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Volumn 303, Issue 3, 2013, Pages 114-123

Distribution and infection-related functions of bacillithiol in Staphylococcus aureus

Author keywords

Bacillithiol; BshC; Glutathione; Low molecular weight thiol; Staphylococcus aureus

Indexed keywords

ANTIBIOTIC AGENT; BACILLITHIOL; FOSFOMYCIN; HYDROGEN PEROXIDE; HYPOCHLORITE; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84875956912     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2013.01.003     Document Type: Article
Times cited : (42)

References (67)
  • 1
    • 59249084463 scopus 로고    scopus 로고
    • Glutathione provides a source of cysteine essential for intracellular multiplication of Francisella tularensis
    • Alkhuder K., Meibom K.L., Dubail I., Dupuis M., Charbit A. Glutathione provides a source of cysteine essential for intracellular multiplication of Francisella tularensis. PLoS Pathog. 2009, 5:e1000284.
    • (2009) PLoS Pathog. , vol.5
    • Alkhuder, K.1    Meibom, K.L.2    Dubail, I.3    Dupuis, M.4    Charbit, A.5
  • 3
    • 44149113314 scopus 로고    scopus 로고
    • Epidemiology of methicillin-resistant Staphylococcus aureus
    • Boucher H.W., Corey G.R. Epidemiology of methicillin-resistant Staphylococcus aureus. Clin. Infect. Dis. 2008, 46(Suppl. 5):S344-S349.
    • (2008) Clin. Infect. Dis. , vol.46 , Issue.SUPPL. 5
    • Boucher, H.W.1    Corey, G.R.2
  • 4
    • 0027528612 scopus 로고
    • Characterization of a sucrase gene from Staphylococcus xylosus
    • Brückner R., Wagner E., Götz F. Characterization of a sucrase gene from Staphylococcus xylosus. J. Bacteriol. 1993, 175:851-857.
    • (1993) J. Bacteriol. , vol.175 , pp. 851-857
    • Brückner, R.1    Wagner, E.2    Götz, F.3
  • 5
    • 80052929972 scopus 로고    scopus 로고
    • S-Bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics
    • M111 009506
    • Chi B.K., Gronau K., Mäder U., Hessling B., Becher D., Antelmann H. S-Bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics. Mol. Cell Proteomics 2011, 10. M111 009506.
    • (2011) Mol. Cell Proteomics , vol.10
    • Chi, B.K.1    Gronau, K.2    Mäder, U.3    Hessling, B.4    Becher, D.5    Antelmann, H.6
  • 7
    • 33746601080 scopus 로고    scopus 로고
    • Staphyloxanthin plays a role in the fitness of Staphylococcus aureus and its ability to cope with oxidative stress
    • Clauditz A., Resch A., Wieland K.P., Peschel A., Gotz F. Staphyloxanthin plays a role in the fitness of Staphylococcus aureus and its ability to cope with oxidative stress. Infect. Immun. 2006, 74:4950-4953.
    • (2006) Infect. Immun. , vol.74 , pp. 4950-4953
    • Clauditz, A.1    Resch, A.2    Wieland, K.P.3    Peschel, A.4    Gotz, F.5
  • 9
    • 33846561089 scopus 로고    scopus 로고
    • Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus
    • Cosgrove K., Coutts G., Jonsson I.M., Tarkowski A., Kokai-Kun J.F., Mond J.J., Foster S.J. Catalase (KatA) and alkyl hydroperoxide reductase (AhpC) have compensatory roles in peroxide stress resistance and are required for survival, persistence, and nasal colonization in Staphylococcus aureus. J. Bacteriol. 2007, 189:1025-1035.
