메뉴 건너뛰기




Volumn 21, Issue 4, 2013, Pages 187-195

Streptococcus pneumoniae and reactive oxygen species: An unusual approach to living with radicals

Author keywords

Hydrogen peroxide; Oxidative stress defence; Reactive oxygen species; Streptococcus pneumoniae

Indexed keywords

ALKYLHYDROPEROXIDASE; BACTERIAL ANTIGEN; CATALASE; CYTOCHROME C; DNA BINDING FERRITIN LIKE PROTEIN; FERRITIN; GLUTATHIONE PEROXIDASE; HEAT SHOCK INDUCED SERINE PROTEASE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; METHIONINE SULFOXIDE REDUCTASE; PEROXIDASE; PNEUMOCOCCAL SURFACE ANTIGEN A; PROTEIN NOXA; PROTEINASE; PYRUVATE OXIDASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SUPEROXIDE DISMUTASE; THIOL PEROXIDASE; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 84875859494     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2013.01.004     Document Type: Review
Times cited : (85)

References (78)
  • 2
    • 70349547204 scopus 로고    scopus 로고
    • Management of oxidative stress in Bacillus
    • Zuber P. Management of oxidative stress in Bacillus. Annu. Rev. Microbiol. 2009, 63:575-597.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 575-597
    • Zuber, P.1
  • 3
    • 0345687929 scopus 로고    scopus 로고
    • Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the Fenton reaction
    • Pericone C.D., et al. Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the Fenton reaction. J. Bacteriol. 2003, 185:6815-6825.
    • (2003) J. Bacteriol. , vol.185 , pp. 6815-6825
    • Pericone, C.D.1
  • 4
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay J.A. Pathways of oxidative damage. Annu. Rev. Microbiol. 2003, 57:395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 5
    • 9244265524 scopus 로고    scopus 로고
    • Regulation of iron transport in Streptococcus pneumoniae by RitR, an orphan response regulator
    • Ulijasz A.T., et al. Regulation of iron transport in Streptococcus pneumoniae by RitR, an orphan response regulator. J. Bacteriol. 2004, 186:8123-8136.
    • (2004) J. Bacteriol. , vol.186 , pp. 8123-8136
    • Ulijasz, A.T.1
  • 6
    • 84873031631 scopus 로고    scopus 로고
    • Interplay between manganese and iron in pneumococcal pathogenesis: role of the orphan response regulator RitR
    • Ong C.L., et al. Interplay between manganese and iron in pneumococcal pathogenesis: role of the orphan response regulator RitR. Infect. Immun. 2013, 81:421-429.
    • (2013) Infect. Immun. , vol.81 , pp. 421-429
    • Ong, C.L.1
  • 7
    • 53049093959 scopus 로고    scopus 로고
    • PerR confers phagocytic killing resistance and allows pharyngeal colonization by group A Streptococcus
    • Gryllos I., et al. PerR confers phagocytic killing resistance and allows pharyngeal colonization by group A Streptococcus. PLoS Pathog. 2008, 4:e1000145.
    • (2008) PLoS Pathog. , vol.4
    • Gryllos, I.1
  • 8
    • 77952356390 scopus 로고    scopus 로고
    • The 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae
    • Lechardeur D., et al. The 2-Cys peroxiredoxin alkyl hydroperoxide reductase c binds heme and participates in its intracellular availability in Streptococcus agalactiae. J. Biol. Chem. 2010, 285:16032-16041.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16032-16041
    • Lechardeur, D.1
  • 9
    • 51949087233 scopus 로고    scopus 로고
    • An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses
    • Tsou C.C., et al. An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses. Infect. Immun. 2008, 76:4038-4045.
    • (2008) Infect. Immun. , vol.76 , pp. 4038-4045
    • Tsou, C.C.1
  • 10
    • 77955276650 scopus 로고    scopus 로고
    • Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr
    • Haikarainen T., et al. Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr. Biochem. Biophys. Res. Commun. 2010, 398:361-365.
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 361-365
    • Haikarainen, T.1
  • 11
    • 0033797110 scopus 로고    scopus 로고
    • Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes
    • King K.Y., et al. Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes. J. Bacteriol. 2000, 182:5290-5299.
