioukhanov, A.L.1    Netrusov, A.I.2
  • 7
    • 0030690926 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents
    • Casillas-Martinez, L., and P. Setlow. 1997. Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents. J. Bacteriol. 179:7420-7425.
    • (1997) J. Bacteriol. , vol.179 , pp. 7420-7425
    • Casillas-Martinez, L.1    Setlow, P.2
  • 8
    • 0942279513 scopus 로고    scopus 로고
    • Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence
    • Cendrowski, S., W. MacArthur, and P. Hanna. 2004. Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence. Mol. Microbiol. 51:407-417.
    • (2004) Mol. Microbiol. , vol.51 , pp. 407-417
    • Cendrowski, S.1    MacArthur, W.2    Hanna, P.3
  • 11
    • 13244255402 scopus 로고    scopus 로고
    • Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax
    • Drysdale, M., S. Heninger, J. Hutt, Y. Chen, C. R. Lyons, and T. M. Koehler. 2005. Capsule synthesis by Bacillus anthracis is required for dissemination in murine inhalation anthrax. EMBO J. 24:221-227.
    • (2005) EMBO J. , vol.24 , pp. 221-227
    • Drysdale, M.1    Heninger, S.2    Hutt, J.3    Chen, Y.4    Lyons, C.R.5    Koehler, T.M.6
  • 17
    • 28044450837 scopus 로고    scopus 로고
    • Characterization of Bacillus anthracis germinant receptors in vitro
    • Fisher, N., and P. Hanna. 2005. Characterization of Bacillus anthracis germinant receptors in vitro. J. Bacteriol. 187:8055-8062.
    • (2005) J. Bacteriol. , vol.187 , pp. 8055-8062
    • Fisher, N.1    Hanna, P.2
  • 18
    • 0025138704 scopus 로고
    • Contribution of superoxide dismutase and catalase activities to Shigella flexneri pathogenesis
    • Franzon, V. L., J. Arondel, and P. J. Sansonetti. 1990. Contribution of superoxide dismutase and catalase activities to Shigella flexneri pathogenesis. Infect. Immun. 58:529-535.
    • (1990) Infect. Immun. , vol.58 , pp. 529-535
    • Franzon, V.L.1    Arondel, J.2    Sansonetti, P.J.3
  • 19
    • 24344479210 scopus 로고    scopus 로고
    • Manganese superoxide dismutase in pathogenic fungi: An issue with pathophysiological and phylogenetic involvements
    • Frealle, E., C. Noel, E. Viscogliosi, D. Camus, E. Dei-Cas, and L. Delhaes. 2005. Manganese superoxide dismutase in pathogenic fungi: an issue with pathophysiological and phylogenetic involvements. FEMS Immunol. Med. Microbiol. 45:411-422.
    • (2005) FEMS Immunol. Med. Microbiol. , vol.45 , pp. 411-422
    • Frealle, E.1    Noel, C.2    Viscogliosi, E.3    Camus, D.4    Dei-Cas, E.5    Delhaes, L.6
  • 21
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guerout-Fleury, A. M., K. Shazand, N. Frandsen, and P. Stragier 1995. Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167:335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guerout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 22
    • 25444434412 scopus 로고    scopus 로고
    • NO-mediated cytoprotection: Instant adaptation to oxidative stress in bacteria
    • Gusarov, I., and E. Nudler. 2005. NO-mediated cytoprotection: instant adaptation to oxidative stress in bacteria. Proc. Natl. Acad. Sci. USA 102: 13855-13860.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13855-13860
    • Gusarov, I.1    Nudler, E.2
  • 23
    • 0031955996 scopus 로고    scopus 로고
    • Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis
    • Henriques, A. O., L. R. Melsen, and C. P. Moran, Jr. 1998. Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis. J. Bacteriol. 180:2285-2291.
    • (1998) J. Bacteriol. , vol.180 , pp. 2285-2291
    • Henriques, A.O.1    Melsen, L.R.2    Moran Jr., C.P.3
  • 25
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay, J. 2006. Iron-sulphur clusters and the problem with oxygen. Mol. Microbiol. 59:1073-1082.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1073-1082
    • Imlay, J.1
  • 26
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 27
    • 0032464905 scopus 로고    scopus 로고
    • Molecular cloning and nucleotide sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis
    • Inaoka, T., Y. Matsumura, and T. Tsuchido. 1998. Molecular cloning and nucleotide sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis. J. Bacteriol. 180:3697-3703.
