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Volumn 81, Issue 8, 2013, Pages 2743-2752

Manganese and zinc regulate virulence determinants in borrelia burgdorferi

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MANGANESE; MESSENGER RNA; OUTER SURFACE PROTEIN C; SIGMA FACTOR RPOS; UNCLASSIFIED DRUG; VIRULENCE FACTOR; ZINC ION;

EID: 84879745505     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00507-13     Document Type: Article
Times cited : (40)

References (100)
  • 4
    • 0033984294 scopus 로고    scopus 로고
    • Temporal changes in outer surface proteins A and C of the Lyme disease-associated spirochete, Borrelia burgdorferi, during the chain of infection in ticks and mice
    • Schwan TG, Piesman J. 2000. Temporal changes in outer surface proteins A and C of the Lyme disease-associated spirochete, Borrelia burgdorferi, during the chain of infection in ticks and mice. J. Clin. Microbiol. 38:382-388.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 382-388
    • Schwan, T.G.1    Piesman, J.2
  • 5
    • 13444293534 scopus 로고    scopus 로고
    • The burgeoning molecular genetics of the Lyme disease spirochaete
    • Rosa PA, Tilly K, Stewart PE. 2005. The burgeoning molecular genetics of the Lyme disease spirochaete. Nat. Rev. Microbiol. 3:129-143.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 129-143
    • Rosa, P.A.1    Tilly, K.2    Stewart, P.E.3
  • 6
    • 80053278392 scopus 로고    scopus 로고
    • Gene regulation in Borrelia burgdorferi
    • Samuels DS. 2011. Gene regulation in Borrelia burgdorferi. Annu. Rev. Microbiol. 65:479-499.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 479-499
    • Samuels, D.S.1
  • 7
    • 84855900042 scopus 로고    scopus 로고
    • Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes
    • Radolf JD, Caimano MJ, Stevenson B, Hu LT. 2012. Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes. Nat. Rev. Microbiol. 10:87-99.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 87-99
    • Radolf, J.D.1    Caimano, M.J.2    Stevenson, B.3    Hu, L.T.4
  • 8
    • 0030025949 scopus 로고    scopus 로고
    • Borrelia burgdorferi OspA is an arthropod-specific transmission-blocking Lyme disease vaccine
    • de Silva AM, Telford SR, III, Brunet LR, Barthold SW, Fikrig E. 1996. Borrelia burgdorferi OspA is an arthropod-specific transmission-blocking Lyme disease vaccine. J. Exp. Med. 183:271-275.
    • (1996) J. Exp. Med. , vol.183 , pp. 271-275
    • de Silva, A.M.1    Telford III, S.R.2    Brunet, L.R.3    Barthold, S.W.4    Fikrig, E.5
  • 9
    • 0030048119 scopus 로고    scopus 로고
    • Direct demonstration of antigenic substitution of Borrelia burgdorferi ex vivo: exploration of the paradox of the early immune response to outer surface proteins A and C in Lyme disease
    • Montgomery RR, Malawista SE, Feen KJ, Bockenstedt LK. 1996. Direct demonstration of antigenic substitution of Borrelia burgdorferi ex vivo: exploration of the paradox of the early immune response to outer surface proteins A and C in Lyme disease. J. Exp. Med. 183:261-269.
    • (1996) J. Exp. Med. , vol.183 , pp. 261-269
    • Montgomery, R.R.1    Malawista, S.E.2    Feen, K.J.3    Bockenstedt, L.K.4
  • 12
    • 1542283705 scopus 로고    scopus 로고
    • Essential role for OspA/B in the life cycle of the Lyme disease spirochete
    • Yang XF, Pal U, Alani SM, Fikrig E, Norgard MV. 2004. Essential role for OspA/B in the life cycle of the Lyme disease spirochete. J. Exp. Med. 199:641-648.
    • (2004) J. Exp. Med. , vol.199 , pp. 641-648
    • Yang, X.F.1    Pal, U.2    Alani, S.M.3    Fikrig, E.4    Norgard, M.V.5
  • 14
    • 0035895241 scopus 로고    scopus 로고
    • Antigenic and genetic heterogeneity of Borrelia burgdorferi populations transmitted by ticks
    • Ohnishi J, Piesman J, de Silva AM. 2001. Antigenic and genetic heterogeneity of Borrelia burgdorferi populations transmitted by ticks. Proc. Natl. Acad. Sci. U. S. A. 98:670-675.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 670-675
    • Ohnishi, J.1    Piesman, J.2    de Silva, A.M.3
  • 18
    • 33847716302 scopus 로고    scopus 로고
    • Complementation of a Borrelia afzelii OspC mutant highlights the crucial role of OspC for dissemination of Borrelia afzelii in Ixodes ricinus
    • Fingerle V, Goettner G, Gern L, Wilske B, Schulte-Spechtel U. 2007. Complementation of a Borrelia afzelii OspC mutant highlights the crucial role of OspC for dissemination of Borrelia afzelii in Ixodes ricinus. Int. J. Med. Microbiol. 297:97-107.
