메뉴 건너뛰기




Volumn 80, Issue 1, 2016, Pages 69-90

Vibrio Iron transport: Evolutionary adaptation to life in multiple environments

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOPHILE; CARBOXYLIC ACID; CATECHOL DERIVATIVE; FERRIC ION; HEME; HYDROXAMIC ACID; IRON COMPLEX; RECEPTOR; SIDEROPHORE; BACTERIAL PROTEIN; CARRIER PROTEIN; CELL SURFACE RECEPTOR; HEME RECEPTOR; IRON; OUTER MEMBRANE PROTEIN; SIDEROPHORE RECEPTORS;

EID: 84963997967     PISSN: 10922172     EISSN: 10985557     Source Type: Journal    
DOI: 10.1128/MMBR.00046-15     Document Type: Review
Times cited : (93)

References (263)
  • 1
    • 0001199114 scopus 로고    scopus 로고
    • The family vibrionaceae
    • Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E ed, Springer, New York, NY
    • Farmer JJI. 2006. The family Vibrionaceae, p 495-507. In Dworkin M, Falkow S, Rosenberg E, Schleifer K-H, Stackebrandt E (ed), The prokaryotes. Springer, New York, NY.
    • (2006) The Prokaryotes , pp. 495-507
    • Farmer, J.J.I.1
  • 2
    • 0032564430 scopus 로고    scopus 로고
    • The Vibrio cholerae genome contains two unique circular chromosomes
    • Trucksis M, Michalski J, Deng YK, Kaper JB. 1998. The Vibrio cholerae genome contains two unique circular chromosomes. Proc Natl Acad Sci U S A 95:14464-14469. http://dx.doi.org/10.1073/pnas.95.24.14464.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14464-14469
    • Trucksis, M.1    Michalski, J.2    Deng, Y.K.3    Kaper, J.B.4
  • 4
    • 33646469858 scopus 로고    scopus 로고
    • Vibrio parahaemolyticus growth under low-iron conditions and survival under high-magnesium conditions
    • Ju C-H, Yeung PSM, Oesterling J, Seigerman DA, Boor KJ. 2006. Vibrio parahaemolyticus growth under low-iron conditions and survival under high-magnesium conditions. J Food Prot 69:1040-1045.
    • (2006) J Food Prot , vol.69 , pp. 1040-1045
    • Ju, C.-H.1    Yeung, P.S.M.2    Oesterling, J.3    Seigerman, D.A.4    Boor, K.J.5
  • 5
    • 0020079667 scopus 로고
    • Effect of iron limitation on growth, siderophore production, and expression of outer membrane proteins of Vibrio cholerae
    • Sigel SP, Payne SM. 1982. Effect of iron limitation on growth, siderophore production, and expression of outer membrane proteins of Vibrio cholerae. J Bacteriol 150:148-155.
    • (1982) J Bacteriol , vol.150 , pp. 148-155
    • Sigel, S.P.1    Payne, S.M.2
  • 8
    • 0013636309 scopus 로고
    • Chemical factors that influence the availability of iron and manganese in aqueous systems
    • Hem JD. 1972. Chemical factors that influence the availability of iron and manganese in aqueous systems. Geol Soc Am Spec Pap 140:17-24. http://dx.doi.org/10.1130/SPE140-p17.
    • (1972) Geol Soc Am Spec Pap , vol.140 , pp. 17-24
    • Hem, J.D.1
  • 9
    • 0026363720 scopus 로고
    • Iron limitation? The case for iron
    • Martin JH, Gordon RM, Fitzwater SE. 1991. Iron limitation? The case for iron. Limnol Oceanogr 36:1793-1802. http://dx.doi.org/10.4319/lo.1991.36.8.1793.
    • (1991) Limnol Oceanogr , vol.36 , pp. 1793-1802
    • Martin, J.H.1    Gordon, R.M.2    Fitzwater, S.E.3
  • 10
    • 84904195913 scopus 로고    scopus 로고
    • Quantification of dissolved iron sources to the North Atlantic Ocean
    • Conway TM, John SG. 2014. Quantification of dissolved iron sources to the North Atlantic Ocean. Nature 511:212-215. http://dx.doi.org/10.1038/nature13482.
    • (2014) Nature , vol.511 , pp. 212-215
    • Conway, T.M.1    John, S.G.2
  • 11
    • 84893876198 scopus 로고    scopus 로고
    • Microbial iron uptake as a mechanism for dispersing iron from deep-sea hydrothermal vents
    • Li M, Toner BM, Baker BJ, Breier JA, Sheik CS, Dick GJ. 2014. Microbial iron uptake as a mechanism for dispersing iron from deep-sea hydrothermal vents. Nat Commun 5:3192. http://dx.doi.org/10.1038/ncomms4192.
    • (2014) Nat Commun , vol.5 , pp. 3192
    • Li, M.1    Toner, B.M.2    Baker, B.J.3    Breier, J.A.4    Sheik, C.S.5    Dick, G.J.6
  • 12
    • 0028908183 scopus 로고
    • Effect of iron and pH on the survival of Vibrio cholerae in water
    • Patel M, Isaäcson M, Gouws E. 1995. Effect of iron and pH on the survival of Vibrio cholerae in water. Trans R Soc Trop Med Hyg 89:175-177. http://dx.doi.org/10.1016/0035-9203 (95) 90484-0.
    • (1995) Trans R Soc Trop Med Hyg , vol.89 , pp. 175-177
    • Patel, M.1    Isaäcson, M.2    Gouws, E.3
  • 13
    • 0033946154 scopus 로고    scopus 로고
    • Effect of iron on the survival of Vibrio cholerae in water
    • Joseph S, Bhat KG. 2000. Effect of iron on the survival of Vibrio cholerae in water. Indian J Med Res 111:115-117.
    • (2000) Indian J Med Res , vol.111 , pp. 115-117
    • Joseph, S.1    Bhat, K.G.2
  • 14
    • 0026317736 scopus 로고
    • Resuscitation of Vibrio vulnificus from the viable but nonculturable state
    • Nilsson L, Oliver JD, Kjelleberg S. 1991. Resuscitation of Vibrio vulnificus from the viable but nonculturable state. J Bacteriol 173:5054-5059.
    • (1991) J Bacteriol , vol.173 , pp. 5054-5059
    • Nilsson, L.1    Oliver, J.D.2    Kjelleberg, S.3
  • 15
    • 0020286856 scopus 로고
    • Survival and viability of nonculturable Escherichia coli and Vibrio cholerae in the estuarine and marine environment
    • Xu HS, Roberts N, Singleton FL, Attwell RW, Grimes DJ, Colwell RR. 1982. Survival and viability of nonculturable Escherichia coli and Vibrio cholerae in the estuarine and marine environment. Microb Ecol 8:313-323. http://dx.doi.org/10.1007/BF02010671.
    • (1982) Microb Ecol , vol.8 , pp. 313-323
    • Xu, H.S.1    Roberts, N.2    Singleton, F.L.3    Attwell, R.W.4    Grimes, D.J.5    Colwell, R.R.6
  • 16
    • 33947155774 scopus 로고    scopus 로고
    • Gene expression profile of Vibrio cholerae in the cold stress-induced viable but non-culturable state
    • Asakura H, Ishiwa A, Arakawa E, Makino S, Okada Y, Yamamoto S, Igimi S. 2007. Gene expression profile of Vibrio cholerae in the cold stress-induced viable but non-culturable state. Environ Microbiol 9:869-879. http://dx.doi.org/10.1111/j.1462-2920.2006.01206.x.
    • (2007) Environ Microbiol , vol.9 , pp. 869-879
    • Asakura, H.1    Ishiwa, A.2    Arakawa, E.3    Makino, S.4    Okada, Y.5    Yamamoto, S.6    Igimi, S.7
  • 17
    • 61449151985 scopus 로고    scopus 로고
    • Vibrio biofilms: So much the same yet so different
    • Yildiz FH, Visick KL. 2009. Vibrio biofilms: so much the same yet so different. Trends Microbiol 17:109-118. http://dx.doi.org/10.1016/j.tim.2008.12.004.
    • (2009) Trends Microbiol , vol.17 , pp. 109-118
    • Yildiz, F.H.1    Visick, K.L.2
  • 18
    • 0035152224 scopus 로고    scopus 로고
    • Biofilm exopolysaccharides: A strong and sticky framework
    • Sutherland IW. 2001. Biofilm exopolysaccharides: a strong and sticky framework. Microbiology 147:3-9. http://dx.doi.org/10.1099/00221287-147-1-3.
    • (2001) Microbiology , vol.147 , pp. 3-9
    • Sutherland, I.W.1
  • 19
    • 0037372799 scopus 로고    scopus 로고
    • Diffusion in biofilms
    • Stewart PS. 2003. Diffusion in biofilms. J Bacteriol 185:1485-1491. http://dx.doi.org/10.1128/JB.185.5.1485-1491.2003.
    • (2003) J Bacteriol , vol.185 , pp. 1485-1491
    • Stewart, P.S.1
  • 20
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh PK, Parsek MR, Greenberg EP, Welsh MJ. 2002. A component of innate immunity prevents bacterial biofilm development. Nature 417:552-555. http://dx.doi.org/10.1038/417552a.
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 21
    • 23944509113 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae RyhB: The RyhB regulon and role of ryhB in biofilm formation
    • Mey AR, Craig SA, Payne SM. 2005. Characterization of Vibrio cholerae RyhB: the RyhB regulon and role of ryhB in biofilm formation. Infect Immun 73:5706-5719. http://dx.doi.org/10.1128/IAI.73.9.5706-5719.2005.
    • (2005) Infect Immun , vol.73 , pp. 5706-5719
    • Mey, A.R.1    Craig, S.A.2    Payne, S.M.3
  • 22
    • 0025259560 scopus 로고
    • Long-term persistence of toxigenic Vibrio cholerae 01 in the mucilaginous sheath of a blue-green alga, Anabaena variabilis
    • Islam MS, Drasar BS, Bradley DJ. 1990. Long-term persistence of toxigenic Vibrio cholerae 01 in the mucilaginous sheath of a blue-green alga, Anabaena variabilis. J Trop Med Hyg 93:133-139.
    • (1990) J Trop Med Hyg , vol.93 , pp. 133-139
    • Islam, M.S.1    Drasar, B.S.2    Bradley, D.J.3
  • 23
    • 0026625769 scopus 로고
    • A squid that glows in the night: Development of an animal-bacterial mutualism
    • Ruby EG, McFall-Ngai MJ. 1992. A squid that glows in the night: development of an animal-bacterial mutualism. J Bacteriol 174:4865-4870.
    • (1992) J Bacteriol , vol.174 , pp. 4865-4870
    • Ruby, E.G.1    McFall-Ngai, M.J.2
  • 24
    • 0031962855 scopus 로고    scopus 로고
    • A new niche for Vibrio logei, the predominant light organ symbiont of squids in the genus Sepiola
    • Fidopiastis PM, von Boletzky S, Ruby EG. 1998. A new niche for Vibrio logei, the predominant light organ symbiont of squids in the genus Sepiola. J Bacteriol 180:59-64.
    • (1998) J Bacteriol , vol.180 , pp. 59-64
    • Fidopiastis, P.M.1    Von Boletzky, S.2    Ruby, E.G.3
  • 25
    • 37449011476 scopus 로고    scopus 로고
    • Reclassification of Vibrio fischeri, Vibrio logei, Vibrio salmonicida and Vibrio wodanis as Aliivibrio fischeri gen. Nov., comb. Nov., Aliivibrio logei comb. Nov., Aliivibrio salmonicida comb. Nov. and Aliivibrio wodanis comb. Nov
    • Urbanczyk H, Ast JC, Higgins MJ, Carson J, Dunlap PV. 2007. Reclassification of Vibrio fischeri, Vibrio logei, Vibrio salmonicida and Vibrio wodanis as Aliivibrio fischeri gen. Nov., comb. Nov., Aliivibrio logei comb. Nov., Aliivibrio salmonicida comb. Nov. and Aliivibrio wodanis comb. Nov. Int J Syst Evol Microbiol 57:2823-2829. http://dx.doi.org/10.1099/ijs.0.65081-0.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 2823-2829
    • Urbanczyk, H.1    Ast, J.C.2    Higgins, M.J.3    Carson, J.4    Dunlap, P.V.5
  • 26
    • 0028363843 scopus 로고
    • Bacterial symbionts induce host organ morphogenesis during early postembryonic development of the squid Euprymna scolopes
    • Montgomery MK, McFall-Ngai M. 1994. Bacterial symbionts induce host organ morphogenesis during early postembryonic development of the squid Euprymna scolopes. Development 120:1719-1729.
