메뉴 건너뛰기




Volumn 290, Issue 31, 2015, Pages 18967-18974

Microbial copper-binding siderophores at the host-pathogen interface

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; METAL IONS; MICROORGANISMS; MOLECULES;

EID: 84940505431     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R115.644328     Document Type: Review
Times cited : (54)

References (89)
  • 1
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands, J. B. (1995) Siderophores: Structure and function of microbial iron transport compounds. J. Biol. Chem. 270, 26723-26726
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 2
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke, M., and Marahiel, M. A. (2007) Siderophore-based iron acquisition and pathogen control. Microbiol. Mol. Biol. Rev. 71, 413-451
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 5
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands, J. B. (1981) Microbial iron compounds. Annu. Rev. Biochem. 50, 715-731
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 6
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg, A., and Neilands, J. B. (1987) Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26, 5471-5477
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 7
    • 0029806389 scopus 로고    scopus 로고
    • YbtA, an AraCtype regulator of the Yersinia pestis pesticin/yersiniabactin receptor
    • Fetherston, J. D., Bearden, S. W., and Perry, R. D. (1996) YbtA, an AraCtype regulator of the Yersinia pestis pesticin/yersiniabactin receptor. Mol. Microbiol. 22, 315-325
    • (1996) Mol. Microbiol. , vol.22 , pp. 315-325
    • Fetherston, J.D.1    Bearden, S.W.2    Perry, R.D.3
  • 9
    • 0001569222 scopus 로고
    • Coordination chemistry of microbial iron transport compounds 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes
    • 10.1021/ja00514a037
    • Harris, W. R., Carrano, C. J., Cooper, S. R., Sofen, S. R., Avdeef, A. E., McArdle, J. V., and Raymond, K. N. (1979) Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes. J. Am. Chem. Soc. 101, 6097-6104, 10.1021/ja00514a037
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 6097-6104
    • Harris, W.R.1    Carrano, C.J.2    Cooper, S.R.3    Sofen, S.R.4    Avdeef, A.E.5    McArdle, J.V.6    Raymond, K.N.7
  • 11
    • 79960837602 scopus 로고    scopus 로고
    • Yersiniabactin iron uptake: Mechanisms and role in Yersinia pestis pathogenesis
    • Perry, R. D., and Fetherston, J. D. (2011) Yersiniabactin iron uptake: Mechanisms and role in Yersinia pestis pathogenesis. Microbes Infect. 13, 808-817
    • (2011) Microbes Infect. , vol.13 , pp. 808-817
    • Perry, R.D.1    Fetherston, J.D.2
  • 12
    • 0032921490 scopus 로고    scopus 로고
    • YbtP and YbtQ: Two ABC transporters required for iron uptake in Yersinia pestis
    • Fetherston, J. D., Bertolino, V. J., and Perry, R. D. (1999) YbtP and YbtQ: Two ABC transporters required for iron uptake in Yersinia pestis. Mol. Microbiol. 32, 289-299
    • (1999) Mol. Microbiol. , vol.32 , pp. 289-299
    • Fetherston, J.D.1    Bertolino, V.J.2    Perry, R.D.3
  • 13
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: An archetype for microbial iron transport
    • Raymond, K. N., Dertz, E. A., and Kim, S. S. (2003) Enterobactin: An archetype for microbial iron transport. Proc. Natl. Acad. Sci. U.S.A. 100, 3584-3588
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 14
    • 41949113530 scopus 로고    scopus 로고
    • Metal trafficking via siderophores in Gram-negative bacteria: Specificities and characteristics of the pyoverdine pathway
    • Schalk, I. J. (2008) Metal trafficking via siderophores in Gram-negative bacteria: Specificities and characteristics of the pyoverdine pathway. J. Inorg. Biochem. 102, 1159-1169
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1159-1169
    • Schalk, I.J.1
  • 15
    • 0034999145 scopus 로고    scopus 로고