    • (2007) Int. J. Med. Microbiol. , vol.297 , pp. 97-107
    • Fingerle, V.1    Goettner, G.2    Gern, L.3    Wilske, B.4    Schulte-Spechtel, U.5
  • 22
    • 33947427165 scopus 로고    scopus 로고
    • Evidence that RpoS (sigmaS) in Borrelia burgdorferi is controlled directly by RpoN (sigma54/sigmaN)
    • Smith AH, Blevins JS, Bachlani GN, Yang XF, Norgard MV. 2007. Evidence that RpoS (sigmaS) in Borrelia burgdorferi is controlled directly by RpoN (sigma54/sigmaN). J. Bacteriol. 189:2139-2144.
    • (2007) J. Bacteriol. , vol.189 , pp. 2139-2144
    • Smith, A.H.1    Blevins, J.S.2    Bachlani, G.N.3    Yang, X.F.4    Norgard, M.V.5
  • 23
    • 34547879640 scopus 로고    scopus 로고
    • Analysis of the RpoS regulon in Borrelia burgdorferi in response to mammalian host signals provides insight into RpoS function during the enzootic cycle
    • Caimano MJ, Iyer R, Eggers CH, Gonzalez C, Morton EA, Gilbert MA, Schwartz I, Radolf JD. 2007. Analysis of the RpoS regulon in Borrelia burgdorferi in response to mammalian host signals provides insight into RpoS function during the enzootic cycle. Mol. Microbiol. 65:1193-1217.
    • (2007) Mol. Microbiol. , vol.65 , pp. 1193-1217
    • Caimano, M.J.1    Iyer, R.2    Eggers, C.H.3    Gonzalez, C.4    Morton, E.A.5    Gilbert, M.A.6    Schwartz, I.7    Radolf, J.D.8
  • 24
    • 53449090658 scopus 로고    scopus 로고
    • Transcriptional interplay among the regulators Rrp2, RpoN, and RpoS in Borrelia burgdorferi
    • Ouyang Z, Blevins JS, Norgard MV. 2008. Transcriptional interplay among the regulators Rrp2, RpoN, and RpoS in Borrelia burgdorferi. Microbiology 154:2641-2658.
    • (2008) Microbiology , vol.154 , pp. 2641-2658
    • Ouyang, Z.1    Blevins, J.S.2    Norgard, M.V.3
  • 25
    • 51949106515 scopus 로고    scopus 로고
    • Essential role of the response regulator Rrp2 in the infectious cycle of Borrelia burgdorferi
    • Boardman BK, He M, Ouyang Z, Xu H, Pang X, Yang XF. 2008. Essential role of the response regulator Rrp2 in the infectious cycle of Borrelia burgdorferi. Infect. Immun. 76:3844-3853.
    • (2008) Infect. Immun. , vol.76 , pp. 3844-3853
    • Boardman, B.K.1    He, M.2    Ouyang, Z.3    Xu, H.4    Pang, X.5    Yang, X.F.6
  • 26
    • 34248398787 scopus 로고    scopus 로고
    • Temperature-induced regulation of RpoS by a small RNA in Borrelia burgdorferi
    • Lybecker MC, Samuels DS. 2007. Temperature-induced regulation of RpoS by a small RNA in Borrelia burgdorferi. Mol. Microbiol. 64:1075-1089.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1075-1089
    • Lybecker, M.C.1    Samuels, D.S.2
  • 27
    • 77958605759 scopus 로고    scopus 로고
    • Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Bor-relia burgdorferi
    • Lybecker MC, Abel CA, Feig AL, Samuels DS. 2010. Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Bor-relia burgdorferi. Mol. Microbiol. 78:622-635.
    • (2010) Mol. Microbiol. , vol.78 , pp. 622-635
    • Lybecker, M.C.1    Abel, C.A.2    Feig, A.L.3    Samuels, D.S.4
  • 28
    • 7044233312 scopus 로고    scopus 로고
    • RpoS is not central to the general stress response in Borrelia burgdorferi but does control expression of one or more essential virulence determinants
    • Caimano MJ, Eggers CH, Hazlett KR, Radolf JD. 2004. RpoS is not central to the general stress response in Borrelia burgdorferi but does control expression of one or more essential virulence determinants. Infect. Immun. 72:6433-6445.