    • (1994) Development , vol.120 , pp. 1719-1729
    • Montgomery, M.K.1    McFall-Ngai, M.2
  • 27
    • 84877869322 scopus 로고    scopus 로고
    • Iron in infection and immunity
    • Cassat JE, Skaar EP. 2013. Iron in infection and immunity. Cell Host Microbe 13:509-519. http://dx.doi.org/10.1016/j.chom.2013.04.010.
    • (2013) Cell Host Microbe , vol.13 , pp. 509-519
    • Cassat, J.E.1    Skaar, E.P.2
  • 28
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg ED. 2009. Iron availability and infection. Biochim Biophys Acta 1790:600-605. http://dx.doi.org/10.1016/j.bbagen. 2008.07.002.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 600-605
    • Weinberg, E.D.1
  • 29
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands JB. 1981. Microbial iron compounds. Annu Rev Biochem 50:715-731. http://dx.doi.org/10.1146/annurev. bi.50.070181.003435.
    • (1981) Annu Rev Biochem , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 30
    • 0020346483 scopus 로고
    • Microbial envelope proteins related to iron
    • Neilands JB. 1982. Microbial envelope proteins related to iron. Annu Rev Microbiol 36:285-309. http://dx.doi.org/10.1146/annurev. mi.36.100182.001441.
    • (1982) Annu Rev Microbiol , vol.36 , pp. 285-309
    • Neilands, J.B.1
  • 31
    • 34248669292 scopus 로고    scopus 로고
    • Iron acquisition in Vibrio cholerae
    • Wyckoff EE, Mey AR, Payne SM. 2007. Iron acquisition in Vibrio cholerae. Biometals 20:405-416. http://dx.doi.org/10.1007/s10534-006-9073-4.
    • (2007) Biometals , vol.20 , pp. 405-416
    • Wyckoff, E.E.1    Mey, A.R.2    Payne, S.M.3
  • 32
    • 34248647893 scopus 로고    scopus 로고
    • TonB-dependent energy transduction between outer and cytoplasmic membranes
    • Postle K, Larsen RA. 2007. TonB-dependent energy transduction between outer and cytoplasmic membranes. Biometals 20:453-465. http://dx.doi.org/10.1007/s10534-006-9071-6.
    • (2007) Biometals , vol.20 , pp. 453-465
    • Postle, K.1    Larsen, R.A.2
  • 33
    • 0031689477 scopus 로고    scopus 로고
    • Vibrio cholerae iron transport: Haem transport genes are linked to one of two sets of tonB, exbB, exbD genes
    • Occhino DA, Wyckoff EE, Henderson DP, Wrona TJ, Payne SM. 1998. Vibrio cholerae iron transport: haem transport genes are linked to one of two sets of tonB, exbB, exbD genes. Mol Microbiol 29:1493-1507.
    • (1998) Mol Microbiol , vol.29 , pp. 1493-1507
    • Occhino, D.A.1    Wyckoff, E.E.2    Henderson, D.P.3    Wrona, T.J.4    Payne, S.M.5
  • 34
    • 78651359481 scopus 로고    scopus 로고
    • A structural and functional analysis of type III periplasmic and substrate binding proteins: Their role in bacterial siderophore and heme transport
    • Chu BCH, Vogel HJ. 2011. A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport. Biol Chem 392:39-52. http://dx.doi.org/10.1515/BC.2011.012.
    • (2011) Biol Chem , vol.392 , pp. 39-52
    • Chu, B.C.H.1    Vogel, H.J.2
  • 35
    • 79953302147 scopus 로고    scopus 로고
    • Recent insights into iron import by bacteria
    • Braun V, Hantke K. 2011. Recent insights into iron import by bacteria. Curr Opin Chem Biol 15:328-334. http://dx.doi.org/10.1016/j.cbpa.2011.01.005.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 328-334
    • Braun, V.1    Hantke, K.2
  • 36
    • 0026724913 scopus 로고
    • Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex
    • Brickman TJ, McIntosh MA. 1992. Overexpression and purification of ferric enterobactin esterase from Escherichia coli. Demonstration of enzymatic hydrolysis of enterobactin and its iron complex J Biol Chem 267:12350-12355.
    • (1992) J Biol Chem , vol.267 , pp. 12350-12355
    • Brickman, T.J.1    McIntosh, M.A.2
  • 37
    • 0027983767 scopus 로고
    • Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae
    • Butterton JR, Calderwood SB. 1994. Identification, cloning, and sequencing of a gene required for ferric vibriobactin utilization by Vibrio cholerae. J Bacteriol 176:5631-5638.
    • (1994) J Bacteriol , vol.176 , pp. 5631-5638
    • Butterton, J.R.1    Calderwood, S.B.2
  • 38
    • 0033909896 scopus 로고    scopus 로고
    • Novel effects of a transposon insertion in the Vibrio fischeri glnD gene: Defects in iron uptake and symbiotic persistence in addition to nitrogen utilization
    • Graf J, Ruby EG. 2000. Novel effects of a transposon insertion in the Vibrio fischeri glnD gene: defects in iron uptake and symbiotic persistence in addition to nitrogen utilization. Mol Microbiol 37:168-179. http://dx.doi.org/10.1046/j.1365-2958.2000.01984.x.
    • (2000) Mol Microbiol , vol.37 , pp. 168-179
    • Graf, J.1    Ruby, E.G.2
  • 39
    • 0014945206 scopus 로고
    • The structure of enterochelin and related 2, 3-dihydroxy-N-benzoylserine conjugates from Escherichia coli
    • O'Brien IG, Gibson F. 1970. The structure of enterochelin and related 2, 3-dihydroxy-N-benzoylserine conjugates from Escherichia coli. Biochim Biophys Acta 215:393-402. http://dx.doi.org/10.1016/0304-4165 (70) 90038-3.
    • (1970) Biochim Biophys Acta , vol.215 , pp. 393-402
    • O'Brien, I.G.1    Gibson, F.2
  • 40
    • 0014942235 scopus 로고
    • Enterobactin, an iron transport compound from Salmonella typhimurium
    • Pollack JR, Neilands JB. 1970. Enterobactin, an iron transport compound from Salmonella typhimurium. Biochem Biophys Res Commun 38:989-992. http://dx.doi.org/10.1016/0006-291X (70) 90819-3.
    • (1970) Biochem Biophys Res Commun , vol.38 , pp. 989-992
    • Pollack, J.R.1    Neilands, J.B.2
  • 41
    • 0020525402 scopus 로고
    • Expression of hydroxamate and phenolate siderophores by Shigella flexneri
    • Payne SM, Niesel DW, Peixotto SS, Lawlor KM. 1983. Expression of hydroxamate and phenolate siderophores by Shigella flexneri. J Bacteriol 155:949-955.
    • (1983) J Bacteriol , vol.155 , pp. 949-955
    • Payne, S.M.1    Niesel, D.W.2    Peixotto, S.S.3    Lawlor, K.M.4
  • 42
    • 0018568059 scopus 로고
    • Siderophore synthesis in Klebsiella pneumoniae and Shigella sonnei during iron deficiency
    • Perry RD, San Clemente CL. 1979. Siderophore synthesis in Klebsiella pneumoniae and Shigella sonnei during iron deficiency. J Bacteriol 140:1129-1132.
    • (1979) J Bacteriol , vol.140 , pp. 1129-1132
    • Perry, R.D.1    San Clemente, C.L.2
  • 43
    • 0037388150 scopus 로고    scopus 로고
    • Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
    • Hantke K, Nicholson G, Rabsch W, Winkelmann G. 2003. Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN. Proc Natl Acad Sci U S A 100:3677-3682. http://dx.doi.org/10.1073/pnas.0737682100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3677-3682
    • Hantke, K.1    Nicholson, G.2    Rabsch, W.3    Winkelmann, G.4
  • 45
    • 0020966712 scopus 로고
    • Polyamine distribution in Vibrionaceae: Norspermidine as a general constituent of Vibrio species
    • Yamamoto S, Shinoda S, Kawaguchi M, Wakamatsu K, Makita M. 1983. Polyamine distribution in Vibrionaceae: norspermidine as a general constituent of Vibrio species. Can J Microbiol 29:724-728. http://dx.doi.org/10.1139/m83-118.
    • (1983) Can J Microbiol , vol.29 , pp. 724-728
    • Yamamoto, S.1    Shinoda, S.2    Kawaguchi, M.3    Wakamatsu, K.4    Makita, M.5
  • 46
    • 0034687759 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH
    • Keating TA, Marshall CG, Walsh CT. 2000. Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH. Biochemistry 39:15522-15530. http://dx.doi.org/10.1021/bi0016523.
    • (2000) Biochemistry , vol.39 , pp. 15522-15530
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3
  • 47
    • 0034687767 scopus 로고    scopus 로고
    • Vibriobactin biosynthesis in Vibrio cholerae: VibH is an amide synthase homologous to nonribosomal peptide synthetase condensation domains
    • Keating TA, Marshall CG, Walsh CT. 2000. Vibriobactin biosynthesis in Vibrio cholerae: VibH is an amide synthase homologous to nonribosomal peptide synthetase condensation domains. Biochemistry 39:15513-15521. http://dx.doi.org/10.1021/bi001651a.
    • (2000) Biochemistry , vol.39 , pp. 15513-15521
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3
  • 48
    • 0035807043 scopus 로고    scopus 로고
    • Heterocycle formation in vibriobactin biosynthesis: Alternative substrate utilization and identification of a condensed intermediate
    • Marshall CG, Burkart MD, Keating TA, Walsh CT. 2001. Heterocycle formation in vibriobactin biosynthesis: alternative substrate utilization and identification of a condensed intermediate. Biochemistry 40:10655-10663. http://dx.doi.org/10.1021/bi010937s.
    • (2001) Biochemistry , vol.40 , pp. 10655-10663
    • Marshall, C.G.1    Burkart, M.D.2    Keating, T.A.3    Walsh, C.T.4
  • 49
    • 0037039287 scopus 로고    scopus 로고
    • Catalytic mapping of the vibriobactin biosynthetic enzyme VibF
    • Marshall CG, Hillson NJ, Walsh CT. 2002. Catalytic mapping of the vibriobactin biosynthetic enzyme VibF. Biochemistry 41:244-250. http://dx.doi.org/10.1021/bi011852u.
    • (2002) Biochemistry , vol.41 , pp. 244-250
    • Marshall, C.G.1    Hillson, N.J.2    Walsh, C.T.3
  • 50
    • 0030729715 scopus 로고    scopus 로고
    • Cloning of a Vibrio cholerae vibriobactin gene cluster: Identification of genes required for early steps in siderophore biosynthesis
    • Wyckoff EE, Stoebner JA, Reed KE, Payne SM. 1997. Cloning of a Vibrio cholerae vibriobactin gene cluster: identification of genes required for early steps in siderophore biosynthesis. J Bacteriol 179:7055-7062.
    • (1997) J Bacteriol , vol.179 , pp. 7055-7062
    • Wyckoff, E.E.1    Stoebner, J.A.2    Reed, K.E.3    Payne, S.M.4
  • 51
    • 0015042997 scopus 로고
    • Biosynthesis of the iron-transport compound enterochelin: Mutants of Escherichia coli unable to synthesize 2, 3-dihydroxybenzoate
    • Young IG, Langman L, Luke RK, Gibson F. 1971. Biosynthesis of the iron-transport compound enterochelin: mutants of Escherichia coli unable to synthesize 2, 3-dihydroxybenzoate. J Bacteriol 106:51-57.
    • (1971) J Bacteriol , vol.106 , pp. 51-57
    • Young, I.G.1    Langman, L.2    Luke, R.K.3    Gibson, F.4
  • 52
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa JH, Walsh CT. 2002. Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol Mol Biol Rev 66:223-249. http://dx.doi.org/10.1128/MMBR.66.2.223-249.2002.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 53
    • 80053337515 scopus 로고    scopus 로고
    • Production of bioactive secondary metabolites by marine vibrionaceae
    • Mansson M, Gram L, Larsen TO. 2011. Production of bioactive secondary metabolites by marine vibrionaceae. Mar. Drugs 9:1440-1468. http://dx.doi.org/10.3390/md9091440.
    • (2011) Mar. Drugs , vol.9 , pp. 1440-1468
    • Mansson, M.1    Gram, L.2    Larsen, T.O.3
  • 54
    • 68149132445 scopus 로고    scopus 로고
    • Structural insights into nonribosomal peptide enzymatic assembly lines
    • Koglin A, Walsh CT. 2009. Structural insights into nonribosomal peptide enzymatic assembly lines. Nat Prod Rep 26:987-1000. http://dx.doi.org/10.1039/b904543k.
