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Volumn 6, Issue JUL, 2015, Pages

Regulation of oxidative stress resistance in Campylobacter jejuni, a microaerophilic foodborne pathogen

Author keywords

Campylobacter jejuni; Oxidative stress; Regulation of gene expression; Stress response; Survival mechanisms

Indexed keywords

PEROXIDE; SUPEROXIDE;

EID: 84938850731     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2015.00751     Document Type: Review
Times cited : (72)

References (149)
  • 1
    • 0028891661 scopus 로고
    • Heat-resistance of Escherichia coli O157:H7 in meat and poultry as affected by product composition
    • Ahmed, N. M., Conner, D. E., and Huffman, D. L. (1995). Heat-resistance of Escherichia coli O157:H7 in meat and poultry as affected by product composition. J. Food Sci. 60, 606-610. doi: 10.1111/j.1365-2621.1995.tb09838.x
    • (1995) J. Food Sci , vol.60 , pp. 606-610
    • Ahmed, N.M.1    Conner, D.E.2    Huffman, D.L.3
  • 2
    • 49949117088 scopus 로고    scopus 로고
    • Examination of stress and virulence gene expression in Escherichia coli O157:H7 using targeted microarray analysis
    • Allen, K. J., Lepp, D., Mckellar, R. C., and Griffiths, M. W. (2008). Examination of stress and virulence gene expression in Escherichia coli O157:H7 using targeted microarray analysis. Foodborne Pathog. Dis. 5, 437-447. doi: 10.1089/fpd.2008.0100
    • (2008) Foodborne Pathog. Dis , vol.5 , pp. 437-447
    • Allen, K.J.1    Lepp, D.2    Mckellar, R.C.3    Griffiths, M.W.4
  • 4
    • 48149094202 scopus 로고    scopus 로고
    • The Campylobacter jejuni thiol peroxidases Tpx and Bcp both contribute to aerotolerance and peroxide-mediated stress resistance but have distinct substrate specificities
    • Atack, J. M., Harvey, P., Jones, M. A., and Kelly, D. J. (2008). The Campylobacter jejuni thiol peroxidases Tpx and Bcp both contribute to aerotolerance and peroxide-mediated stress resistance but have distinct substrate specificities. J. Bacteriol. 190, 5279-5290. doi: 10.1128/JB.00100-08
    • (2008) J. Bacteriol , vol.190 , pp. 5279-5290
    • Atack, J.M.1    Harvey, P.2    Jones, M.A.3    Kelly, D.J.4
  • 5
    • 51149100536 scopus 로고    scopus 로고
    • Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni
    • Atack, J. M., and Kelly, D. J. (2008). Contribution of the stereospecific methionine sulphoxide reductases MsrA and MsrB to oxidative and nitrosative stress resistance in the food-borne pathogen Campylobacter jejuni. Microbiology 154, 2219-2230. doi: 10.1099/mic.0.2008/019711-0
    • (2008) Microbiology , vol.154 , pp. 2219-2230
    • Atack, J.M.1    Kelly, D.J.2
  • 6
    • 84912077212 scopus 로고    scopus 로고
    • Enhanced transmission of antibiotic resistance in Campylobacter jejuni biofilms by natural transformation
    • Bae, J., Oh, E., and Jeon, B. (2014). Enhanced transmission of antibiotic resistance in Campylobacter jejuni biofilms by natural transformation. Antimicrob. Agents Chemother. 58, 7573-7575. doi: 10.1128/AAC.04066-14
    • (2014) Antimicrob. Agents Chemother , vol.58 , pp. 7573-7575
    • Bae, J.1    Oh, E.2    Jeon, B.3
  • 7
    • 0032837846 scopus 로고    scopus 로고
    • An iron-regulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen Campylobacter jejuni
    • Baillon, M. L., Van Vliet, A. H., Ketley, J. M., Constantinidou, C., and Penn, C. W. (1999). An iron-regulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen Campylobacter jejuni. J. Bacteriol. 181, 4798-4804.
    • (1999) J. Bacteriol , vol.181 , pp. 4798-4804
    • Baillon, M.L.1    Van Vliet, A.H.2    Ketley, J.M.3    Constantinidou, C.4    Penn, C.W.5
  • 8
    • 14944350031 scopus 로고    scopus 로고
    • Adaptation of microorganisms to cold temperatures, weak acid preservatives, low pH, and osmotic stress: a review
    • Beales, N. (2004). Adaptation of microorganisms to cold temperatures, weak acid preservatives, low pH, and osmotic stress: a review. Compr. Rev. Food Sci. Food 3, 1-20. doi: 10.1111/j.1541-4337.2004.tb00057.x
    • (2004) Compr. Rev. Food Sci. Food , vol.3 , pp. 1-20
    • Beales, N.1
  • 9
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker, J., and Craig, E. A. (1994). Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219, 11-23. doi: 10.1111/j.1432-1033.1994.tb19910.x
    • (1994) Eur. J. Biochem , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 10
  • 11
    • 40749084835 scopus 로고    scopus 로고
    • Characterization of two putative cytochrome c peroxidases of Campylobacter jejuni involved in promoting commensal colonization of poultry
    • Bingham-Ramos, L. K., and Hendrixson, D. R. (2008). Characterization of two putative cytochrome c peroxidases of Campylobacter jejuni involved in promoting commensal colonization of poultry. Infect. Immun. 76, 1105-1114. doi: 10.1128/IAI.01430-07
    • (2008) Infect. Immun , vol.76 , pp. 1105-1114
    • Bingham-Ramos, L.K.1    Hendrixson, D.R.2
  • 12
    • 84864799433 scopus 로고    scopus 로고
    • Acid stress response and protein induction in Campylobacter jejuni isolates with different acid tolerance
    • Birk, T., Wik, M. T., Lametsch, R., and Knochel, S. (2012). Acid stress response and protein induction in Campylobacter jejuni isolates with different acid tolerance. BMC Microbiol. 12:174. doi: 10.1186/1471-2180-12-174
    • (2012) BMC Microbiol , vol.12 , pp. 174
    • Birk, T.1    Wik, M.T.2    Lametsch, R.3    Knochel, S.4
  • 13
    • 0020325804 scopus 로고
    • Campylobacter jejuni survival in chicken meat as a function of temperature
    • Blankenship, L. C., and Craven, S. E. (1982). Campylobacter jejuni survival in chicken meat as a function of temperature. Appl. Environ. Microbiol. 44, 88-92.
    • (1982) Appl. Environ. Microbiol , vol.44 , pp. 88-92
    • Blankenship, L.C.1    Craven, S.E.2
  • 14
    • 0033811333 scopus 로고    scopus 로고
    • Recovery of hydrogen peroxide-sensitive culturable cells of Vibrio vulnificus gives the appearance of resuscitation from a viable but nonculturable state
    • Bogosian, G., Aardema, N. D., Bourneuf, E. V., Morris, P. J., and O'neil, J. P. (2000). Recovery of hydrogen peroxide-sensitive culturable cells of Vibrio vulnificus gives the appearance of resuscitation from a viable but nonculturable state. J. Bacteriol. 182, 5070-5075. doi: 10.1128/JB.182.18.5070-5075.2000
    • (2000) J. Bacteriol , vol.182 , pp. 5070-5075
    • Bogosian, G.1    Aardema, N.D.2    Bourneuf, E.V.3    Morris, P.J.4    O'neil, J.P.5
  • 15
    • 0020469043 scopus 로고
    • A most probable number method for estimating small numbers of campylobacters in water
    • Bolton, F. J., Hinchliffe, P. M., Coates, D., and Robertson, L. (1982). A most probable number method for estimating small numbers of campylobacters in water. J. Hyg. (Lond.) 89, 185-190. doi: 10.1017/S0022172400070716
    • (1982) J. Hyg. (Lond.) , vol.89 , pp. 185-190
    • Bolton, F.J.1    Hinchliffe, P.M.2    Coates, D.3    Robertson, L.4
  • 16
    • 58549116867 scopus 로고    scopus 로고
    • 'Bergey's manual of systematic bacteriology,'
    • 2nd Edn, eds G. Garrity, D. J. Brenner, N. R. Krieg, and J. T. Staley (New York, NY: Springer)
    • Brenner, D. J., and Staley, J. T. (2005). "Bergey's manual of systematic bacteriology," in The Proteobacteria. Part C. The Alpha-, Beta-, Selta-, and Epsilonproteobacteria, Vol. 2, 2nd Edn, eds G. Garrity, D. J. Brenner, N. R. Krieg, and J. T. Staley (New York, NY: Springer).
