메뉴 건너뛰기




Volumn 83, Issue 6, 2015, Pages 2255-2263

Roles of reactive oxygen species-degrading enzymes of Francisella tularensis SCHU S4

Author keywords

[No Author keywords available]

Indexed keywords

ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT C; BACTERIAL ENZYME; CATALASE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; LIVE VACCINE; PARAQUAT; PEROXIDASE; PEROXYNITRITE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; HERBICIDE;

EID: 84929492791     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.02488-14     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 34748912454 scopus 로고    scopus 로고
    • Tularemia: history, epidemiology, pathogen physiology, and clinical manifestations
    • Sjöstedt A. 2007. Tularemia: history, epidemiology, pathogen physiology, and clinical manifestations. Ann N Y Acad Sci 1105:1-29. http://dx.doi.org/10.1196/annals.1409.009.
    • (2007) Ann N Y Acad Sci , vol.1105 , pp. 1-29
    • Sjöstedt, A.1
  • 3
    • 3042583015 scopus 로고    scopus 로고
    • Vaccines against Francisella tularensis-past, present and future
    • Conlan JW. 2004. Vaccines against Francisella tularensis-past, present and future. Expert Rev Vaccines 3:307-314. http://dx.doi.org/10.1586/14760584.3.3.307.
    • (2004) Expert Rev Vaccines , vol.3 , pp. 307-314
    • Conlan, J.W.1
  • 5
    • 0026520203 scopus 로고
    • Activation of macrophages for destruction of Francisella tularensis: identification of cytokines, effector cells, and effector molecules
    • Fortier AH, Polsinelli T, Green SJ, Nacy CA. 1992. Activation of macrophages for destruction of Francisella tularensis: identification of cytokines, effector cells, and effector molecules. Infect Immun 60:817-825.
    • (1992) Infect Immun , vol.60 , pp. 817-825
    • Fortier, A.H.1    Polsinelli, T.2    Green, S.J.3    Nacy, C.A.4
  • 6
    • 18044362697 scopus 로고    scopus 로고
    • The contribution of reactive nitrogen and oxygen species to the killing of Francisella tularensis LVS by murine macrophages
    • Lindgren H, Stenman L, Tarnvik A, Sjöstedt A. 2005. The contribution of reactive nitrogen and oxygen species to the killing of Francisella tularensis LVS by murine macrophages. Microbes Infect 7:467-475. http://dx.doi.org/10.1016/j.micinf.2004.11.020.
    • (2005) Microbes Infect , vol.7 , pp. 467-475
    • Lindgren, H.1    Stenman, L.2    Tarnvik, A.3    Sjöstedt, A.4
  • 7
    • 0028341477 scopus 로고
    • Nitric oxide-independent killing of Francisella tularensis by IFN-gamma-stimulated murine alveolar macrophages
    • Polsinelli T, Meltzer MS, Fortier AH. 1994. Nitric oxide-independent killing of Francisella tularensis by IFN-gamma-stimulated murine alveolar macrophages. J Immunol 153:1238-1245.
    • (1994) J Immunol , vol.153 , pp. 1238-1245
    • Polsinelli, T.1    Meltzer, M.S.2    Fortier, A.H.3
  • 8
    • 76449110473 scopus 로고    scopus 로고
    • Restricted cytosolic growth of Francisella tularensis subsp. tularensis by IFN-gamma activation of macrophages
    • Edwards JA, Rockx-Brouwer D, Nair V, Celli J. 2010. Restricted cytosolic growth of Francisella tularensis subsp. tularensis by IFN-gamma activation of macrophages Microbiology 156:327-339. http://dx.doi.org/10.1099/mic.0.031716-0.
    • (2010) Microbiology , vol.156 , pp. 327-339
    • Edwards, J.A.1    Rockx-Brouwer, D.2    Nair, V.3    Celli, J.4
  • 9
    • 70350449301 scopus 로고    scopus 로고
    • Identification of Francisella tularensis live vaccine strain CuZn superoxide dismutase as critical for resistance to extracellularly generated reactive oxygen species
    • Melillo AA, Mahawar M, Sellati TJ, Malik M, Metzger DW, Melendez JA, Bakshi CS. 2009. Identification of Francisella tularensis live vaccine strain CuZn superoxide dismutase as critical for resistance to extracellularly generated reactive oxygen species. J Bacteriol 191:6447-6456. http://dx.doi.org/10.1128/JB.00534-09.