    • (2009) Nat Prod Rep , vol.26 , pp. 987-1000
    • Koglin, A.1    Walsh, C.T.2
  • 55
    • 0034006506 scopus 로고    scopus 로고
    • Vibrio cholerae VibF is required for vibriobactin synthesis and is a member of the family of nonribosomal peptide synthetases
    • Butterton JR, Choi MH, Watnick PI, Carroll PA, Calderwood SB. 2000. Vibrio cholerae VibF is required for vibriobactin synthesis and is a member of the family of nonribosomal peptide synthetases. J Bacteriol 182:1731-1738. http://dx.doi.org/10.1128/JB.182.6.1731-1738.2000.
    • (2000) J Bacteriol , vol.182 , pp. 1731-1738
    • Butterton, J.R.1    Choi, M.H.2    Watnick, P.I.3    Carroll, P.A.4    Calderwood, S.B.5
  • 56
    • 0028281932 scopus 로고
    • Structure of vulnibactin, a new polyamine-containing siderophore from Vibrio vulnificus
    • Okujo N, Saito M, Yamamoto S, Yoshida T, Miyoshi S, Shinoda S. 1994. Structure of vulnibactin, a new polyamine-containing siderophore from Vibrio vulnificus. Biometals 7:109-116.
    • (1994) Biometals , vol.7 , pp. 109-116
    • Okujo, N.1    Saito, M.2    Yamamoto, S.3    Yoshida, T.4    Miyoshi, S.5    Shinoda, S.6
  • 57
    • 0027175401 scopus 로고
    • Structures of two polyamine-containing catecholate siderophores from Vibrio fluvialis
    • Yamamoto S, Okujo N, Fujita Y, Saito M, Yoshida T, Shinoda S. 1993. Structures of two polyamine-containing catecholate siderophores from Vibrio fluvialis. J Biochem 113:538-544.
    • (1993) J Biochem , vol.113 , pp. 538-544
    • Yamamoto, S.1    Okujo, N.2    Fujita, Y.3    Saito, M.4    Yoshida, T.5    Shinoda, S.6
  • 58
    • 84893638218 scopus 로고    scopus 로고
    • Molecular characterization of vulnibactin biosynthesis in Vibrio vulnificus indicates the existence of an alternative siderophore
    • Tan W, Verma V, Jeong K, Kim SY, Jung C-H, Lee SE, Rhee JH. 2014. Molecular characterization of vulnibactin biosynthesis in Vibrio vulnificus indicates the existence of an alternative siderophore. Front Microbiol 5:1. http://dx.doi.org/10.3389/fmicb.2014.00001.
    • (2014) Front Microbiol , vol.5 , pp. 1
    • Tan, W.1    Verma, V.2    Jeong, K.3    Kim, S.Y.4    Jung, C.-H.5    Lee, S.E.6    Rhee, J.H.7
  • 59
    • 0030012953 scopus 로고    scopus 로고
    • Role of catechol siderophore synthesis in Vibrio vulnificus virulence
    • Litwin CM, Rayback TW, Skinner J. 1996. Role of catechol siderophore synthesis in Vibrio vulnificus virulence. Infect Immun 64:2834-2838.
    • (1996) Infect Immun , vol.64 , pp. 2834-2838
    • Litwin, C.M.1    Rayback, T.W.2    Skinner, J.3
  • 61
    • 6044238248 scopus 로고    scopus 로고
    • A nonribosomal peptide synthetase with a novel domain organization is essential for siderophore biosynthesis in Vibrio anguillarum
    • Di Lorenzo M, Poppelaars S, Stork M, Nagasawa M, Tolmasky ME, Crosa JH. 2004. A nonribosomal peptide synthetase with a novel domain organization is essential for siderophore biosynthesis in Vibrio anguillarum. J Bacteriol 186:7327-7336. http://dx.doi.org/10.1128/JB.186.21.7327-7336.2004.
    • (2004) J Bacteriol , vol.186 , pp. 7327-7336
    • Di Lorenzo, M.1    Poppelaars, S.2    Stork, M.3    Nagasawa, M.4    Tolmasky, M.E.5    Crosa, J.H.6
  • 62
    • 55149116296 scopus 로고    scopus 로고
    • Tandem heterocyclization domains in a nonribosomal peptide synthetase essential for siderophore biosynthesis in Vibrio anguillarum
    • Di Lorenzo M, Stork M, Naka H, Tolmasky ME, Crosa JH. 2008. Tandem heterocyclization domains in a nonribosomal peptide synthetase essential for siderophore biosynthesis in Vibrio anguillarum. Biometals 21:635-648. http://dx.doi.org/10.1007/s10534-008-9149-4.
    • (2008) Biometals , vol.21 , pp. 635-648
    • Di Lorenzo, M.1    Stork, M.2    Naka, H.3    Tolmasky, M.E.4    Crosa, J.H.5
  • 63
    • 0028900632 scopus 로고
    • A histidine decarboxylase gene encoded by the Vibrio anguillarum plasmid pJM1 is essential for virulence: Histamine is a precursor in the biosynthesis of anguibactin
    • Tolmasky ME, Actis LA, Crosa JH. 1995. A histidine decarboxylase gene encoded by the Vibrio anguillarum plasmid pJM1 is essential for virulence: histamine is a precursor in the biosynthesis of anguibactin. Mol Microbiol 15:87-95. http://dx.doi.org/10.1111/j.1365-2958.1995.tb02223.x.
    • (1995) Mol Microbiol , vol.15 , pp. 87-95
    • Tolmasky, M.E.1    Actis, L.A.2    Crosa, J.H.3
  • 64
    • 14644393581 scopus 로고    scopus 로고
    • Plasmid- and chromosomeencoded redundant and specific functions are involved in biosynthesis of the siderophore anguibactin in Vibrio anguillarum 775: A case of chance and necessity?
    • Alice AF, López CS, Crosa JH. 2005. Plasmid- and chromosomeencoded redundant and specific functions are involved in biosynthesis of the siderophore anguibactin in Vibrio anguillarum 775: a case of chance and necessity? J Bacteriol 187:2209-2214. http://dx.doi.org/10.1128/JB.187.6.2209-2214.2005.
    • (2005) J Bacteriol , vol.187 , pp. 2209-2214
    • Alice, A.F.1    López, C.S.2    Crosa, J.H.3
  • 66
    • 0029064456 scopus 로고
    • Iron transport genes of the pJM1-mediated iron uptake system of Vibrio anguillarum are included in a transposonlike structure
    • Tolmasky ME, Crosa JH. 1995. Iron transport genes of the pJM1-mediated iron uptake system of Vibrio anguillarum are included in a transposonlike structure. Plasmid 33:180-190. http://dx.doi.org/10.1006/plas.1995.1019.
    • (1995) Plasmid , vol.33 , pp. 180-190
    • Tolmasky, M.E.1    Crosa, J.H.2
  • 67
    • 84881312903 scopus 로고    scopus 로고
    • The anguibactin biosynthesis and transport genes are encoded in the chromosome of Vibrio harveyi: A possible evolutionary origin for the pJM1 plasmid-encoded system of Vibrio anguillarum?
    • Naka H, Actis LA, Crosa JH. 2013. The anguibactin biosynthesis and transport genes are encoded in the chromosome of Vibrio harveyi: a possible evolutionary origin for the pJM1 plasmid-encoded system of Vibrio anguillarum? Microbiologyopen 2:182-194. http://dx.doi.org/10.1002/mbo3.65.
    • (2013) Microbiologyopen , vol.2 , pp. 182-194
    • Naka, H.1    Actis, L.A.2    Crosa, J.H.3
  • 68
    • 0026000610 scopus 로고
    • Distribution of plasmid- and chromosome-mediated iron uptake systems in Vibrio anguillarum strains of different origins
    • Conchas RF, Lemos ML, Barja JL, Toranzo AE. 1991. Distribution of plasmid- and chromosome-mediated iron uptake systems in Vibrio anguillarum strains of different origins. Appl Environ Microbiol 57:2956-2962.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2956-2962
    • Conchas, R.F.1    Lemos, M.L.2    Barja, J.L.3    Toranzo, A.E.4
  • 69
    • 0023952019 scopus 로고
    • Chromosomemediated iron uptake system in pathogenic strains of Vibrio anguillarum
    • Lemos ML, Salinas P, Toranzo AE, Barja JL, Crosa JH. 1988. Chromosomemediated iron uptake system in pathogenic strains of Vibrio anguillarum. J Bacteriol 170:1920-1925.
    • (1988) J Bacteriol , vol.170 , pp. 1920-1925
    • Lemos, M.L.1    Salinas, P.2    Toranzo, A.E.3    Barja, J.L.4    Crosa, J.H.5
  • 70
    • 77957256131 scopus 로고    scopus 로고
    • Anguibactin-versus vanchrobactinmediated iron uptake in Vibrio anguillarum: Evolution and ecology of a fish pathogen
    • Lemos ML, Balado M, Osorio CR. 2010. Anguibactin-versus vanchrobactinmediated iron uptake in Vibrio anguillarum: evolution and ecology of a fish pathogen. Environ Microbiol Rep 2:19-26. http://dx.doi.org/10.1111/j.1758-2229.2009.00103.x.
    • (2010) Environ Microbiol Rep , vol.2 , pp. 19-26
    • Lemos, M.L.1    Balado, M.2    Osorio, C.R.3
  • 71
    • 33747801782 scopus 로고    scopus 로고
    • Structural characterization of vanchrobactin, a new catechol siderophore produced by the fish pathogen Vibrio anguillarum serotype O2
    • Soengas RG, Anta C, Espada A, Paz V, Ares IR, Balado M, Rodríguez J, Lemos ML, Jiménez C. 2006. Structural characterization of vanchrobactin, a new catechol siderophore produced by the fish pathogen Vibrio anguillarum serotype O2. Tetrahedron Lett 47:7113-7116. http://dx.doi.org/10.1016/j.tetlet.2006.07.104.
    • (2006) Tetrahedron Lett , vol.47 , pp. 7113-7116
    • Soengas, R.G.1    Anta, C.2    Espada, A.3    Paz, V.4    Ares, I.R.5    Balado, M.6    Rodríguez, J.7    Lemos, M.L.8    Jiménez, C.9
  • 72
    • 0028310352 scopus 로고
    • Structure and iron transport activity of vibrioferrin, a new siderophore of Vibrio parahaemolyticus
    • Yamamoto S, Okujo N, Yoshida T, Matsuura S, Shinoda S. 1994. Structure and iron transport activity of vibrioferrin, a new siderophore of Vibrio parahaemolyticus. J Biochem 115:868-874.
    • (1994) J Biochem , vol.115 , pp. 868-874
    • Yamamoto, S.1    Okujo, N.2    Yoshida, T.3    Matsuura, S.4    Shinoda, S.5
  • 73
    • 72949094050 scopus 로고    scopus 로고
    • Vibrioferrin, an unusual marine siderophore: Iron binding, photochemistry, and biological implications
    • Amin SA, Green DH, Küpper FC, Carrano CJ. 2009. Vibrioferrin, an unusual marine siderophore: iron binding, photochemistry, and biological implications. Inorg Chem 48:11451-11458. http://dx.doi.org/10.1021/ic9016883.
    • (2009) Inorg Chem , vol.48 , pp. 11451-11458
    • Amin, S.A.1    Green, D.H.2    Küpper, F.C.3    Carrano, C.J.4
  • 74
  • 75
    • 0034520733 scopus 로고    scopus 로고
    • Carbon versus iron limitation of bacterial growth in the California upwelling regime
    • Kirchman DL, Meon B, Cottrell MT, Hutchins DA, Weeks D, Bruland KW. 2000. Carbon versus iron limitation of bacterial growth in the California upwelling regime. Limnol Oceanogr 45:1681-1688. http://dx.doi.org/10.4319/lo.2000.45.8.1681.
    • (2000) Limnol Oceanogr , vol.45 , pp. 1681-1688
    • Kirchman, D.L.1    Meon, B.2    Cottrell, M.T.3    Hutchins, D.A.4    Weeks, D.5    Bruland, K.W.6
  • 76
    • 0026145134 scopus 로고
    • Attachment of Vibrio parahaemolyticus strains to estuarine algae
    • Kumazawa NH, Fukuma N, Komoda Y. 1991. Attachment of Vibrio parahaemolyticus strains to estuarine algae. J Vet Med Sci 53:201-205. http://dx.doi.org/10.1292/jvms.53.201.
    • (1991) J Vet Med Sci , vol.53 , pp. 201-205
    • Kumazawa, N.H.1    Fukuma, N.2    Komoda, Y.3
  • 77
    • 2442636217 scopus 로고    scopus 로고
    • Identification and characterization of two contiguous operons required for aerobactin transport and biosynthesis in Vibrio mimicus
    • Moon Y-H, Tanabe T, Funahashi T, Shiuchi K, Nakao H, Yamamoto S. 2004. Identification and characterization of two contiguous operons required for aerobactin transport and biosynthesis in Vibrio mimicus. Microbiol Immunol 48:389-398. http://dx.doi.org/10.1111/j.1348-0421.2004.tb03528.x.