    • (2004) Infect. Immun. , vol.72 , pp. 6433-6445
    • Caimano, M.J.1    Eggers, C.H.2    Hazlett, K.R.3    Radolf, J.D.4
  • 29
    • 0141482029 scopus 로고    scopus 로고
    • Borrelia oxidative stress response regulator, BosR: a distinctive Zn-dependent transcriptional activator
    • Boylan JA, Posey JE, Gherardini FC. 2003. Borrelia oxidative stress response regulator, BosR: a distinctive Zn-dependent transcriptional activator. Proc. Natl. Acad. Sci. U. S. A. 100:11684-11689.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11684-11689
    • Boylan, J.A.1    Posey, J.E.2    Gherardini, F.C.3
  • 31
    • 72049101202 scopus 로고    scopus 로고
    • The BosR regulatory protein of Borrelia burgdorferi interfaces with the RpoS regulatory pathway and modulates both the oxidative stress response and pathogenic properties of the Lyme disease spirochete
    • Hyde JA, Shaw DK, Smith Iii R, Trzeciakowski JP, Skare JT. 2009. The BosR regulatory protein of Borrelia burgdorferi interfaces with the RpoS regulatory pathway and modulates both the oxidative stress response and pathogenic properties of the Lyme disease spirochete. Mol. Microbiol. 74:1344-1355.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1344-1355
    • Hyde, J.A.1    Shaw, D.K.2    Smith Iii, R.3    Trzeciakowski, J.P.4    Skare, J.T.5
  • 33
    • 72049132926 scopus 로고    scopus 로고
    • Who is the BosR around here anyway?
    • Samuels DS, Radolf JD. 2009. Who is the BosR around here anyway? Mol. Microbiol. 74:1295-1299.
    • (2009) Mol. Microbiol. , vol.74 , pp. 1295-1299
    • Samuels, D.S.1    Radolf, J.D.2
  • 35
    • 1342323757 scopus 로고    scopus 로고
    • Dissolved oxygen levels alter gene expression and antigen profiles in Borrelia burgdorferi
    • Seshu J, Boylan JA, Gherardini FC, Skare JT. 2004. Dissolved oxygen levels alter gene expression and antigen profiles in Borrelia burgdorferi. Infect. Immun. 72:1580-1586.
    • (2004) Infect. Immun. , vol.72 , pp. 1580-1586
    • Seshu, J.1    Boylan, J.A.2    Gherardini, F.C.3    Skare, J.T.4
  • 36
    • 33645056190 scopus 로고    scopus 로고
    • Borrelia burgdorferi bb0728 encodes a coenzyme A disulphide reductase whose function suggests a role in in-tracellular redox and the oxidative stress response
    • Boylan JA, Hummel CS, Benoit S, Garcia-Lara J, Treglown-Downey J, Crane EJ, III, Gherardini FC. 2006. Borrelia burgdorferi bb0728 encodes a coenzyme A disulphide reductase whose function suggests a role in in-tracellular redox and the oxidative stress response. Mol. Microbiol. 59: 475-486.
    • (2006) Mol. Microbiol. , vol.59 , pp. 475-486
    • Boylan, J.A.1    Hummel, C.S.2    Benoit, S.3    Garcia-Lara, J.4    Treglown-Downey, J.5    Crane III, E.J.6    Gherardini, F.C.7
  • 37
    • 0033912262 scopus 로고    scopus 로고
    • The bacterial enhancer-dependent sigma 54 (sigma N) transcription factor
    • Buck M, Gallegos MT, Studholme DJ, Guo Y, Gralla JD. 2000. The bacterial enhancer-dependent sigma 54 (sigma N) transcription factor. J. Bacteriol. 182:4129-4136.
    • (2000) J. Bacteriol. , vol.182 , pp. 4129-4136
    • Buck, M.1    Gallegos, M.T.2    Studholme, D.J.3    Guo, Y.4    Gralla, J.D.5
  • 40
    • 39749161043 scopus 로고    scopus 로고
    • Differential role of ferritins in iron metabolism and virulence of the plant-pathogenic bacterium Erwinia chrysanthemi 3937
    • Boughammoura A, Matzanke BF, Bottger L, Reverchon S, Lesuisse E, Expert D, Franza T. 2008. Differential role of ferritins in iron metabolism and virulence of the plant-pathogenic bacterium Erwinia chrysanthemi 3937. J. Bacteriol. 190:1518-1530.