    • (2005) The Proteobacteria. Part C. The Alpha-, Beta-, Selta-, and Epsilonproteobacteria , vol.2
    • Brenner, D.J.1    Staley, J.T.2
  • 17
    • 0035210924 scopus 로고    scopus 로고
    • Heat and salt stress in the food pathogen Bacillus cereus
    • Browne, N., and Dowds, B. (2001). Heat and salt stress in the food pathogen Bacillus cereus. J. Appl. Microbiol. 91, 1085-1094. doi: 10.1046/j.1365-2672.2001.01478.x
    • (2001) J. Appl. Microbiol , vol.91 , pp. 1085-1094
    • Browne, N.1    Dowds, B.2
  • 18
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat, N., Herbig, A., Casillas-Martinez, L., Setlow, P., and Helmann, J. D. (1998). Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol. Microbiol. 29, 189-198. doi: 10.1046/j.1365-2958.1998.00921.x
    • (1998) Mol. Microbiol , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 19
    • 84862548944 scopus 로고    scopus 로고
    • Structure and regulon of Campylobacter jejuni ferric uptake regulator Fur define apo-Fur regulation
    • Butcher, J., Sarvan, S., Brunzelle, J. S., Couture, J. F., and Stintzi, A. (2012). Structure and regulon of Campylobacter jejuni ferric uptake regulator Fur define apo-Fur regulation. Proc. Natl. Acad. Sci. U.S.A. 109, 10047-10052. doi: 10.1073/pnas.1118321109
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 10047-10052
    • Butcher, J.1    Sarvan, S.2    Brunzelle, J.S.3    Couture, J.F.4    Stintzi, A.5
  • 20
    • 84869102723 scopus 로고    scopus 로고
    • Hyperosmotic stress response of Campylobacter jejuni
    • Cameron, A., Frirdich, E., Huynh, S., Parker, C. T., and Gaynor, E. C. (2012). Hyperosmotic stress response of Campylobacter jejuni. J. Bacteriol. 194, 6116-6130. doi: 10.1128/JB.01409-12
    • (2012) J. Bacteriol , vol.194 , pp. 6116-6130
    • Cameron, A.1    Frirdich, E.2    Huynh, S.3    Parker, C.T.4    Gaynor, E.C.5
  • 21
    • 68949098194 scopus 로고    scopus 로고
    • Bacterial stressors in minimally processed food
    • Capozzi, V., Fiocco, D., Amodio, M. L., Gallone, A., and Spano, G. (2009). Bacterial stressors in minimally processed food. Int. J. Mol. Sci. 10, 3076-3105. doi: 10.3390/ijms10073076
    • (2009) Int. J. Mol. Sci , vol.10 , pp. 3076-3105
    • Capozzi, V.1    Fiocco, D.2    Amodio, M.L.3    Gallone, A.4    Spano, G.5
  • 22
    • 84893004074 scopus 로고    scopus 로고
    • The Vps/VacJ ABC transporter is required for intercellular spread of Shigella flexneri
    • Carpenter, C. D., Cooley, B. J., Needham, B. D., Fisher, C. R., Trent, M. S., Gordon, V., et al. (2014). The Vps/VacJ ABC transporter is required for intercellular spread of Shigella flexneri. Infect. Immun. 82, 660-669. doi: 10.1128/IAI.01057-13
    • (2014) Infect. Immun , vol.82 , pp. 660-669
    • Carpenter, C.D.1    Cooley, B.J.2    Needham, B.D.3    Fisher, C.R.4    Trent, M.S.5    Gordon, V.6
  • 24
    • 85126812130 scopus 로고    scopus 로고
    • Microbiological safety of chicken litter or chicken litter-based organic fertilizers: a review
    • Chen, Z., and Jiang, X. (2014). Microbiological safety of chicken litter or chicken litter-based organic fertilizers: a review. Agriculture 4, 1-29. doi: 10.3390/agriculture4010001
    • (2014) Agriculture , vol.4 , pp. 1-29
    • Chen, Z.1    Jiang, X.2
  • 25
    • 84864600170 scopus 로고    scopus 로고
    • Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria
    • Chiang, S. M., and Schellhorn, H. E. (2012). Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria. Arch. Biochem. Biophys. 525, 161-169. doi: 10.1016/j.abb.2012.02.007
    • (2012) Arch. Biochem. Biophys , vol.525 , pp. 161-169
    • Chiang, S.M.1    Schellhorn, H.E.2
  • 26
    • 0033823598 scopus 로고    scopus 로고
    • Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157: H7
    • Choi, S. H., Baumler, D. J., and Kaspar, C. W. (2000). Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157: H7. Appl. Environ. Microbiol. 66, 3911-3916. doi: 10.1128/AEM.66.9.3911-3916.2000
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 3911-3916
    • Choi, S.H.1    Baumler, D.J.2    Kaspar, C.W.3
  • 27
    • 0000413318 scopus 로고    scopus 로고
    • Stress response in pathogenic bacteria
    • Chowdhury, R., Sahu, G. K., and Das, J. (1996). Stress response in pathogenic bacteria. J. Biosci. 21, 149-160. doi: 10.1007/BF02703105
    • (1996) J. Biosci , vol.21 , pp. 149-160
    • Chowdhury, R.1    Sahu, G.K.2    Das, J.3
  • 28
    • 33750561881 scopus 로고    scopus 로고
    • Stress response of Escherichia coli
    • Chung, H., Bang, W., and Drake, M. (2006). Stress response of Escherichia coli. Compr. Rev. Food Sci. Food 5, 52-64. doi: 10.1111/j.1541-4337.2006.00002.x
    • (2006) Compr. Rev. Food Sci. Food , vol.5 , pp. 52-64
    • Chung, H.1    Bang, W.2    Drake, M.3
  • 29
    • 0033788137 scopus 로고    scopus 로고
    • Role of catalase in Campylobacter jejuni intracellular survival
    • Day, W. A. Jr., Sajecki, J. L., Pitts, T. M., and Joens, L. A. (2000). Role of catalase in Campylobacter jejuni intracellular survival. Infect. Immun. 68, 6337-6345. doi: 10.1128/IAI.68.11.6337-6345.2000
    • (2000) Infect. Immun , vol.68 , pp. 6337-6345
    • Day, W.A.1    Sajecki, J.L.2    Pitts, T.M.3    Joens, L.A.4
  • 30
    • 67149131592 scopus 로고    scopus 로고
    • Phenotypic and transcriptomic analyses of mildly and severely salt-stressed Bacillus cereus ATCC 14579 cells
    • den Besten, H. M., Mols, M., Moezelaar, R., Zwietering, M. H., and Abee, T. (2009). Phenotypic and transcriptomic analyses of mildly and severely salt-stressed Bacillus cereus ATCC 14579 cells. Appl. Environ. Microbiol. 75, 4111-4119. doi: 10.1128/AEM.02891-08
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 4111-4119
    • den Besten, H.M.1    Mols, M.2    Moezelaar, R.3    Zwietering, M.H.4    Abee, T.5
  • 31
    • 0036260466 scopus 로고    scopus 로고
    • Quorum sensing in Campylobacter jejuni: detection of a luxS encoded signalling molecule
    • Elvers, K. T., and Park, S. F. (2002). Quorum sensing in Campylobacter jejuni: detection of a luxS encoded signalling molecule. Microbiology 148, 1475-1481.
    • (2002) Microbiology , vol.148 , pp. 1475-1481
    • Elvers, K.T.1    Park, S.F.2
  • 33
    • 12844259524 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases in prokaryotes
    • Ezraty, B., Aussel, L., and Barras, F. (2005). Methionine sulfoxide reductases in prokaryotes. Biochim. Biophys. Acta 1703, 221-229. doi: 10.1016/j.bbapap.2004.08.017
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 221-229
    • Ezraty, B.1    Aussel, L.2    Barras, F.3
  • 34
    • 84864106096 scopus 로고    scopus 로고
    • Bactericidal antibiotics do not appear to cause oxidative stress in Listeria monocytogenes
    • Feld, L., Knudsen, G. M., and Gram, L. (2012). Bactericidal antibiotics do not appear to cause oxidative stress in Listeria monocytogenes. Appl. Environ. Microbiol. 78, 4353-4357. doi: 10.1128/AEM.00324-12
    • (2012) Appl. Environ. Microbiol , vol.78 , pp. 4353-4357
    • Feld, L.1    Knudsen, G.M.2    Gram, L.3
  • 35
    • 42549091148 scopus 로고    scopus 로고
    • Campylobacter jejuni CsrA mediates oxidative stress responses, biofilm formation, and host cell invasion
    • Fields, J. A., and Thompson, S. A. (2008). Campylobacter jejuni CsrA mediates oxidative stress responses, biofilm formation, and host cell invasion. J. Bacteriol. 190, 3411-3416. doi: 10.1128/JB.01928-07
    • (2008) J. Bacteriol , vol.190 , pp. 3411-3416
    • Fields, J.A.1    Thompson, S.A.2
  • 36
    • 84867237164 scopus 로고    scopus 로고
    • Campylobacter jejuni CsrA complements an Escherichia coli csrA mutation for the regulation of biofilm formation, motility and cellular morphology but not glycogen accumulation
    • Fields, J. A., and Thompson, S. A. (2012). Campylobacter jejuni CsrA complements an Escherichia coli csrA mutation for the regulation of biofilm formation, motility and cellular morphology but not glycogen accumulation. BMC Microbiol. 12:233. doi: 10.1186/1471-2180-12-233
    • (2012) BMC Microbiol , vol.12 , pp. 233
    • Fields, J.A.1    Thompson, S.A.2
  • 37
    • 84900517226 scopus 로고    scopus 로고
    • Phenotypic screening of a targeted mutant library reveals Campylobacter jejuni defenses against oxidative stress
    • Flint, A., Sun, Y. Q., Butcher, J., Stahl, M., Huang, H., and Stintzi, A. (2014). Phenotypic screening of a targeted mutant library reveals Campylobacter jejuni defenses against oxidative stress. Infect. Immun. 82, 2266-2275. doi: 10.1128/IAI.01528-13
    • (2014) Infect. Immun , vol.82 , pp. 2266-2275
    • Flint, A.1    Sun, Y.Q.2    Butcher, J.3    Stahl, M.4    Huang, H.5    Stintzi, A.6
  • 38
    • 84862908910 scopus 로고    scopus 로고
    • Cj1386 is an ankyrin-containing protein involved in heme trafficking to catalase in Campylobacter jejuni