    • (2007) J. Bacteriol. , vol.189 , pp. 1025-1035
    • Cosgrove, K.1    Coutts, G.2    Jonsson, I.M.3    Tarkowski, A.4    Kokai-Kun, J.F.5    Mond, J.J.6    Foster, S.J.7
  • 12
    • 0032489438 scopus 로고    scopus 로고
    • Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus
    • delCardayré S.B., Stock K.P., Newton G.L., Fahey R.C., Davies J.E. Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. J. Biol. Chem. 1998, 273:5744-5751.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5744-5751
    • DelCardayré, S.B.1    Stock, K.P.2    Newton, G.L.3    Fahey, R.C.4    Davies, J.E.5
  • 13
    • 84875700077 scopus 로고    scopus 로고
    • Glutathione analogs in prokaryotes
    • Fahey R.C. Glutathione analogs in prokaryotes. Biochim. Biophys. Acta 2012, 10.1016/j.bbagen.2012.1010.1006.
    • (2012) Biochim. Biophys. Acta
    • Fahey, R.C.1
  • 15
    • 15244357417 scopus 로고    scopus 로고
    • The Staphylococcus aureus " superbug"
    • Foster T.J. The Staphylococcus aureus " superbug" J. Clin. Invest. 2004, 114:1693-1696.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1693-1696
    • Foster, T.J.1
  • 18
    • 60349085142 scopus 로고    scopus 로고
    • Staphylococcus aureus: new evidence for intracellular persistence
    • Garzoni C., Kelley W.L. Staphylococcus aureus: new evidence for intracellular persistence. Trends Microbiol. 2009, 17:59-65.
    • (2009) Trends Microbiol. , vol.17 , pp. 59-65
    • Garzoni, C.1    Kelley, W.L.2
  • 19
    • 18944397128 scopus 로고    scopus 로고
    • A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis
    • Gopal S., Borovok I., Ofer A., Yanku M., Cohen G., Goebel W., Kreft J., Aharonowitz Y. A multidomain fusion protein in Listeria monocytogenes catalyzes the two primary activities for glutathione biosynthesis. J. Bacteriol. 2005, 187:3839-3847.
    • (2005) J. Bacteriol. , vol.187 , pp. 3839-3847
    • Gopal, S.1    Borovok, I.2    Ofer, A.3    Yanku, M.4    Cohen, G.5    Goebel, W.6    Kreft, J.7    Aharonowitz, Y.8
  • 20
    • 0033972395 scopus 로고    scopus 로고
    • A peptide permease mutant of Mycobacterium bovis BCG resistant to the toxic peptides glutathione and S-nitrosoglutathione
    • Green R.M., Seth A., Connell N.D. A peptide permease mutant of Mycobacterium bovis BCG resistant to the toxic peptides glutathione and S-nitrosoglutathione. Infect. Immun. 2000, 68:429-436.
    • (2000) Infect. Immun. , vol.68 , pp. 429-436
    • Green, R.M.1    Seth, A.2    Connell, N.D.3
  • 21
    • 84869211845 scopus 로고    scopus 로고
    • Bacillus anthracis thioredoxin systems - characterization and role as electron donors for ribonucleotide reductase
    • Gustafsson T.N., Sahlin M., Lu J., Sjoberg B.M., Holmgren A. Bacillus anthracis thioredoxin systems - characterization and role as electron donors for ribonucleotide reductase. J. Biol. Chem. 2012, 287:39686-39697.
    • (2012) J. Biol. Chem. , vol.287 , pp. 39686-39697
    • Gustafsson, T.N.1    Sahlin, M.2    Lu, J.3    Sjoberg, B.M.4    Holmgren, A.5
  • 22
    • 79958216714 scopus 로고    scopus 로고
    • Bacillithiol, a new player in bacterial redox homeostasis
    • Helmann J.D. Bacillithiol, a new player in bacterial redox homeostasis. Antioxid. Redox Signal. 2011, 15:123-133.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 123-133
    • Helmann, J.D.1
  • 23
    • 77955933961 scopus 로고    scopus 로고
    • Characterization of the transposase encoded by IS256, the prototype of a major family of bacterial insertion sequence elements
    • Hennig S., Ziebuhr W. Characterization of the transposase encoded by IS256, the prototype of a major family of bacterial insertion sequence elements. J. Bacteriol. 2010, 192:4153-4163.