    • (2009) J Bacteriol , vol.191 , pp. 6447-6456
    • Melillo, A.A.1    Mahawar, M.2    Sellati, T.J.3    Malik, M.4    Metzger, D.W.5    Melendez, J.A.6    Bakshi, C.S.7
  • 10
    • 70349420956 scopus 로고    scopus 로고
    • The 58-kilodalton major virulence factor of Francisella tularensis is required for efficient utilization of iron
    • Lindgren H, Honn M, Golovlev I, Kadzhaev K, Conlan W, Sjöstedt A. 2009. The 58-kilodalton major virulence factor of Francisella tularensis is required for efficient utilization of iron. Infect Immun 77:4429-4436. http://dx.doi.org/10.1128/IAI.00702-09.
    • (2009) Infect Immun , vol.77 , pp. 4429-4436
    • Lindgren, H.1    Honn, M.2    Golovlev, I.3    Kadzhaev, K.4    Conlan, W.5    Sjöstedt, A.6
  • 12
    • 80052479082 scopus 로고    scopus 로고
    • Macrophage replication screen identifies a novel Francisella hydroperoxide resistance protein involved in virulence
    • Llewellyn AC, Jones CL, Napier BA, Bina JE, Weiss DS. 2011. Macrophage replication screen identifies a novel Francisella hydroperoxide resistance protein involved in virulence. PLoS One 6:e24201. http://dx.doi.org/10.1371/journal.pone.0024201.
    • (2011) PLoS One , vol.6
    • Llewellyn, A.C.1    Jones, C.L.2    Napier, B.A.3    Bina, J.E.4    Weiss, D.S.5
  • 14
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R, Griffin P, Nathan C. 2000. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407:211-215. http://dx.doi.org/10.1038/35025109.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 15
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione-and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • Carmel-Harel O, Storz G. 2000. Roles of the glutathione-and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu Rev Microbiol 54: 439-461. http://dx.doi.org/10.1146/annurev.micro.54.1.439.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 16
    • 33645865262 scopus 로고    scopus 로고
    • Probing the structure and bifunctionality of catalase-peroxidase (KatG)
    • Smulevich G, Jakopitsch C, Droghetti E, Obinger C. 2006. Probing the structure and bifunctionality of catalase-peroxidase (KatG). J Inorg Biochem 100:568-585. http://dx.doi.org/10.1016/j.jinorgbio.2006.01.033.
    • (2006) J Inorg Biochem , vol.100 , pp. 568-585
    • Smulevich, G.1    Jakopitsch, C.2    Droghetti, E.3    Obinger, C.4
  • 17
    • 33847716729 scopus 로고    scopus 로고
    • Resistance of Francisella tularensis strains against reactive nitrogen and oxygen species with special reference to the role of KatG
    • Lindgren H, Shen H, Zingmark C, Golovliov I, Conlan W, Sjöstedt A. 2007. Resistance of Francisella tularensis strains against reactive nitrogen and oxygen species with special reference to the role of KatG. Infect Immun 75:1303-1309. http://dx.doi.org/10.1128/IAI.01717-06.
    • (2007) Infect Immun , vol.75 , pp. 1303-1309
    • Lindgren, H.1    Shen, H.2    Zingmark, C.3    Golovliov, I.4    Conlan, W.5    Sjöstedt, A.6
  • 19
    • 67651202552 scopus 로고    scopus 로고
    • Reintroduction of two deleted virulence loci restores full virulence to the live vaccine strain of Francisella tularensis
    • Salomonsson E, Kuoppa K, Forslund AL, Zingmark C, Golovliov I, Sjöstedt A, Noppa L, Forsberg A. 2009. Reintroduction of two deleted virulence loci restores full virulence to the live vaccine strain of Francisella tularensis. Infect Immun 77:3424-3431. http://dx.doi.org/10.1128/IAI.00196-09.
    • (2009) Infect Immun , vol.77 , pp. 3424-3431
    • Salomonsson, E.1    Kuoppa, K.2    Forslund, A.L.3    Zingmark, C.4    Golovliov, I.5    Sjöstedt, A.6    Noppa, L.7    Forsberg, A.8
  • 20
    • 0037721461 scopus 로고    scopus 로고