    • Flint, A., Sun, Y. Q., and Stintzi, A. (2012). Cj1386 is an ankyrin-containing protein involved in heme trafficking to catalase in Campylobacter jejuni. J. Bacteriol. 194, 334-345. doi: 10.1128/JB.05740-11
    • (2012) J. Bacteriol , vol.194 , pp. 334-345
    • Flint, A.1    Sun, Y.Q.2    Stintzi, A.3
  • 39
    • 0036224487 scopus 로고    scopus 로고
    • Public health implications of Campylobacter outbreaks in England and Wales, 1995-9: epidemiological and microbiological investigations
    • Frost, J. A., Gillespie, I. A., and O'brien, S. J. (2002). Public health implications of Campylobacter outbreaks in England and Wales, 1995-9: epidemiological and microbiological investigations. Epidemiol. Infect. 128, 111-118. doi: 10.1017/S0950268802006799
    • (2002) Epidemiol. Infect , vol.128 , pp. 111-118
    • Frost, J.A.1    Gillespie, I.A.2    O'brien, S.J.3
  • 40
    • 0036267391 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible
    • Fuangthong, M., Herbig, A. F., Bsat, N., and Helmann, J. D. (2002). Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. J. Bacteriol. 184, 3276-3286. doi: 10.1128/JB.184.12.3276-3286.2002
    • (2002) J. Bacteriol , vol.184 , pp. 3276-3286
    • Fuangthong, M.1    Herbig, A.F.2    Bsat, N.3    Helmann, J.D.4
  • 41
    • 11444263858 scopus 로고    scopus 로고
    • Survival strategies of infectious biofilms
    • Fux, C., Costerton, J., Stewart, P., and Stoodley, P. (2005). Survival strategies of infectious biofilms. Trends Microbiol. 13, 34-40. doi: 10.1016/j.tim.2004.11.010
    • (2005) Trends Microbiol , vol.13 , pp. 34-40
    • Fux, C.1    Costerton, J.2    Stewart, P.3    Stoodley, P.4
  • 42
    • 57049101937 scopus 로고    scopus 로고
    • Role of the Cj1371 periplasmic protein and the Cj0355c two-component regulator in the Campylobacter jejuni NCTC 11168 response to oxidative stress caused by paraquat
    • Garénaux, A., Guillou, S., Ermel, G., Wren, B., Federighi, M., and Ritz, M. (2008a). Role of the Cj1371 periplasmic protein and the Cj0355c two-component regulator in the Campylobacter jejuni NCTC 11168 response to oxidative stress caused by paraquat. Res. Microbiol. 159, 718-726. doi: 10.1016/j.resmic.2008.08.001
    • (2008) Res. Microbiol , vol.159 , pp. 718-726
    • Garénaux, A.1    Guillou, S.2    Ermel, G.3    Wren, B.4    Federighi, M.5    Ritz, M.6
  • 43
    • 40149103609 scopus 로고    scopus 로고
    • Survival of Campylobacter jejuni strains from different origins under oxidative stress conditions: effect of temperature
    • Garénaux, A., Jugiau, F., Rama, F., De Jonge, R., Denis, M., Federighi, M., et al. (2008b). Survival of Campylobacter jejuni strains from different origins under oxidative stress conditions: effect of temperature. Curr. Microbiol. 56, 293-297. doi: 10.1007/s00284-007-9082-8
    • (2008) Curr. Microbiol , vol.56 , pp. 293-297
    • Garénaux, A.1    Jugiau, F.2    Rama, F.3    De Jonge, R.4    Denis, M.5    Federighi, M.6
  • 44
    • 58249120640 scopus 로고    scopus 로고
    • Role of oxidative stress in C. jejuni inactivation during freeze-thaw treatment
    • Garénaux, A., Ritz, M., Jugiau, F., Rama, F., Federighi, M., and De Jonge, R. (2009). Role of oxidative stress in C. jejuni inactivation during freeze-thaw treatment. Curr. Microbiol. 58, 134-138. doi: 10.1007/s00284-008-9289-3
    • (2009) Curr. Microbiol , vol.58 , pp. 134-138
    • Garénaux, A.1    Ritz, M.2    Jugiau, F.3    Rama, F.4    Federighi, M.5    De Jonge, R.6
  • 46
    • 0029045134 scopus 로고
    • Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange
    • Grant, K. A., and Park, S. F. (1995). Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange. Microbiology 141(Pt 6), 1369-1376. doi: 10.1099/13500872-141-6-1369
    • (1995) Microbiology , vol.141 , pp. 1369-1376
    • Grant, K.A.1    Park, S.F.2
  • 47
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg, J. T., Monach, P., Chou, J. H., Josephy, P. D., and Demple, B. (1990). Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 87, 6181-6185. doi: 10.1073/pnas.87.16.6181
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 48
    • 79951789722 scopus 로고    scopus 로고
    • The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide
    • Gu, M., and Imlay, J. A. (2011). The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide. Mol. Microbiol. 79, 1136-1150. doi: 10.1111/j.1365-2958.2010.07520.x
    • (2011) Mol. Microbiol , vol.79 , pp. 1136-1150
    • Gu, M.1    Imlay, J.A.2
  • 49
    • 79961151311 scopus 로고    scopus 로고
    • The Campylobacter jejuni transcriptional regulator Cj1556 plays a role in the oxidative and aerobic stress response and is important for bacterial survival in vivo
    • Gundogdu, O., Mills, D. C., Elmi, A., Martin, M. J., Wren, B. W., and Dorrell, N. (2011). The Campylobacter jejuni transcriptional regulator Cj1556 plays a role in the oxidative and aerobic stress response and is important for bacterial survival in vivo. J. Bacteriol. 193, 4238-4249. doi: 10.1128/JB.05189-11
    • (2011) J. Bacteriol , vol.193 , pp. 4238-4249
    • Gundogdu, O.1    Mills, D.C.2    Elmi, A.3    Martin, M.J.4    Wren, B.W.5    Dorrell, N.6
  • 50
    • 84901006261 scopus 로고    scopus 로고
    • Stress-induced remodeling of the bacterial proteome
    • Guo, M. S., and Gross, C. A. (2014). Stress-induced remodeling of the bacterial proteome. Curr. Biol. 24, R424-R434. doi: 10.1016/j.cub.2014.03.023
    • (2014) Curr. Biol , vol.24 , pp. R424-R434
    • Guo, M.S.1    Gross, C.A.2
  • 51
    • 11444262730 scopus 로고    scopus 로고
    • Biofilm formation and dispersal and the transmission of human pathogens
    • Hall-Stoodley, L., and Stoodley, P. (2005). Biofilm formation and dispersal and the transmission of human pathogens. Trends Microbiol. 13, 7-10. doi: 10.1016/j.tim.2004.11.004
    • (2005) Trends Microbiol , vol.13 , pp. 7-10
    • Hall-Stoodley, L.1    Stoodley, P.2
  • 52
    • 33846572919 scopus 로고    scopus 로고
    • Prevalence, genetic diversity, and antibiotic resistance patterns of Campylobacter jejuni from retail raw chickens in Korea
    • Han, K., Jang, S. S., Choo, E., Heu, S., and Ryu, S. (2007). Prevalence, genetic diversity, and antibiotic resistance patterns of Campylobacter jejuni from retail raw chickens in Korea. Int. J. Food Microbiol. 114, 50-59. doi: 10.1016/j.ijfoodmicro.2006.10.042
    • (2007) Int. J. Food Microbiol , vol.114 , pp. 50-59
    • Han, K.1    Jang, S.S.2    Choo, E.3    Heu, S.4    Ryu, S.5
  • 53
    • 0031711911 scopus 로고    scopus 로고
    • Physiological activity of Campylobacter jejuni far below the minimal growth temperature
    • Hazeleger, W. C., Wouters, J. A., Rombouts, F. M., and Abee, T. (1998). Physiological activity of Campylobacter jejuni far below the minimal growth temperature. Appl. Environ. Microbiol. 64, 3917-3922.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 3917-3922
    • Hazeleger, W.C.1    Wouters, J.A.2    Rombouts, F.M.3    Abee, T.4
  • 54
    • 49949103398 scopus 로고    scopus 로고
    • Analysis of AI-2/LuxS-dependent transcription in Campylobacter jejuni strain 81-176
    • He, Y., Frye, J. G., Strobaugh, T. P., and Chen, C. Y. (2008). Analysis of AI-2/LuxS-dependent transcription in Campylobacter jejuni strain 81-176. Foodborne Pathog. Dis. 5, 399-415. doi: 10.1089/fpd.2008.0106
    • (2008) Foodborne Pathog. Dis , vol.5 , pp. 399-415
    • He, Y.1    Frye, J.G.2    Strobaugh, T.P.3    Chen, C.Y.4
  • 55
    • 84907833692 scopus 로고    scopus 로고
    • Specificity of metal sensing: iron and manganese homeostasis in Bacillus subtilis
    • Helmann, J. D. (2014). Specificity of metal sensing: iron and manganese homeostasis in Bacillus subtilis. J. Biol. Chem. 289, 28112-28120. doi: 10.1074/jbc.R114.587071
    • (2014) J. Biol. Chem , vol.289 , pp. 28112-28120
    • Helmann, J.D.1
  • 56
    • 0035050923 scopus 로고    scopus 로고
    • Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility
    • Hendrixson, D. R., Akerley, B. J., and Dirita, V. J. (2001). Transposon mutagenesis of Campylobacter jejuni identifies a bipartite energy taxis system required for motility. Mol. Microbiol. 40, 214-224. doi: 10.1046/j.1365-2958.2001.02376.x
    • (2001) Mol. Microbiol , vol.40 , pp. 214-224
    • Hendrixson, D.R.1    Akerley, B.J.2    Dirita, V.J.3
  • 57
    • 1942532926 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract
    • Hendrixson, D. R., and DiRita, V. J. (2004). Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract. Mol. Microbiol. 52, 471-484. doi: 10.1111/j.1365-2958.2004.03988.x
    • (2004) Mol. Microbiol , vol.52 , pp. 471-484
    • Hendrixson, D.R.1    DiRita, V.J.2
  • 58
    • 0036198628 scopus 로고    scopus 로고
    • Recent insights into the general stress response regulatory network in Escherichia coli
    • Hengge-Aronis, R. (2002). Recent insights into the general stress response regulatory network in Escherichia coli. J. Mol. Microbiol. Biotechnol. 4, 341-346.