    • (2010) J. Bacteriol. , vol.192 , pp. 4153-4163
    • Hennig, S.1    Ziebuhr, W.2
  • 24
    • 34447543004 scopus 로고    scopus 로고
    • Only one of four oligopeptide transport systems mediates nitrogen nutrition in Staphylococcus aureus
    • Hiron A., Borezee-Durant E., Piard J.C., Juillard V. Only one of four oligopeptide transport systems mediates nitrogen nutrition in Staphylococcus aureus. J. Bacteriol. 2007, 189:5119-5129.
    • (2007) J. Bacteriol. , vol.189 , pp. 5119-5129
    • Hiron, A.1    Borezee-Durant, E.2    Piard, J.C.3    Juillard, V.4
  • 25
    • 47249088762 scopus 로고    scopus 로고
    • Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus
    • Hochgräfe F., Wolf C., Fuchs S., Liebeke M., Lalk M., Engelmann S., Hecker M. Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus. J. Bacteriol. 2008, 190:4997-5008.
    • (2008) J. Bacteriol. , vol.190 , pp. 4997-5008
    • Hochgräfe, F.1    Wolf, C.2    Fuchs, S.3    Liebeke, M.4    Lalk, M.5    Engelmann, S.6    Hecker, M.7
  • 26
    • 2042476756 scopus 로고
    • Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione
    • Holmgren A. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. U.S.A. 1976, 73:2275-2279.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2275-2279
    • Holmgren, A.1
  • 27
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 1989, 264:13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 28
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh M.J., Clements M.O., Crossley H., Ingham E., Foster S.J. PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect. Immun. 2001, 69:3744-3754.
    • (2001) Infect. Immun. , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 29
    • 58949091991 scopus 로고    scopus 로고
    • Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular weight thiol in actinomycetes
    • Jothivasan V.K., Hamilton C.J. Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular weight thiol in actinomycetes. Nat. Prod. Rep. 2008, 25:1091-1117.
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 1091-1117
    • Jothivasan, V.K.1    Hamilton, C.J.2
  • 30
    • 0029006990 scopus 로고
    • Diamide: an oxidant probe for thiols
    • Kosower N.S., Kosower E.M. Diamide: an oxidant probe for thiols. Methods Enzymol. 1995, 251:123-133.
    • (1995) Methods Enzymol. , vol.251 , pp. 123-133
    • Kosower, N.S.1    Kosower, E.M.2
  • 31
    • 0842326187 scopus 로고    scopus 로고
    • The bacterial insertion sequence element IS256 occurs preferentially in nosocomial Staphylococcus epidermidis isolates: association with biofilm formation and resistance to aminoglycosides
    • Kozitskaya S., Cho S.H., Dietrich K., Marre R., Naber K., Ziebuhr W. The bacterial insertion sequence element IS256 occurs preferentially in nosocomial Staphylococcus epidermidis isolates: association with biofilm formation and resistance to aminoglycosides. Infect. Immun. 2004, 72:1210-1215.
    • (2004) Infect. Immun. , vol.72 , pp. 1210-1215
    • Kozitskaya, S.1    Cho, S.H.2    Dietrich, K.3    Marre, R.4    Naber, K.5    Ziebuhr, W.6
  • 32
    • 0037846500 scopus 로고    scopus 로고
    • The parasite-specific trypanothione metabolism of trypanosoma and leishmania
    • Krauth-Siegel R.L., Meiering S.K., Schmidt H. The parasite-specific trypanothione metabolism of trypanosoma and leishmania. Biol. Chem. 2003, 384:539-549.
    • (2003) Biol. Chem. , vol.384 , pp. 539-549
    • Krauth-Siegel, R.L.1    Meiering, S.K.2    Schmidt, H.3
  • 35
    • 0037334843 scopus 로고    scopus 로고
    • Global characterization of disulfide stress in Bacillus subtilis
    • Leichert L.I., Scharf C., Hecker M. Global characterization of disulfide stress in Bacillus subtilis. J. Bacteriol. 2003, 185:1967-1975.
    • (2003) J. Bacteriol. , vol.185 , pp. 1967-1975
    • Leichert, L.I.1    Scharf, C.2    Hecker, M.3
  • 36
    • 0034528705 scopus 로고    scopus 로고
    • Antibiotic resistance in staphylococci
    • Livermore D.M. Antibiotic resistance in staphylococci. Int. J. Antimicrob. Agents 2000, 16(Suppl. 1):S3-S10.