    • (2000) J. Bacteriol. , vol.182 , pp. 5290-5299
    • King, K.Y.1
  • 12
    • 0030029521 scopus 로고    scopus 로고
    • Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae
    • Spellerberg B., et al. Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae. Mol. Microbiol. 1996, 19:803-813.
    • (1996) Mol. Microbiol. , vol.19 , pp. 803-813
    • Spellerberg, B.1
  • 13
    • 38449092559 scopus 로고    scopus 로고
    • Polymorphism and regulation of the spxB (pyruvate oxidase) virulence factor gene by a CBS-HotDog domain protein (SpxR) in serotype 2 Streptococcus pneumoniae
    • Ramos-Montanez S., et al. Polymorphism and regulation of the spxB (pyruvate oxidase) virulence factor gene by a CBS-HotDog domain protein (SpxR) in serotype 2 Streptococcus pneumoniae. Mol. Microbiol. 2008, 67:729-746.
    • (2008) Mol. Microbiol. , vol.67 , pp. 729-746
    • Ramos-Montanez, S.1
  • 14
    • 0033945724 scopus 로고    scopus 로고
    • Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract
    • Pericone C.D., et al. Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract. Infect. Immun. 2000, 68:3990-3997.
    • (2000) Infect. Immun. , vol.68 , pp. 3990-3997
    • Pericone, C.D.1
  • 15
    • 0036334551 scopus 로고    scopus 로고
    • Short-sequence tandem and nontandem DNA repeats and endogenous hydrogen peroxide production contribute to genetic instability of Streptococcus pneumoniae
    • Pericone C.D., et al. Short-sequence tandem and nontandem DNA repeats and endogenous hydrogen peroxide production contribute to genetic instability of Streptococcus pneumoniae. J. Bacteriol. 2002, 184:4392-4399.
    • (2002) J. Bacteriol. , vol.184 , pp. 4392-4399
    • Pericone, C.D.1
  • 16
    • 34548583324 scopus 로고    scopus 로고
    • SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model
    • Regev-Yochay G., et al. SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model. J. Bacteriol. 2007, 189:6532-6539.
    • (2007) J. Bacteriol. , vol.189 , pp. 6532-6539
    • Regev-Yochay, G.1
  • 17
    • 33847016108 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide production and the Fenton reaction on membrane composition of Streptococcus pneumoniae
    • Pesakhov S., et al. Effect of hydrogen peroxide production and the Fenton reaction on membrane composition of Streptococcus pneumoniae. Biochim. Biophys. Acta 2007, 1768:590-597.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 590-597
    • Pesakhov, S.1
  • 18
    • 0027377225 scopus 로고
    • Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells
    • Duane P.G., et al. Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells. Infect. Immun. 1993, 61:4392-4397.
    • (1993) Infect. Immun. , vol.61 , pp. 4392-4397
    • Duane, P.G.1
  • 19
    • 33745850132 scopus 로고    scopus 로고
    • The many faces of glutathione in bacteria
    • Masip L., et al. The many faces of glutathione in bacteria. Antioxid. Redox Signal. 2006, 8:753-762.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 753-762
    • Masip, L.1
  • 20
    • 84869105723 scopus 로고    scopus 로고
    • Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
    • Potter A.J., et al. Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity. J. Bacteriol. 2012, 194:6248-6254.
    • (2012) J. Bacteriol. , vol.194 , pp. 6248-6254
    • Potter, A.J.1
  • 21
    • 33750002912 scopus 로고    scopus 로고
    • The Group B Streptococcus NADH oxidase Nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence
    • Yamamoto Y., et al. The Group B Streptococcus NADH oxidase Nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence. Mol. Microbiol. 2006, 62:772-785.
    • (2006) Mol. Microbiol. , vol.62 , pp. 772-785
    • Yamamoto, Y.1
  • 22
    • 0033405777 scopus 로고    scopus 로고
    • The NADH oxidase of Streptococcus pneumoniae: its involvement in competence and virulence
    • Auzat I., et al. The NADH oxidase of Streptococcus pneumoniae: its involvement in competence and virulence. Mol. Microbiol. 1999, 34:1018-1028.