    • (2008) J. Bacteriol. , vol.190 , pp. 1518-1530
    • Boughammoura, A.1    Matzanke, B.F.2    Bottger, L.3    Reverchon, S.4    Lesuisse, E.5    Expert, D.6    Franza, T.7
  • 41
    • 79952237303 scopus 로고    scopus 로고
    • BosR (BB0647) controls the RpoN-RpoS regulatory pathway and virulence expression in Borrelia burgdorferi by a novel DNA-binding mechanism
    • doi: 10.1371/journal.ppat.1001272
    • Ouyang Z, Deka RK, Norgard MV. 2011. BosR (BB0647) controls the RpoN-RpoS regulatory pathway and virulence expression in Borrelia burgdorferi by a novel DNA-binding mechanism. PLoS Pathog. 7:e1001272. doi: 10.1371/journal.ppat.1001272.
    • (2011) PLoS Pathog. , vol.7
    • Ouyang, Z.1    Deka, R.K.2    Norgard, M.V.3
  • 42
    • 0029671310 scopus 로고    scopus 로고
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence
    • 2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84: 165-174.
    • (1996) Cell , vol.84 , pp. 165-174
    • Garcia Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 43
    • 38749084963 scopus 로고    scopus 로고
    • Fur regulates expression of the Salmonella pathogenicity island 1 type III secretion system through HilD
    • Ellermeier JR, Slauch JM. 2008. Fur regulates expression of the Salmonella pathogenicity island 1 type III secretion system through HilD. J. Bacteriol. 190:476-486.
    • (2008) J. Bacteriol. , vol.190 , pp. 476-486
    • Ellermeier, J.R.1    Slauch, J.M.2
  • 44
    • 78650868303 scopus 로고    scopus 로고
    • Fur negatively regulates hns and is required for the expression of HilA and virulence in Salmonella enterica serovar Typhimu-rium
    • Troxell B, Sikes ML, Fink RC, Vazquez-Torres A, Jones-Carson J, Hassan HM. 2011. Fur negatively regulates hns and is required for the expression of HilA and virulence in Salmonella enterica serovar Typhimu-rium. J. Bacteriol. 193:497-505.
    • (2011) J. Bacteriol. , vol.193 , pp. 497-505
    • Troxell, B.1    Sikes, M.L.2    Fink, R.C.3    Vazquez-Torres, A.4    Jones-Carson, J.5    Hassan, H.M.6
  • 45
    • 79955815576 scopus 로고    scopus 로고
    • Fur activates the expression of Salmonella enterica pathogenicity island 1 by directly interacting with the hilD operator in vivo and in vitro
    • doi: 10.1371/journal.pone.0019711
    • Teixido L, Carrasco B, Alonso JC, Barbe J, Campoy S. 2011. Fur activates the expression of Salmonella enterica pathogenicity island 1 by directly interacting with the hilD operator in vivo and in vitro. PLoS One 6:e19711. doi: 10.1371/journal.pone.0019711.
    • (2011) PLoS One , vol.6
    • Teixido, L.1    Carrasco, B.2    Alonso, J.C.3    Barbe, J.4    Campoy, S.5
  • 49
    • 62549151384 scopus 로고    scopus 로고
    • A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi
    • Ouyang Z, He M, Oman T, Yang XF, Norgard MV. 2009. A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi. Proc. Natl. Acad. Sci. U. S. A. 106:3449-3454.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3449-3454
    • Ouyang, Z.1    He, M.2    Oman, T.3    Yang, X.F.4    Norgard, M.V.5
  • 51
    • 0029200874 scopus 로고
    • Electrotransformationofthe Spirochete Borrelia burgdorferi
    • In NickoloffJA (ed), Humana Press, Totowa, NJ
    • Samuels DS. 1995. Electrotransformationofthe Spirochete Borrelia burgdorferi, p 253-259. In NickoloffJA (ed), Methods in molecular biology. Humana Press, Totowa, NJ.
    • (1995) Methods in molecular biology , pp. 253-259
    • Samuels, D.S.1
  • 53
    • 0021671855 scopus 로고
    • Isolation and cultivation of Lyme disease spirochetes
    • Barbour AG. 1984. Isolation and cultivation of Lyme disease spirochetes. Yale J. Biol. Med. 57:521-525.
    • (1984) Yale J. Biol. Med. , vol.57 , pp. 521-525
    • Barbour, A.G.1
  • 54
    • 84861724029 scopus 로고    scopus 로고
    • Borrelia burgdorferi, a pathogen that lacks iron, encodes a manganese-dependent superoxide dismutase essential for resistance to streptonigrin
    • Troxell B, Xu H, Yang XF. 2012. Borrelia burgdorferi, a pathogen that lacks iron, encodes a manganese-dependent superoxide dismutase essential for resistance to streptonigrin. J. Biol. Chem. 287:19284-19293.