    • (2000) Int. J. Antimicrob. Agents , vol.16 , Issue.SUPPL. 1
    • Livermore, D.M.1
  • 37
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy F.D. Staphylococcus aureus infections. N. Engl. J. Med. 1998, 339:520-532.
    • (1998) N. Engl. J. Med. , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 39
    • 33749000257 scopus 로고    scopus 로고
    • Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54Å resolution
    • Mallett T.C., Wallen J.R., Karplus P.A., Sakai H., Tsukihara T., Claiborne A. Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54Å resolution. Biochemistry 2006, 45:11278-11289.
    • (2006) Biochemistry , vol.45 , pp. 11278-11289
    • Mallett, T.C.1    Wallen, J.R.2    Karplus, P.A.3    Sakai, H.4    Tsukihara, T.5    Claiborne, A.6
  • 41
    • 33747357184 scopus 로고    scopus 로고
    • Arsenate reduction: thiol cascade chemistry with convergent evolution
    • Messens J., Silver S. Arsenate reduction: thiol cascade chemistry with convergent evolution. J. Mol. Biol. 2006, 362:1-17.
    • (2006) J. Mol. Biol. , vol.362 , pp. 1-17
    • Messens, J.1    Silver, S.2
  • 43
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz J., Scharf C., Hecker M., Homuth G. Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress. Microbiology 2004, 150:497-512.
    • (2004) Microbiology , vol.150 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 46
    • 84859140103 scopus 로고    scopus 로고
    • Detoxification of toxins by bacillithiol in Staphylococcus aureus
    • Newton G.L., Fahey R.C., Rawat M. Detoxification of toxins by bacillithiol in Staphylococcus aureus. Microbiology 2012, 158:1117-1126.
    • (2012) Microbiology , vol.158 , pp. 1117-1126
    • Newton, G.L.1    Fahey, R.C.2    Rawat, M.3
  • 48
    • 0041761698 scopus 로고    scopus 로고
    • Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities
    • Ortenberg R., Beckwith J. Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities. Antioxid. Redox Signal. 2003, 5:403-411.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 403-411
    • Ortenberg, R.1    Beckwith, J.2
  • 52
    • 84869105723 scopus 로고    scopus 로고
    • Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion toxicity
    • Potter A.J., Trappetti C., Paton J.C. 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    Trappetti, C.2    Paton, J.C.3
  • 53
    • 0017115997 scopus 로고
    • Lysozyme synthesis by established human and murine histiocytic lymphoma cell lines
    • Ralph P., Moore M.A., Nilsson K. Lysozyme synthesis by established human and murine histiocytic lymphoma cell lines. J. Exp. Med. 1976, 143:1528-1533.
    • (1976) J. Exp. Med. , vol.143 , pp. 1528-1533
    • Ralph, P.1    Moore, M.A.2    Nilsson, K.3
  • 54
    • 0036178932 scopus 로고    scopus 로고
    • Virulence gene identification by differential fluorescence induction analysis of Staphylococcus aureus gene expression during infection-simulating culture
    • Schneider W.P., Ho S.K., Christine J., Yao M., Marra A., Hromockyj A.E. Virulence gene identification by differential fluorescence induction analysis of Staphylococcus aureus gene expression during infection-simulating culture. Infect. Immun. 2002, 70:1326-1333.
    • (2002) Infect. Immun. , vol.70 , pp. 1326-1333
    • Schneider, W.P.1    Ho, S.K.2    Christine, J.3    Yao, M.4    Marra, A.5    Hromockyj, A.E.6
  • 55
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal A.W. How neutrophils kill microbes. Annu. Rev. Immunol. 2005, 23:197-223.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 57
    • 0031894921 scopus 로고    scopus 로고
    • Import and metabolism of glutathione by Streptococcus mutans
    • Sherrill C., Fahey R.C. Import and metabolism of glutathione by Streptococcus mutans. J. Bacteriol. 1998, 180:1454-1459.
