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Volumn 6, Issue 11, 2011, Pages

Methionine sulfoxide reductases are essential for virulence of Salmonella typhimurium

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; CHLORAMPHENICOL; HYDROGEN PEROXIDE; KANAMYCIN; METHIONINE SULFOXIDE REDUCTASE; METHIONINE SULFOXIDE REDUCTASE A; METHIONINE SULFOXIDE REDUCTASE B; METHIONINE SULFOXIDE REDUCTASE C; UNCLASSIFIED DRUG;

EID: 80355143377     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026974     Document Type: Article
Times cited : (54)

References (39)
  • 2
    • 44649113673 scopus 로고    scopus 로고
    • Salmonella infections in immunocompromised adults
    • Gordon MA, (2008) Salmonella infections in immunocompromised adults. J Infect 56: 413-422.
    • (2008) J Infect , vol.56 , pp. 413-422
    • Gordon, M.A.1
  • 3
    • 0034679577 scopus 로고    scopus 로고
    • Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro
    • Vazquez-Torres A, Jones-Carson J, Mastroeni P, Ischiropoulos H, Fang FC, (2000) Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. I. Effects on microbial killing by activated peritoneal macrophages in vitro. J Exp Med 192: 227-236.
    • (2000) J Exp Med , vol.192 , pp. 227-236
    • Vazquez-Torres, A.1    Jones-Carson, J.2    Mastroeni, P.3    Ischiropoulos, H.4    Fang, F.C.5
  • 4
    • 67650299991 scopus 로고    scopus 로고
    • Redundant hydrogen peroxide scavengers contribute to Salmonella virulence and oxidative stress resistance
    • Hebrard M, Viala JP, Meresse S, Barras F, Aussel L, (2009) Redundant hydrogen peroxide scavengers contribute to Salmonella virulence and oxidative stress resistance. J Bacteriol 191: 4605-4614.
    • (2009) J Bacteriol , vol.191 , pp. 4605-4614
    • Hebrard, M.1    Viala, J.P.2    Meresse, S.3    Barras, F.4    Aussel, L.5
  • 5
    • 77952579100 scopus 로고    scopus 로고
    • Thiol peroxidase protects Salmonella enterica from hydrogen peroxide stress in vitro and facilitates intracellular growth
    • Horst SA, Jaeger T, Denkel LA, Rouf SF, Rhen M, et al. (2010) Thiol peroxidase protects Salmonella enterica from hydrogen peroxide stress in vitro and facilitates intracellular growth. J Bacteriol 192: 2929-2932.
    • (2010) J Bacteriol , vol.192 , pp. 2929-2932
    • Horst, S.A.1    Jaeger, T.2    Denkel, L.A.3    Rouf, S.F.4    Rhen, M.5
  • 6
    • 79955043484 scopus 로고    scopus 로고
    • Salmonella detoxifying enzymes are sufficient to cope with the host oxidative burst
    • Aussel L, Zhao W, Hebrard M, Guilhon AA, Viala JP, et al. (2011) Salmonella detoxifying enzymes are sufficient to cope with the host oxidative burst. Mol Microbiol 80: 628-640.
    • (2011) Mol Microbiol , vol.80 , pp. 628-640
    • Aussel, L.1    Zhao, W.2    Hebrard, M.3    Guilhon, A.A.4    Viala, J.P.5
  • 7
    • 0037082129 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function
    • Weissbach H, Etienne F, Hoshi T, Heinemann SH, Lowther WT, et al. (2002) Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function. Arch Biochem Biophys 397: 172-178.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 172-178
    • Weissbach, H.1    Etienne, F.2    Hoshi, T.3    Heinemann, S.H.4    Lowther, W.T.5
  • 9
  • 10
    • 34447308960 scopus 로고    scopus 로고
    • Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function
    • Lin Z, Johnson LC, Weissbach H, Brot N, Lively MO, et al. (2007) Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function. Proc Natl Acad Sci U S A 104: 9597-9602.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9597-9602
    • Lin, Z.1    Johnson, L.C.2    Weissbach, H.3    Brot, N.4    Lively, M.O.5
  • 11
    • 63249128682 scopus 로고    scopus 로고
    • Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae
    • Le DT, Lee BC, Marino SM, Zhang Y, Fomenko DE, et al. (2009) Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae. J Biol Chem 284: 4354-4364.