    • (2004) Microbiol Immunol , vol.48 , pp. 389-398
    • Moon, Y.-H.1    Tanabe, T.2    Funahashi, T.3    Shiuchi, K.4    Nakao, H.5    Yamamoto, S.6
  • 78
    • 33748466139 scopus 로고    scopus 로고
    • Identification and transcriptional organization of aerobactin transport and biosynthesis cluster genes of Vibrio hollisae
    • Suzuki K, Tanabe T, Moon Y-H, Funahashi T, Nakao H, Narimatsu S, Yamamoto S. 2006. Identification and transcriptional organization of aerobactin transport and biosynthesis cluster genes of Vibrio hollisae. Res Microbiol 157:730-740. http://dx.doi.org/10.1016/j.resmic.2006.05.001.
    • (2006) Res Microbiol , vol.157 , pp. 730-740
    • Suzuki, K.1    Tanabe, T.2    Moon, Y.-H.3    Funahashi, T.4    Nakao, H.5    Narimatsu, S.6    Yamamoto, S.7
  • 79
    • 0027806641 scopus 로고
    • Aerobactin production by a planktonic marine Vibrio sp
    • Haygood MG, Holt PD, Butler A. 1993. Aerobactin production by a planktonic marine Vibrio sp. Limnol Oceanogr 38:1091-1097. http://dx.doi.org/10.4319/lo.1993.38.5.1091.
    • (1993) Limnol Oceanogr , vol.38 , pp. 1091-1097
    • Haygood, M.G.1    Holt, P.D.2    Butler, A.3
  • 80
    • 0021923818 scopus 로고
    • Composite IS1 elements encoding hydroxamate-mediated iron uptake in FIme plasmids from epidemic Salmonella spp
    • Colonna B, Nicoletti M, Visca P, Casalino M, Valenti P, Maimone F. 1985. Composite IS1 elements encoding hydroxamate-mediated iron uptake in FIme plasmids from epidemic Salmonella spp. J Bacteriol 162:307-316.
    • (1985) J Bacteriol , vol.162 , pp. 307-316
    • Colonna, B.1    Nicoletti, M.2    Visca, P.3    Casalino, M.4    Valenti, P.5    Maimone, F.6
  • 81
    • 0022443738 scopus 로고
    • Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12
    • De Lorenzo V, Bindereif A, Paw BH, Neilands JB. 1986. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J Bacteriol 165:570-578.
    • (1986) J Bacteriol , vol.165 , pp. 570-578
    • De Lorenzo, V.1    Bindereif, A.2    Paw, B.H.3    Neilands, J.B.4
  • 82
    • 0023387003 scopus 로고
    • Flanking and internal regions of chromosomal genes mediating aerobactin iron uptake systems in enteroinvasive Escherichia coli and Shigella flexneri
    • Marolda CL, Valvano MA, Lawlor KM, Payne SM, Crosa JH. 1987. Flanking and internal regions of chromosomal genes mediating aerobactin iron uptake systems in enteroinvasive Escherichia coli and Shigella flexneri. J Gen Microbiol 133:2269-2278.
    • (1987) J Gen Microbiol , vol.133 , pp. 2269-2278
    • Marolda, C.L.1    Valvano, M.A.2    Lawlor, K.M.3    Payne, S.M.4    Crosa, J.H.5
  • 83
    • 0032971083 scopus 로고    scopus 로고
    • The selCassociated SHI-2 pathogenicity island of Shigella flexneri
    • Moss JE, Cardozo TJ, Zychlinsky A, Groisman EA. 1999. The selCassociated SHI-2 pathogenicity island of Shigella flexneri. Mol Microbiol 33:74-83. http://dx.doi.org/10.1046/j.1365-2958.1999.01449.x.
    • (1999) Mol Microbiol , vol.33 , pp. 74-83
    • Moss, J.E.1    Cardozo, T.J.2    Zychlinsky, A.3    Groisman, E.A.4
  • 84
    • 0034977704 scopus 로고    scopus 로고
    • The SHI-3 iron transport island of Shigella boydii 0-1392 carries the genes for aerobactin synthesis and transport
    • Purdy GE, Payne SM. 2001. The SHI-3 iron transport island of Shigella boydii 0-1392 carries the genes for aerobactin synthesis and transport. J Bacteriol 183:4176-4182. http://dx.doi.org/10.1128/JB.183.14.4176-4182.2001.
    • (2001) J Bacteriol , vol.183 , pp. 4176-4182
    • Purdy, G.E.1    Payne, S.M.2
  • 85
    • 0033046336 scopus 로고    scopus 로고
    • The aerobactin iron transport system genes in Shigella flexneri are present within a pathogenicity island
    • Vokes SA, Reeves SA, Torres AG, Payne SM. 1999. The aerobactin iron transport system genes in Shigella flexneri are present within a pathogenicity island. Mol Microbiol 33:63-73. http://dx.doi.org/10.1046/j.1365-2958.1999.01448.x.
    • (1999) Mol Microbiol , vol.33 , pp. 63-73
    • Vokes, S.A.1    Reeves, S.A.2    Torres, A.G.3    Payne, S.M.4
  • 86
    • 79951672216 scopus 로고    scopus 로고
    • Chemical and structural characterization of hydroxamate siderophore produced by marine Vibrio harveyi
    • Murugappan RM, Aravinth A, Karthikeyan M. 2011. Chemical and structural characterization of hydroxamate siderophore produced by marine Vibrio harveyi. J Ind Microbiol Biotechnol 38:265-273. http://dx.doi.org/10.1007/s10295-010-0769-7.
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 265-273
    • Murugappan, R.M.1    Aravinth, A.2    Karthikeyan, M.3
  • 87
    • 0020615792 scopus 로고
    • Siderophore production by Vibrio vulnificus
    • Simpson LM, Oliver JD. 1983. Siderophore production by Vibrio vulnificus. Infect Immun 41:644-649.
    • (1983) Infect Immun , vol.41 , pp. 644-649
    • Simpson, L.M.1    Oliver, J.D.2
  • 89
    • 0037389594 scopus 로고    scopus 로고
    • Structure and membrane affinity of a suite of amphiphilic siderophores produced by a marine bacterium
    • Martinez JS, Carter-Franklin JN, Mann EL, Martin JD, Haygood MG, Butler A. 2003. Structure and membrane affinity of a suite of amphiphilic siderophores produced by a marine bacterium. Proc Natl Acad Sci U S A 100:3754-3759. http://dx.doi.org/10.1073/pnas.0637444100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 3754-3759
    • Martinez, J.S.1    Carter-Franklin, J.N.2    Mann, E.L.3    Martin, J.D.4    Haygood, M.G.5    Butler, A.6
  • 90
    • 79951724694 scopus 로고    scopus 로고
    • Identification of new members within suites of amphiphilic marine siderophores
    • Vraspir JM, Holt PD, Butler A. 2011. Identification of new members within suites of amphiphilic marine siderophores. Biometals 24:85-92. http://dx.doi.org/10.1007/s10534-010-9378-1.
    • (2011) Biometals , vol.24 , pp. 85-92
    • Vraspir, J.M.1    Holt, P.D.2    Butler, A.3
  • 91
    • 84878722349 scopus 로고    scopus 로고
    • Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species
    • Gauglitz JM, Butler A. 2013. Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species. J Biol Inorg Chem 18:489-497. http://dx.doi.org/10.1007/s00775-013-0995-3.
    • (2013) J Biol Inorg Chem , vol.18 , pp. 489-497
    • Gauglitz, J.M.1    Butler, A.2
  • 92
    • 84898982654 scopus 로고    scopus 로고
    • Biosynthesis of amphi-enterobactin siderophores by Vibrio harveyi BAA-1116: Identification of a bifunctional nonribosomal peptide synthetase condensation domain
    • Zane HK, Naka H, Rosconi F, Sandy M, Haygood MG, Butler A. 2014. Biosynthesis of amphi-enterobactin siderophores by Vibrio harveyi BAA-1116: identification of a bifunctional nonribosomal peptide synthetase condensation domain. JAmChem Soc 136:5615-5618. http://dx.doi.org/10.1021/ja5019942.
    • (2014) JAmChem Soc , vol.136 , pp. 5615-5618
    • Zane, H.K.1    Naka, H.2    Rosconi, F.3    Sandy, M.4    Haygood, M.G.5    Butler, A.6
  • 93
    • 84899628015 scopus 로고    scopus 로고
    • Microbial tailoring of acyl peptidic siderophores
    • Gauglitz JM, Iinishi A, Ito Y, Butler A. 2014. Microbial tailoring of acyl peptidic siderophores. Biochemistry 53:2624-2631. http://dx.doi.org/10.1021/bi500266x.
    • (2014) Biochemistry , vol.53 , pp. 2624-2631
    • Gauglitz, J.M.1    Iinishi, A.2    Ito, Y.3    Butler, A.4
  • 94
    • 0026748433 scopus 로고
    • Cloning, sequencing, and transcriptional regulation of viuA, the gene encoding the ferric vibriobactin receptor of Vibrio cholerae
    • Butterton JR, Stoebner JA, Payne SM, Calderwood SB. 1992. Cloning, sequencing, and transcriptional regulation of viuA, the gene encoding the ferric vibriobactin receptor of Vibrio cholerae. J Bacteriol 174:3729-3738.
    • (1992) J Bacteriol , vol.174 , pp. 3729-3738
    • Butterton, J.R.1    Stoebner, J.A.2    Payne, S.M.3    Calderwood, S.B.4
  • 96
    • 0032763652 scopus 로고    scopus 로고
    • A multifunctional ATP-binding cassette transporter system from Vibrio cholerae transports vibriobactin and enterobactin
    • Wyckoff EE, Valle AM, Smith SL, Payne SM. 1999. A multifunctional ATP-binding cassette transporter system from Vibrio cholerae transports vibriobactin and enterobactin. J Bacteriol 181:7588-7596.
    • (1999) J Bacteriol , vol.181 , pp. 7588-7596
    • Wyckoff, E.E.1    Valle, A.M.2    Smith, S.L.3    Payne, S.M.4
  • 97
    • 0036151995 scopus 로고    scopus 로고
    • Identification and characterization of pvuA, a gene encoding the ferric vibrioferrin receptor protein in Vibrio parahaemolyticus
    • Funahashi T, Moriya K, Uemura S, Miyoshi S, Shinoda S, Narimatsu S, Yamamoto S. 2002. Identification and characterization of pvuA, a gene encoding the ferric vibrioferrin receptor protein in Vibrio parahaemolyticus. J Bacteriol 184:936-946. http://dx.doi.org/10.1128/jb.184.4.936-946.2002.
    • (2002) J Bacteriol , vol.184 , pp. 936-946
    • Funahashi, T.1    Moriya, K.2    Uemura, S.3    Miyoshi, S.4    Shinoda, S.5    Narimatsu, S.6    Yamamoto, S.7
  • 98
    • 0033958801 scopus 로고    scopus 로고
    • Cloning and characterization of vuuA, a gene encoding the Vibrio vulnificus ferric vulnibactin receptor
    • Webster AC, Litwin CM. 2000. Cloning and characterization of vuuA, a gene encoding the Vibrio vulnificus ferric vulnibactin receptor. Infect Immun 68:526-534. http://dx.doi.org/10.1128/IAI.68.2.526-534.2000.
    • (2000) Infect Immun , vol.68 , pp. 526-534
    • Webster, A.C.1    Litwin, C.M.2
  • 99
    • 65549163793 scopus 로고    scopus 로고
    • FvtA is the receptor for the siderophore vanchrobactin in Vibrio anguillarum: Utility as a route of entry for vanchrobactin analogues
    • Balado M, Osorio CR, Lemos ML. 2009. FvtA is the receptor for the siderophore vanchrobactin in Vibrio anguillarum: utility as a route of entry for vanchrobactin analogues. Appl Environ Microbiol 75:2775-2783. http://dx.doi.org/10.1128/AEM.02897-08.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2775-2783
    • Balado, M.1    Osorio, C.R.2    Lemos, M.L.3
  • 100
    • 0023854777 scopus 로고
    • Genetic and molecular characterization of essential components of the Vibrio anguillarum plasmid-mediated iron-transport system
    • Actis LA, Tolmasky ME, Farrell DH, Crosa JH. 1988. Genetic and molecular characterization of essential components of the Vibrio anguillarum plasmid-mediated iron-transport system. J Biol Chem 263:2853-2860.