    • Functional analysis of yersiniabactin transport genes of Yersinia enterocolitica
    • Brem, D., Pelludat, C., Rakin, A., Jacobi, C. A., and Heesemann, J. (2001) Functional analysis of yersiniabactin transport genes of Yersinia enterocolitica. Microbiology 147, 1115-1127
    • (2001) Microbiology , vol.147 , pp. 1115-1127
    • Brem, D.1    Pelludat, C.2    Rakin, A.3    Jacobi, C.A.4    Heesemann, J.5
  • 16
    • 30744441922 scopus 로고    scopus 로고
    • Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis
    • Rodriguez, G. M., and Smith, I. (2006) Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J. Bacteriol. 188, 424-430
    • (2006) J. Bacteriol. , vol.188 , pp. 424-430
    • Rodriguez, G.M.1    Smith, I.2
  • 17
    • 84873060682 scopus 로고    scopus 로고
    • The copper supply pathway to a Salmonella Cu,Zn-superoxide dismutase (SodCII) involves P1B-type ATPase copper efflux and periplasmic CueP
    • Osman, D., Patterson, C. J., Bailey, K., Fisher, K., Robinson, N. J., Rigby, S. E., and Cavet, J. S. (2013) The copper supply pathway to a Salmonella Cu,Zn-superoxide dismutase (SodCII) involves P1B-type ATPase copper efflux and periplasmic CueP. Mol. Microbiol. 87, 466-477
    • (2013) Mol. Microbiol. , vol.87 , pp. 466-477
    • Osman, D.1    Patterson, C.J.2    Bailey, K.3    Fisher, K.4    Robinson, N.J.5    Rigby, S.E.6    Cavet, J.S.7
  • 18
    • 0026724913 scopus 로고
    • Overexpression and purification of ferric enterobactin esterase from Escherichia coli: Demonstration of enzymatic hydrolysis of enterobactin and its iron complex
    • Brickman, T. J., and McIntosh, M. A. (1992) Overexpression and purification of ferric enterobactin esterase from Escherichia coli: Demonstration of enzymatic hydrolysis of enterobactin and its iron complex. J. Biol. Chem. 267, 12350-12355
    • (1992) J. Biol. Chem. , vol.267 , pp. 12350-12355
    • Brickman, T.J.1    McIntosh, M.A.2
  • 19
    • 84863899006 scopus 로고    scopus 로고
    • Nutritional immunity: Transition metals at the pathogen-host interface
    • Hood, M. I., and Skaar, E. P. (2012) Nutritional immunity: Transition metals at the pathogen-host interface. Nat. Rev. Microbiol. 10, 525-537
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 525-537
    • Hood, M.I.1    Skaar, E.P.2
  • 20
    • 77951242175 scopus 로고    scopus 로고
    • The yersiniabactin transport system is critical for the pathogenesis of bubonic and pneumonic plague
    • Fetherston, J. D., Kirillina, O., Bobrov, A. G., Paulley, J. T., and Perry, R. D. (2010) The yersiniabactin transport system is critical for the pathogenesis of bubonic and pneumonic plague. Infect. Immun. 78, 2045-2052
    • (2010) Infect. Immun. , vol.78 , pp. 2045-2052
    • Fetherston, J.D.1    Kirillina, O.2    Bobrov, A.G.3    Paulley, J.T.4    Perry, R.D.5
  • 21
    • 34247875921 scopus 로고    scopus 로고
    • Host-pathogen interactions: Can micronutrients tip the balance?
    • Prentice, A. M., Ghattas, H., and Cox, S. E. (2007) Host-pathogen interactions: Can micronutrients tip the balance? J. Nutr. 137, 1334-1337
    • (2007) J. Nutr. , vol.137 , pp. 1334-1337
    • Prentice, A.M.1    Ghattas, H.2    Cox, S.E.3
  • 23
    • 79251526849 scopus 로고    scopus 로고
    • Escherichia coli global gene expression in urine from women with urinary tract infection
    • Hagan, E. C., Lloyd, A. L., Rasko, D. A., Faerber, G. J., and Mobley, H. L. T. (2010) Escherichia coli global gene expression in urine from women with urinary tract infection. PLoS Pathog. 6, e1001187
    • (2010) PLoS Pathog. , vol.6 , pp. e1001187
    • Hagan, E.C.1    Lloyd, A.L.2    Rasko, D.A.3    Faerber, G.J.4    Mobley, H.L.T.5
  • 24
    • 34547121698 scopus 로고    scopus 로고
    • Functional genomic studies of uropathogenic Escherichia coli and host urothelial cells when intracellular bacterial communities are assembled