    • (1998) J. Bacteriol. , vol.180 , pp. 1454-1459
    • Sherrill, C.1    Fahey, R.C.2
  • 59
    • 0021334514 scopus 로고
    • Disulfide reduction and sulfhydryl uptake by Streptococcus mutans
    • Thomas E.L. Disulfide reduction and sulfhydryl uptake by Streptococcus mutans. J. Bacteriol. 1984, 157:240-246.
    • (1984) J. Bacteriol. , vol.157 , pp. 240-246
    • Thomas, E.L.1
  • 60
    • 77956628119 scopus 로고    scopus 로고
    • Michael acceptor-containing coenzyme A analogues as inhibitors of the atypical coenzyme A disulfide reductase from Staphylococcus aureus
    • van der Westhuyzen R., Strauss E. Michael acceptor-containing coenzyme A analogues as inhibitors of the atypical coenzyme A disulfide reductase from Staphylococcus aureus. J. Am. Chem. Soc. 2010, 132:12853-12855.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12853-12855
    • van der Westhuyzen, R.1    Strauss, E.2
  • 61
    • 0019125693 scopus 로고
    • The level and half-life of glutathione in human plasma
    • Wendel A., Cikryt P. The level and half-life of glutathione in human plasma. FEBS Lett. 1980, 120:209-211.
    • (1980) FEBS Lett. , vol.120 , pp. 209-211
    • Wendel, A.1    Cikryt, P.2
  • 63
    • 21344481228 scopus 로고
    • Glutathione accumulation in lactococci
    • Wiederholt K.M., Steele J.L. Glutathione accumulation in lactococci. J. Dairy Sci. 1994, 77:1183-1188.
    • (1994) J. Dairy Sci. , vol.77 , pp. 1183-1188
    • Wiederholt, K.M.1    Steele, J.L.2
  • 64
    • 84872476329 scopus 로고    scopus 로고
    • Redox reactions and microbial killing in the neutrophil phagosome
    • Winterbourn C.C., Kettle A.J. Redox reactions and microbial killing in the neutrophil phagosome. Antioxid. Redox Signal. 2013, 18:642-660.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 642-660
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 65
    • 49749101196 scopus 로고    scopus 로고
    • Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants
    • Wolf C., Hochgräfe F., Kusch H., Albrecht D., Hecker M., Engelmann S. Proteomic analysis of antioxidant strategies of Staphylococcus aureus: diverse responses to different oxidants. Proteomics 2008, 8:3139-3153.
    • (2008) Proteomics , vol.8 , pp. 3139-3153
    • Wolf, C.1    Hochgräfe, F.2    Kusch, H.3    Albrecht, D.4    Hecker, M.5    Engelmann, S.6
  • 66
    • 0034007311 scopus 로고    scopus 로고
    • Chromosomal rearrangements affecting biofilm production and antibiotic resistance in a Staphylococcus epidermidis strain causing shunt-associated ventriculitis
    • Ziebuhr W., Dietrich K., Trautmann M., Wilhelm M. Chromosomal rearrangements affecting biofilm production and antibiotic resistance in a Staphylococcus epidermidis strain causing shunt-associated ventriculitis. Int. J. Med. Microbiol. 2000, 290:115-120.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 115-120
    • Ziebuhr, W.1    Dietrich, K.2    Trautmann, M.3    Wilhelm, M.4
  • 67
    • 0032896896 scopus 로고    scopus 로고
    • A novel mechanism of phase variation of virulence in Staphylococcus epidermidis: evidence for control of the polysaccharide intercellular adhesin synthesis by alternating insertion and excision of the insertion sequence element IS256
    • Ziebuhr W., Krimmer V., Rachid S., Lossner I., Gotz F., Hacker J. A novel mechanism of phase variation of virulence in Staphylococcus epidermidis: evidence for control of the polysaccharide intercellular adhesin synthesis by alternating insertion and excision of the insertion sequence element IS256. Mol. Microbiol. 1999, 32:345-356.
    • (1999) Mol. Microbiol. , vol.32 , pp. 345-356
    • Ziebuhr, W.1    Krimmer, V.2    Rachid, S.3    Lossner, I.4    Gotz, F.5    Hacker, J.6


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