메뉴 건너뛰기




Volumn 82, Issue 4, 2011, Pages 952-963

Either periplasmic tethering or protease resistance is sufficient to allow a SodC to protect Salmonella enterica serovar Typhimurium from phagocytic superoxide

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; SUPEROXIDE; SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE C; SUPEROXIDE DISMUTASE CI; SUPEROXIDE DISMUTASE CII; UNCLASSIFIED DRUG;

EID: 80855132841     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07884.x     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 46649107577 scopus 로고    scopus 로고
    • Regulatory and structural differences in the Cu,Zn-superoxide dismutases of Salmonella enterica and their significance for virulence
    • Ammendola, S., Pasquali, P., Pacello, F., Rotilio, G., Castor, M., Libby, S.J., etal. (2008) Regulatory and structural differences in the Cu, Zn-superoxide dismutases of Salmonella enterica and their significance for virulence. J Biol Chem 283: 13688-13699.
    • (2008) J Biol Chem , vol.283 , pp. 13688-13699
    • Ammendola, S.1    Pasquali, P.2    Pacello, F.3    Rotilio, G.4    Castor, M.5    Libby, S.J.6
  • 2
    • 79955043484 scopus 로고    scopus 로고
    • Salmonella detoxifying enzymes are sufficient to cope with the host oxidative burst
    • Aussel, L., Zhao, W., Hebrard, M., Guilhon, A.A., Viala, J.P., Henri, S., etal. (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    Henri, S.6
  • 3
    • 23744504984 scopus 로고    scopus 로고
    • Recognition of antimicrobial peptides by a bacterial sensor kinase
    • Bader, M.W., Sanowar, S., Daley, M.E., Schneider, A.R., Cho, U., Xu, W., etal. (2005) Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 122: 461-472.
    • (2005) Cell , vol.122 , pp. 461-472
    • Bader, M.W.1    Sanowar, S.2    Daley, M.E.3    Schneider, A.R.4    Cho, U.5    Xu, W.6
  • 4
    • 0033534518 scopus 로고    scopus 로고
    • Evolutionary constraints for dimer formation in prokaryotic Cu,Zn superoxide dismutase
    • Bordo, D., Matak, D., Djinovic-Carugo, K., Rosano, C., Pesce, A., Bolognesi, M., etal. (1999) Evolutionary constraints for dimer formation in prokaryotic Cu, Zn superoxide dismutase. J Mol Biol 285: 283-296.
    • (1999) J Mol Biol , vol.285 , pp. 283-296
    • Bordo, D.1    Matak, D.2    Djinovic-Carugo, K.3    Rosano, C.4    Pesce, A.5    Bolognesi, M.6
  • 5
    • 63349084165 scopus 로고    scopus 로고
    • Phagocytic superoxide specifically damages an extracytoplasmic target to inhibit or kill Salmonella
    • Craig, M., and Slauch, J.M. (2009) Phagocytic superoxide specifically damages an extracytoplasmic target to inhibit or kill Salmonella. PLoS ONE 4: e4975.
    • (2009) PLoS ONE , vol.4
    • Craig, M.1    Slauch, J.M.2
  • 6
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 7
    • 0009543864 scopus 로고    scopus 로고
    • Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase
    • De Groote, M.A., Ochsner, U.A., Shiloh, M.U., Nathan, C., McCord, J.M., Dinauer, M.C., etal. (1997) Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase. Proc Natl Acad Sci USA 94: 13997-14001.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13997-14001
    • De Groote, M.A.1    Ochsner, U.A.2    Shiloh, M.U.3    Nathan, C.4    McCord, J.M.5    Dinauer, M.C.6
  • 8
    • 10244226790 scopus 로고    scopus 로고
    • Bacteriophage-encoded type III effectors in Salmonella enterica subspecies 1 serovar Typhimurium
    • Ehrbar, K., and Hardt, W.D. (2005) Bacteriophage-encoded type III effectors in Salmonella enterica subspecies 1 serovar Typhimurium. Infect Genet Evol 5: 1-9.
    • (2005) Infect Genet Evol , vol.5 , pp. 1-9
    • Ehrbar, K.1    Hardt, W.D.2
  • 9
    • 0037094370 scopus 로고    scopus 로고
    • Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria
    • Ellermeier, C.D., Janakiraman, A., and Slauch, J.M. (2002) Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria. Gene 290: 153-161.
    • (2002) Gene , vol.290 , pp. 153-161
    • Ellermeier, C.D.1    Janakiraman, A.2    Slauch, J.M.3
  • 11
    • 0033009419 scopus 로고    scopus 로고
    • Inducible prophages contribute to Salmonella virulence in mice
    • Figueroa-Bossi, N., and Bossi, L. (1999) Inducible prophages contribute to Salmonella virulence in mice. Mol Microbiol 33: 167-176.