    • Reigstad, C. S., Hultgren, S. J., and Gordon, J. I. (2007) Functional genomic studies of uropathogenic Escherichia coli and host urothelial cells when intracellular bacterial communities are assembled. J. Biol. Chem. 282, 21259-21267
    • (2007) J. Biol. Chem. , vol.282 , pp. 21259-21267
    • Reigstad, C.S.1    Hultgren, S.J.2    Gordon, J.I.3
  • 26
    • 84896776600 scopus 로고    scopus 로고
    • Metabolomic analysis of siderophore cheater mutants reveals metabolic costs of expression in uropathogenic Escherichia coli
    • Lv, H., Hung, C. S., and Henderson, J. P. (2014) Metabolomic analysis of siderophore cheater mutants reveals metabolic costs of expression in uropathogenic Escherichia coli. J. Proteome Res. 13, 1397-1404
    • (2014) J. Proteome Res. , vol.13 , pp. 1397-1404
    • Lv, H.1    Hung, C.S.2    Henderson, J.P.3
  • 27
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., and Strong, R. K. (2002) The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 10, 1033-1043
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 29
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., and Aderem, A. (2004) Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432, 917-921
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5    Strong, R.K.6    Akira, S.7    Aderem, A.8
  • 31
    • 33745952290 scopus 로고    scopus 로고
    • Enzymatic tailoring of enterobactin alters membrane partitioning and iron acquisition
    • Luo, M., Lin, H., Fischbach, M. A., Liu, D. R., Walsh, C. T., and Groves, J. T. (2006) Enzymatic tailoring of enterobactin alters membrane partitioning and iron acquisition. ACS Chem. Biol. 1, 29-32
    • (2006) ACS Chem. Biol. , vol.1 , pp. 29-32
    • Luo, M.1    Lin, H.2    Fischbach, M.A.3    Liu, D.R.4    Walsh, C.T.5    Groves, J.T.6
  • 32
    • 33750622338 scopus 로고    scopus 로고
    • Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain Nissle 1917
    • Valdebenito, M., Crumbliss, A. L., Winkelmann, G., and Hantke, K. (2006) Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain Nissle 1917. Int. J. Med. Microbiol. 296, 513-520
    • (2006) Int. J. Med. Microbiol. , vol.296 , pp. 513-520
    • Valdebenito, M.1    Crumbliss, A.L.2    Winkelmann, G.3    Hantke, K.4
  • 33
    • 33745945434 scopus 로고    scopus 로고
    • Enterobactin protonation and iron release: Structural characterization of the salicylate coordination shift in ferric enterobactin
    • Abergel, R. J., Warner, J. A., Shuh, D. K., and Raymond, K. N. (2006) Enterobactin protonation and iron release: Structural characterization of the salicylate coordination shift in ferric enterobactin. J. Am. Chem. Soc. 128, 8920-8931
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8920-8931
    • Abergel, R.J.1    Warner, J.A.2    Shuh, D.K.3    Raymond, K.N.4
  • 34
    • 0027488861 scopus 로고
    • Purification of yersiniabactin: A siderophore and possible virulence factor of Yersinia enterocolitica
    • Haag, H., Hantke, K., Drechsel, H., Stojiljkovic, I., Jung, G., and Zähner, H. (1993) Purification of yersiniabactin: A siderophore and possible virulence factor of Yersinia enterocolitica. J. Gen. Microbiol. 139, 2159-2165
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2159-2165
    • Haag, H.1    Hantke, K.2    Drechsel, H.3    Stojiljkovic, I.4    Jung, G.5    Zähner, H.6
  • 35
    • 0027238303 scopus 로고
    • Virulence of Yersinia enterocolitica is closely asso- ciated with siderophore production, expression of an iron-repressible outer membrane polypeptide of 65,000 da and pesticin sensitivity
    • Heesemann, J., Hantke, K., Vocke, T., Saken, E., Rakin, A., Stojiljkovic, I., and Berner, R. (1993) Virulence of Yersinia enterocolitica is closely asso-ciated with siderophore production, expression of an iron-repressible outer membrane polypeptide of 65,000 Da and pesticin sensitivity. Mol. Microbiol. 8, 397-408