    • (2012) J. Biol. Chem. , vol.287 , pp. 19284-19293
    • Troxell, B.1    Xu, H.2    Yang, X.F.3
  • 55
    • 0032523936 scopus 로고    scopus 로고
    • A new animal model for studying Lyme disease spirochetes in a mammalian host-adapted state
    • Akins DR, Bourell KW, Caimano MJ, Norgard MV, Radolf JD. 1998. A new animal model for studying Lyme disease spirochetes in a mammalian host-adapted state. J. Clin. Invest. 101:2240-2250.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2240-2250
    • Akins, D.R.1    Bourell, K.W.2    Caimano, M.J.3    Norgard, M.V.4    Radolf, J.D.5
  • 56
    • 0033778628 scopus 로고    scopus 로고
    • Interdependence of environmental factors influencing reciprocal patterns of gene expression in virulent Borrelia burgdor-feri
    • Yang X, Goldberg MS, Popova TG, Schoeler GB, Wikel SK, Hagman KE, Norgard MV. 2000. Interdependence of environmental factors influencing reciprocal patterns of gene expression in virulent Borrelia burgdor-feri. Mol. Microbiol. 37:1470-1479.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1470-1479
    • Yang, X.1    Goldberg, M.S.2    Popova, T.G.3    Schoeler, G.B.4    Wikel, S.K.5    Hagman, K.E.6    Norgard, M.V.7
  • 57
    • 0028828202 scopus 로고
    • Temperature-related differential expression of antigens in the Lyme disease spirochete, Borrelia burg-dorferi
    • Stevenson B, Schwan TG, Rosa PA. 1995. Temperature-related differential expression of antigens in the Lyme disease spirochete, Borrelia burg-dorferi. Infect. Immun. 63:4535-4539.
    • (1995) Infect. Immun. , vol.63 , pp. 4535-4539
    • Stevenson, B.1    Schwan, T.G.2    Rosa, P.A.3
  • 58
    • 0041823456 scopus 로고    scopus 로고
    • Regulation of expression of the paralogous Mlp family in Borrelia burg-dorferi
    • Yang XF, Hubner A, Popova TG, Hagman KE, Norgard MV. 2003. Regulation of expression of the paralogous Mlp family in Borrelia burg-dorferi. Infect. Immun. 71:5012-5020.
    • (2003) Infect. Immun. , vol.71 , pp. 5012-5020
    • Yang, X.F.1    Hubner, A.2    Popova, T.G.3    Hagman, K.E.4    Norgard, M.V.5
  • 59
  • 60
    • 0141814623 scopus 로고    scopus 로고
    • The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in Borrelia burgdorferi
    • Yang XF, Alani SM, Norgard MV. 2003. The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in Borrelia burgdorferi. Proc. Natl. Acad. Sci. U. S. A. 100:11001-11006.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11001-11006
    • Yang, X.F.1    Alani, S.M.2    Norgard, M.V.3
  • 62
    • 84870976588 scopus 로고    scopus 로고
    • A novel iron- and copper-binding protein in the Lyme disease spirochaete
    • Wang P, Lutton A, Olesik J, Vali H, Li X. 2012. A novel iron- and copper-binding protein in the Lyme disease spirochaete. Mol. Microbiol. 86:1441-1451.
    • (2012) Mol. Microbiol. , vol.86 , pp. 1441-1451
    • Wang, P.1    Lutton, A.2    Olesik, J.3    Vali, H.4    Li, X.5
  • 64
    • 56749175216 scopus 로고    scopus 로고
    • Abrogation of ospAB constitutively activates the Rrp2-RpoN-RpoS pathway (sigmaN-sigmaS cascade) in Borrelia burgdorferi
    • He M, Oman T, Xu H, Blevins J, Norgard MV, Yang XF. 2008. Abrogation of ospAB constitutively activates the Rrp2-RpoN-RpoS pathway (sigmaN-sigmaS cascade) in Borrelia burgdorferi. Mol. Microbiol. 70: 1453-1464.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1453-1464
    • He, M.1    Oman, T.2    Xu, H.3    Blevins, J.4    Norgard, M.V.5    Yang, X.F.6
  • 65
    • 0032967572 scopus 로고    scopus 로고
    • Effects of environmental pH on membrane proteins in Borrelia burgdorferi
    • Carroll JA, Garon CF, Schwan TG. 1999. Effects of environmental pH on membrane proteins in Borrelia burgdorferi. Infect. Immun. 67:3181-3187.