    • (2009) J Biol Chem , vol.284 , pp. 4354-4364
    • Le, D.T.1    Lee, B.C.2    Marino, S.M.3    Zhang, Y.4    Fomenko, D.E.5
  • 12
    • 57649119783 scopus 로고    scopus 로고
    • Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductase
    • Lee BC, Le DT, Gladyshev VN, (2008) Mammals reduce methionine-S-sulfoxide with MsrA and are unable to reduce methionine-R-sulfoxide, and this function can be restored with a yeast reductase. J Biol Chem 283: 28361-28369.
    • (2008) J Biol Chem , vol.283 , pp. 28361-28369
    • Lee, B.C.1    Le, D.T.2    Gladyshev, V.N.3
  • 13
    • 2442701595 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages
    • Douglas T, Daniel DS, Parida BK, Jagannath C, Dhandayuthapani S, (2004) Methionine sulfoxide reductase A (MsrA) deficiency affects the survival of Mycobacterium smegmatis within macrophages. J Bacteriol 186: 3590-3598.
    • (2004) J Bacteriol , vol.186 , pp. 3590-3598
    • Douglas, T.1    Daniel, D.S.2    Parida, B.K.3    Jagannath, C.4    Dhandayuthapani, S.5
  • 14
    • 0142074786 scopus 로고    scopus 로고
    • Multiple methionine sulfoxide reductase genes in Staphylococcus aureus: expression of activity and roles in tolerance of oxidative stress
    • Singh VK, Moskovitz J, (2003) Multiple methionine sulfoxide reductase genes in Staphylococcus aureus: expression of activity and roles in tolerance of oxidative stress. Microbiology 149: 2739-2747.
    • (2003) Microbiology , vol.149 , pp. 2739-2747
    • Singh, V.K.1    Moskovitz, J.2
  • 15
    • 0035859807 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates
    • St John G, Brot N, Ruan J, Erdjument-Bromage H, Tempst P, et al. (2001) Peptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediates. Proc Natl Acad Sci U S A 98: 9901-9906.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9901-9906
    • John St., G.1    Brot, N.2    Ruan, J.3    Erdjument-Bromage, H.4    Tempst, P.5
  • 16
    • 69949102433 scopus 로고    scopus 로고
    • Oxidative stress in Campylobacter jejuni: responses, resistance and regulation
    • Atack JM, Kelly DJ, (2009) Oxidative stress in Campylobacter jejuni: responses, resistance and regulation. Future Microbiol 4: 677-690.
    • (2009) Future Microbiol , vol.4 , pp. 677-690
    • Atack, J.M.1    Kelly, D.J.2
  • 17
    • 77956641493 scopus 로고    scopus 로고
    • Role of methionine sulfoxide reductases A and B of Enterococcus faecalis in oxidative stress and virulence
    • Zhao C, Hartke A, La Sorda M, Posteraro B, Laplace JM, et al. (2010) Role of methionine sulfoxide reductases A and B of Enterococcus faecalis in oxidative stress and virulence. Infect Immun 78: 3889-3897.
    • (2010) Infect Immun , vol.78 , pp. 3889-3897
    • Zhao, C.1    Hartke, A.2    la Sorda, M.3    Posteraro, B.4    Laplace, J.M.5
  • 18
    • 4444275438 scopus 로고    scopus 로고
    • Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori
    • Alamuri P, Maier RJ, (2004) Methionine sulphoxide reductase is an important antioxidant enzyme in the gastric pathogen Helicobacter pylori. Mol Microbiol 53: 1397-1406.
    • (2004) Mol Microbiol , vol.53 , pp. 1397-1406
    • Alamuri, P.1    Maier, R.J.2
  • 19
    • 0037162478 scopus 로고    scopus 로고
    • The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species
    • Skaar EP, Tobiason DM, Quick J, Judd RC, Weissbach H, et al. (2002) The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species. Proc Natl Acad Sci U S A 99: 10108-10113.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10108-10113
    • Skaar, E.P.1    Tobiason, D.M.2    Quick, J.3    Judd, R.C.4    Weissbach, H.5
  • 20
    • 58449097413 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite
    • Lee WL, Gold B, Darby C, Brot N, Jiang X, et al. (2009) Mycobacterium tuberculosis expresses methionine sulphoxide reductases A and B that protect from killing by nitrite and hypochlorite. Mol Microbiol 71: 583-593.