    • (1993) Mol. Microbiol. , vol.8 , pp. 397-408
    • Heesemann, J.1    Hantke, K.2    Vocke, T.3    Saken, E.4    Rakin, A.5    Stojiljkovic, I.6    Berner, R.7
  • 37
    • 0344823693 scopus 로고    scopus 로고
    • Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by Fourier transform mass spectrometry: The polyketide module of yersiniabactin synthetase
    • Mazur, M. T., Walsh, C. T., and Kelleher, N. L. (2003) Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by Fourier transform mass spectrometry: The polyketide module of yersiniabactin synthetase. Biochemistry 42, 13393-13400
    • (2003) Biochemistry , vol.42 , pp. 13393-13400
    • Mazur, M.T.1    Walsh, C.T.2    Kelleher, N.L.3
  • 38
    • 0036009334 scopus 로고    scopus 로고
    • Yersiniabactin synthetase: A four-protein assembly line producing the nonribosomal peptide/polyketide hybrid siderophore of Yersinia pestis
    • Miller, D. A., Luo, L., Hillson, N., Keating, T. A., and Walsh, C. T. (2002) Yersiniabactin synthetase: A four-protein assembly line producing the nonribosomal peptide/polyketide hybrid siderophore of Yersinia pestis. Chem. Biol. 9, 333-344
    • (2002) Chem. Biol. , vol.9 , pp. 333-344
    • Miller, D.A.1    Luo, L.2    Hillson, N.3    Keating, T.A.4    Walsh, C.T.5
  • 39
    • 34447561728 scopus 로고    scopus 로고
    • Mobility of the Yersinia High-Pathogenicity Island (HPI): Transfer mechanisms of pathogenicity islands (PAIS) revisited (a review)
    • Benedek, O., and Schubert, S. (2007) Mobility of the Yersinia High-Pathogenicity Island (HPI): Transfer mechanisms of pathogenicity islands (PAIS) revisited (a review). Acta Microbiol. Immunol. Hung. 54, 89-105
    • (2007) Acta Microbiol. Immunol. Hung. , vol.54 , pp. 89-105
    • Benedek, O.1    Schubert, S.2
  • 40
    • 84863192539 scopus 로고    scopus 로고
    • The PvdRT-OpmQ efflux pump controls the metal selectivity of the iron uptake pathway mediated by the siderophore pyoverdine in Pseudomonas aeruginosa
    • Hannauer, M., Braud, A., Hoegy, F., Ronot, P., Boos, A., and Schalk, I. J. (2012) The PvdRT-OpmQ efflux pump controls the metal selectivity of the iron uptake pathway mediated by the siderophore pyoverdine in Pseudomonas aeruginosa. Environ. Microbiol. 14, 1696-1708
    • (2012) Environ. Microbiol. , vol.14 , pp. 1696-1708
    • Hannauer, M.1    Braud, A.2    Hoegy, F.3    Ronot, P.4    Boos, A.5    Schalk, I.J.6
  • 41
    • 84857527566 scopus 로고    scopus 로고
    • Pyochelin, a siderophore of Pseudomonas aeruginosa: Physicochemical characterization of the iron(III), copper(II) and zinc(II) complexes
    • Brandel, J., Humbert, N., Elhabiri, M., Schalk, I. J., Mislin, G. L., and Albrecht-Gary, A. M. (2012) Pyochelin, a siderophore of Pseudomonas aeruginosa: Physicochemical characterization of the iron(III), copper(II) and zinc(II) complexes. Dalton Trans. 41, 2820-2834
    • (2012) Dalton Trans. , vol.41 , pp. 2820-2834
    • Brandel, J.1    Humbert, N.2    Elhabiri, M.3    Schalk, I.J.4    Mislin, G.L.5    Albrecht-Gary, A.M.6
  • 42
    • 84857509084 scopus 로고    scopus 로고
    • Chemistry and biology of the copper chelator methanobactin
    • Kenney, G. E., and Rosenzweig, A. C. (2012) Chemistry and biology of the copper chelator methanobactin. ACS Chem. Biol. 7, 260-268
    • (2012) ACS Chem. Biol. , vol.7 , pp. 260-268
    • Kenney, G.E.1    Rosenzweig, A.C.2
  • 44
    • 0020806506 scopus 로고
    • Iron uptake from ferrichromeAand iron citrate in Ustilago sphaerogena
    • Ecker, D. J., and Emery, T. (1983) Iron uptake from ferrichromeAand iron citrate in Ustilago sphaerogena. J. Bacteriol. 155, 616-622
    • (1983) J. Bacteriol. , vol.155 , pp. 616-622
    • Ecker, D.J.1    Emery, T.2
  • 45
    • 71749115454 scopus 로고    scopus 로고
    • A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity
    • White, C., Lee, J., Kambe, T., Fritsche, K., and Petris, M. J. (2009) A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity. J. Biol. Chem. 284, 33949-33956
    • (2009) J. Biol. Chem. , vol.284 , pp. 33949-33956
    • White, C.1    Lee, J.2    Kambe, T.3    Fritsche, K.4    Petris, M.J.5
  • 46
    • 84918555449 scopus 로고    scopus 로고
    • Copper transport and trafficking at the host-bacterial pathogen interface
    • Fu, Y., Chang, F. M., and Giedroc, D. P. (2014) Copper transport and trafficking at the host-bacterial pathogen interface. Acc. Chem. Res. 47, 3605-3613
    • (2014) Acc. Chem. Res. , vol.47 , pp. 3605-3613
    • Fu, Y.1    Chang, F.M.2    Giedroc, D.P.3
  • 47
    • 0030895052 scopus 로고    scopus 로고
    • Genetic organization of the yersiniabactin biosynthetic region and construction of avirulent mutants in Yersinia pestis
    • Bearden, S. W., Fetherston, J. D., and Perry, R. D. (1997) Genetic organization of the yersiniabactin biosynthetic region and construction of avirulent mutants in Yersinia pestis. Infect. Immun. 65, 1659-1668
    • (1997) Infect. Immun. , vol.65 , pp. 1659-1668
    • Bearden, S.W.1    Fetherston, J.D.2    Perry, R.D.3
  • 48
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman, N. E., and Gitlin, J. D. (2002) Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22, 439-458
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 49
    • 84862649408 scopus 로고    scopus 로고
    • Urinary copper elevation in a mouse model of Wilson's disease is a regulated process to specifically decrease the hepatic copper load
    • Gray, L. W., Peng, F., Molloy, S. A., Pendyala, V. S., Muchenditsi, A., Muzik, O., Lee, J., Kaplan, J. H., and Lutsenko, S. (2012) Urinary copper elevation in a mouse model of Wilson's disease is a regulated process to specifically decrease the hepatic copper load. PLoS One 7, e38327
    • (2012) PLoS One , vol.7 , pp. e38327
    • Gray, L.W.1    Peng, F.2    Molloy, S.A.3    Pendyala, V.S.4    Muchenditsi, A.5    Muzik, O.6    Lee, J.7    Kaplan, J.H.8    Lutsenko, S.9
  • 50
    • 0025058305 scopus 로고
    • The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships
    • 10.1111/j.1432-1033. 1990.tb15311.x
    • Messerschmidt, A., and Huber, R. (1990) The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Eur. J. Biochem. 187, 341-352, 10.1111/j.1432-1033.1990.tb15311.x
    • (1990) Eur. J. Biochem. , vol.187 , pp. 341-352
    • Messerschmidt, A.1    Huber, R.2
  • 53
    • 44449115227 scopus 로고    scopus 로고
    • Comparative genomic analyses of copper transporters and cuproproteomes reveal evolutionary dynamics of copper utilization and its link to oxygen
    • Ridge, P. G., Zhang, Y., and Gladyshev, V. N. (2008) Comparative genomic analyses of copper transporters and cuproproteomes reveal evolutionary dynamics of copper utilization and its link to oxygen. PLoS One 3, e1378
    • (2008) PLoS One , vol.3 , pp. e1378
    • Ridge, P.G.1    Zhang, Y.2    Gladyshev, V.N.3
  • 54
    • 79959872475 scopus 로고    scopus 로고
    • Comparative genomics of trace element dependence in biology
    • Zhang, Y., and Gladyshev, V. N. (2011) Comparative genomics of trace element dependence in biology. J. Biol. Chem. 286, 23623-23629
    • (2011) J. Biol. Chem. , vol.286 , pp. 23623-23629
    • Zhang, Y.1    Gladyshev, V.N.2
  • 56
    • 34547516631 scopus 로고    scopus 로고
    • Methane monooxygenase gene expression mediated by methanobactin in the presence of mineral copper sources
    • Knapp, C. W., Fowle, D. A., Kulczycki, E., Roberts, J. A., and Graham, D. W. (2007) Methane monooxygenase gene expression mediated by methanobactin in the presence of mineral copper sources. Proc. Natl. Acad. Sci. U.S.A. 104, 12040-12045
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12040-12045
    • Knapp, C.W.1    Fowle, D.A.2    Kulczycki, E.3    Roberts, J.A.4    Graham, D.W.5
  • 57