    • (1999) Mol Microbiol , vol.33 , pp. 167-176
    • Figueroa-Bossi, N.1    Bossi, L.2
  • 12
    • 0034635343 scopus 로고    scopus 로고
    • Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface
    • Forest, K.T., Langford, P.R., Kroll, J.S., and Getzoff, E.D. (2000) Cu, Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface. J Mol Biol 296: 145-153.
    • (2000) J Mol Biol , vol.296 , pp. 145-153
    • Forest, K.T.1    Langford, P.R.2    Kroll, J.S.3    Getzoff, E.D.4
  • 13
    • 79960418330 scopus 로고    scopus 로고
    • Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution
    • Fricke, W.F., Mammel, M.K., McDermott, P.F., Tartera, C., White, D.G., Leclerc, J.E., etal. (2011) Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution. J Bacteriol 193: 3556-3568.
    • (2011) J Bacteriol , vol.193 , pp. 3556-3568
    • Fricke, W.F.1    Mammel, M.K.2    McDermott, P.F.3    Tartera, C.4    White, D.G.5    Leclerc, J.E.6
  • 15
    • 17644362734 scopus 로고    scopus 로고
    • The Brucella abortus Cu,Zn superoxide dismutase is required for optimal resistance to oxidative killing by murine macrophages and wild-type virulence in experimentally infected mice
    • Gee, J.M., Valderas, M.W., Kovach, M.E., Grippe, V.K., Robertson, G.T., Ng, W.L., etal. (2005) The Brucella abortus Cu, Zn superoxide dismutase is required for optimal resistance to oxidative killing by murine macrophages and wild-type virulence in experimentally infected mice. Infect Immun 73: 2873-2880.
    • (2005) Infect Immun , vol.73 , pp. 2873-2880
    • Gee, J.M.1    Valderas, M.W.2    Kovach, M.E.3    Grippe, V.K.4    Robertson, G.T.5    Ng, W.L.6
  • 16
    • 33751120167 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium periplasmic superoxide dismutase SodCI is a member of the PhoPQ regulon and is induced in macrophages
    • Golubeva, Y.A., and Slauch, J.M. (2006) Salmonella enterica serovar Typhimurium periplasmic superoxide dismutase SodCI is a member of the PhoPQ regulon and is induced in macrophages. J Bacteriol 188: 7853-7861.
    • (2006) J Bacteriol , vol.188 , pp. 7853-7861
    • Golubeva, Y.A.1    Slauch, J.M.2
  • 17
    • 0032934815 scopus 로고    scopus 로고
    • The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli
    • Gort, A.S., Ferber, D.M., and Imlay, J.A. (1999) The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli. Mol Microbiol 32: 179-191.
    • (1999) Mol Microbiol , vol.32 , pp. 179-191
    • Gort, A.S.1    Ferber, D.M.2    Imlay, J.A.3
  • 18
    • 0036776780 scopus 로고    scopus 로고
    • Identification of GtgE, a novel virulence factor encoded on the Gifsy-2 bacteriophage of Salmonella enterica serovar Typhimurium
    • Ho, T.D., Figueroa-Bossi, N., Wang, M., Uzzau, S., Bossi, L., and Slauch, J.M. (2002) Identification of GtgE, a novel virulence factor encoded on the Gifsy-2 bacteriophage of Salmonella enterica serovar Typhimurium. J Bacteriol 184: 5234-5239.
    • (2002) J Bacteriol , vol.184 , pp. 5234-5239
    • Ho, T.D.1    Figueroa-Bossi, N.2    Wang, M.3    Uzzau, S.4    Bossi, L.5    Slauch, J.M.6
  • 19
    • 77950638212 scopus 로고    scopus 로고
    • Protecting from antimicrobial effectors in the phagosome allows SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium
    • Kim, B., Richards, S.M., Gunn, J.S., and Slauch, J.M. (2010) Protecting from antimicrobial effectors in the phagosome allows SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium. J Bacteriol 192: 2140-2149.
    • (2010) J Bacteriol , vol.192 , pp. 2140-2149
    • Kim, B.1    Richards, S.M.2    Gunn, J.S.3    Slauch, J.M.4
  • 20
    • 3843084999 scopus 로고    scopus 로고
    • Differences in enzymatic properties allow SodCI but not SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium strain 14028
    • Krishnakumar, R., Craig, M., Imlay, J.A., and Slauch, J.M. (2004) Differences in enzymatic properties allow SodCI but not SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium strain 14028. J Bacteriol 186: 5230-5238.