    • (1999) Mol. Microbiol. , vol.34 , pp. 1018-1028
    • Auzat, I.1
  • 23
    • 0035131745 scopus 로고    scopus 로고
    • Characterization of the Streptococcus pneumoniae NADH oxidase that is required for infection
    • Yu J., et al. Characterization of the Streptococcus pneumoniae NADH oxidase that is required for infection. Microbiology 2001, 147:431-438.
    • (2001) Microbiology , vol.147 , pp. 431-438
    • Yu, J.1
  • 25
    • 0025986138 scopus 로고
    • Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function
    • Fee J.A. Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function. Mol. Microbiol. 1991, 5:2599-2610.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2599-2610
    • Fee, J.A.1
  • 26
    • 0346788887 scopus 로고    scopus 로고
    • Prokaryotic Cu,Zn superoxide dismutases
    • Desideri A., Falconi M. Prokaryotic Cu,Zn superoxide dismutases. Biochem. Soc. Trans. 2003, 31:1322-1325.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1322-1325
    • Desideri, A.1    Falconi, M.2
  • 27
    • 2942556712 scopus 로고    scopus 로고
    • Crystal structure of nickel-containing superoxide dismutase reveals another type of active site
    • Wuerges J., et al. Crystal structure of nickel-containing superoxide dismutase reveals another type of active site. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:8569-8574.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8569-8574
    • Wuerges, J.1
  • 28
    • 0034098917 scopus 로고    scopus 로고
    • Role of manganese-containing superoxide dismutase in oxidative stress and virulence of Streptococcus pneumoniae
    • Yesilkaya H., et al. Role of manganese-containing superoxide dismutase in oxidative stress and virulence of Streptococcus pneumoniae. Infect. Immun. 2000, 68:2819-2826.
    • (2000) Infect. Immun. , vol.68 , pp. 2819-2826
    • Yesilkaya, H.1
  • 29
    • 84864574150 scopus 로고    scopus 로고
    • Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
    • Mishra S., Imlay J. Why do bacteria use so many enzymes to scavenge hydrogen peroxide?. Arch. Biochem. Biophys. 2012, 525:145-160.
    • (2012) Arch. Biochem. Biophys. , vol.525 , pp. 145-160
    • Mishra, S.1    Imlay, J.2
  • 30
    • 33645300106 scopus 로고    scopus 로고
    • An operon in Streptococcus pneumoniae containing a putative alkylhydroperoxidase D homologue contributes to virulence and the response to oxidative stress
    • Paterson G.K., et al. An operon in Streptococcus pneumoniae containing a putative alkylhydroperoxidase D homologue contributes to virulence and the response to oxidative stress. Microb. Pathog. 2006, 40:152-160.
    • (2006) Microb. Pathog. , vol.40 , pp. 152-160
    • Paterson, G.K.1
  • 31
    • 84870841949 scopus 로고    scopus 로고
    • Thiol peroxidase is an important component of Streptococcus pneumoniae in oxygenated environments
    • Hajaj B., et al. Thiol peroxidase is an important component of Streptococcus pneumoniae in oxygenated environments. Infect. Immun. 2012, 80:4333-4343.
    • (2012) Infect. Immun. , vol.80 , pp. 4333-4343
    • Hajaj, B.1
  • 32
    • 3843125485 scopus 로고    scopus 로고
    • Molecular analysis of the psa permease complex of Streptococcus pneumoniae
    • McAllister L.J., et al. Molecular analysis of the psa permease complex of Streptococcus pneumoniae. Mol. Microbiol. 2004, 53:889-901.
    • (2004) Mol. Microbiol. , vol.53 , pp. 889-901
    • McAllister, L.J.1
  • 33
    • 0029846414 scopus 로고    scopus 로고
    • Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential for virulence of Streptococcus pneumoniae
    • Berry A.M., Paton J.C. Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential for virulence of Streptococcus pneumoniae. Infect. Immun. 1996, 64:5255-5262.
    • (1996) Infect. Immun. , vol.64 , pp. 5255-5262
    • Berry, A.M.1    Paton, J.C.2
  • 34
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C., et al. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 1999, 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1
  • 35
    • 0036074050 scopus 로고    scopus 로고
    • Microarray-based identification of htrA, a Streptococcus pneumoniae gene that is regulated by the CiaRH two-component system and contributes to nasopharyngeal colonization
    • Sebert M.E., et al. Microarray-based identification of htrA, a Streptococcus pneumoniae gene that is regulated by the CiaRH two-component system and contributes to nasopharyngeal colonization. Infect. Immun. 2002, 70:4059-4067.