    • 80054823349 scopus 로고    scopus 로고
    • Dual pathways for copper uptake by methanotrophic bacteria
    • Balasubramanian, R., Kenney, G. E., and Rosenzweig, A. C. (2011) Dual pathways for copper uptake by methanotrophic bacteria. J. Biol. Chem. 286, 37313-37319
    • (2011) J. Biol. Chem. , vol.286 , pp. 37313-37319
    • Balasubramanian, R.1    Kenney, G.E.2    Rosenzweig, A.C.3
  • 58
    • 83455196180 scopus 로고    scopus 로고
    • Aminobenzoates as building blocks for natural product assembly lines
    • Walsh, C. T., Haynes, S. W., and Ames, B. D. (2012) Aminobenzoates as building blocks for natural product assembly lines. Nat. Prod. Rep. 29, 37-59
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 37-59
    • Walsh, C.T.1    Haynes, S.W.2    Ames, B.D.3
  • 59
    • 33746867123 scopus 로고    scopus 로고
    • Crystal structure of ferric-yersiniabactin, a virulence factor of Yersinia pestis
    • Miller, M. C., Parkin, S., Fetherston, J. D., Perry, R. D., and Demoll, E. (2006) Crystal structure of ferric-yersiniabactin, a virulence factor of Yersinia pestis. J. Inorg. Biochem. 100, 1495-1500
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 1495-1500
    • Miller, M.C.1    Parkin, S.2    Fetherston, J.D.3    Perry, R.D.4    DeMoll, E.5
  • 62
    • 84931091151 scopus 로고    scopus 로고
    • Metal selectivity by the virulence-associated yersiniabactin metallophore system
    • Koh, E. I., Hung, C. S., Parker, K. S., Crowley, J. R., Giblin, D. E., and Henderson, J. P. (2015) Metal selectivity by the virulence-associated yersiniabactin metallophore system. Metallomics 7, 1011-1022
    • (2015) Metallomics , vol.7 , pp. 1011-1022
    • Koh, E.I.1    Hung, C.S.2    Parker, K.S.3    Crowley, J.R.4    Giblin, D.E.5    Henderson, J.P.6
  • 64
    • 84860012637 scopus 로고    scopus 로고
    • Copper homeostasis at the hostpathogen interface
    • Hodgkinson, V., and Petris, M. J. (2012) Copper homeostasis at the hostpathogen interface. J. Biol. Chem. 287, 13549-13555
    • (2012) J. Biol. Chem. , vol.287 , pp. 13549-13555
    • Hodgkinson, V.1    Petris, M.J.2
  • 65
    • 0026904263 scopus 로고
    • Interaction of nutrition and infection: Effect of copper deficiency on resistance to Trypanosoma lewisi
    • Crocker, A., Lee, C., Aboko-Cole, G., and Durham, C. (1992) Interaction of nutrition and infection: Effect of copper deficiency on resistance to Trypanosoma lewisi. J. Natl. Med. Assoc. 84, 697-706
    • (1992) J. Natl. Med. Assoc. , vol.84 , pp. 697-706
    • Crocker, A.1    Lee, C.2    Aboko-Cole, G.3    Durham, C.4
  • 66
    • 0027498899 scopus 로고
    • Changes in the total content of iron, copper, and zinc in serum, heart, liver, spleen, and skeletal muscle tissues of rats infected with Trypanosoma cruzi
    • Matousek De Abel De La Cruz, A. J., Burguera, J. L., Burguera, M., and An?ez, N. (1993) Changes in the total content of iron, copper, and zinc in serum, heart, liver, spleen, and skeletal muscle tissues of rats infected with Trypanosoma cruzi. Biol. Trace Elem. Res. 37, 51-70
    • (1993) Biol. Trace Elem. Res. , vol.37 , pp. 51-70
    • Matousek De Abel De La Cruz, A.J.1    Burguera, J.L.2    Burguera, M.3    Anez, N.4
  • 67
    • 0037298986 scopus 로고    scopus 로고
    • Sequential changes in Fe Cu, and Zn in target organs during early Coxsackievirus B3 infection in mice
    • Ilbäck, N. G., Benyamin, G., Lindh, U., and Friman, G. (2003) Sequential changes in Fe, Cu, and Zn in target organs during early Coxsackievirus B3 infection in mice. Biol. Trace Elem. Res. 91, 111-124
    • (2003) Biol. Trace Elem. Res. , vol.91 , pp. 111-124
    • Ilbäck, N.G.1    Benyamin, G.2    Lindh, U.3    Friman, G.4
  • 68
    • 0024101816 scopus 로고
    • Effects of Escherichia coli on iron, copper, and zinc metabolism in chicks