    • (1988) J Biol Chem , vol.263 , pp. 2853-2860
    • Actis, L.A.1    Tolmasky, M.E.2    Farrell, D.H.3    Crosa, J.H.4
  • 101
    • 0026333507 scopus 로고
    • Molecular characterization of the iron transport system mediated by the pJM1 plasmid in Vibrio anguillarum 775
    • Köster WL, Actis LA, Waldbeser LS, Tolmasky ME, Crosa JH. 1991. Molecular characterization of the iron transport system mediated by the pJM1 plasmid in Vibrio anguillarum 775. J Biol Chem 266:23829-23833.
    • (1991) J Biol Chem , vol.266 , pp. 23829-23833
    • Köster, W.L.1    Actis, L.A.2    Waldbeser, L.S.3    Tolmasky, M.E.4    Crosa, J.H.5
  • 102
    • 23944511214 scopus 로고    scopus 로고
    • Novel role of the lipopolysaccharide O1 side chain in ferric siderophore transport and virulence of Vibrio anguillarum
    • Welch TJ, Crosa JH. 2005. Novel role of the lipopolysaccharide O1 side chain in ferric siderophore transport and virulence of Vibrio anguillarum. Infect Immun 73:5864-5872. http://dx.doi.org/10.1128/IAI.73.9.5864-5872.2005.
    • (2005) Infect Immun , vol.73 , pp. 5864-5872
    • Welch, T.J.1    Crosa, J.H.2
  • 103
    • 79956089442 scopus 로고    scopus 로고
    • Kin discrimination and cooperation in microbes
    • Strassmann JE, Gilbert OM, Queller DC. 2011. Kin discrimination and cooperation in microbes. Annu Rev Microbiol 65:349-367. http://dx.doi.org/10.1146/annurev. micro.112408.134109.
    • (2011) Annu Rev Microbiol , vol.65 , pp. 349-367
    • Strassmann, J.E.1    Gilbert, O.M.2    Queller, D.C.3
  • 104
    • 29144506940 scopus 로고    scopus 로고
    • Chitin induces natural competence in Vibrio cholerae
    • Meibom KL, Blokesch M, Dolganov NA, Wu C-Y, Schoolnik GK. 2005. Chitin induces natural competence in Vibrio cholerae. Science 310:1824-1827. http://dx.doi.org/10.1126/science.1120096.
    • (2005) Science , vol.310 , pp. 1824-1827
    • Meibom, K.L.1    Blokesch, M.2    Dolganov, N.A.3    Wu, C.-Y.4    Schoolnik, G.K.5
  • 105
    • 84881554800 scopus 로고    scopus 로고
    • Competence and natural transformation in vibrios
    • Sun Y, Bernardy EE, Hammer BK, Miyashiro T. 2013. Competence and natural transformation in vibrios. Mol Microbiol 89:583-595. http://dx.doi.org/10.1111/mmi.12307.
    • (2013) Mol Microbiol , vol.89 , pp. 583-595
    • Sun, Y.1    Bernardy, E.E.2    Hammer, B.K.3    Miyashiro, T.4
  • 106
    • 0036084292 scopus 로고    scopus 로고
    • Identification of the Vibrio cholerae enterobactin receptors VctA and IrgA: IrgA is not required for virulence
    • Mey AR, Wyckoff EE, Oglesby AG, Rab E, Taylor RK, Payne SM. 2002. Identification of the Vibrio cholerae enterobactin receptors VctA and IrgA: IrgA is not required for virulence. Infect Immun 70:3419-3426. http://dx.doi.org/10.1128/IAI.70.7.3419-3426.2002.
    • (2002) Infect Immun , vol.70 , pp. 3419-3426
    • Mey, A.R.1    Wyckoff, E.E.2    Oglesby, A.G.3    Rab, E.4    Taylor, R.K.5    Payne, S.M.6
  • 107
    • 0034068917 scopus 로고    scopus 로고
    • Identification of an operon required for ferrichrome iron utilization in Vibrio cholerae
    • Rogers MB, Sexton JA, DeCastro GJ, Calderwood SB. 2000. Identification of an operon required for ferrichrome iron utilization in Vibrio cholerae. J Bacteriol 182:2350-2353. http://dx.doi.org/10.1128/JB.182.8.2350-2353.2000.
    • (2000) J Bacteriol , vol.182 , pp. 2350-2353
    • Rogers, M.B.1    Sexton, J.A.2    DeCastro, G.J.3    Calderwood, S.B.4
  • 108
    • 84938869828 scopus 로고    scopus 로고
    • Catechol siderophore transport by Vibrio cholerae
    • Wyckoff EE, Allred BE, Raymond KN, Payne SM. 2015. Catechol siderophore transport by Vibrio cholerae. J Bacteriol 197:2840-2849. http://dx.doi.org/10.1128/JB.00417-15.
    • (2015) J Bacteriol , vol.197 , pp. 2840-2849
    • Wyckoff, E.E.1    Allred, B.E.2    Raymond, K.N.3    Payne, S.M.4
  • 109
    • 0037854326 scopus 로고    scopus 로고
    • An iron-regulated gene required for utilization of aerobactin as an exogenous siderophore in Vibrio parahaemolyticus
    • Funahashi T, Tanabe T, Aso H, Nakao H, Fujii Y, Okamoto K, Narimatsu S, Yamamoto S. 2003. An iron-regulated gene required for utilization of aerobactin as an exogenous siderophore in Vibrio parahaemolyticus. Microbiology 149:1217-1225. http://dx.doi.org/10.1099/mic.0.26066-0.
    • (2003) Microbiology , vol.149 , pp. 1217-1225
    • Funahashi, T.1    Tanabe, T.2    Aso, H.3    Nakao, H.4    Fujii, Y.5    Okamoto, K.6    Narimatsu, S.7    Yamamoto, S.8
  • 110
    • 63149096715 scopus 로고    scopus 로고
    • Identification and characterization of genes required for utilization of desferri-ferrichrome and aerobactin in Vibrio parahaemolyticus
    • Funahashi T, Tanabe T, Shiuchi K, Nakao H, Yamamoto S. 2009. Identification and characterization of genes required for utilization of desferri-ferrichrome and aerobactin in Vibrio parahaemolyticus. Biol Pharm Bull 32:359-365. http://dx.doi.org/10.1248/bpb.32.359.
    • (2009) Biol Pharm Bull , vol.32 , pp. 359-365
    • Funahashi, T.1    Tanabe, T.2    Shiuchi, K.3    Nakao, H.4    Yamamoto, S.5
  • 111
    • 0037129839 scopus 로고    scopus 로고
    • Induction of an outer membrane protein of 78 kDa in Vibrio vulnificus cultured in the presence of desferrioxamine B under iron-limiting conditions
    • Aso H, Miyoshi S, Nakao H, Okamoto K, Yamamoto S. 2002. Induction of an outer membrane protein of 78 kDa in Vibrio vulnificus cultured in the presence of desferrioxamine B under iron-limiting conditions. FEMS Microbiol Lett 212:65-70. http://dx.doi.org/10.1111/j.1574-6968.2002.tb11246.x.
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 65-70
    • Aso, H.1    Miyoshi, S.2    Nakao, H.3    Okamoto, K.4    Yamamoto, S.5
  • 112
    • 38449118832 scopus 로고    scopus 로고
    • A widespread deferoxaminemediated iron-uptake system in Vibrio vulnificus
    • Kim C-M, Park Y-J, Shin S-H. 2007. A widespread deferoxaminemediated iron-uptake system in Vibrio vulnificus. J Infect Dis 196:1537-1545. http://dx.doi.org/10.1086/523108.
    • (2007) J Infect Dis , vol.196 , pp. 1537-1545
    • Kim, C.-M.1    Park, Y.-J.2    Shin, S.-H.3
  • 113
    • 79953795327 scopus 로고    scopus 로고
    • Identification of genes, desR and desA, required for utilization of desferrioxamine B as a xenosiderophore in Vibrio furnissii
    • Tanabe T, Funahashi T, Miyamoto K, Tsujibo H, Yamamoto S. 2011. Identification of genes, desR and desA, required for utilization of desferrioxamine B as a xenosiderophore in Vibrio furnissii. Biol Pharm Bull 34:570-574. http://dx.doi.org/10.1248/bpb.34.570.
    • (2011) Biol Pharm Bull , vol.34 , pp. 570-574
    • Tanabe, T.1    Funahashi, T.2    Miyamoto, K.3    Tsujibo, H.4    Yamamoto, S.5
  • 114
    • 0037307780 scopus 로고    scopus 로고
    • Elucidation of the Vibrio anguillarum genetic response to the potential fish probiont Pseudomonas fluorescens AH2, using RNA-arbitrarily primed PCR
    • Holmstrøm K, Gram L. 2003. Elucidation of the Vibrio anguillarum genetic response to the potential fish probiont Pseudomonas fluorescens AH2, using RNA-arbitrarily primed PCR. J Bacteriol 185:831-842. http://dx.doi.org/10.1128/JB.185.3.831-842.2003.
    • (2003) J Bacteriol , vol.185 , pp. 831-842
    • Holmstrøm, K.1    Gram, L.2
  • 115
    • 84896455159 scopus 로고    scopus 로고
    • A chimeric siderophore halts swarming Vibrio
    • Böttcher T, Clardy J. 2014. A chimeric siderophore halts swarming Vibrio. Angew Chem Int Ed Engl 53:3510-3513. http://dx.doi.org/10.1002/anie.201310729.
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 3510-3513
    • Böttcher, T.1    Clardy, J.2
  • 116
    • 55449127247 scopus 로고    scopus 로고
    • Characterization of two TonB systems in marine fish pathogen Vibrio alginolyticus: Their roles in iron utilization and virulence
    • Wang Q, Liu Q, Cao X, Yang M, Zhang Y. 2008. Characterization of two TonB systems in marine fish pathogen Vibrio alginolyticus: their roles in iron utilization and virulence. Arch Microbiol 190:595-603. http://dx.doi.org/10.1007/s00203-008-0407-1.
    • (2008) Arch Microbiol , vol.190 , pp. 595-603
    • Wang, Q.1    Liu, Q.2    Cao, X.3    Yang, M.4    Zhang, Y.5
  • 117
    • 0021019714 scopus 로고
    • Synthesis of siderophores by pathogenic Vibrio species
    • Andrus CR, Walter M, Crosa JH, Payne SM. 1983. Synthesis of siderophores by pathogenic Vibrio species. Curr Microbiol 9:209-214. http://dx.doi.org/10.1007/BF01567583.
    • (1983) Curr Microbiol , vol.9 , pp. 209-214
    • Andrus, C.R.1    Walter, M.2    Crosa, J.H.3    Payne, S.M.4
  • 118
    • 0027417443 scopus 로고
    • Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobin
    • Henderson DP, Payne SM. 1993. Cloning and characterization of the Vibrio cholerae genes encoding the utilization of iron from haemin and haemoglobin. Mol Microbiol 7:461-469. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01137.x.
    • (1993) Mol Microbiol , vol.7 , pp. 461-469
    • Henderson, D.P.1    Payne, S.M.2
  • 119
    • 0028338619 scopus 로고
    • Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: Sequence of the gene, regulation of expression, and homology to the family of TonBdependent proteins
    • Henderson DP, Payne SM. 1994. Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonBdependent proteins. J Bacteriol 176:3269-3277.
    • (1994) J Bacteriol , vol.176 , pp. 3269-3277
    • Henderson, D.P.1    Payne, S.M.2
  • 120
    • 0035168497 scopus 로고    scopus 로고
    • Haem utilization in Vibrio cholerae involves multiple TonB-dependent haem receptors
    • Mey AR, Payne SM. 2001. Haem utilization in Vibrio cholerae involves multiple TonB-dependent haem receptors. Mol Microbiol 42:835-849.
    • (2001) Mol Microbiol , vol.42 , pp. 835-849
    • Mey, A.R.1    Payne, S.M.2
  • 122
    • 3042606663 scopus 로고    scopus 로고
    • HutZ is required for efficient heme utilization in Vibrio cholerae
    • Wyckoff EE, Schmitt M, Wilks A, Payne SM. 2004. HutZ is required for efficient heme utilization in Vibrio cholerae. J Bacteriol 186:4142-4151. http://dx.doi.org/10.1128/JB.186.13.4142-4151.2004.
    • (2004) J Bacteriol , vol.186 , pp. 4142-4151
    • Wyckoff, E.E.1    Schmitt, M.2    Wilks, A.3    Payne, S.M.4
  • 124
    • 0031842732 scopus 로고    scopus 로고
    • Cloning and characterization of an outer membrane protein of Vibrio vulnificus required for heme utilization: Regulation of expression and determination of the gene sequence
    • Litwin CM, Byrne BL. 1998. Cloning and characterization of an outer membrane protein of Vibrio vulnificus required for heme utilization: regulation of expression and determination of the gene sequence. Infect Immun 66:3134-3141.