    • (2002) Infect. Immun. , vol.70 , pp. 4059-4067
    • Sebert, M.E.1
  • 36
    • 0037214390 scopus 로고    scopus 로고
    • The Streptococcus pneumoniae cia regulon: CiaR target sites and transcription profile analysis
    • Mascher T., et al. The Streptococcus pneumoniae cia regulon: CiaR target sites and transcription profile analysis. J. Bacteriol. 2003, 185:60-70.
    • (2003) J. Bacteriol. , vol.185 , pp. 60-70
    • Mascher, T.1
  • 37
    • 3843128524 scopus 로고    scopus 로고
    • Control of virulence by the two-component system CiaR/H is mediated via HtrA, a major virulence factor of Streptococcus pneumoniae
    • Ibrahim Y.M., et al. Control of virulence by the two-component system CiaR/H is mediated via HtrA, a major virulence factor of Streptococcus pneumoniae. J. Bacteriol. 2004, 186:5258-5266.
    • (2004) J. Bacteriol. , vol.186 , pp. 5258-5266
    • Ibrahim, Y.M.1
  • 38
    • 2542617706 scopus 로고    scopus 로고
    • Role of HtrA in the virulence and competence of Streptococcus pneumoniae
    • Ibrahim Y.M., et al. Role of HtrA in the virulence and competence of Streptococcus pneumoniae. Infect. Immun. 2004, 72:3584-3591.
    • (2004) Infect. Immun. , vol.72 , pp. 3584-3591
    • Ibrahim, Y.M.1
  • 39
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman S., et al. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 1998, 12:1338-1347.
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1
  • 40
    • 0032902058 scopus 로고    scopus 로고
    • New insights into the ATP-dependent Clp protease: Escherichia coli and beyond
    • Porankiewicz J., et al. New insights into the ATP-dependent Clp protease: Escherichia coli and beyond. Mol. Microbiol. 1999, 32:449-458.
    • (1999) Mol. Microbiol. , vol.32 , pp. 449-458
    • Porankiewicz, J.1
  • 41
    • 34447511284 scopus 로고    scopus 로고
    • ClpP: a distinctive family of cylindrical energy-dependent serine proteases
    • Yu A.Y., Houry W.A. ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 2007, 581:3749-3757.
    • (2007) FEBS Lett. , vol.581 , pp. 3749-3757
    • Yu, A.Y.1    Houry, W.A.2
  • 42
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 1996, 30:465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 43
    • 33645805882 scopus 로고    scopus 로고
    • Self-compartmentalized bacterial proteases and pathogenesis
    • Butler S.M., et al. Self-compartmentalized bacterial proteases and pathogenesis. Mol. Microbiol. 2006, 60:553-562.
    • (2006) Mol. Microbiol. , vol.60 , pp. 553-562
    • Butler, S.M.1
  • 44
    • 0036279922 scopus 로고    scopus 로고
    • Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence
    • Robertson G.T., et al. Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence. J. Bacteriol. 2002, 184:3508-3520.
    • (2002) J. Bacteriol. , vol.184 , pp. 3508-3520
    • Robertson, G.T.1
  • 45
    • 12844281219 scopus 로고    scopus 로고
    • Contribution of the ATP-dependent protease ClpCP to the autolysis and virulence of Streptococcus pneumoniae
    • Ibrahim Y.M., et al. Contribution of the ATP-dependent protease ClpCP to the autolysis and virulence of Streptococcus pneumoniae. Infect. Immun. 2005, 73:730-740.
    • (2005) Infect. Immun. , vol.73 , pp. 730-740
    • Ibrahim, Y.M.1
  • 46
    • 77951987422 scopus 로고    scopus 로고
    • Virulence attenuation of Streptococcus pneumoniae clpP mutant by sensitivity to oxidative stress in macrophages via an NO-mediated pathway
    • Park C.Y., et al. Virulence attenuation of Streptococcus pneumoniae clpP mutant by sensitivity to oxidative stress in macrophages via an NO-mediated pathway. J. Microbiol. 2010, 48:229-235.