    • Tufft, L. S., Nockels, C. F., and Fettman, M. J. (1988) Effects of Escherichia coli on iron, copper, and zinc metabolism in chicks. Avian Dis. 32, 779-786
    • (1988) Avian Dis. , vol.32 , pp. 779-786
    • Tufft, L.S.1    Nockels, C.F.2    Fettman, M.J.3
  • 69
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing
    • Winterbourn, C. C., Hampton, M. B., Livesey, J. H., and Kettle, A. J. (2006) Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing. J. Biol. Chem. 281, 39860-39869
    • (2006) J. Biol. Chem. , vol.281 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 70
    • 0029836110 scopus 로고    scopus 로고
    • Large-scale isolation of candidate virulence genes of Pseudomonas aeruginosa by in vivo selection
    • Wang, J., Mushegian, A., Lory, S., and Jin, S. (1996) Large-scale isolation of candidate virulence genes of Pseudomonas aeruginosa by in vivo selection. Proc. Natl. Acad. Sci. U.S.A. 93, 10434-10439
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10434-10439
    • Wang, J.1    Mushegian, A.2    Lory, S.3    Jin, S.4
  • 71
    • 0037076382 scopus 로고    scopus 로고
    • Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa
    • Lamont, I. L., Beare, P. A., Ochsner, U., Vasil, A. I., and Vasil, M. L. (2002) Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U.S.A. 99, 7072-7077
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7072-7077
    • Lamont, I.L.1    Beare, P.A.2    Ochsner, U.3    Vasil, A.I.4    Vasil, M.L.5
  • 72
    • 78649732156 scopus 로고    scopus 로고
    • Presence of the siderophores pyoverdine and pyochelin in the extracellular medium reduces toxic metal accumulation in Pseudomonas aeruginosa and increases bacterial metal tolerance
    • Braud, A., Geoffroy, V., Hoegy, F., Mislin, G. L., and Schalk, I. J. (2010) Presence of the siderophores pyoverdine and pyochelin in the extracellular medium reduces toxic metal accumulation in Pseudomonas aeruginosa and increases bacterial metal tolerance. Environ. Microbiol. Rep. 2, 419-425
    • (2010) Environ. Microbiol. Rep. , vol.2 , pp. 419-425
    • Braud, A.1    Geoffroy, V.2    Hoegy, F.3    Mislin, G.L.4    Schalk, I.J.5
  • 73
    • 22544432254 scopus 로고    scopus 로고
    • Mutations in the cueA gene encoding a copper homeostasis P-type ATPase reduce the pathogenicity of Pseudomonas aeruginosa in mice
    • Schwan, W. R., Warrener, P., Keunz, E., Stover, C. K., and Folger, K. R. (2005) Mutations in the cueA gene encoding a copper homeostasis P-type ATPase reduce the pathogenicity of Pseudomonas aeruginosa in mice. Int. J. Med. Microbiol. 295, 237-242
    • (2005) Int. J. Med. Microbiol. , vol.295 , pp. 237-242
    • Schwan, W.R.1    Warrener, P.2    Keunz, E.3    Stover, C.K.4    Folger, K.R.5
  • 74
    • 4344580278 scopus 로고    scopus 로고
    • Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli
    • Grass, G., Thakali, K., Klebba, P. E., Thieme, D., Müller, A., Wildner, G. F., and Rensing, C. (2004) Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli. J. Bacteriol. 186, 5826-5833
    • (2004) J. Bacteriol. , vol.186 , pp. 5826-5833
    • Grass, G.1    Thakali, K.2    Klebba, P.E.3    Thieme, D.4    Müller, A.5    Wildner, G.F.6    Rensing, C.7
  • 75
    • 0035903128 scopus 로고    scopus 로고
    • The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli
    • Outten, F. W., Huffman, D. L., Hale, J. A., and O'Halloran, T. V. (2001) The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J. Biol. Chem. 276, 30670-30677
    • (2001) J. Biol. Chem. , vol.276 , pp. 30670-30677
    • Outten, F.W.1    Huffman, D.L.2    Hale, J.A.3    O'Halloran, T.V.4
  • 76
    • 0017068538 scopus 로고
    • Copper toxicity: Evidence for the conversion of cupric to cuprous copper in vivo under anaerobic conditions
    • Beswick, P. H., Hall, G. H., Hook, A. J., Little, K., McBrien, D. C., and Lott, K. A. (1976) Copper toxicity: Evidence for the conversion of cupric to cuprous copper in vivo under anaerobic conditions. Chem. Biol. Interact. 14, 347-356