    • (1998) Infect Immun , vol.66 , pp. 3134-3141
    • Litwin, C.M.1    Byrne, B.L.2
  • 125
    • 84862728166 scopus 로고    scopus 로고
    • Identification and characterization of a novel outer membrane protein receptor required for hemin utilization in Vibrio vulnificus
    • Datta S, Crosa JH. 2012. Identification and characterization of a novel outer membrane protein receptor required for hemin utilization in Vibrio vulnificus. Biometals 25:275-283. http://dx.doi.org/10.1007/s10534-011-9501-y.
    • (2012) Biometals , vol.25 , pp. 275-283
    • Datta, S.1    Crosa, J.H.2
  • 126
    • 12844260218 scopus 로고    scopus 로고
    • Identification of an iron-regulated hemin-binding outer membrane protein, HupO, in Vibrio fluvialis: Effects on hemolytic activity and the oxidative stress response
    • Ahn S-H, Han J-H, Lee J-H, Park K-J, Kong I-S. 2005. Identification of an iron-regulated hemin-binding outer membrane protein, HupO, in Vibrio fluvialis: effects on hemolytic activity and the oxidative stress response. Infect Immun 73:722-729. http://dx.doi.org/10.1128/IAI.73.2.722-729.2005.
    • (2005) Infect Immun , vol.73 , pp. 722-729
    • Ahn, S.-H.1    Han, J.-H.2    Lee, J.-H.3    Park, K.-J.4    Kong, I.-S.5
  • 127
    • 0030058367 scopus 로고    scopus 로고
    • Identification of heme-binding proteins in the cell membranes of Vibrio anguillarum
    • Mazoy R, Lemos ML. 1996. Identification of heme-binding proteins in the cell membranes of Vibrio anguillarum. FEMS Microbiol Lett 135:265-270. http://dx.doi.org/10.1111/j.1574-6968.1996.tb07999.x.
    • (1996) FEMS Microbiol Lett , vol.135 , pp. 265-270
    • Mazoy, R.1    Lemos, M.L.2
  • 128
    • 0037952996 scopus 로고    scopus 로고
    • Isolation of mutants of Vibrio anguillarum defective in haeme utilisation and cloning of huvA, a gene coding for an outer membrane protein involved in the use of haeme as iron source
    • Mazoy R, Osorio CR, Toranzo AE, Lemos ML. 2003. Isolation of mutants of Vibrio anguillarum defective in haeme utilisation and cloning of huvA, a gene coding for an outer membrane protein involved in the use of haeme as iron source. Arch Microbiol 179:329-338.
    • (2003) Arch Microbiol , vol.179 , pp. 329-338
    • Mazoy, R.1    Osorio, C.R.2    Toranzo, A.E.3    Lemos, M.L.4
  • 129
    • 77957936057 scopus 로고    scopus 로고
    • Identification and characterization of a Vibrio mimicus gene encoding the heme/hemoglobin receptor
    • Tanabe T, Funahashi T, Moon Y-H, Tamai E, Yamamoto S. 2010. Identification and characterization of a Vibrio mimicus gene encoding the heme/hemoglobin receptor. Microbiol Immunol 54:606-617. http://dx.doi.org/10.1111/j.1348-0421.2010.00256.x.
    • (2010) Microbiol Immunol , vol.54 , pp. 606-617
    • Tanabe, T.1    Funahashi, T.2    Moon, Y.-H.3    Tamai, E.4    Yamamoto, S.5
  • 131
    • 0025788234 scopus 로고
    • Iron-binding proteins and heme compounds as iron sources for Vibrio anguillarum
    • Mazoy R, Lemos DML. 1991. Iron-binding proteins and heme compounds as iron sources for Vibrio anguillarum. Curr Microbiol 23:221-226. http://dx.doi.org/10.1007/BF02092282.
    • (1991) Curr Microbiol , vol.23 , pp. 221-226
    • Mazoy, R.1    Lemos, D.M.L.2
  • 132
    • 0031573037 scopus 로고    scopus 로고
    • Isolation of a hemin and hemoglobin binding outer membrane protein of Vibrio vulnificus biotype 2 (serogroup E)
    • Fouz B, Mazoy R, Vázquez F, Lemos ML, Amaro C. 1997. Isolation of a hemin and hemoglobin binding outer membrane protein of Vibrio vulnificus biotype 2 (serogroup E). FEMS Microbiol Lett 156:187-191. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12725.x.
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 187-191
    • Fouz, B.1    Mazoy, R.2    Vázquez, F.3    Lemos, M.L.4    Amaro, C.5
  • 134
    • 0026734829 scopus 로고
    • Significant role of an exocellular protease in utilization of heme by Vibrio vulnificus
    • Nishina Y, Miyoshi S, Nagase A, Shinoda S. 1992. Significant role of an exocellular protease in utilization of heme by Vibrio vulnificus. Infect Immun 60:2128-2132.
    • (1992) Infect Immun , vol.60 , pp. 2128-2132
    • Nishina, Y.1    Miyoshi, S.2    Nagase, A.3    Shinoda, S.4
  • 135
    • 0035136784 scopus 로고    scopus 로고
    • The two TonB systems of Vibrio cholerae: Redundant and specific functions
    • Seliger SS, Mey AR, Valle AM, Payne SM. 2001. The two TonB systems of Vibrio cholerae: redundant and specific functions. Mol Microbiol 39:801-812. http://dx.doi.org/10.1046/j.1365-2958.2001.02273.x.
    • (2001) Mol Microbiol , vol.39 , pp. 801-812
    • Seliger, S.S.1    Mey, A.R.2    Valle, A.M.3    Payne, S.M.4
  • 136
    • 9244255835 scopus 로고    scopus 로고
    • Two tonB systems function in iron transport in Vibrio anguillarum, but only one is essential for virulence
    • Stork M, Di Lorenzo M, Mouriño S, Osorio CR, Lemos ML, Crosa JH. 2004. Two tonB systems function in iron transport in Vibrio anguillarum, but only one is essential for virulence. Infect Immun 72:7326-7329. http://dx.doi.org/10.1128/IAI.72.12.7326-7329.2004.
    • (2004) Infect Immun , vol.72 , pp. 7326-7329
    • Stork, M.1    Di Lorenzo, M.2    Mouriño, S.3    Osorio, C.R.4    Lemos, M.L.5    Crosa, J.H.6
  • 137
    • 84861218646 scopus 로고    scopus 로고
    • The TonB3 system in the human pathogen Vibrio vulnificus is under the control of the global regulators Lrp and cyclic AMP receptor protein
    • Alice AF, Crosa JH. 2012. The TonB3 system in the human pathogen Vibrio vulnificus is under the control of the global regulators Lrp and cyclic AMP receptor protein. J Bacteriol 194:1897-1911. http://dx.doi.org/10.1128/JB.06614-11.
    • (2012) J Bacteriol , vol.194 , pp. 1897-1911
    • Alice, A.F.1    Crosa, J.H.2
  • 138
    • 59449090702 scopus 로고    scopus 로고
    • Molecular and genetic characterization of the TonB2-cluster TtpC protein in pathogenic vibrios
    • Kuehl CJ, Crosa JH. 2009. Molecular and genetic characterization of the TonB2-cluster TtpC protein in pathogenic vibrios. Biometals 22:109-115. http://dx.doi.org/10.1007/s10534-008-9194-z.
    • (2009) Biometals , vol.22 , pp. 109-115
    • Kuehl, C.J.1    Crosa, J.H.2
  • 139
    • 84864014074 scopus 로고    scopus 로고
    • The ttpC gene is contained in two of three TonB systems in the human pathogen Vibrio vulnificus, but only one is active in iron transport and virulence
    • Kustusch RJ, Kuehl CJ, Crosa JH. 2012. The ttpC gene is contained in two of three TonB systems in the human pathogen Vibrio vulnificus, but only one is active in iron transport and virulence. J Bacteriol 194:3250-3259. http://dx.doi.org/10.1128/JB.00155-12.
    • (2012) J Bacteriol , vol.194 , pp. 3250-3259
    • Kustusch, R.J.1    Kuehl, C.J.2    Crosa, J.H.3
  • 140
    • 33947364406 scopus 로고    scopus 로고
    • A novel protein, TtpC, is a required component of the TonB2 complex for specific iron transport in the pathogens Vibrio anguillarum and Vibrio cholerae
    • Stork M, Otto BR, Crosa JH. 2007. A novel protein, TtpC, is a required component of the TonB2 complex for specific iron transport in the pathogens Vibrio anguillarum and Vibrio cholerae. J Bacteriol 189:1803-1815. http://dx.doi.org/10.1128/JB.00451-06.
    • (2007) J Bacteriol , vol.189 , pp. 1803-1815
    • Stork, M.1    Otto, B.R.2    Crosa, J.H.3
  • 141
    • 0037312519 scopus 로고    scopus 로고
    • Analysis of residues determining specificity of Vibrio cholerae TonB1 for its receptors
    • Mey AR, Payne SM. 2003. Analysis of residues determining specificity of Vibrio cholerae TonB1 for its receptors. J Bacteriol 185:1195-1207. http://dx.doi.org/10.1128/JB.185.4.1195-1207.2003.
    • (2003) J Bacteriol , vol.185 , pp. 1195-1207
    • Mey, A.R.1    Payne, S.M.2
  • 142
    • 0017703597 scopus 로고
    • Periplasmic space in Salmonella typhimurium and Escherichia coli
    • Stock JB, Rauch B, Roseman S. 1977. Periplasmic space in Salmonella typhimurium and Escherichia coli. J Biol Chem 252:7850-7861.
    • (1977) J Biol Chem , vol.252 , pp. 7850-7861
    • Stock, J.B.1    Rauch, B.2    Roseman, S.3
  • 143
    • 0031610907 scopus 로고    scopus 로고
    • Bacterial iron transport: Mechanisms, genetics, and regulation
    • Braun V, Hantke K, Köster W. 1998. Bacterial iron transport: mechanisms, genetics, and regulation. Met Ions Biol Syst 35:67-145.
    • (1998) Met Ions Biol Syst , vol.35 , pp. 67-145
    • Braun, V.1    Hantke, K.2    Köster, W.3
  • 144
    • 83455262902 scopus 로고    scopus 로고
    • The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli
    • Miethke M, Hou J, Marahiel MA. 2011. The siderophore-interacting protein YqjH acts as a ferric reductase in different iron assimilation pathways of Escherichia coli. Biochemistry 50:10951-10964. http://dx.doi.org/10.1021/bi201517h.
    • (2011) Biochemistry , vol.50 , pp. 10951-10964
    • Miethke, M.1    Hou, J.2    Marahiel, M.A.3
  • 145
    • 33845994362 scopus 로고    scopus 로고
    • A gene cluster involved in the biosynthesis of vanchrobactin, a chromosome-encoded siderophore produced by Vibrio anguillarum
    • Balado M, Osorio CR, Lemos ML. 2006. A gene cluster involved in the biosynthesis of vanchrobactin, a chromosome-encoded siderophore produced by Vibrio anguillarum. Microbiology 152:3517-3528. http://dx.doi.org/10.1099/mic.0.29298-0.
    • (2006) Microbiology , vol.152 , pp. 3517-3528
    • Balado, M.1    Osorio, C.R.2    Lemos, M.L.3
  • 146
    • 84886054254 scopus 로고    scopus 로고
    • FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB
    • Weaver EA, Wyckoff EE, Mey AR, Morrison R, Payne SM. 2013. FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB. J Bacteriol 195:4826-4835. http://dx.doi.org/10.1128/JB.00738-13.
    • (2013) J Bacteriol , vol.195 , pp. 4826-4835
    • Weaver, E.A.1    Wyckoff, E.E.2    Mey, A.R.3    Morrison, R.4    Payne, S.M.5
  • 147
    • 0027487221 scopus 로고
    • Characterization of the ferrous iron uptake system of Escherichia coli
    • Kammler M, Schon C, Hantke K. 1993. Characterization of the ferrous iron uptake system of Escherichia coli. J Bacteriol 175:6212-6219.
    • (1993) J Bacteriol , vol.175 , pp. 6212-6219
    • Kammler, M.1    Schon, C.2    Hantke, K.3
  • 148
    • 33748766356 scopus 로고    scopus 로고
    • Characterization of ferric and ferrous iron transport systems in Vibrio cholerae
    • Wyckoff EE, Mey AR, Leimbach A, Fisher CF, Payne SM. 2006. Characterization of ferric and ferrous iron transport systems in Vibrio cholerae. J Bacteriol 188:6515-6523. http://dx.doi.org/10.1128/JB.00626-06.