    • (2009) Mol Microbiol , vol.71 , pp. 583-593
    • Lee, W.L.1    Gold, B.2    Darby, C.3    Brot, N.4    Jiang, X.5
  • 21
    • 77955292569 scopus 로고    scopus 로고
    • Structural and kinetic analysis of free methionine-R-sulfoxide reductase from Staphylococcus aureus: conformational changes during catalysis and implications for the catalytic and inhibitory mechanisms
    • Bong SM, Kwak GH, Moon JH, Lee KS, Kim HS, et al. (2010) Structural and kinetic analysis of free methionine-R-sulfoxide reductase from Staphylococcus aureus: conformational changes during catalysis and implications for the catalytic and inhibitory mechanisms. J Biol Chem 285: 25044-25052.
    • (2010) J Biol Chem , vol.285 , pp. 25044-25052
    • Bong, S.M.1    Kwak, G.H.2    Moon, J.H.3    Lee, K.S.4    Kim, H.S.5
  • 22
    • 77955299408 scopus 로고    scopus 로고
    • Structural and biochemical characterization of free methionine-R-sulfoxide reductase from Neisseria meningitidis
    • Gruez A, Libiad M, Boschi-Muller S, Branlant G, (2010) Structural and biochemical characterization of free methionine-R-sulfoxide reductase from Neisseria meningitidis. J Biol Chem 285: 25033-25043.
    • (2010) J Biol Chem , vol.285 , pp. 25033-25043
    • Gruez, A.1    Libiad, M.2    Boschi-Muller, S.3    Branlant, G.4
  • 23
    • 0035950182 scopus 로고    scopus 로고
    • Complete genome sequence of Salmonella enterica serovar Typhimurium LT2
    • McClelland M, Sanderson KE, Spieth J, Clifton SW, Latreille P, et al. (2001) Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature 413: 852-856.
    • (2001) Nature , vol.413 , pp. 852-856
    • McClelland, M.1    Sanderson, K.E.2    Spieth, J.3    Clifton, S.W.4    Latreille, P.5
  • 24
    • 0035966062 scopus 로고    scopus 로고
    • Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase
    • Grimaud R, Ezraty B, Mitchell JK, Lafitte D, Briand C, et al. (2001) Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase. J Biol Chem 276: 48915-48920.
    • (2001) J Biol Chem , vol.276 , pp. 48915-48920
    • Grimaud, R.1    Ezraty, B.2    Mitchell, J.K.3    Lafitte, D.4    Briand, C.5
  • 25
    • 0042850506 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase (MsrA) is not a major virulence determinant for the oral pathogen Actinobacillus actinomycetemcomitans
    • Mintz KP, Moskovitz J, Wu H, Fives-Taylor PM, (2002) Peptide methionine sulfoxide reductase (MsrA) is not a major virulence determinant for the oral pathogen Actinobacillus actinomycetemcomitans. Microbiology 148: 3695-3703.
    • (2002) Microbiology , vol.148 , pp. 3695-3703
    • Mintz, K.P.1    Moskovitz, J.2    Wu, H.3    Fives-Taylor, P.M.4
  • 26
    • 0035671378 scopus 로고    scopus 로고
    • Use of mixed infections with Salmonella strains to study virulence genes and their interactions in vivo
    • Beuzon CR, Holden DW, (2001) Use of mixed infections with Salmonella strains to study virulence genes and their interactions in vivo. Microbes Infect 3: 1345-1352.
    • (2001) Microbes Infect , vol.3 , pp. 1345-1352
    • Beuzon, C.R.1    Holden, D.W.2
  • 27
    • 0018423074 scopus 로고
    • Reduction of methionine sulfoxide to methionine by Escherichia coli
    • Ejiri SI, Weissbach H, Brot N, (1979) Reduction of methionine sulfoxide to methionine by Escherichia coli. J Bacteriol 139: 161-164.
    • (1979) J Bacteriol , vol.139 , pp. 161-164
    • Ejiri, S.I.1    Weissbach, H.2    Brot, N.3
  • 28
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
    • Weissbach H, Resnick L, Brot N, (2005) Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim Biophys Acta 1703: 203-212.