    • (2010) J. Microbiol. , vol.48 , pp. 229-235
    • Park, C.Y.1
  • 47
    • 4644372119 scopus 로고    scopus 로고
    • The ClpP protease of Streptococcus pneumoniae modulates virulence gene expression and protects against fatal pneumococcal challenge
    • Kwon H.Y., et al. The ClpP protease of Streptococcus pneumoniae modulates virulence gene expression and protects against fatal pneumococcal challenge. Infect. Immun. 2004, 72:5646-5653.
    • (2004) Infect. Immun. , vol.72 , pp. 5646-5653
    • Kwon, H.Y.1
  • 48
    • 84857678559 scopus 로고    scopus 로고
    • Pneumococcal gene complex involved in resistance to extracellular oxidative stress
    • Andisi V.F., et al. Pneumococcal gene complex involved in resistance to extracellular oxidative stress. Infect. Immun. 2012, 80:1037-1049.
    • (2012) Infect. Immun. , vol.80 , pp. 1037-1049
    • Andisi, V.F.1
  • 49
    • 33845945906 scopus 로고    scopus 로고
    • The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases
    • Brot N., et al. The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases. J. Biol. Chem. 2006, 281:32668-32675.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32668-32675
    • Brot, N.1
  • 50
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes: in vitro
    • Archibald F.S., Fridovich I. The scavenging of superoxide radical by manganous complexes: in vitro. Arch. Biochem. Biophys. 1982, 214:452-463.
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 51
    • 0037893024 scopus 로고    scopus 로고
    • The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen
    • Kehres D.G., et al. The NRAMP proteins of Salmonella typhimurium and Escherichia coli are selective manganese transporters involved in the response to reactive oxygen. Mol. Microbiol. 2000, 36:1085-1100.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1085-1100
    • Kehres, D.G.1
  • 52
    • 0036842345 scopus 로고    scopus 로고
    • Manganese: elemental defence for a life with oxygen
    • Horsburgh M.J., et al. Manganese: elemental defence for a life with oxygen. Trends Microbiol. 2002, 10:496-501.
    • (2002) Trends Microbiol. , vol.10 , pp. 496-501
    • Horsburgh, M.J.1
  • 53
    • 4644305043 scopus 로고    scopus 로고
    • Lipoprotein PsaA in virulence of Streptococcus pneumoniae: surface accessibility and role in protection from superoxide
    • Johnston J.W., et al. Lipoprotein PsaA in virulence of Streptococcus pneumoniae: surface accessibility and role in protection from superoxide. Infect. Immun. 2004, 72:5858-5867.
    • (2004) Infect. Immun. , vol.72 , pp. 5858-5867
    • Johnston, J.W.1
  • 54
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A., et al. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 2009, 72:844-858.
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1
  • 55
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac A., et al. Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol. Microbiol. 1997, 25:727-739.
    • (1997) Mol. Microbiol. , vol.25 , pp. 727-739
    • Dintilhac, A.1
  • 56
    • 0036264178 scopus 로고    scopus 로고
    • In vivo characterization of the psa genes from Streptococcus pneumoniae in multiple models of infection
    • Marra A., et al. In vivo characterization of the psa genes from Streptococcus pneumoniae in multiple models of infection. Microbiology 2002, 148:1483-1491.
    • (2002) Microbiology , vol.148 , pp. 1483-1491
    • Marra, A.1
  • 57
    • 77956505339 scopus 로고    scopus 로고
    • Central role of manganese in regulation of stress responses, physiology, and metabolism in Streptococcus pneumoniae
    • Ogunniyi A.D., et al. Central role of manganese in regulation of stress responses, physiology, and metabolism in Streptococcus pneumoniae. J. Bacteriol. 2010, 192:4489-4497.
    • (2010) J. Bacteriol. , vol.192 , pp. 4489-4497
    • Ogunniyi, A.D.1
  • 58
    • 31844444872 scopus 로고    scopus 로고
    • 2+-dependent regulation of multiple genes in Streptococcus pneumoniae through PsaR and the resultant impact on virulence
    • 2+-dependent regulation of multiple genes in Streptococcus pneumoniae through PsaR and the resultant impact on virulence. Infect. Immun. 2006, 74:1171-1180.