    • (2002) J. Mol. Microbiol. Biotechnol , vol.4 , pp. 341-346
    • Hengge-Aronis, R.1
  • 59
    • 0029588658 scopus 로고
    • Acid adaptation and food poisoning microorganisms
    • Hill, C., O'driscoll, B., and Booth, I. (1995). Acid adaptation and food poisoning microorganisms. Int. J. Food Microbiol. 28, 245-254. doi: 10.1016/0168-1605(95)00060-7
    • (1995) Int. J. Food Microbiol , vol.28 , pp. 245-254
    • Hill, C.1    O'driscoll, B.2    Booth, I.3
  • 60
    • 13444312215 scopus 로고    scopus 로고
    • Campylobacter jejuni gene expression in response to iron limitation and the role of Fur
    • Holmes, K., Mulholland, F., Pearson, B. M., Pin, C., Mcnicholl-Kennedy, J., Ketley, J. M., et al. (2005). Campylobacter jejuni gene expression in response to iron limitation and the role of Fur. Microbiology 151, 243-257. doi: 10.1099/mic.0.27412-0
    • (2005) Microbiology , vol.151 , pp. 243-257
    • Holmes, K.1    Mulholland, F.2    Pearson, B.M.3    Pin, C.4    Mcnicholl-Kennedy, J.5    Ketley, J.M.6
  • 61
    • 0032765193 scopus 로고    scopus 로고
    • Seasonal variation of Campylobacter types from human cases, veterinary cases, raw chicken, milk and water
    • Hudson, J. A., Nicol, C., Wright, J., Whyte, R., and Hasell, S. K. (1999). Seasonal variation of Campylobacter types from human cases, veterinary cases, raw chicken, milk and water. J. Appl. Microbiol. 87, 115-124. doi: 10.1046/j.1365-2672.1999.00806.x
    • (1999) J. Appl. Microbiol , vol.87 , pp. 115-124
    • Hudson, J.A.1    Nicol, C.2    Wright, J.3    Whyte, R.4    Hasell, S.K.5
  • 62
    • 84876191281 scopus 로고    scopus 로고
    • Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide
    • Huergo, L. F., Rahman, H., Ibrahimovic, A., Day, C. J., and Korolik, V. (2013). Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide. J. Bacteriol. 195, 1970-1978. doi: 10.1128/JB.00059-13
    • (2013) J. Bacteriol , vol.195 , pp. 1970-1978
    • Huergo, L.F.1    Rahman, H.2    Ibrahimovic, A.3    Day, C.J.4    Korolik, V.5
  • 63
    • 27644558148 scopus 로고    scopus 로고
    • Guillain-Barré syndrome
    • Hughes, R. A., and Cornblath, D. R. (2005). Guillain-Barré syndrome. Lancet 366, 1653-1666. doi: 10.1016/S0140-6736(05)67665-9
    • (2005) Lancet , vol.366 , pp. 1653-1666
    • Hughes, R.A.1    Cornblath, D.R.2
  • 64
    • 34250830856 scopus 로고    scopus 로고
    • Campylobacters as zoonotic pathogens: a food production perspective
    • Humphrey, T., O'brien, S., and Madsen, M. (2007). Campylobacters as zoonotic pathogens: a food production perspective. Int. J. Food Microbiol. 117, 237-257. doi: 10.1016/j.ijfoodmicro.2007.01.006
    • (2007) Int. J. Food Microbiol , vol.117 , pp. 237-257
    • Humphrey, T.1    O'brien, S.2    Madsen, M.3
  • 65
    • 80053174243 scopus 로고    scopus 로고
    • Roles of RpoN in the resistance of Campylobacter jejuni under various stress conditions
    • Hwang, S., Jeon, B., Yun, J., and Ryu, S. (2011a). Roles of RpoN in the resistance of Campylobacter jejuni under various stress conditions. BMC Microbiol. 11:207. doi: 10.1186/1471-2180-11-207
    • (2011) BMC Microbiol , vol.11 , pp. 207
    • Hwang, S.1    Jeon, B.2    Yun, J.3    Ryu, S.4
  • 66
    • 79960465228 scopus 로고    scopus 로고
    • Regulation of oxidative stress response by CosR, an essential response regulator in Campylobacter jejuni
    • Hwang, S., Kim, M., Ryu, S., and Jeon, B. (2011b). Regulation of oxidative stress response by CosR, an essential response regulator in Campylobacter jejuni. PLoS ONE 6:e22300. doi: 10.1371/journal.pone.0022300
    • (2011) PLoS ONE , vol.6
    • Hwang, S.1    Kim, M.2    Ryu, S.3    Jeon, B.4
  • 67
    • 84896530181 scopus 로고    scopus 로고
    • Divergent distribution of the sensor kinase CosS in non-thermotolerant Campylobacter species and its functional incompatibility with the response regulator CosR of Campylobacter jejuni
    • Hwang, S., Miller, W. G., Ryu, S., and Jeon, B. (2014). Divergent distribution of the sensor kinase CosS in non-thermotolerant Campylobacter species and its functional incompatibility with the response regulator CosR of Campylobacter jejuni. PLoS ONE 9:e89774. doi: 10.1371/journal.pone.0089774
    • (2014) PLoS ONE , vol.9
    • Hwang, S.1    Miller, W.G.2    Ryu, S.3    Jeon, B.4
  • 68
    • 84879649479 scopus 로고    scopus 로고
    • Roles of the superoxide dismutase SodB and the catalase KatA in the antibiotic resistance of Campylobacter jejuni
    • Hwang, S., Ryu, S., and Jeon, B. (2013). Roles of the superoxide dismutase SodB and the catalase KatA in the antibiotic resistance of Campylobacter jejuni. J. Antibiot. (Tokyo) 66, 351-353. doi: 10.1038/ja.2013.20
    • (2013) J. Antibiot. (Tokyo) , vol.66 , pp. 351-353
    • Hwang, S.1    Ryu, S.2    Jeon, B.3
  • 69
    • 84870694009 scopus 로고    scopus 로고
    • Transcriptional regulation of the CmeABC multidrug effux pump and the KatA catalase by CosR in Campylobacter jejuni
    • Hwang, S., Zhang, Q., Ryu, S., and Jeon, B. (2012). Transcriptional regulation of the CmeABC multidrug effux pump and the KatA catalase by CosR in Campylobacter jejuni. J. Bacteriol. 194, 6883-6891. doi: 10.1128/JB.01636-12
    • (2012) J. Bacteriol , vol.194 , pp. 6883-6891
    • Hwang, S.1    Zhang, Q.2    Ryu, S.3    Jeon, B.4
  • 70
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. (2003). Pathways of oxidative damage. Annu. Rev. Microbiol. 57, 395-418. doi: 10.1146/annurev.micro.57.030502.090938
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 71
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. (2008). Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 77, 755-776. doi: 10.1146/annurev.biochem.77.061606.161055
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 72
    • 84923003460 scopus 로고    scopus 로고
    • Diagnosing oxidative stress in bacteria: not as easy as you might think
    • Imlay, J. A. (2015). Diagnosing oxidative stress in bacteria: not as easy as you might think. Curr. Opin. Microbiol. 24, 124-131. doi: 10.1016/j.mib.2015.01.004
    • (2015) Curr. Opin. Microbiol , vol.24 , pp. 124-131
    • Imlay, J.A.1
  • 73
    • 0037309086 scopus 로고    scopus 로고
    • The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni
    • Ishikawa, T., Mizunoe, Y., Kawabata, S., Takade, A., Harada, M., Wai, S. N., et al. (2003). The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J. Bacteriol. 185, 1010-1017. doi: 10.1128/JB.185.3.1010-1017.2003
    • (2003) J. Bacteriol , vol.185 , pp. 1010-1017
    • Ishikawa, T.1    Mizunoe, Y.2    Kawabata, S.3    Takade, A.4    Harada, M.5    Wai, S.N.6
  • 75
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties
    • Jacobson, F. S., Morgan, R. W., Christman, M. F., and Ames, B. N. (1989). An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage. Purification and properties. J. Biol. Chem. 264, 1488-1496.
    • (1989) J. Biol. Chem , vol.264 , pp. 1488-1496
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.N.4
  • 76
    • 0025332515 scopus 로고
    • Starvation-induced cross protection against osmotic challenge in Escherichia coli
    • Jenkins, D. E., Chaisson, S. A., and Matin, A. (1990). Starvation-induced cross protection against osmotic challenge in Escherichia coli. J. Bacteriol. 172, 2779-2781.