    • (2004) J Bacteriol , vol.186 , pp. 5230-5238
    • Krishnakumar, R.1    Craig, M.2    Imlay, J.A.3    Slauch, J.M.4
  • 21
    • 34250348371 scopus 로고    scopus 로고
    • Structural properties of periplasmic SodCI that correlate with virulence in Salmonella enterica serovar Typhimurium
    • Krishnakumar, R., Kim, B., Mollo, E.A., Imlay, J.A., and Slauch, J.M. (2007) Structural properties of periplasmic SodCI that correlate with virulence in Salmonella enterica serovar Typhimurium. J Bacteriol 189: 4343-4352.
    • (2007) J Bacteriol , vol.189 , pp. 4343-4352
    • Krishnakumar, R.1    Kim, B.2    Mollo, E.A.3    Imlay, J.A.4    Slauch, J.M.5
  • 22
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J.M., and Fridovich, I. (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
  • 24
    • 0033023921 scopus 로고    scopus 로고
    • An intracellular iron chelator pleiotropically suppresses enzymatic and growth defects of superoxide dismutase-deficient Escherichia coli
    • Maringanti, S., and Imlay, J.A. (1999) An intracellular iron chelator pleiotropically suppresses enzymatic and growth defects of superoxide dismutase-deficient Escherichia coli. J Bacteriol 181: 3792-3802.
    • (1999) J Bacteriol , vol.181 , pp. 3792-3802
    • Maringanti, S.1    Imlay, J.A.2
  • 25
    • 0034679699 scopus 로고    scopus 로고
    • Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. II. Effects on microbial proliferation and host survival in vivo
    • Mastroeni, P., Vazquez-Torres, A., Fang, F.C., Xu, Y., Khan, S., Hormaeche, C.E., and Dougan, G. (2000) Antimicrobial actions of the NADPH phagocyte oxidase and inducible nitric oxide synthase in experimental salmonellosis. II. Effects on microbial proliferation and host survival in vivo. J Exp Med 192: 237-248.
    • (2000) J Exp Med , vol.192 , pp. 237-248
    • Mastroeni, P.1    Vazquez-Torres, A.2    Fang, F.C.3    Xu, Y.4    Khan, S.5    Hormaeche, C.E.6    Dougan, G.7
  • 26
    • 57449098473 scopus 로고    scopus 로고
    • The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure
    • Mori, M., Jimenez, B., Piccioli, M., Battistoni, A., and Sette, M. (2008) The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure. Biochemistry 47: 12954-12963.
    • (2008) Biochemistry , vol.47 , pp. 12954-12963
    • Mori, M.1    Jimenez, B.2    Piccioli, M.3    Battistoni, A.4    Sette, M.5
  • 27
    • 0034665626 scopus 로고    scopus 로고
    • Functional and crystallographic characterization of Salmonella typhimurium Cu,Zn superoxide dismutase coded by the sodCI virulence gene
    • Pesce, A., Battistoni, A., Stroppolo, M.E., Polizio, F., Nardini, M., Kroll, J.S., etal. (2000) Functional and crystallographic characterization of Salmonella typhimurium Cu, Zn superoxide dismutase coded by the sodCI virulence gene. J Mol Biol 302: 465-478.
    • (2000) J Mol Biol , vol.302 , pp. 465-478
    • Pesce, A.1    Battistoni, A.2    Stroppolo, M.E.3    Polizio, F.4    Nardini, M.5    Kroll, J.S.6
  • 29
    • 79954992063 scopus 로고    scopus 로고
    • How does the oxidative burst of macrophages kill bacteria? Still an open question
    • Slauch, J.M. (2011) How does the oxidative burst of macrophages kill bacteria? Still an open question. Mol Microbiol 80: 580-583.
    • (2011) Mol Microbiol , vol.80 , pp. 580-583
    • Slauch, J.M.1
  • 31
    • 0036033879 scopus 로고    scopus 로고
    • Differential accumulation of Salmonella [Cu, Zn] superoxide dismutases SodCI and SodCII in intracellular bacteria: correlation with their relative contribution to pathogenicity
    • Uzzau, S., Bossi, L., and Figueroa-Bossi, N. (2002) Differential accumulation of Salmonella [Cu, Zn] superoxide dismutases SodCI and SodCII in intracellular bacteria: correlation with their relative contribution to pathogenicity. Mol Microbiol 46: 147-156.
    • (2002) Mol Microbiol , vol.46 , pp. 147-156
    • Uzzau, S.1    Bossi, L.2    Figueroa-Bossi, N.3
  • 32
    • 0025782890 scopus 로고
    • Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli
    • Wang, R.F., and Kushner, S.R. (1991) Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli. Gene 100: 195-199.
    • (1991) Gene , vol.100 , pp. 195-199
    • Wang, R.F.1    Kushner, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.