    • (2006) Infect. Immun. , vol.74 , pp. 1171-1180
    • Johnston, J.W.1
  • 59
    • 0036178058 scopus 로고    scopus 로고
    • Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress
    • Tseng H.J., et al. Virulence of Streptococcus pneumoniae: PsaA mutants are hypersensitive to oxidative stress. Infect. Immun. 2002, 70:1635-1639.
    • (2002) Infect. Immun. , vol.70 , pp. 1635-1639
    • Tseng, H.J.1
  • 60
    • 0032971891 scopus 로고    scopus 로고
    • Penicillin tolerance in Streptococcus pneumoniae, autolysis and the Psa ATP-binding cassette (ABC) manganese permease
    • Claverys J.P., et al. Penicillin tolerance in Streptococcus pneumoniae, autolysis and the Psa ATP-binding cassette (ABC) manganese permease. Mol. Microbiol. 1999, 32:881-883.
    • (1999) Mol. Microbiol. , vol.32 , pp. 881-883
    • Claverys, J.P.1
  • 61
    • 0031689661 scopus 로고    scopus 로고
    • Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa
    • Novak R., et al. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Mol. Microbiol. 1998, 29:1285-1296.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1285-1296
    • Novak, R.1
  • 62
    • 1442268877 scopus 로고    scopus 로고
    • A two-component system that controls the expression of pneumococcal surface antigen A (PsaA) and regulates virulence and resistance to oxidative stress in Streptococcus pneumoniae
    • McCluskey J., et al. A two-component system that controls the expression of pneumococcal surface antigen A (PsaA) and regulates virulence and resistance to oxidative stress in Streptococcus pneumoniae. Mol. Microbiol. 2004, 51:1661-1675.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1661-1675
    • McCluskey, J.1
  • 63
    • 48149087575 scopus 로고    scopus 로고
    • 2+ on PsaR-mediated expression of the virulence genes pcpA, prtA, and psaBCA of Streptococcus pneumoniae
    • 2+ on PsaR-mediated expression of the virulence genes pcpA, prtA, and psaBCA of Streptococcus pneumoniae. J. Bacteriol. 2008, 190:5382-5393.
    • (2008) J. Bacteriol. , vol.190 , pp. 5382-5393
    • Kloosterman, T.G.1
  • 64
    • 66849083733 scopus 로고    scopus 로고
    • Strain-specific impact of PsaR of Streptococcus pneumoniae on global gene expression and virulence
    • Hendriksen W.T., et al. Strain-specific impact of PsaR of Streptococcus pneumoniae on global gene expression and virulence. Microbiology 2009, 155:1569-1579.
    • (2009) Microbiology , vol.155 , pp. 1569-1579
    • Hendriksen, W.T.1
  • 65
    • 62949119234 scopus 로고    scopus 로고
    • Role of the manganese efflux system mntE for signalling and pathogenesis in Streptococcus pneumoniae
    • Rosch J.W., et al. Role of the manganese efflux system mntE for signalling and pathogenesis in Streptococcus pneumoniae. Mol. Microbiol. 2009, 72:12-25.
    • (2009) Mol. Microbiol. , vol.72 , pp. 12-25
    • Rosch, J.W.1
  • 66
    • 0032534754 scopus 로고    scopus 로고
    • The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein
    • Lawrence M.C., et al. The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein. Structure 1998, 6:1553-1561.
    • (1998) Structure , vol.6 , pp. 1553-1561
    • Lawrence, M.C.1
  • 67
    • 81755162996 scopus 로고    scopus 로고
    • A molecular mechanism for bacterial susceptibility to zinc
    • McDevitt C.A., et al. A molecular mechanism for bacterial susceptibility to zinc. PLoS Pathog. 2011, 7:e1002357.
    • (2011) PLoS Pathog. , vol.7
    • McDevitt, C.A.1
  • 68
    • 33750505883 scopus 로고    scopus 로고
    • S100A8 and S100A9 in inflammation and cancer
    • Gebhardt C., et al. S100A8 and S100A9 in inflammation and cancer. Biochem. Pharmacol. 2006, 72:1622-1631.