    • (1990) J. Bacteriol , vol.172 , pp. 2779-2781
    • Jenkins, D.E.1    Chaisson, S.A.2    Matin, A.3
  • 78
    • 77953579655 scopus 로고    scopus 로고
    • Advances in Campylobacter biology and implications for biotechnological applications
    • Jeon, B., Muraoka, W. T., and Zhang, Q. (2010). Advances in Campylobacter biology and implications for biotechnological applications. Microb. Biotechnol. 3, 242-258. doi: 10.1111/j.1751-7915.2009.00118.x
    • (2010) Microb. Biotechnol , vol.3 , pp. 242-258
    • Jeon, B.1    Muraoka, W.T.2    Zhang, Q.3
  • 79
    • 78650381828 scopus 로고    scopus 로고
    • Contribution of CmeG to antibiotic and oxidative stress resistance in Campylobacter jejuni
    • Jeon, B., Wang, Y., Hao, H., Barton, Y. W., and Zhang, Q. (2011). Contribution of CmeG to antibiotic and oxidative stress resistance in Campylobacter jejuni. J. Antimicrob. Chemother. 66, 79-85. doi: 10.1093/jac/dkq418
    • (2011) J. Antimicrob. Chemother , vol.66 , pp. 79-85
    • Jeon, B.1    Wang, Y.2    Hao, H.3    Barton, Y.W.4    Zhang, Q.5
  • 80
    • 64649104323 scopus 로고    scopus 로고
    • Sensitization of Campylobacter jejuni to fluoroquinolone and macrolide antibiotics by antisense inhibition of the CmeABC multidrug effux transporter
    • Jeon, B., and Zhang, Q. (2009). Sensitization of Campylobacter jejuni to fluoroquinolone and macrolide antibiotics by antisense inhibition of the CmeABC multidrug effux transporter. J. Antimicrob. Chemother. 63, 946-948. doi: 10.1093/jac/dkp067
    • (2009) J. Antimicrob. Chemother , vol.63 , pp. 946-948
    • Jeon, B.1    Zhang, Q.2
  • 81
    • 57049124285 scopus 로고    scopus 로고
    • Acid stress damage of DNA is prevented by Dps binding in Escherichia coli O157: H7
    • Jeong, K. C., Hung, K. F., Baumler, D. J., Byrd, J. J., and Kaspar, C. W. (2008). Acid stress damage of DNA is prevented by Dps binding in Escherichia coli O157: H7. BMC Microbiol. 8:181. doi: 10.1186/1471-2180-8-181
    • (2008) BMC Microbiol , vol.8 , pp. 181
    • Jeong, K.C.1    Hung, K.F.2    Baumler, D.J.3    Byrd, J.J.4    Kaspar, C.W.5
  • 82
    • 84934444233 scopus 로고    scopus 로고
    • Genotypes and antibiotic resistance of bovine Campylobacter and their contribution to human campylobacteriosis
    • Jonas, R., Kittl, S., Overesch, G., and Kuhnert, P. (2015). Genotypes and antibiotic resistance of bovine Campylobacter and their contribution to human campylobacteriosis. Epidemiol. Infect. 143, 2373-2380. doi: 10.1017/S095026881400341
    • (2015) Epidemiol. Infect , vol.143 , pp. 2373-2380
    • Jonas, R.1    Kittl, S.2    Overesch, G.3    Kuhnert, P.4
  • 83
    • 0037024074 scopus 로고    scopus 로고
    • Prevalence and numbers of Salmonella and Campylobacter spp. on raw, whole chickens in relation to sampling methods
    • Jorgensen, F., Bailey, R., Williams, S., Henderson, P., Wareing, D. R., Bolton, F. J., et al. (2002). Prevalence and numbers of Salmonella and Campylobacter spp. on raw, whole chickens in relation to sampling methods. Int. J. Food Microbiol. 76, 151-164. doi: 10.1016/S0168-1605(02)00027-2
    • (2002) Int. J. Food Microbiol , vol.76 , pp. 151-164
    • Jorgensen, F.1    Bailey, R.2    Williams, S.3    Henderson, P.4    Wareing, D.R.5    Bolton, F.J.6
  • 84
    • 72649100393 scopus 로고    scopus 로고
    • Insights into the molecular basis of the microaerophily of three Campylobacterales: a comparative study
    • Kaakoush, N. O., Baar, C., Mackichan, J., Schmidt, P., Fox, E. M., Schuster, S. C., et al. (2009). Insights into the molecular basis of the microaerophily of three Campylobacterales: a comparative study. Antonie Van Leeuwenhoek 96, 545-557. doi: 10.1007/s10482-009-9370-3
    • (2009) Antonie Van Leeuwenhoek , vol.96 , pp. 545-557
    • Kaakoush, N.O.1    Baar, C.2    Mackichan, J.3    Schmidt, P.4    Fox, E.M.5    Schuster, S.C.6
  • 85
    • 33744967758 scopus 로고    scopus 로고
    • Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation
    • Kalmokoff, M., Lanthier, P., Tremblay, T.-L., Foss, M., Lau, P. C., Sanders, G., et al. (2006). Proteomic analysis of Campylobacter jejuni 11168 biofilms reveals a role for the motility complex in biofilm formation. J. Bacteriol. 188, 4312-4320. doi: 10.1128/JB.01975-05
    • (2006) J. Bacteriol , vol.188 , pp. 4312-4320
    • Kalmokoff, M.1    Lanthier, P.2    Tremblay, T.-L.3    Foss, M.4    Lau, P.C.5    Sanders, G.6
  • 86
    • 84885339746 scopus 로고    scopus 로고
    • Of energy and survival incognito: a relationship between viable but non-culturable cells formation and inorganic polyphosphate and formate metabolism in Campylobacter jejuni
    • Kassem, II, Chandrashekhar, K., and Rajashekara, G. (2013). Of energy and survival incognito: a relationship between viable but non-culturable cells formation and inorganic polyphosphate and formate metabolism in Campylobacter jejuni. Front. Microbiol. 4:183. doi: 10.3389/fmicb.2013.00183
    • (2013) Front. Microbiol , vol.4 , pp. 183
    • Kassem, I.I.1    Chandrashekhar, K.2    Rajashekara, G.3
  • 87
    • 84927518242 scopus 로고    scopus 로고
    • Non-selective regulation of peroxide and superoxide resistance genes by PerR in Campylobacter jejuni
    • Kim, J. C., Oh, E., Hwang, S., Ryu, S., and Jeon, B. (2015). Non-selective regulation of peroxide and superoxide resistance genes by PerR in Campylobacter jejuni. Front. Microbiol. 6:126. doi: 10.3389/fmicb.2015.00126
    • (2015) Front. Microbiol , vol.6 , pp. 126
    • Kim, J.C.1    Oh, E.2    Hwang, S.3    Ryu, S.4    Jeon, B.5
  • 88
    • 80655125466 scopus 로고    scopus 로고
    • Regulation of perR expression by iron and PerR in Campylobacter jejuni
    • Kim, M., Hwang, S., Ryu, S., and Jeon, B. (2011). Regulation of perR expression by iron and PerR in Campylobacter jejuni. J. Bacteriol. 193, 6171-6178. doi: 10.1128/JB.05493-11
    • (2011) J. Bacteriol , vol.193 , pp. 6171-6178
    • Kim, M.1    Hwang, S.2    Ryu, S.3    Jeon, B.4
  • 89
    • 33845582991 scopus 로고    scopus 로고
    • The role of periplasmic antioxidant enzymes (superoxide dismutase and thiol peroxidase) of the Shiga toxin-producing Escherichia coli O157: H7 in the formation of biofilms
    • Kim, Y. H., Lee, Y., Kim, S., Yeom, J., Yeom, S., Seok Kim, B., et al. (2006). The role of periplasmic antioxidant enzymes (superoxide dismutase and thiol peroxidase) of the Shiga toxin-producing Escherichia coli O157: H7 in the formation of biofilms. Proteomics 6, 6181-6193. doi: 10.1002/pmic.200600320
    • (2006) Proteomics , vol.6 , pp. 6181-6193
    • Kim, Y.H.1    Lee, Y.2    Kim, S.3    Yeom, J.4    Yeom, S.5    Seok Kim, B.6
  • 90
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski, M. A., Dwyer, D. J., Hayete, B., Lawrence, C. A., and Collins, J. J. (2007). A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130, 797-810. doi: 10.1016/j.cell.2007.06.049
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 91
    • 8344225373 scopus 로고    scopus 로고
    • Role of catalase and oxyR in the viable but nonculturable state of Vibrio vulnificus
    • Kong, I. S., Bates, T. C., Hulsmann, A., Hassan, H., Smith, B. E., and Oliver, J. D. (2004). Role of catalase and oxyR in the viable but nonculturable state of Vibrio vulnificus. FEMS Microbiol. Ecol. 50, 133-142. doi: 10.1016/j.femsec.2004.06.004
    • (2004) FEMS Microbiol. Ecol , vol.50 , pp. 133-142
    • Kong, I.S.1    Bates, T.C.2    Hulsmann, A.3    Hassan, H.4    Smith, B.E.5    Oliver, J.D.6
  • 92
    • 0034473805 scopus 로고    scopus 로고
    • Campylobacter contamination of raw meat and poultry at retail sale: identification of multiple types and comparison with isolates from human infection
    • Kramer, J. M., Frost, J. A., Bolton, F. J., and Wareing, D. R. (2000). Campylobacter contamination of raw meat and poultry at retail sale: identification of multiple types and comparison with isolates from human infection. J. Food Prot. 63, 1654-1659.