    • (2006) J Bacteriol , vol.188 , pp. 6515-6523
    • Wyckoff, E.E.1    Mey, A.R.2    Leimbach, A.3    Fisher, C.F.4    Payne, S.M.5
  • 149
    • 0037059058 scopus 로고    scopus 로고
    • The membrane protein FeoB contains an intramolecular G protein essential for Fe (II) uptake in bacteria
    • Marlovits TC, Haase W, Herrmann C, Aller SG, Unger VM. 2002. The membrane protein FeoB contains an intramolecular G protein essential for Fe (II) uptake in bacteria. Proc Natl Acad Sci U S A 99:16243-16248. http://dx.doi.org/10.1073/pnas.242338299.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16243-16248
    • Marlovits, T.C.1    Haase, W.2    Herrmann, C.3    Aller, S.G.4    Unger, V.M.5
  • 150
    • 84880688675 scopus 로고    scopus 로고
    • The FeoC protein leads to high cellular levels of the Fe (II) transporter FeoB by preventing FtsH protease regulation of FeoB in Salmonella enterica
    • Kim H, Lee H, Shin D. 2013. The FeoC protein leads to high cellular levels of the Fe (II) transporter FeoB by preventing FtsH protease regulation of FeoB in Salmonella enterica. J Bacteriol 195:3364-3370. http://dx.doi.org/10.1128/JB.00343-13.
    • (2013) J Bacteriol , vol.195 , pp. 3364-3370
    • Kim, H.1    Lee, H.2    Shin, D.3
  • 151
    • 84863816918 scopus 로고    scopus 로고
    • The FeoA protein is necessary for the FeoB transporter to import ferrous iron
    • Kim H, Lee H, Shin D. 2012. The FeoA protein is necessary for the FeoB transporter to import ferrous iron. Biochem Biophys Res Commun 423:733-738. http://dx.doi.org/10.1016/j.bbrc.2012.06.027.
    • (2012) Biochem Biophys Res Commun , vol.423 , pp. 733-738
    • Kim, H.1    Lee, H.2    Shin, D.3
  • 152
    • 50249085014 scopus 로고    scopus 로고
    • Vibrio cholerae VciB promotes iron uptake via ferrous iron transporters
    • Mey AR, Wyckoff EE, Hoover LA, Fisher CR, Payne SM. 2008. Vibrio cholerae VciB promotes iron uptake via ferrous iron transporters. J Bacteriol 190:5953-5962. http://dx.doi.org/10.1128/JB.00569-08.
    • (2008) J Bacteriol , vol.190 , pp. 5953-5962
    • Mey, A.R.1    Wyckoff, E.E.2    Hoover, L.A.3    Fisher, C.R.4    Payne, S.M.5
  • 153
    • 0033044276 scopus 로고    scopus 로고
    • Ferric-reductase activities in Vibrio vulnificus biotypes 1 and 2
    • Mazoy R, Lopez EM, Fouz B, Amaro C, Lemos ML. 1999. Ferric-reductase activities in Vibrio vulnificus biotypes 1 and 2. FEMS Microbiol Lett 172:205-211. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13470.x.
    • (1999) FEMS Microbiol Lett , vol.172 , pp. 205-211
    • Mazoy, R.1    Lopez, E.M.2    Fouz, B.3    Amaro, C.4    Lemos, M.L.5
  • 154
    • 80052743066 scopus 로고    scopus 로고
    • The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand
    • Wyckoff EE, Payne SM. 2011. The Vibrio cholerae VctPDGC system transports catechol siderophores and a siderophore-free iron ligand. Mol Microbiol 81:1446-1458. http://dx.doi.org/10.1111/j.1365-2958.2011.07775.x.
    • (2011) Mol Microbiol , vol.81 , pp. 1446-1458
    • Wyckoff, E.E.1    Payne, S.M.2
  • 155
    • 78449290415 scopus 로고    scopus 로고
    • The struggle for iron- A metal at the host-pathogen interface
    • Nairz M, Schroll A, Sonnweber T, Weiss G. 2010. The struggle for iron-a metal at the host-pathogen interface. Cell Microbiol 12:1691-1702. http://dx.doi.org/10.1111/j.1462-5822.2010.01529.x.
    • (2010) Cell Microbiol , vol.12 , pp. 1691-1702
    • Nairz, M.1    Schroll, A.2    Sonnweber, T.3    Weiss, G.4
  • 156
    • 84904768122 scopus 로고    scopus 로고
    • Iron at the interface of immunity and infection
    • Nairz M, Haschka D, Demetz E, Weiss G. 2014. Iron at the interface of immunity and infection. Front Pharmacol 5:152. http://dx.doi.org/10.3389/fphar.2014.00152.
    • (2014) Front Pharmacol , vol.5 , pp. 152
    • Nairz, M.1    Haschka, D.2    Demetz, E.3    Weiss, G.4
  • 157
    • 33645111877 scopus 로고    scopus 로고
    • Natural resistance, iron and infection: A challenge for clinical medicine
    • Bullen JJ, Rogers HJ, Spalding PB, Ward CG. 2006. Natural resistance, iron and infection: a challenge for clinical medicine. J Med Microbiol 55:251-258. http://dx.doi.org/10.1099/jmm.0.46386-0.
    • (2006) J Med Microbiol , vol.55 , pp. 251-258
    • Bullen, J.J.1    Rogers, H.J.2    Spalding, P.B.3    Ward, C.G.4
  • 158
    • 84856327464 scopus 로고    scopus 로고
    • Iron metabolism and the innate immune response to infection
    • Johnson EE, Wessling-Resnick M. 2012. Iron metabolism and the innate immune response to infection. Microbes Infect 14:207-216. http://dx.doi.org/10.1016/j.micinf.2011.10.001.
    • (2012) Microbes Infect , vol.14 , pp. 207-216
    • Johnson, E.E.1    Wessling-Resnick, M.2
  • 159
    • 38549144236 scopus 로고    scopus 로고
    • Iron metabolism and infection
    • Ratledge C. 2007. Iron metabolism and infection. Food Nutr Bull 28:S515-S523.
    • (2007) Food Nutr Bull , vol.28 , pp. S515-S523
    • Ratledge, C.1
  • 160
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold RR, Cole MF, McGhee JR. 1977. A bactericidal effect for human lactoferrin. Science 197:263-265. http://dx.doi.org/10.1126/science.327545.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 161
    • 0018868141 scopus 로고
    • Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms
    • Arnold RR, Brewer M, Gauthier JJ. 1980. Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infect Immun 28:893-898.
    • (1980) Infect Immun , vol.28 , pp. 893-898
    • Arnold, R.R.1    Brewer, M.2    Gauthier, J.J.3
  • 162
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: A lactoferrinderived peptide with antimicrobial, antiviral, antitumor and immunological properties
    • Gifford JL, Hunter HN, Vogel HJ. 2005. Lactoferricin: a lactoferrinderived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell Mol Life Sci 62:2588-2598. http://dx.doi.org/10.1007/s00018-005-5373-z.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 163
    • 84868526205 scopus 로고    scopus 로고
    • Hepcidin and the iron-infection axis
    • Drakesmith H, Prentice AM. 2012. Hepcidin and the iron-infection axis. Science 338:768-772. http://dx.doi.org/10.1126/science.1224577.
    • (2012) Science , vol.338 , pp. 768-772
    • Drakesmith, H.1    Prentice, A.M.2
  • 164
    • 84880693247 scopus 로고    scopus 로고
    • Iron-metabolic function and potential antibacterial role of hepcidin and its correlated genes (ferroportin 1 and transferrin receptor) in turbot (Scophthalmus maximus)
    • Yang C-G, Liu S-S, Sun B, Wang X-L, Wang N, Chen S-L. 2013. Iron-metabolic function and potential antibacterial role of hepcidin and its correlated genes (ferroportin 1 and transferrin receptor) in turbot (Scophthalmus maximus). Fish Shellfish Immunol 34:744-755. http://dx.doi.org/10.1016/j.fsi.2012.11.049.
    • (2013) Fish Shellfish Immunol , vol.34 , pp. 744-755
    • Yang, C.-G.1    Liu, S.-S.2    Sun, B.3    Wang, X.-L.4    Wang, N.5    Chen, S.-L.6
  • 165
    • 0017740442 scopus 로고
    • Infection and iron metabolism
    • Weinberg ED. 1977. Infection and iron metabolism. Am J Clin Nutr 30:1485-1490.
    • (1977) Am J Clin Nutr , vol.30 , pp. 1485-1490
    • Weinberg, E.D.1
  • 166
    • 0034105860 scopus 로고    scopus 로고
    • Microbial pathogens with impaired ability to acquire host iron
    • Weinberg ED. 2000. Microbial pathogens with impaired ability to acquire host iron. Biometals 13:85-89. http://dx.doi.org/10.1023/A:1009293500209.
    • (2000) Biometals , vol.13 , pp. 85-89
    • Weinberg, E.D.1
  • 167
    • 35448938485 scopus 로고    scopus 로고
    • Association of hemochromatosis with infectious diseases: Expanding spectrum
    • Khan FA, Fisher MA, Khakoo RA. 2007. Association of hemochromatosis with infectious diseases: expanding spectrum. Int J Infect Dis 11:482-487. http://dx.doi.org/10.1016/j.ijid.2007.04.007.
    • (2007) Int J Infect Dis , vol.11 , pp. 482-487
    • Khan, F.A.1    Fisher, M.A.2    Khakoo, R.A.3
  • 169
    • 0343527231 scopus 로고    scopus 로고
    • Bacteremic cellulitis caused by non-01, non-0139 Vibrio cholerae: Report of a case in a patient with hemochromatosis
    • Fernández JM, Serrano M, De Arriba JJ, Sánchez MV, Escribano E, Ferreras P. 2000. Bacteremic cellulitis caused by non-01, non-0139 Vibrio cholerae: report of a case in a patient with hemochromatosis. Diagn Microbiol Infect Dis 37:77-80. http://dx.doi.org/10.1016/S0732-8893 (99) 00153-4.
    • (2000) Diagn Microbiol Infect Dis , vol.37 , pp. 77-80
    • Fernández, J.M.1    Serrano, M.2    De Arriba, J.J.3    Sánchez, M.V.4    Escribano, E.5    Ferreras, P.6
  • 170
    • 0028097695 scopus 로고
    • Role of iron, capsule, and toxins in the pathogenicity of Vibrio vulnificus biotype 2 for mice
    • Amaro C, Biosca EG, Fouz B, Toranzo AE, Garay E. 1994. Role of iron, capsule, and toxins in the pathogenicity of Vibrio vulnificus biotype 2 for mice. Infect Immun 62:759-763.
    • (1994) Infect Immun , vol.62 , pp. 759-763
    • Amaro, C.1    Biosca, E.G.2    Fouz, B.3    Toranzo, A.E.4    Garay, E.5
  • 171
    • 0025931055 scopus 로고
    • Growth of Vibrio vulnificus in serum from alcoholics: Association with high transferrin iron saturation
    • Brennt CE, Wright AC, Dutta SK, Morris JG. 1991. Growth of Vibrio vulnificus in serum from alcoholics: association with high transferrin iron saturation. J Infect Dis 164:1030-1032. http://dx.doi.org/10.1093/infdis/164.5.1030.
    • (1991) J Infect Dis , vol.164 , pp. 1030-1032
    • Brennt, C.E.1    Wright, A.C.2    Dutta, S.K.3    Morris, J.G.4
  • 172
    • 0025860867 scopus 로고
    • Hemochromatosis, iron and septicemia caused by Vibrio vulnificus
    • Bullen JJ, Spalding PB, Ward CG, Gutteridge JM. 1991. Hemochromatosis, iron and septicemia caused by Vibrio vulnificus. Arch Intern Med 151:1606-1609. http://dx.doi.org/10.1001/archinte.1991.00400080 096018.
    • (1991) Arch Intern Med , vol.151 , pp. 1606-1609
    • Bullen, J.J.1    Spalding, P.B.2    Ward, C.G.3    Gutteridge, J.M.4
  • 173
    • 0033796597 scopus 로고    scopus 로고
    • Pathogenesis of infection by clinical and environmental strains of Vibrio vulnificus in iron-dextran-treated mice
    • Starks AM, Schoeb TR, Tamplin ML, Parveen S, Doyle TJ, Bomeisl PE, Escudero GM, Gulig PA. 2000. Pathogenesis of infection by clinical and environmental strains of Vibrio vulnificus in iron-dextran-treated mice. Infect Immun 68:5785-5793. http://dx.doi.org/10.1128/IAI.68.10.5785-5793.2000.