    • (2005) Biochim Biophys Acta , vol.1703 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 29
    • 37549011768 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases and virulence of bacterial pathogens
    • Sasindran SJ, Saikolappan S, Dhandayuthapani S, (2007) Methionine sulfoxide reductases and virulence of bacterial pathogens. Future Microbiol 2: 619-630.
    • (2007) Future Microbiol , vol.2 , pp. 619-630
    • Sasindran, S.J.1    Saikolappan, S.2    Dhandayuthapani, S.3
  • 30
    • 11144298158 scopus 로고    scopus 로고
    • Methionine sulfoxide reduction and assimilation in Escherichia coli: new role for the biotin sulfoxide reductase BisC
    • Ezraty B, Bos J, Barras F, Aussel L, (2005) Methionine sulfoxide reduction and assimilation in Escherichia coli: new role for the biotin sulfoxide reductase BisC. J Bacteriol 187: 231-237.
    • (2005) J Bacteriol , vol.187 , pp. 231-237
    • Ezraty, B.1    Bos, J.2    Barras, F.3    Aussel, L.4
  • 31
    • 72049083705 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase B (MsrB) of Mycobacterium smegmatis plays a limited role in resisting oxidative stress
    • Dhandayuthapani S, Jagannath C, Nino C, Saikolappan S, Sasindran SJ, (2009) Methionine sulfoxide reductase B (MsrB) of Mycobacterium smegmatis plays a limited role in resisting oxidative stress. Tuberculosis (Edinb) 89 (Suppl 1): S26-S32.
    • (2009) Tuberculosis (Edinb) , vol.89 , Issue.SUPPL. 1
    • Dhandayuthapani, S.1    Jagannath, C.2    Nino, C.3    Saikolappan, S.4    Sasindran, S.J.5
  • 32
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage
    • Moskovitz J, Rahman MA, Strassman J, Yancey SO, Kushner SR, et al. (1995) Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J Bacteriol 177: 502-507.
    • (1995) J Bacteriol , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5
  • 33
    • 0035173341 scopus 로고    scopus 로고
    • Molecular characterization of a chromosomal locus in Staphylococcus aureus that contributes to oxidative defence and is highly induced by the cell-wall-active antibiotic oxacillin
    • Singh VK, Moskovitz J, Wilkinson BJ, Jayaswal RK, (2001) Molecular characterization of a chromosomal locus in Staphylococcus aureus that contributes to oxidative defence and is highly induced by the cell-wall-active antibiotic oxacillin. Microbiology 147: 3037-3045.
    • (2001) Microbiology , vol.147 , pp. 3037-3045
    • Singh, V.K.1    Moskovitz, J.2    Wilkinson, B.J.3    Jayaswal, R.K.4
  • 34
    • 78651227092 scopus 로고    scopus 로고
    • The biological significance of methionine sulfoxide stereochemistry
    • Lee BC, Gladyshev VN, (2011) The biological significance of methionine sulfoxide stereochemistry. Free Radic Biol Med 50: 221-227.
    • (2011) Free Radic Biol Med , vol.50 , pp. 221-227
    • Lee, B.C.1    Gladyshev, V.N.2
  • 35
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • Moskovitz J, Singh VK, Requena J, Wilkinson BJ, Jayaswal RK, et al. (2002) Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. Biochem Biophys Res Commun 290: 62-65.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 62-65
    • Moskovitz, J.1    Singh, V.K.2    Requena, J.3    Wilkinson, B.J.4    Jayaswal, R.K.5
  • 36
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL, (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 37
    • 0015449701 scopus 로고
    • Phage P22-mutants with increased or decreased transduction abilities
    • Schmieger H, (1972) Phage P22-mutants with increased or decreased transduction abilities. Mol Gen Genet 119: 75-88.
    • (1972) Mol Gen Genet , vol.119 , pp. 75-88
    • Schmieger, H.1
  • 38
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J, (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 39
    • 0037029629 scopus 로고    scopus 로고
    • Salmonella pathogenicity island 2 mediates protection of intracellular Salmonella from reactive nitrogen intermediates
    • Chakravortty D, Hansen-Wester I, Hensel M, (2002) Salmonella pathogenicity island 2 mediates protection of intracellular Salmonella from reactive nitrogen intermediates. J Exp Med 195: 1155-1166.
    • (2002) J Exp Med , vol.195 , pp. 1155-1166
    • Chakravortty, D.1    Hansen-Wester, I.2    Hensel, M.3


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