    • (2000) J. Food Prot , vol.63 , pp. 1654-1659
    • Kramer, J.M.1    Frost, J.A.2    Bolton, F.J.3    Wareing, D.R.4
  • 93
    • 15544377794 scopus 로고    scopus 로고
    • Molecular and evolutionary basis of the cellular stress response
    • Kültz, D. (2005). Molecular and evolutionary basis of the cellular stress response. Annu. Rev. Physiol. 67, 225-257. doi: 10.1146/annurev.physiol.67.040403.103635
    • (2005) Annu. Rev. Physiol , vol.67 , pp. 225-257
    • Kültz, D.1
  • 94
    • 33645037891 scopus 로고    scopus 로고
    • 2 by metal-catalysed histidine oxidation
    • 2 by metal-catalysed histidine oxidation. Nature 440, 363-367. doi: 10.1038/nature04537
    • (2006) Nature , vol.440 , pp. 363-367
    • Lee, J.W.1    Helmann, J.D.2
  • 95
    • 0031253319 scopus 로고    scopus 로고
    • Chronic sequelae of foodborne disease
    • Lindsay, J. A. (1997). Chronic sequelae of foodborne disease. Emerg. Infect. Dis. 3, 443-452. doi: 10.3201/eid0304.970405
    • (1997) Emerg. Infect. Dis , vol.3 , pp. 443-452
    • Lindsay, J.A.1
  • 96
    • 84874695302 scopus 로고    scopus 로고
    • Cell death from antibiotics without the involvement of reactive oxygen species
    • Liu, Y., and Imlay, J. A. (2013). Cell death from antibiotics without the involvement of reactive oxygen species. Science 339, 1210-1213. doi: 10.1126/science.1232751
    • (2013) Science , vol.339 , pp. 1210-1213
    • Liu, Y.1    Imlay, J.A.2
  • 97
    • 63849262661 scopus 로고    scopus 로고
    • Antibiotic resistance in Campylobacter: emergence, transmission and persistence
    • Luangtongkum, T., Jeon, B., Han, J., Plummer, P., Logue, C. M., and Zhang, Q. (2009). Antibiotic resistance in Campylobacter: emergence, transmission and persistence. Fut. Microbiol. 4, 189-200. doi: 10.2217/17460913.4.2.189
    • (2009) Fut. Microbiol , vol.4 , pp. 189-200
    • Luangtongkum, T.1    Jeon, B.2    Han, J.3    Plummer, P.4    Logue, C.M.5    Zhang, Q.6
  • 98
    • 78650598564 scopus 로고    scopus 로고
    • Adaptive response to oxidative stress: bacteria, fungi, plants and animals
    • Lushchak, V. I. (2011). Adaptive response to oxidative stress: bacteria, fungi, plants and animals. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 153, 175-190. doi: 10.1016/j.cbpc.2010.10.004
    • (2011) Comp. Biochem. Physiol. C Toxicol. Pharmacol , vol.153 , pp. 175-190
    • Lushchak, V.I.1
  • 99
    • 0036532548 scopus 로고    scopus 로고
    • Exploiting genome sequence: predictions for mechanisms of Campylobacter chemotaxis
    • Marchant, J., Wren, B., and Ketley, J. (2002). Exploiting genome sequence: predictions for mechanisms of Campylobacter chemotaxis. Trends Microbiol. 10, 155-159. doi: 10.1016/S0966-842X(02)02323-5
    • (2002) Trends Microbiol , vol.10 , pp. 155-159
    • Marchant, J.1    Wren, B.2    Ketley, J.3
  • 100
    • 0034489261 scopus 로고    scopus 로고
    • D-and Z-values of Salmonella in ground chicken breast meat
    • Mazzotta, A. S. (2000). D-and Z-values of Salmonella in ground chicken breast meat. J. Food Safety 20, 217-223. doi: 10.1111/j.1745-4565.2000.tb00300.x
    • (2000) J. Food Safety , vol.20 , pp. 217-223
    • Mazzotta, A.S.1
  • 102
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk, S., and Helmann, J. D. (2002). Regulation of inducible peroxide stress responses. Mol. Microbiol. 45, 9-15. doi: 10.1046/j.1365-2958.2002.03015.x
    • (2002) Mol. Microbiol , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 103
    • 0037532415 scopus 로고    scopus 로고
    • Induction of an adaptive tolerance response in the foodborne pathogen, Campylobacter jejuni
    • Murphy, C., Carroll, C., and Jordan, K. N. (2003). Induction of an adaptive tolerance response in the foodborne pathogen, Campylobacter jejuni. FEMS Microbiol. Lett. 223, 89-93. doi: 10.1016/S0378-1097(03)00348-3
    • (2003) FEMS Microbiol. Lett , vol.223 , pp. 89-93
    • Murphy, C.1    Carroll, C.2    Jordan, K.N.3
  • 104
    • 33645104244 scopus 로고    scopus 로고
    • Environmental survival mechanisms of the foodborne pathogen Campylobacter jejuni
    • Murphy, C., Carroll, C., and Jordan, K. N. (2006). Environmental survival mechanisms of the foodborne pathogen Campylobacter jejuni. J. Appl. Microbiol. 100, 623-632. doi: 10.1111/j.1365-2672.2006.02903.x
    • (2006) J. Appl. Microbiol , vol.100 , pp. 623-632
    • Murphy, C.1    Carroll, C.2    Jordan, K.N.3
  • 105
    • 84900329114 scopus 로고    scopus 로고
    • Role of alkyl hydroperoxide reductase (AhpC) in the biofilm formation of Campylobacter jejuni
    • Oh, E., and Jeon, B. (2014). Role of alkyl hydroperoxide reductase (AhpC) in the biofilm formation of Campylobacter jejuni. PLoS ONE 9:e87312. doi: 10.1371/journal.pone.0087312
    • (2014) PLoS ONE , vol.9
    • Oh, E.1    Jeon, B.2
  • 106
    • 84930935901 scopus 로고    scopus 로고
    • Impact of oxidative stress defense on bacterial survival and morphological change in Campylobacter jejuni under aerobic conditions
    • Oh, E., Mcmullen, L., and Jeon, B. (2015). Impact of oxidative stress defense on bacterial survival and morphological change in Campylobacter jejuni under aerobic conditions. Front. Microbiol. 6:295. doi: 10.3389/fmicb.2015.00295
    • (2015) Front. Microbiol , vol.6 , pp. 295
    • Oh, E.1    Mcmullen, L.2    Jeon, B.3
  • 107
    • 77953206132 scopus 로고    scopus 로고
    • Recent findings on the viable but nonculturable state in pathogenic bacteria
    • Oliver, J. D. (2010). Recent findings on the viable but nonculturable state in pathogenic bacteria. FEMS Microbiol. Rev. 34, 415-425. doi: 10.1111/j.1574-6976.2009.00200.x
    • (2010) FEMS Microbiol. Rev , vol.34 , pp. 415-425
    • Oliver, J.D.1
  • 108
    • 70549097051 scopus 로고    scopus 로고
    • Characterization of the oxidative stress stimulon and PerR regulon of Campylobacter jejuni
    • Palyada, K., Sun, Y. Q., Flint, A., Butcher, J., Naikare, H., and Stintzi, A. (2009). Characterization of the oxidative stress stimulon and PerR regulon of Campylobacter jejuni. BMC Genom. 10:481. doi: 10.1186/1471-2164-10-481
    • (2009) BMC Genom , vol.10 , pp. 481
    • Palyada, K.1    Sun, Y.Q.2    Flint, A.3    Butcher, J.4    Naikare, H.5    Stintzi, A.6
  • 109
    • 3042855363 scopus 로고    scopus 로고
    • Iron acquisition and regulation in Campylobacter jejuni
    • Palyada, K., Threadgill, D., and Stintzi, A. (2004). Iron acquisition and regulation in Campylobacter jejuni. J. Bacteriol. 186, 4714-4729. doi: 10.1128/JB.186.14.4714-4729.2004
    • (2004) J. Bacteriol , vol.186 , pp. 4714-4729
    • Palyada, K.1    Threadgill, D.2    Stintzi, A.3
  • 110
    • 0037023234 scopus 로고    scopus 로고
    • The physiology of Campylobacter species and its relevance to their role as foodborne pathogens
    • Park, S. F. (2002). The physiology of Campylobacter species and its relevance to their role as foodborne pathogens. Int. J. Food Microbiol. 74, 177-188. doi: 10.1016/S0168-1605(01)00678-X
    • (2002) Int. J. Food Microbiol , vol.74 , pp. 177-188
    • Park, S.F.1
  • 111
    • 0034628526 scopus 로고    scopus 로고
    • The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences
    • Parkhill, J., Wren, B. W., Mungall, K., Ketley, J. M., Churcher, C., Basham, D., et al. (2000). The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403, 665-668. doi: 10.1038/35001088
    • (2000) Nature , vol.403 , pp. 665-668
    • Parkhill, J.1    Wren, B.W.2    Mungall, K.3    Ketley, J.M.4    Churcher, C.5    Basham, D.6
  • 112
    • 0242523776 scopus 로고    scopus 로고
    • Bacterial biofilms: an emerging link to disease pathogenesis
    • Parsek, M. R., and Singh, P. K. (2003). Bacterial biofilms: an emerging link to disease pathogenesis. Annu. Rev. Microbiol. 57, 677-701. doi: 10.1146/annurev.micro.57.030502.090720
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 677-701
    • Parsek, M.R.1    Singh, P.K.2
  • 113
    • 0028236403 scopus 로고
    • Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni
    • Pesci, E. C., Cottle, D. L., and Pickett, C. L. (1994). Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni. Infect. Immun. 62, 2687-2694.