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 1622-1631
    • Gebhardt, C.1
  • 69
    • 39349117867 scopus 로고    scopus 로고
    • Metal chelation and inhibition of bacterial growth in tissue abscesses
    • Corbin B.D., et al. Metal chelation and inhibition of bacterial growth in tissue abscesses. Science 2008, 319:962-965.
    • (2008) Science , vol.319 , pp. 962-965
    • Corbin, B.D.1
  • 70
    • 52649112223 scopus 로고    scopus 로고
    • Calcium efflux is essential for bacterial survival in the eukaryotic host
    • Rosch J.W., et al. Calcium efflux is essential for bacterial survival in the eukaryotic host. Mol. Microbiol. 2008, 70:435-444.
    • (2008) Mol. Microbiol. , vol.70 , pp. 435-444
    • Rosch, J.W.1
  • 71
    • 71449095015 scopus 로고    scopus 로고
    • The pneumococcal response to oxidative stress includes a role for Rgg
    • Bortoni M.E., et al. The pneumococcal response to oxidative stress includes a role for Rgg. Microbiology 2009, 155:4123-4134.
    • (2009) Microbiology , vol.155 , pp. 4123-4134
    • Bortoni, M.E.1
  • 72
    • 77955299893 scopus 로고    scopus 로고
    • The MerR/NmlR family transcription factor of Streptococcus pneumoniae responds to carbonyl stress and modulates hydrogen peroxide production
    • Potter A.J., et al. The MerR/NmlR family transcription factor of Streptococcus pneumoniae responds to carbonyl stress and modulates hydrogen peroxide production. J. Bacteriol. 2010, 192:4063-4066.
    • (2010) J. Bacteriol. , vol.192 , pp. 4063-4066
    • Potter, A.J.1
  • 73
    • 39149119282 scopus 로고    scopus 로고
    • A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence
    • Stroeher U.H., et al. A pneumococcal MerR-like regulator and S-nitrosoglutathione reductase are required for systemic virulence. J. Infect. Dis. 2007, 196:1820-1826.
    • (2007) J. Infect. Dis. , vol.196 , pp. 1820-1826
    • Stroeher, U.H.1
  • 74
    • 70149089300 scopus 로고    scopus 로고
    • Human neutrophils kill Streptococcus pneumoniae via serine proteases
    • Standish A.J., Weiser J.N. Human neutrophils kill Streptococcus pneumoniae via serine proteases. J. Immunol. 2009, 183:2602-2609.
    • (2009) J. Immunol. , vol.183 , pp. 2602-2609
    • Standish, A.J.1    Weiser, J.N.2
  • 75
    • 51949113536 scopus 로고    scopus 로고
    • Pneumolysin released during Streptococcus pneumoniae autolysis is a potent activator of intracellular oxygen radical production in neutrophils
    • Martner A., et al. Pneumolysin released during Streptococcus pneumoniae autolysis is a potent activator of intracellular oxygen radical production in neutrophils. Infect. Immun. 2008, 76:4079-4087.
    • (2008) Infect. Immun. , vol.76 , pp. 4079-4087
    • Martner, A.1
  • 76
    • 77956531058 scopus 로고    scopus 로고
    • Streptococcus pneumoniae modulates the respiratory burst response in human neutrophils
    • Barbuti G., et al. Streptococcus pneumoniae modulates the respiratory burst response in human neutrophils. FEMS Immunol. Med. Microbiol. 2010, 60:57-62.
    • (2010) FEMS Immunol. Med. Microbiol. , vol.60 , pp. 57-62
    • Barbuti, G.1
  • 77
    • 0037972445 scopus 로고    scopus 로고
    • Differential effect of p47phox and gp91phox deficiency on the course of pneumococcal meningitis
    • Schaper M., et al. Differential effect of p47phox and gp91phox deficiency on the course of pneumococcal meningitis. Infect. Immun. 2003, 71:4087-4092.
    • (2003) Infect. Immun. , vol.71 , pp. 4087-4092
    • Schaper, M.1
  • 78
    • 79955532516 scopus 로고    scopus 로고
    • TLR signalling augments macrophage bactericidal activity through mitochondrial ROS
    • West A.P., et al. TLR signalling augments macrophage bactericidal activity through mitochondrial ROS. Nature 2011, 472:476-480.
    • (2011) Nature , vol.472 , pp. 476-480
    • West, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.