    • (1998) J. Bacteriol. , vol.180 , pp. 3697-3703
    • Inaoka, T.1    Matsumura, Y.2    Tsuchido, T.3
  • 28
    • 0031888044 scopus 로고    scopus 로고
    • An analysis of structural similarity in the iron and manganese superoxide dismutases based on known structures and sequences
    • Jackson, S. M., and J. B. Cooper. 1998. An analysis of structural similarity in the iron and manganese superoxide dismutases based on known structures and sequences. Biometals 11:159-173.
    • (1998) Biometals , vol.11 , pp. 159-173
    • Jackson, S.M.1    Cooper, J.B.2
  • 29
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer, K., and J. A. Imlay. 1996. Superoxide accelerates DNA damage by elevating free-iron levels. Proc. Natl. Acad. Sci. USA 93:13635-13640.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 30
    • 0028804901 scopus 로고
    • Bacterial [Cu,Zn]-superoxide dismutase: Phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!
    • Kroll, J. S., P. R. Langford, K. E. Wilks, and A. D. Keil. 1995. Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all! Microbiology 141(Pt. 9):2271-2279.
    • (1995) Microbiology , vol.141 , Issue.PART 9 , pp. 2271-2279
    • Kroll, J.S.1    Langford, P.R.2    Wilks, K.E.3    Keil, A.D.4
  • 32
    • 0035907349 scopus 로고    scopus 로고
    • Oxidative protein cross-linking reactions involving L-tyrosine in transforming growth factor-β1-stimulated fibroblasts
    • Larios, J. M., R. Budhiraja, B. L. Fanburg, and V. J. Thannickal. 2001. Oxidative protein cross-linking reactions involving L-tyrosine in transforming growth factor-β1-stimulated fibroblasts. J. Biol. Chem. 276:17437-17441.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17437-17441
    • Larios, J.M.1    Budhiraja, R.2    Fanburg, B.L.3    Thannickal, V.J.4
  • 34
    • 0033829129 scopus 로고    scopus 로고
    • Expression and role of superoxide dismutases (SOD) in pathogenic bacteria
    • Lynch, M., and H. Kuramitsu. 2000. Expression and role of superoxide dismutases (SOD) in pathogenic bacteria. Microbes Infect. 2:1245-1255.
    • (2000) Microbes Infect. , vol.2 , pp. 1245-1255
    • Lynch, M.1    Kuramitsu, H.2
  • 36
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M., and I. Fridovich. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 39
    • 0023945399 scopus 로고
    • Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures
    • Parker, M. W., and C. C. Blake. 1988. Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett. 229:377-382.
    • (1988) FEBS Lett. , vol.229 , pp. 377-382
    • Parker, M.W.1    Blake, C.C.2
  • 41
    • 0034917354 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst
    • Piddington, D. L., F. C. Fang, T. Laessig, A. M. Cooper, I. M. Orme, and N. A. Buchmeier. 2001. Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Infect. Immun. 69:4980-4987.
    • (2001) Infect. Immun. , vol.69 , pp. 4980-4987
    • Piddington, D.L.1    Fang, F.C.2    Laessig, T.3    Cooper, A.M.4    Orme, I.M.5    Buchmeier, N.A.6
  • 43
    • 0029151295 scopus 로고
    • The Bacillus subtilis dacB gene, encoding penicillin-binding protein 5*, is part of a three-gene operon required for proper spore cortex synthesis and spore core dehydration
    • Popham, D. L., B. Illades-Aguiar, and P. Setlow. 1995. The Bacillus subtilis dacB gene, encoding penicillin-binding protein 5*, is part of a three-gene operon required for proper spore cortex synthesis and spore core dehydration. J. Bacteriol. 177:4721-4729.
    • (1995) J. Bacteriol. , vol.177 , pp. 4721-4729
    • Popham, D.L.1    Illades-Aguiar, B.2    Setlow, P.3
  • 44
    • 0034924910 scopus 로고    scopus 로고
    • Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae
    • Poyart, C., E. Pellegrini, O. Gaillot, C. Boumaila, M. Baptista, and P. Trieu-Cuot. 2001. Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae. Infect. Immun. 69:5098-5106.