    • (1999) Infect. Immun. , vol.67 , pp. 3181-3187
    • Carroll, J.A.1    Garon, C.F.2    Schwan, T.G.3
  • 66
    • 67650094768 scopus 로고    scopus 로고
    • This is not your mother's repressor: the complex role of fur in pathogenesis
    • Carpenter BM, Whitmire JM, Merrell DS. 2009. This is not your mother's repressor: the complex role of fur in pathogenesis. Infect. Immun. 77:2590-2601.
    • (2009) Infect. Immun. , vol.77 , pp. 2590-2601
    • Carpenter, B.M.1    Whitmire, J.M.2    Merrell, D.S.3
  • 67
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke K. 2001. Iron and metal regulation in bacteria. Curr. Opin. Microbiol. 4:172-177.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 172-177
    • Hantke, K.1
  • 69
    • 65549107862 scopus 로고    scopus 로고
    • Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli
    • Anjem A, Varghese S, Imlay JA. 2009. Manganese import is a key element of the OxyR response to hydrogen peroxide in Escherichia coli. Mol. Microbiol. 72:844-858.
    • (2009) Mol. Microbiol. , vol.72 , pp. 844-858
    • Anjem, A.1    Varghese, S.2    Imlay, J.A.3
  • 70
    • 80054719570 scopus 로고    scopus 로고
    • The Fur regulon in anaerobically grown Salmonella enterica sv. Typhimurium: identification of new Fur targets
    • doi: 10.1186/1471-2180-11-236
    • Troxell B, Fink RC, Porwollik S, McClelland M, Hassan HM. 2011. The Fur regulon in anaerobically grown Salmonella enterica sv. Typhimurium: identification of new Fur targets. BMC Microbiol. 11:236. doi: 10.1186/1471-2180-11-236.
    • (2011) BMC Microbiol. , vol.11 , pp. 236
    • Troxell, B.1    Fink, R.C.2    Porwollik, S.3    McClelland, M.4    Hassan, H.M.5
  • 71
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metallo-regulatory proteins controlling zinc homeostasis
    • Outten CE, O'Halloran TV. 2001. Femtomolar sensitivity of metallo-regulatory proteins controlling zinc homeostasis. Science 292:2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 72
    • 0035016446 scopus 로고    scopus 로고
    • zur: a Zn(2+)-responsive regulatory element of Staphylococcus aureus
    • Lindsay JA, Foster SJ. 2001. zur: a Zn(2+)-responsive regulatory element of Staphylococcus aureus. Microbiology 147:1259-1266.
    • (2001) Microbiology , vol.147 , pp. 1259-1266
    • Lindsay, J.A.1    Foster, S.J.2
  • 73
    • 0034637471 scopus 로고    scopus 로고
    • The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli
    • Patzer SI, Hantke K. 2000. The zinc-responsive regulator Zur and its control of the znu gene cluster encoding the ZnuABC zinc uptake system in Escherichia coli. J. Biol. Chem. 275:24321-24332.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24321-24332
    • Patzer, S.I.1    Hantke, K.2
  • 74
    • 0032922903 scopus 로고    scopus 로고
    • Characterisation of a new operon encoding a Zur-like protein and an associated ABC zinc permease in Listeria monocytogenes
    • Dalet K, Gouin E, Cenatiempo Y, Cossart P, Hechard Y. 1999. Characterisation of a new operon encoding a Zur-like protein and an associated ABC zinc permease in Listeria monocytogenes. FEMS Microbiol. Lett. 174:111-116.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 111-116
    • Dalet, K.1    Gouin, E.2    Cenatiempo, Y.3    Cossart, P.4    Hechard, Y.5
  • 75
    • 0031733646 scopus 로고    scopus 로고
    • Identification of a zinc-specific metallo-regulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis
    • Gaballa A, Helmann JD. 1998. Identification of a zinc-specific metallo-regulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis. J. Bacteriol. 180:5815-5821.
    • (1998) J. Bacteriol. , vol.180 , pp. 5815-5821
    • Gaballa, A.1    Helmann, J.D.2
  • 76
    • 0031798662 scopus 로고    scopus 로고
    • The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli
    • Patzer SI, Hantke K. 1998. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Mol. Microbiol. 28:1199-1210.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1199-1210
    • Patzer, S.I.1    Hantke, K.2
  • 77
    • 52649116664 scopus 로고    scopus 로고
    • Treponema denticola TroR is a manganese- and iron-dependent transcriptional re-pressor
    • Brett PJ, Burtnick MN, Fenno JC, Gherardini FC. 2008. Treponema denticola TroR is a manganese- and iron-dependent transcriptional re-pressor. Mol. Microbiol. 70:396-409.