    • (1976) Chem. Biol. Interact. , vol.14 , pp. 347-356
    • Beswick, P.H.1    Hall, G.H.2    Hook, A.J.3    Little, K.4    McBrien, D.C.5    Lott, K.A.6
  • 77
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber, L., Rensing, C., and Imlay, J. A. (2007) Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J. Bacteriol. 189, 1616-1626
    • (2007) J. Bacteriol. , vol.189 , pp. 1616-1626
    • Macomber, L.1    Rensing, C.2    Imlay, J.A.3
  • 78
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber, L., and Imlay, J. A. (2009) The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. Proc. Natl. Acad. Sci. U.S.A. 106, 8344-8349
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 79
    • 77952056332 scopus 로고    scopus 로고
    • Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis
    • Chillappagari, S., Seubert, A., Trip, H., Kuipers, O. P., Marahiel, M. A., and Miethke, M. (2010) Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis. J. Bacteriol. 192, 2512-2524
    • (2010) J. Bacteriol. , vol.192 , pp. 2512-2524
    • Chillappagari, S.1    Seubert, A.2    Trip, H.3    Kuipers, O.P.4    Marahiel, M.A.5    Miethke, M.6
  • 80
    • 84886505032 scopus 로고    scopus 로고
    • Antimicrobial action of copper is amplified via inhibition of heme biosynthesis
    • Djoko, K. Y., and McEwan, A. G. (2013) Antimicrobial action of copper is amplified via inhibition of heme biosynthesis. ACS Chem. Biol. 8, 2217-2223
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2217-2223
    • Djoko, K.Y.1    McEwan, A.G.2
  • 81
    • 84858974142 scopus 로고    scopus 로고
    • Glutathione is a key player in metal-induced oxidative stress defenses
    • Jozefczak, M., Remans, T., Vangronsveld, J., and Cuypers, A. (2012) Glutathione is a key player in metal-induced oxidative stress defenses. Int. J. Mol. Sci. 13, 3145-3175
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 3145-3175
    • Jozefczak, M.1    Remans, T.2    Vangronsveld, J.3    Cuypers, A.4
  • 82
    • 84861138966 scopus 로고    scopus 로고
    • Silver(I), mercury(II), cadmium(II), and zinc(II) target exposed enzymic iron-sulfur clusters when they toxify Escherichia coli
    • Xu, F. F., and Imlay, J. A. (2012) Silver(I), mercury(II), cadmium(II), and zinc(II) target exposed enzymic iron-sulfur clusters when they toxify Escherichia coli. Appl. Environ. Microbiol. 78, 3614-3621
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 3614-3621
    • Xu, F.F.1    Imlay, J.A.2
  • 84
    • 0021158356 scopus 로고
    • The role of oxygen and its derivatives in microbial pathogenesis and host defense
    • Beaman, L., and Beaman, B. L. (1984) The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annu. Rev. Microbiol. 38, 27-48
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 27-48
    • Beaman, L.1    Beaman, B.L.2
  • 86
    • 77950638212 scopus 로고    scopus 로고
    • Protecting against 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 against 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
  • 88
    • 84863875650 scopus 로고    scopus 로고
    • Mycobacteria and the intraphagosomal environment: Take it with a pinch of salt(s)!
    • Soldati, T., and Neyrolles, O. (2012) Mycobacteria and the intraphagosomal environment: Take it with a pinch of salt(s)! Traffic 13, 1042-1052
    • (2012) Traffic , vol.13 , pp. 1042-1052
    • Soldati, T.1    Neyrolles, O.2
  • 89
    • 84885386368 scopus 로고    scopus 로고
    • Regulation of the NADPHoxidase and associated ion fluxes during phagocytosis
    • Nunes, P., Demaurex, N., and Dinauer, M. C. (2013) Regulation of the NADPHoxidase and associated ion fluxes during phagocytosis. Traffic 14, 1118-1131
    • (2013) Traffic , vol.14 , pp. 1118-1131
    • Nunes, P.1    Demaurex, N.2    Dinauer, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.