    • (2001) Infect. Immun. , vol.69 , pp. 5098-5106
    • Poyart, C.1    Pellegrini, E.2    Gaillot, O.3    Boumaila, C.4    Baptista, M.5    Trieu-Cuot, P.6
  • 45
    • 0025345676 scopus 로고
    • Transformation of vegetative cells of Bacillus anthracis with plasmid DNA
    • Quinn, C. P., and B. N. Dancer. 1990. Transformation of vegetative cells of Bacillus anthracis with plasmid DNA. J. Gen. Microbiol. 136:1211-1215.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1211-1215
    • Quinn, C.P.1    Dancer, B.N.2
  • 48
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent endpoints
    • Reed, L. J., and H. Muench. 1938. A simple method of estimating fifty per cent endpoints. Am. J. Hyg. 27:493-497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 50
    • 0042028316 scopus 로고    scopus 로고
    • Reassessment of the microbicidal activity of reactive oxygen species and hypochlorous acid with reference to the phagocytic vacuole of the neutrophil granulocyte
    • Reeves, E. P., M. Nagl, J. Godovac-Zimmermann, and A. W. Segal. 2003. Reassessment of the microbicidal activity of reactive oxygen species and hypochlorous acid with reference to the phagocytic vacuole of the neutrophil granulocyte. J. Med. Microbiol. 52:643-651.
    • (2003) J. Med. Microbiol. , vol.52 , pp. 643-651
    • Reeves, E.P.1    Nagl, M.2    Godovac-Zimmermann, J.3    Segal, A.W.4
  • 51
    • 1842450833 scopus 로고    scopus 로고
    • Time-lapse confocal imaging of development of Bacillus anthracis in macrophages
    • Ruthel, G., W. J. Ribot, S. Bavari, and T. A. Hoover. 2004. Time-lapse confocal imaging of development of Bacillus anthracis in macrophages. J. Infect. Dis. 189:1313-1316.
    • (2004) J. Infect. Dis. , vol.189 , pp. 1313-1316
    • Ruthel, G.1    Ribot, W.J.2    Bavari, S.3    Hoover, T.A.4
  • 52
    • 0026730439 scopus 로고
    • Use of a new integrational vector to investigate compartment-specific expression of the Bacillus subtilis spoIIM gene
    • Smith, K., and P. Youngman. 1992. Use of a new integrational vector to investigate compartment-specific expression of the Bacillus subtilis spoIIM gene. Biochimie 74:705-711.
    • (1992) Biochimie , vol.74 , pp. 705-711
    • Smith, K.1    Youngman, P.2
  • 53
    • 4043057281 scopus 로고    scopus 로고
    • Unique features of the sodC-encoded Superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site
    • Spagnolo, L., I. Toro, M. D'Orazio, P. O'Neill, J. Z. Pedersen, O. Carugo, G. Rotilio, A. Battistoni, and K. Djinovic-Carugo. 2004. Unique features of the sodC-encoded Superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site. J. Biol. Chem. 279:33447-33455.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33447-33455
    • Spagnolo, L.1    Toro, I.2    D'Orazio, M.3    O'Neill, P.4    Pedersen, J.Z.5    Carugo, O.6    Rotilio, G.7    Battistoni, A.8    Djinovic-Carugo, K.9
  • 56
    • 0030457111 scopus 로고    scopus 로고
    • Molecular genetics of sporulation in Bacillus subtilis
    • Stragier, P., and R. Losick. 1996. Molecular genetics of sporulation in Bacillus subtilis. Annu. Rev. Genet. 30:297-341.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 297-341
    • Stragier, P.1    Losick, R.2
  • 58
    • 0037214021 scopus 로고    scopus 로고
    • The paradox of reactive oxygen species: Injury, signaling, or both?
    • Thannickal, V. J. 2003. The paradox of reactive oxygen species: injury, signaling, or both? Am. J. Physiol. Lung Cell Mol. Physiol. 284:L24-L25.
    • (2003) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.284
    • Thannickal, V.J.1
  • 59
    • 0028927433 scopus 로고
    • Role of Salmonella typhimurium Mn-superoxide dismutase (SodA) in protection against early killing by J774 macrophages
    • Tsolis, R. M., A. J. Baumler, and F. Heffron. 1995. Role of Salmonella typhimurium Mn-superoxide dismutase (SodA) in protection against early killing by J774 macrophages. Infect. Immun. 63:1739-1744.
    • (1995) Infect. Immun. , vol.63 , pp. 1739-1744
    • Tsolis, R.M.1    Baumler, A.J.2    Heffron, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.