    • (2008) Mol. Microbiol. , vol.70 , pp. 396-409
    • Brett, P.J.1    Burtnick, M.N.2    Fenno, J.C.3    Gherardini, F.C.4
  • 78
    • 0032851843 scopus 로고    scopus 로고
    • Characterization of a manganese-dependent regulatory protein, TroR, from Trepo-nema pallidum
    • Posey JE, Hardham JM, Norris SJ, Gherardini FC. 1999. Characterization of a manganese-dependent regulatory protein, TroR, from Trepo-nema pallidum. Proc. Natl. Acad. Sci. U. S. A. 96:10887-10892.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10887-10892
    • Posey, J.E.1    Hardham, J.M.2    Norris, S.J.3    Gherardini, F.C.4
  • 79
    • 0038081029 scopus 로고    scopus 로고
    • The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent tran-scriptional repressor, and a semi-autonomously expressed phosphoglyc-erate mutase
    • Hazlett KR, Rusnak F, Kehres DG, Bearden SW, La Vake CJ, La Vake ME, Maguire ME, Perry RD, Radolf JD. 2003. The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent tran-scriptional repressor, and a semi-autonomously expressed phosphoglyc-erate mutase. J. Biol. Chem. 278:20687-20694.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20687-20694
    • Hazlett, K.R.1    Rusnak, F.2    Kehres, D.G.3    Bearden, S.W.4    La Vake, C.J.5    La Vake, M.E.6    Maguire, M.E.7    Perry, R.D.8    Radolf, J.D.9
  • 80
  • 81
    • 79957992260 scopus 로고    scopus 로고
    • Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis
    • Faulkner MJ, Hellmann JD. 2011. Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis. Antioxid. Redox Signal. 15:175-189.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 175-189
    • Faulkner, M.J.1    Hellmann, J.D.2
  • 82
    • 4544350205 scopus 로고    scopus 로고
    • Combined effects of blood and temperature shift on Borrelia burgdorferi gene expression as determined by whole genome DNA array
    • Tokarz R, Anderton JM, Katona LI, Benach JL. 2004. Combined effects of blood and temperature shift on Borrelia burgdorferi gene expression as determined by whole genome DNA array. Infect. Immun. 72:5419-5432.
    • (2004) Infect. Immun. , vol.72 , pp. 5419-5432
    • Tokarz, R.1    Anderton, J.M.2    Katona, L.I.3    Benach, J.L.4
  • 84
    • 84861675491 scopus 로고    scopus 로고
    • Effect of levels of acetate on the mevalonate pathway of Borrelia burgdorferi
    • doi: 10.1371/journal.pone.0038171
    • Van Laar TA, Lin Y-H, Miller CL, Karna SLR, Chambers JP, Seshu J. 2012. Effect of levels of acetate on the mevalonate pathway of Borrelia burgdorferi. PLoS One 7:e38171. doi :10.1371/journal.pone.0038171.
    • (2012) PLoS One , vol.7
    • Van Laar, T.A.1    Lin, Y.-H.2    Miller, C.L.3    Karna, S.L.R.4    Chambers, J.P.5    Seshu, J.6
  • 85
    • 79952286835 scopus 로고    scopus 로고
    • Inactivation of bb0184, which encodes carbon storage regulator A, represses the infectivity of Borrelia burgdorferi
    • Sze CW, Li C. 2011. Inactivation of bb0184, which encodes carbon storage regulator A, represses the infectivity of Borrelia burgdorferi. Infect. Immun. 79:1270-1279.
    • (2011) Infect. Immun. , vol.79 , pp. 1270-1279
    • Sze, C.W.1    Li, C.2
  • 86
    • 79251480381 scopus 로고    scopus 로고
    • CsrA modulates levels of lipoproteins and key regulators of gene expression critical for pathogenic mechanisms of Borrelia burgdor-feri
    • Karna SL, Sanjuan E, Esteve-Gassent MD, Miller CL, Maruskova M, Seshu J. 2011. CsrA modulates levels of lipoproteins and key regulators of gene expression critical for pathogenic mechanisms of Borrelia burgdor-feri. Infect. Immun. 79:732-744.
    • (2011) Infect. Immun. , vol.79 , pp. 732-744
    • Karna, S.L.1    Sanjuan, E.2    Esteve-Gassent, M.D.3    Miller, C.L.4    Maruskova, M.5    Seshu, J.6
  • 88
    • 0028340662 scopus 로고
    • Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli
    • Pruss BM, Wolfe AJ. 1994. Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli. Mol. Microbiol. 12:973-984.