    • (1994) Infect. Immun , vol.62 , pp. 2687-2694
    • Pesci, E.C.1    Cottle, D.L.2    Pickett, C.L.3
  • 114
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello, P. J., Bennik, M. H., and Demple, B. (2001). Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J. Bacteriol. 183, 3890-3902. doi: 10.1128/JB.183.13.3890-3902.2001
    • (2001) J. Bacteriol , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 115
    • 18944374541 scopus 로고    scopus 로고
    • The Campylobacter jejuni response regulator, CbrR, modulates sodium deoxycholate resistance and chicken colonization
    • Raphael, B. H., Pereira, S., Flom, G. A., Zhang, Q., Ketley, J. M., and Konkel, M. E. (2005). The Campylobacter jejuni response regulator, CbrR, modulates sodium deoxycholate resistance and chicken colonization. J. Bacteriol. 187, 3662-3670. doi: 10.1128/JB.187.11.3662-3670.2005
    • (2005) J. Bacteriol , vol.187 , pp. 3662-3670
    • Raphael, B.H.1    Pereira, S.2    Flom, G.A.3    Zhang, Q.4    Ketley, J.M.5    Konkel, M.E.6
  • 116
    • 77950291207 scopus 로고    scopus 로고
    • Biofilm formation by Campylobacter jejuni is increased under aerobic conditions
    • Reuter, M., Mallett, A., Pearson, B. M., and Van Vliet, A. H. (2010). Biofilm formation by Campylobacter jejuni is increased under aerobic conditions. Appl. Environ. Microbiol. 76, 2122-2128. doi: 10.1128/AEM.01878-09
    • (2010) Appl. Environ. Microbiol , vol.76 , pp. 2122-2128
    • Reuter, M.1    Mallett, A.2    Pearson, B.M.3    Van Vliet, A.H.4
  • 117
    • 33847082547 scopus 로고    scopus 로고
    • The health burden of Campylobacter infection and the impact of antimicrobial resistance: playing chicken
    • Ruiz-Palacios, G. M. (2007). The health burden of Campylobacter infection and the impact of antimicrobial resistance: playing chicken. Clin. Infect. Dis. 44, 701-703. doi: 10.1086/509936
    • (2007) Clin. Infect. Dis , vol.44 , pp. 701-703
    • Ruiz-Palacios, G.M.1
  • 118
    • 11144353967 scopus 로고    scopus 로고
    • Epidemiology of sporadic Campylobacter infection in the United States and declining trend in incidence, FoodNet 1996-1999
    • Samuel, M. C., Vugia, D. J., Shallow, S., Marcus, R., Segler, S., Mcgivern, T., et al. (2004). Epidemiology of sporadic Campylobacter infection in the United States and declining trend in incidence, FoodNet 1996-1999. Clin. Infect. Dis. 38(Suppl. 3), S165-S174. doi: 10.1086/381583
    • (2004) Clin. Infect. Dis , vol.38 , pp. S165-S174
    • Samuel, M.C.1    Vugia, D.J.2    Shallow, S.3    Marcus, R.4    Segler, S.5    Mcgivern, T.6
  • 119
    • 84855432040 scopus 로고    scopus 로고
    • Economic burden from health losses due to foodborne illness in the United States
    • Scharff, R. L. (2012). Economic burden from health losses due to foodborne illness in the United States. J. Food Prot. 75, 123-131. doi: 10.4315/0362-028X.JFP-11-058
    • (2012) J. Food Prot , vol.75 , pp. 123-131
    • Scharff, R.L.1
  • 120
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L. C., and Imlay, J. A. (2001). Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183, 7173-7181. doi: 10.1128/JB.183.24.7173-7181.2001
    • (2001) J. Bacteriol , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 121
    • 38449119456 scopus 로고    scopus 로고
    • Emerging fluoroquinolone and macrolide resistance of Campylobacter jejuni and Campylobacter coli isolates and their serotypes in Thai children from 1991 to 2000
    • Serichantalergs, O., Dalsgaard, A., Bodhidatta, L., Krasaesub, S., Pitarangsi, C., Srijan, A., et al. (2007). Emerging fluoroquinolone and macrolide resistance of Campylobacter jejuni and Campylobacter coli isolates and their serotypes in Thai children from 1991 to 2000. Epidemiol. Infect. 135, 1299-1306. doi: 10.1017/S0950268807008096
    • (2007) Epidemiol. Infect , vol.135 , pp. 1299-1306
    • Serichantalergs, O.1    Dalsgaard, A.2    Bodhidatta, L.3    Krasaesub, S.4    Pitarangsi, C.5    Srijan, A.6
  • 122
    • 0033932215 scopus 로고    scopus 로고
    • Roles of Fe superoxide dismutase and catalase in resistance of Campylobacter coli to freeze-thaw stress
    • Stead, D., and Park, S. F. (2000). Roles of Fe superoxide dismutase and catalase in resistance of Campylobacter coli to freeze-thaw stress. Appl. Environ. Microbiol. 66, 3110-3112. doi: 10.1128/AEM.66.7.3110-3112.2000
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 3110-3112
    • Stead, D.1    Park, S.F.2
  • 123
    • 0037337513 scopus 로고    scopus 로고
    • Gene expression profile of Campylobacter jejuni in response to growth temperature variation
    • Stintzi, A. (2003). Gene expression profile of Campylobacter jejuni in response to growth temperature variation. J. Bacteriol. 185, 2009-2016. doi: 10.1128/JB.185.6.2009-2016.2003
    • (2003) J. Bacteriol , vol.185 , pp. 2009-2016
    • Stintzi, A.1
  • 124
    • 3042726376 scopus 로고    scopus 로고
    • Investigation of the Campylobacter jejuni cold-shock response by global transcript profiling
    • Stintzi, A., and Whitworth, L. (2003). Investigation of the Campylobacter jejuni cold-shock response by global transcript profiling. Genome Lett. 2, 18-27.
    • (2003) Genome Lett , vol.2 , pp. 18-27
    • Stintzi, A.1    Whitworth, L.2
  • 125
    • 0033118910 scopus 로고    scopus 로고
    • Oxidative stress
    • Storz, G., and Imlay, J. A. (1999). Oxidative stress. Curr. Opin. Microbiol. 2, 188-194. doi: 10.1016/S1369-5274(99)80033-2
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 188-194
    • Storz, G.1    Imlay, J.A.2
  • 126
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp
    • Storz, G., Jacobson, F. S., Tartaglia, L. A., Morgan, R. W., Silveira, L. A., and Ames, B. N. (1989). An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J. Bacteriol. 171, 2049-2055.
    • (1989) J. Bacteriol , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 127
    • 0028233079 scopus 로고
    • Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri
    • Suzuki, T., Murai, T., Fukuda, I., Tobe, T., Yoshikawa, M., and Sasakawa, C. (1994). Identification and characterization of a chromosomal virulence gene, vacJ, required for intercellular spreading of Shigella flexneri. Mol. Microbiol. 11, 31-41. doi: 10.1111/j.1365-2958.1994.tb00287.x
    • (1994) Mol. Microbiol , vol.11 , pp. 31-41
    • Suzuki, T.1    Murai, T.2    Fukuda, I.3    Tobe, T.4    Yoshikawa, M.5    Sasakawa, C.6
  • 128
    • 58149105541 scopus 로고    scopus 로고
    • The CprS sensor kinase of the zoonotic pathogen Campylobacter jejuni influences biofilm formation and is required for optimal chick colonization
    • Svensson, S. L., Davis, L. M., Mackichan, J. K., Allan, B. J., Pajaniappan, M., Thompson, S. A., et al. (2009). The CprS sensor kinase of the zoonotic pathogen Campylobacter jejuni influences biofilm formation and is required for optimal chick colonization. Mol. Microbiol. 71, 253-272. doi: 10.1111/j.1365-2958.2008.06534.x
    • (2009) Mol. Microbiol , vol.71 , pp. 253-272
    • Svensson, S.L.1    Davis, L.M.2    Mackichan, J.K.3    Allan, B.J.4    Pajaniappan, M.5    Thompson, S.A.6
  • 129
    • 84925408769 scopus 로고    scopus 로고
    • The Campylobacter jejuni CprRS two-component regulatory system regulates aspects of the cell envelope
    • Svensson, S. L., Hyunh, S., Parker, C. T., and Gaynor, E. C. (2015). The Campylobacter jejuni CprRS two-component regulatory system regulates aspects of the cell envelope. Mol. Microbiol. 96, 189-209. doi: 10.1111/mmi.12927
    • (2015) Mol. Microbiol , vol.96 , pp. 189-209
    • Svensson, S.L.1    Hyunh, S.2    Parker, C.T.3    Gaynor, E.C.4
  • 130
    • 0027416847 scopus 로고
    • Involvement of the RNA polymerase alpha subunit C-terminal region in co-operative interaction and transcriptional activation with OxyR protein
    • Tao, K., Fujita, N., and Ishihama, A. (1993). Involvement of the RNA polymerase alpha subunit C-terminal region in co-operative interaction and transcriptional activation with OxyR protein. Mol. Microbiol. 7, 859-864. doi: 10.1111/j.1365-2958.1993.tb01176.x
    • (1993) Mol. Microbiol , vol.7 , pp. 859-864
    • Tao, K.1    Fujita, N.2    Ishihama, A.3
  • 131
    • 84875988295 scopus 로고    scopus 로고
    • Common source outbreaks of Campylobacter infection in the USA, 1997-2008
    • Taylor, E. V., Herman, K. M., Ailes, E. C., Fitzgerald, C., Yoder, J. S., Mahon, B. E., et al. (2013). Common source outbreaks of Campylobacter infection in the USA, 1997-2008. Epidemiol. Infect. 141, 987-996. doi: 10.1017/S0950268812001744
    • (2013) Epidemiol. Infect , vol.141 , pp. 987-996
    • Taylor, E.V.1    Herman, K.M.2    Ailes, E.C.3    Fitzgerald, C.4    Yoder, J.S.5    Mahon, B.E.6
  • 132
    • 0036118981 scopus 로고    scopus 로고
    • Culturability, injury and morphological dynamics of thermophilic Campylobacter spp. within a laboratory-based aquatic model system
    • Thomas, C., Hill, D., and Mabey, M. (2002). Culturability, injury and morphological dynamics of thermophilic Campylobacter spp. within a laboratory-based aquatic model system. J. Appl. Microbiol. 92, 433-442. doi: 10.1046/j.1365-2672.2002.01550.x
    • (2002) J. Appl. Microbiol , vol.92 , pp. 433-442
    • Thomas, C.1    Hill, D.2    Mabey, M.3
  • 133
    • 0032976736 scopus 로고    scopus 로고
    • Evaluation of the effect of temperature and nutrients on the survival of Campylobacter spp. in water microcosms
    • Thomas, C., Hill, D. J., and Mabey, M. (1999). Evaluation of the effect of temperature and nutrients on the survival of Campylobacter spp. in water microcosms. J. Appl. Microbiol. 86, 1024-1032. doi: 10.1046/j.1365-2672.1999.00789.x
    • (1999) J. Appl. Microbiol , vol.86 , pp. 1024-1032
    • Thomas, C.1    Hill, D.J.2    Mabey, M.3
  • 134
    • 33749459445 scopus 로고    scopus 로고
    • Estimated numbers of community cases of illness due to Salmonella, Campylobacter and Verotoxigenic Escherichia coli: pathogen-specific community rates
    • Thomas, M. K., Majowicz, S. E., Sockett, P. N., Fazil, A., Pollari, F., Dore, K., et al. (2006). Estimated numbers of community cases of illness due to Salmonella, Campylobacter and Verotoxigenic Escherichia coli: pathogen-specific community rates. Can. J. Infect. Dis. Med. Microbiol. 17, 229-234.