    • A method for allelic replacement in Francisella tularensis
    • Golovliov I, Sjöstedt A, Mokrievich A, Pavlov V. 2003. A method for allelic replacement in Francisella tularensis. FEMS Microbiol Lett 222:273-280. http://dx.doi.org/10.1016/S0378-1097(03)00313-6.
    • (2003) FEMS Microbiol Lett , vol.222 , pp. 273-280
    • Golovliov, I.1    Sjöstedt, A.2    Mokrievich, A.3    Pavlov, V.4
  • 21
    • 0028287442 scopus 로고
    • Deferration of laboratory media and assays for ferric and ferrous ions
    • Cox CD. 1994. Deferration of laboratory media and assays for ferric and ferrous ions. Methods Enzymol 235:315-329. http://dx.doi.org/10.1016/0076-6879(94)35150-3.
    • (1994) Methods Enzymol , vol.235 , pp. 315-329
    • Cox, C.D.1
  • 22
    • 0000695637 scopus 로고
    • Evaluation of live tularemia vaccine prepared in a chemically defined medium
    • Chamberlain RE. 1965. Evaluation of live tularemia vaccine prepared in a chemically defined medium. Appl Microbiol 13:232-235.
    • (1965) Appl Microbiol , vol.13 , pp. 232-235
    • Chamberlain, R.E.1
  • 23
    • 67650886051 scopus 로고    scopus 로고
    • Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact
    • Letoffe S, Heuck G, Delepelaire P, Lange N, Wandersman C. 2009. Bacteria capture iron from heme by keeping tetrapyrrol skeleton intact. Proc Natl Acad Sci USA 106:11719-11724. http://dx.doi.org/10.1073/pnas.0903842106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11719-11724
    • Letoffe, S.1    Heuck, G.2    Delepelaire, P.3    Lange, N.4    Wandersman, C.5
  • 25
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • Sugano Y. 2009. DyP-type peroxidases comprise a novel heme peroxidase family. Cell Mol Life Sci 66:1387-1403. http://dx.doi.org/10.1007/s00018-008-8651-8.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1387-1403
    • Sugano, Y.1
  • 26
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical
    • Hassan HM, Fridovich I. 1979. Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J Biol Chem 254:10846-10852.
    • (1979) J Biol Chem , vol.254 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 27
    • 36849030710 scopus 로고    scopus 로고
    • Methods of in vitro macrophage maturation confer variable inflammatory responses in association with altered expression of cell surface dectin-1
    • Gersuk GM, Razai LW, Marr KA. 2008. Methods of in vitro macrophage maturation confer variable inflammatory responses in association with altered expression of cell surface dectin-1. J Immunol Methods 329:157-166. http://dx.doi.org/10.1016/j.jim.2007.10.003.
    • (2008) J Immunol Methods , vol.329 , pp. 157-166
    • Gersuk, G.M.1    Razai, L.W.2    Marr, K.A.3
  • 28
    • 6344269866 scopus 로고    scopus 로고
    • Factors affecting the escape of Francisella tularensis from the phagolysosome
    • Lindgren H, Golovliov I, Baranov V, Ernst RK, Telepnev M, Sjöstedt A. 2004. Factors affecting the escape of Francisella tularensis from the phagolysosome. J Med Microbiol 53:953-958. http://dx.doi.org/10.1099/jmm.0.45685-0.
    • (2004) J Med Microbiol , vol.53 , pp. 953-958
    • Lindgren, H.1    Golovliov, I.2    Baranov, V.3    Ernst, R.K.4    Telepnev, M.5    Sjöstedt, A.6
  • 29
    • 65549117835 scopus 로고    scopus 로고
    • Identification of genes contributing to the virulence of Francisella tularensis SCHU S4 in a mouse intradermal infection model
    • Kadzhaev K, Zingmark C, Golovliov I, Bolanowski M, Shen H, Conlan W, Sjöstedt A. 2009. Identification of genes contributing to the virulence of Francisella tularensis SCHU S4 in a mouse intradermal infection model. PLoS One 4:e5463. http://dx.doi.org/10.1371/journal.pone.0005463.
    • (2009) PLoS One , vol.4
    • Kadzhaev, K.1    Zingmark, C.2    Golovliov, I.3    Bolanowski, M.4    Shen, H.5    Conlan, W.6    Sjöstedt, A.7