    • (1994) Mol. Microbiol. , vol.12 , pp. 973-984
    • Pruss, B.M.1    Wolfe, A.J.2
  • 90
    • 0005246580 scopus 로고
    • The zinc content of normal human whole blood, plasma, leucocytes, and erythrocytes
    • Vallee BL, Gibson JG, II. 1948. The zinc content of normal human whole blood, plasma, leucocytes, and erythrocytes. J. Biol. Chem. 176:445-457.
    • (1948) J. Biol. Chem. , vol.176 , pp. 445-457
    • Vallee, B.L.1    Gibson II, J.G.2
  • 91
    • 0014629940 scopus 로고
    • Direct determination of zinc in whole blood, plasma and urine by atomic absorption spectroscopy
    • Dawson JB, Walker BE. 1969. Direct determination of zinc in whole blood, plasma and urine by atomic absorption spectroscopy. Clin. Chim. Acta 26:465-475.
    • (1969) Clin. Chim. Acta , vol.26 , pp. 465-475
    • Dawson, J.B.1    Walker, B.E.2
  • 92
    • 0028009584 scopus 로고
    • Concentrations of cadmium, lead, selenium, and zinc in human blood and seminal plasma
    • Xu B, Chia SE, Ong CN. 1994. Concentrations of cadmium, lead, selenium, and zinc in human blood and seminal plasma. Biol. Trace Elem. Res. 40:49-57.
    • (1994) Biol. Trace Elem. Res. , vol.40 , pp. 49-57
    • Xu, B.1    Chia, S.E.2    Ong, C.N.3
  • 93
    • 13244264715 scopus 로고    scopus 로고
    • Transcriptional regulation of sitABCD of Salmonella enterica serovar Ty-phimurium by MntR and Fur
    • Ikeda JS, Janakiraman A, Kehres DG, Maguire ME, Slauch JM. 2005. Transcriptional regulation of sitABCD of Salmonella enterica serovar Ty-phimurium by MntR and Fur. J. Bacteriol. 187:912-922.
    • (2005) J. Bacteriol. , vol.187 , pp. 912-922
    • Ikeda, J.S.1    Janakiraman, A.2    Kehres, D.G.3    Maguire, M.E.4    Slauch, J.M.5
  • 94
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the Lyme disease pathogen
    • Posey JE, Gherardini FC. 2000. Lack of a role for iron in the Lyme disease pathogen. Science 288:1651-1653.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 95
    • 79959554902 scopus 로고    scopus 로고
    • Nitro-sative damage to free and zinc-bound cysteine thiols underlies nitric oxide toxicity in wild-type Borrelia burgdorferi
    • Bourret TJ, Boylan JA, Lawrence KA, Gherardini FC. 2011. Nitro-sative damage to free and zinc-bound cysteine thiols underlies nitric oxide toxicity in wild-type Borrelia burgdorferi. Mol. Microbiol. 81: 259-273.
    • (2011) Mol. Microbiol. , vol.81 , pp. 259-273
    • Bourret, T.J.1    Boylan, J.A.2    Lawrence, K.A.3    Gherardini, F.C.4
  • 97
    • 0015935290 scopus 로고
    • The interaction of phos-phoglucomutase with nucleotide inhibitors
    • Duckworth HW, Barber BH, Sanwal BD. 1973. The interaction of phos-phoglucomutase with nucleotide inhibitors. J. Biol. Chem. 248:1431-1435.
    • (1973) J. Biol. Chem. , vol.248 , pp. 1431-1435
    • Duckworth, H.W.1    Barber, B.H.2    Sanwal, B.D.3
  • 98
    • 0034599751 scopus 로고    scopus 로고
    • Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus
    • Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G. 2000. Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus. EMBO J. 19:1419-1431.
    • (2000) EMBO J. , vol.19 , pp. 1419-1431
    • Jedrzejas, M.J.1    Chander, M.2    Setlow, P.3    Krishnasamy, G.4
  • 100
    • 84873542723 scopus 로고    scopus 로고
    • hanges in bacterial growth rate govern expression of the Borrelia burgdorferi OspC and Erp infec tion-associated surface proteins
    • Jutras BL, Chenail AM, Stevenson B. 2013. Changes in bacterial growth rate govern expression of the Borrelia burgdorferi OspC and Erp infec tion-associated surface proteins. J. Bacteriol. 195:757-764.
    • (2013) J. Bacteriol. , vol.195 , pp. 757-764
    • Jutras, B.L.1    Chenail, A.M.2    Stevenson, B.3


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