    • (2006) Can. J. Infect. Dis. Med. Microbiol , vol.17 , pp. 229-234
    • Thomas, M.K.1    Majowicz, S.E.2    Sockett, P.N.3    Fazil, A.4    Pollari, F.5    Dore, K.6
  • 135
    • 0025369726 scopus 로고
    • soxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • Tsaneva, I. R., and Weiss, B. (1990). soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 172, 4197-4205.
    • (1990) J. Bacteriol , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 136
    • 0035868449 scopus 로고    scopus 로고
    • The iron-induced ferredoxin FdxA of Campylobacter jejuni is involved in aerotolerance
    • van Vliet, A. H., Baillon, M.-L. A., Penn, C. W., and Ketley, J. M. (2001). The iron-induced ferredoxin FdxA of Campylobacter jejuni is involved in aerotolerance. FEMS Microbiol. Lett. 196, 189-193. doi: 10.1016/S0378-1097(01)00067-2
    • (2001) FEMS Microbiol. Lett , vol.196 , pp. 189-193
    • van Vliet, A.H.1    Baillon, M.-L.A.2    Penn, C.W.3    Ketley, J.M.4
  • 137
    • 0032716842 scopus 로고    scopus 로고
    • Campylobacter jejuni contains two fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor
    • van Vliet, A. H., Baillon, M. L., Penn, C. W., and Ketley, J. M. (1999). Campylobacter jejuni contains two fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. J. Bacteriol. 181, 6371-6376.
    • (1999) J. Bacteriol , vol.181 , pp. 6371-6376
    • van Vliet, A.H.1    Baillon, M.L.2    Penn, C.W.3    Ketley, J.M.4
  • 138
    • 0036285109 scopus 로고    scopus 로고
    • The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense
    • van Vliet, A. H., Ketley, J. M., Park, S. F., and Penn, C. W. (2002). The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense. FEMS Microbiol. Rev. 26, 173-186. doi: 10.1111/j.1574-6976.2002.tb00609.x
    • (2002) FEMS Microbiol. Rev , vol.26 , pp. 173-186
    • van Vliet, A.H.1    Ketley, J.M.2    Park, S.F.3    Penn, C.W.4
  • 139
    • 0031690670 scopus 로고    scopus 로고
    • Iron-responsive gene regulation in a Campylobacter jejuni fur mutant
    • van Vliet, A. H., Wooldridge, K. G., and Ketley, J. M. (1998). Iron-responsive gene regulation in a Campylobacter jejuni fur mutant. J. Bacteriol. 180, 5291-5298.
    • (1998) J. Bacteriol , vol.180 , pp. 5291-5298
    • van Vliet, A.H.1    Wooldridge, K.G.2    Ketley, J.M.3
  • 140
    • 66949145150 scopus 로고    scopus 로고
    • Stress, sublethal injury, resuscitation, and virulence of bacterial foodborne pathogens
    • Wesche, A. M., Gurtler, J. B., Marks, B. P., and Ryser, E. T. (2009). Stress, sublethal injury, resuscitation, and virulence of bacterial foodborne pathogens. J. Food Prot. 72, 1121-1138.
    • (2009) J. Food Prot , vol.72 , pp. 1121-1138
    • Wesche, A.M.1    Gurtler, J.B.2    Marks, B.P.3    Ryser, E.T.4
  • 141
    • 0030003864 scopus 로고    scopus 로고
    • Presence of Salmonella spp. and Campylobacter spp. in shellfish
    • Wilson, I. G., and Moore, J. E. (1996). Presence of Salmonella spp. and Campylobacter spp. in shellfish. Epidemiol. Infect. 116, 147-153. doi: 10.1017/S0950268800052377
    • (1996) Epidemiol. Infect , vol.116 , pp. 147-153
    • Wilson, I.G.1    Moore, J.E.2
  • 143
    • 0033923299 scopus 로고    scopus 로고
    • The role of cold-shock proteins in low-temperature adaptation of food-related bacteria
    • Wouters, J. A., Rombouts, F. M., Kuipers, O. P., De Vos, W. M., and Abee, T. (2000). The role of cold-shock proteins in low-temperature adaptation of food-related bacteria. Syst. Appl. Microbiol. 23, 165-173. doi: 10.1016/S0723-2020(00)80001-6
    • (2000) Syst. Appl. Microbiol , vol.23 , pp. 165-173
    • Wouters, J.A.1    Rombouts, F.M.2    Kuipers, O.P.3    De Vos, W.M.4    Abee, T.5
  • 144
    • 61449258411 scopus 로고    scopus 로고
    • Metabolite and transcriptome analysis of Campylobacter jejuni in vitro growth reveals a stationary-phase physiological switch
    • Wright, J. A., Grant, A. J., Hurd, D., Harrison, M., Guccione, E. J., Kelly, D. J., et al. (2009). Metabolite and transcriptome analysis of Campylobacter jejuni in vitro growth reveals a stationary-phase physiological switch. Microbiology 155, 80-94. doi: 10.1099/mic.0.021790-0
    • (2009) Microbiology , vol.155 , pp. 80-94
    • Wright, J.A.1    Grant, A.J.2    Hurd, D.3    Harrison, M.4    Guccione, E.J.5    Kelly, D.J.6
  • 145
    • 2442665515 scopus 로고    scopus 로고
    • Identification of an oxidative stress-sensitive protein from Campylobacter jejuni, homologous to rubredoxin oxidoreductase/rubrerythrin
    • Yamasaki, M., Igimi, S., Katayama, Y., Yamamoto, S., and Amano, F. (2004). Identification of an oxidative stress-sensitive protein from Campylobacter jejuni, homologous to rubredoxin oxidoreductase/rubrerythrin. FEMS Microbiol. Lett. 235, 57-63. doi: 10.1016/j.femsle.2004.04.012S037810970400271X
    • (2004) FEMS Microbiol. Lett , vol.235 , pp. 57-63
    • Yamasaki, M.1    Igimi, S.2    Katayama, Y.3    Yamamoto, S.4    Amano, F.5
  • 146
    • 34548028239 scopus 로고    scopus 로고
    • Campylobacter jejuni: molecular biology and pathogenesis
    • Young, K. T., Davis, L. M., and Dirita, V. J. (2007). Campylobacter jejuni: molecular biology and pathogenesis. Nat. Rev. Microbiol. 5, 665-679. doi: 10.1038/nrmicro1718
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 665-679
    • Young, K.T.1    Davis, L.M.2    Dirita, V.J.3
  • 147
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., et al. (2002). Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli. J. Biol. Chem. 277, 27689-27696. doi: 10.1074/jbc.M202094200
    • (2002) J. Biol. Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6
  • 148
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F., and Storz, G. (1998). Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721. doi: 10.1126/science.279.5357.1718
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 149
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., Wang, X., Templeton, L. J., Smulski, D. R., Larossa, R. A., and Storz, G. (2001). DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 183, 4562-4570. doi: 10.1128/JB.183.15.4562-4570.2001
    • (2001) J. Bacteriol , vol.183 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    Larossa, R.A.5    Storz, G.6


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