  • 30
    • 2542552050 scopus 로고    scopus 로고
    • Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages
    • Clemens DL, Lee BY, Horwitz MA. 2004. Virulent and avirulent strains of Francisella tularensis prevent acidification and maturation of their phagosomes and escape into the cytoplasm in human macrophages. Infect Immun 72:3204-3217. http://dx.doi.org/10.1128/IAI.72.6.3204-3217.2004.
    • (2004) Infect Immun , vol.72 , pp. 3204-3217
    • Clemens, D.L.1    Lee, B.Y.2    Horwitz, M.A.3
  • 31
    • 77649222032 scopus 로고    scopus 로고
    • Cell biology and molecular ecology of Francisella tularensis
    • Santic M, Al-Khodor S, Abu Kwaik Y. 2010. Cell biology and molecular ecology of Francisella tularensis. Cell Microbiol 12:129-139. http://dx.doi.org/10.1111/j.1462-5822.2009.01400.x.
    • (2010) Cell Microbiol , vol.12 , pp. 129-139
    • Santic, M.1    Al-Khodor, S.2    Abu Kwaik, Y.3
  • 32
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA. 2008. Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77:755-776. http://dx.doi.org/10.1146/annurev.biochem.77.061606.161055.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 33
    • 77957350287 scopus 로고    scopus 로고
    • Comparative study of the roles of AhpC and KatE as respiratory antioxidants in Brucella abortus 2308
    • Steele KH, Baumgartner JE, Valderas MW, Roop RM, II. 2010. Comparative study of the roles of AhpC and KatE as respiratory antioxidants in Brucella abortus 2308. J Bacteriol 192:4912-4922. http://dx.doi.org/10.1128/JB.00231-10.
    • (2010) J Bacteriol , vol.192 , pp. 4912-4922
    • Steele, K.H.1    Baumgartner, J.E.2    Valderas, M.W.3    Roop, R.M.4
  • 34
    • 84896732204 scopus 로고    scopus 로고
    • EmrA1 membrane fusion protein of Francisella tularensis LVS is required for resistance to oxidative stress, intramacrophage survival and virulence in mice
    • Ma Z, Banik S, Rane H, Mora VT, Rabadi SM, Doyle CR, Thanassi DG, Bakshi CS, Malik M. 2014. EmrA1 membrane fusion protein of Francisella tularensis LVS is required for resistance to oxidative stress, intramacrophage survival and virulence in mice. Mol Microbiol 91:976-995. http://dx.doi.org/10.1111/mmi.12509.
    • (2014) Mol Microbiol , vol.91 , pp. 976-995
    • Ma, Z.1    Banik, S.2    Rane, H.3    Mora, V.T.4    Rabadi, S.M.5    Doyle, C.R.6    Thanassi, D.G.7    Bakshi, C.S.8    Malik, M.9
  • 35
    • 79952286485 scopus 로고    scopus 로고
    • Iron content differs between Francisella tularensis subspecies tularensis and subspecies holarctica strains and correlates to their susceptibility to H2O2-induced killing
    • Lindgren H, Honn M, Salomonsson E, Kuoppa K, Forsberg A, Sjöstedt A. 2011. Iron content differs between Francisella tularensis subspecies tularensis and subspecies holarctica strains and correlates to their susceptibility to H2O2-induced killing. Infect Immun 79:1218-1224. http://dx.doi.org/10.1128/IAI.01116-10.
    • (2011) Infect Immun , vol.79 , pp. 1218-1224
    • Lindgren, H.1    Honn, M.2    Salomonsson, E.3    Kuoppa, K.4    Forsberg, A.5    Sjöstedt, A.6
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680. http://dx.doi.org/10.1093/nar/22.22.4673.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet P, Robert X, Courcelle E. 2003. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res 31:3320-3323. http://dx.doi.org/10.1093/nar/gkg556.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 38
    • 0000154712 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria
    • Simon R, Priefer U, Pühler A. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Nat Biotechnol 1:787-796.
    • (1983) Nat Biotechnol , vol.1 , pp. 787-796
    • Simon, R.1    Priefer, U.2    Pühler, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.