    • (2000) Infect Immun , vol.68 , pp. 5785-5793
    • Starks, A.M.1    Schoeb, T.R.2    Tamplin, M.L.3    Parveen, S.4    Doyle, T.J.5    Bomeisl, P.E.6    Escudero, G.M.7    Gulig, P.A.8
  • 174
    • 0344420199 scopus 로고    scopus 로고
    • Hepcidin: The missing link between hemochromatosis and infections
    • Ashrafian H. 2003. Hepcidin: the missing link between hemochromatosis and infections. Infect Immun 71:6693-6700. http://dx.doi.org/10.1128/IAI.71.12.6693-6700.2003.
    • (2003) Infect Immun , vol.71 , pp. 6693-6700
    • Ashrafian, H.1
  • 175
    • 84920905125 scopus 로고    scopus 로고
    • Hepcidin-induced hypoferremia is a critical host defense mechanism against the siderophilic bacterium Vibrio vulnificus
    • Arezes J, Jung G, Gabayan V, Valore E, Ruchala P, Gulig PA, Ganz T, Nemeth E, Bulut Y. 2015. Hepcidin-induced hypoferremia is a critical host defense mechanism against the siderophilic bacterium Vibrio vulnificus. Cell Host Microbe 17:47-57. http://dx.doi.org/10.1016/j.chom.2014.12.001.
    • (2015) Cell Host Microbe , vol.17 , pp. 47-57
    • Arezes, J.1    Jung, G.2    Gabayan, V.3    Valore, E.4    Ruchala, P.5    Gulig, P.A.6    Ganz, T.7    Nemeth, E.8    Bulut, Y.9
  • 177
    • 80051915419 scopus 로고    scopus 로고
    • RNA-seq-based monitoring of infection-linked changes in Vibrio cholerae gene expression
    • Mandlik A, Livny J, Robins WP, Ritchie JM, Mekalanos JJ, Waldor MK. 2011. RNA-seq-based monitoring of infection-linked changes in Vibrio cholerae gene expression. Cell Host Microbe 10:165-174. http://dx.doi.org/10.1016/j.chom.2011.07.007.
    • (2011) Cell Host Microbe , vol.10 , pp. 165-174
    • Mandlik, A.1    Livny, J.2    Robins, W.P.3    Ritchie, J.M.4    Mekalanos, J.J.5    Waldor, M.K.6
  • 178
    • 84883317465 scopus 로고    scopus 로고
    • Transcriptome profiling analysis of Vibrio vulnificus during human infection
    • Bisharat N, Bronstein M, Korner M, Schnitzer T, Koton Y. 2013. Transcriptome profiling analysis of Vibrio vulnificus during human infection. Microbiology 159:1878-1887. http://dx.doi.org/10.1099/mic.0.067900-0.
    • (2013) Microbiology , vol.159 , pp. 1878-1887
    • Bisharat, N.1    Bronstein, M.2    Korner, M.3    Schnitzer, T.4    Koton, Y.5
  • 181
    • 84925283832 scopus 로고    scopus 로고
    • Comparative RNA-Seq based dissection of the regulatory networks and environmental stimuli underlying Vibrio parahaemolyticus gene expression during infection
    • Livny J, Zhou X, Mandlik A, Hubbard T, Davis BM, Waldor MK. 2014. Comparative RNA-Seq based dissection of the regulatory networks and environmental stimuli underlying Vibrio parahaemolyticus gene expression during infection. Nucleic Acids Res 42:12212-12223. http://dx.doi.org/10.1093/nar/gku891.
    • (2014) Nucleic Acids Res , vol.42 , pp. 12212-12223
    • Livny, J.1    Zhou, X.2    Mandlik, A.3    Hubbard, T.4    Davis, B.M.5    Waldor, M.K.6
  • 182
    • 80055089802 scopus 로고    scopus 로고
    • The haem-uptake gene cluster in Vibrio fischeri is regulated by Fur and contributes to symbiotic colonization
    • Septer AN, Wang Y, Ruby EG, Stabb EV, Dunn AK. 2011. The haem-uptake gene cluster in Vibrio fischeri is regulated by Fur and contributes to symbiotic colonization. Environ Microbiol 13:2855-2864. http://dx.doi.org/10.1111/j.1462-2920.2011.02558.x.
    • (2011) Environ Microbiol , vol.13 , pp. 2855-2864
    • Septer, A.N.1    Wang, Y.2    Ruby, E.G.3    Stabb, E.V.4    Dunn, A.K.5
  • 183
    • 0031974549 scopus 로고    scopus 로고
    • The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers
    • Cornelissen CN, Kelley M, Hobbs MM, Anderson JE, Cannon JG, Cohen MS, Sparling PF. 1998. The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers. Mol Microbiol 27:611-616. http://dx.doi.org/10.1046/j.1365-2958.1998.00710.x.
    • (1998) Mol Microbiol , vol.27 , pp. 611-616
    • Cornelissen, C.N.1    Kelley, M.2    Hobbs, M.M.3    Anderson, J.E.4    Cannon, J.G.5    Cohen, M.S.6    Sparling, P.F.7
  • 184
    • 84931578557 scopus 로고    scopus 로고
    • Novel hostspecific iron acquisition system in the zoonotic pathogen Vibrio vulnificus
    • Pajuelo D, Lee C-T, Roig F, Hor L-I, Amaro C. 2015. Novel hostspecific iron acquisition system in the zoonotic pathogen Vibrio vulnificus. Environ Microbiol 17:2076-2089. http://dx.doi.org/10.1111/1462-2920.12782.
    • (2015) Environ Microbiol , vol.17 , pp. 2076-2089
    • Pajuelo, D.1    Lee, C.-T.2    Roig, F.3    Hor, L.-I.4    Amaro, C.5
  • 185
    • 84892961984 scopus 로고    scopus 로고
    • Host-nonspecific iron acquisition systems and virulence in the zoonotic serovar of Vibrio vulnificus
    • Pajuelo D, Lee C-T, Roig FJ, Lemos ML, Hor L-I, Amaro C. 2014. Host-nonspecific iron acquisition systems and virulence in the zoonotic serovar of Vibrio vulnificus. Infect Immun 82:731-744. http://dx.doi.org/10.1128/IAI.01117-13.
    • (2014) Infect Immun , vol.82 , pp. 731-744
    • Pajuelo, D.1    Lee, C.-T.2    Roig, F.J.3    Lemos, M.L.4    Hor, L.-I.5    Amaro, C.6
  • 186
    • 0030030286 scopus 로고    scopus 로고
    • Siderophore-mediated iron acquisition mechanisms in Vibrio vulnificus biotype 2
    • Biosca EG, Fouz B, Alcaide E, Amaro C. 1996. Siderophore-mediated iron acquisition mechanisms in Vibrio vulnificus biotype 2. Appl Environ Microbiol 62:928-935.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 928-935
    • Biosca, E.G.1    Fouz, B.2    Alcaide, E.3    Amaro, C.4
  • 187
    • 0028059213 scopus 로고
    • Siderophore-mediated utilization of iron bound to transferrin by Vibrio parahaemolyticus
    • Yamamoto S, Okujo N, Matsuura S, Fujiwara I, Fujita Y, Shinoda S. 1994. Siderophore-mediated utilization of iron bound to transferrin by Vibrio parahaemolyticus. Microbiol Immunol 38:687-693. http://dx.doi.org/10.1111/j.1348-0421.1994.tb01843.x.
    • (1994) Microbiol Immunol , vol.38 , pp. 687-693
    • Yamamoto, S.1    Okujo, N.2    Matsuura, S.3    Fujiwara, I.4    Fujita, Y.5    Shinoda, S.6
  • 188
    • 0031009405 scopus 로고    scopus 로고
    • High affinity iron-uptake systems in Vibrio damsela: Role in the acquisition of iron from transferrin
    • Fouz B, Biosca EG, Amaro C. 1997. High affinity iron-uptake systems in Vibrio damsela: role in the acquisition of iron from transferrin. J Appl Microbiol 82:157-167. http://dx.doi.org/10.1111/j.1365-2672.1997.tb02846.x.
    • (1997) J Appl Microbiol , vol.82 , pp. 157-167
    • Fouz, B.1    Biosca, E.G.2    Amaro, C.3
  • 189
    • 0029787281 scopus 로고    scopus 로고
    • Involvement of vulnibactin and exocellular protease in utilization of transferrin- and lactoferrin-bound iron by Vibrio vulnificus
    • Okujo N, Akiyama T, Miyoshi S, Shinoda S, Yamamoto S. 1996. Involvement of vulnibactin and exocellular protease in utilization of transferrin- and lactoferrin-bound iron by Vibrio vulnificus. Microbiol Immunol 40:595-598. http://dx.doi.org/10.1111/j.1348-0421.1996.tb01114.x.
    • (1996) Microbiol Immunol , vol.40 , pp. 595-598
    • Okujo, N.1    Akiyama, T.2    Miyoshi, S.3    Shinoda, S.4    Yamamoto, S.5
  • 190
    • 20444414112 scopus 로고    scopus 로고
    • Vibrio vulnificus metalloprotease VvpE has no direct effect on the ironassimilation from human holotransferrin
    • Shin S-H, Sun H-Y, Park R-Y, Kim C-M, Kim S-Y, Rhee J-H. 2005. Vibrio vulnificus metalloprotease VvpE has no direct effect on the ironassimilation from human holotransferrin. FEMS Microbiol Lett 247:221-229. http://dx.doi.org/10.1016/j.femsle.2005.05.015.
    • (2005) FEMS Microbiol Lett , vol.247 , pp. 221-229
    • Shin, S.-H.1    Sun, H.-Y.2    Park, R.-Y.3    Kim, C.-M.4    Kim, S.-Y.5    Rhee, J.-H.6
  • 191
    • 33646449037 scopus 로고    scopus 로고
    • Vibrio vulnificus vulnibactin, but not metalloprotease VvpE, is essentially required for iron-uptake from human holotransferrin
    • Kim C-M, Park R-Y, Park J-H, Sun H-Y, Bai Y-H, Ryu P-Y, Kim S-Y, Rhee J-H, Shin S-H. 2006. Vibrio vulnificus vulnibactin, but not metalloprotease VvpE, is essentially required for iron-uptake from human holotransferrin. Biol Pharm Bull 29:911-918. http://dx.doi.org/10.1248/bpb.29.911.
    • (2006) Biol Pharm Bull , vol.29 , pp. 911-918
    • Kim, C.-M.1    Park, R.-Y.2    Park, J.-H.3    Sun, H.-Y.4    Bai, Y.-H.5    Ryu, P.-Y.6    Kim, S.-Y.7    Rhee, J.-H.8    Shin, S.-H.9
  • 192
    • 50249098214 scopus 로고    scopus 로고
    • The siderocalin/enterobactin interaction: A link between mammalian immunity and bacterial iron transport
    • Abergel RJ, Clifton MC, Pizarro JC, Warner JA, Shuh DK, Strong RK, Raymond KN. 2008. The siderocalin/enterobactin interaction: a link between mammalian immunity and bacterial iron transport. JAmChem Soc 130:11524-11534. http://dx.doi.org/10.1021/ja803524w.
    • (2008) JAmChem Soc , vol.130 , pp. 11524-11534
    • Abergel, R.J.1    Clifton, M.C.2    Pizarro, J.C.3    Warner, J.A.4    Shuh, D.K.5    Strong, R.K.6    Raymond, K.N.7
  • 193
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo TH, Smith KD, Sato S, Rodriguez DJ, Holmes MA, Strong RK, Akira S, Aderem A. 2004. Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432:917-921. http://dx.doi.org/10.1038/nature03104.
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5    Strong, R.K.6    Akira, S.7    Aderem, A.8
  • 194
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz DH, Holmes MA, Borregaard N, Bluhm ME, Raymond KN, Strong RK. 2002. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol Cell 10:1033-1043. http://dx.doi.org/10.1016/S1097-2765 (02) 00708-6.
    • (2002) Mol Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 195
    • 84863337997 scopus 로고    scopus 로고
    • Unique iron coordination in iron-chelating molecule vibriobactin helps Vibrio cholerae evade mammalian siderocalin-mediated immune response
    • Li N, Zhang C, Li B, Liu X, Huang Y, Xu S, Gu L. 2012. Unique iron coordination in iron-chelating molecule vibriobactin helps Vibrio cholerae evade mammalian siderocalin-mediated immune response. J Biol Chem 287:8912-8919. http://dx.doi.org/10.1074/jbc. M111.316034.
    • (2012) J Biol Chem , vol.287 , pp. 8912-8919
    • Li, N.1    Zhang, C.2    Li, B.3    Liu, X.4    Huang, Y.5    Xu, S.6    Gu, L.7
  • 196
    • 84884662885 scopus 로고    scopus 로고
    • Siderocalin outwits the coordination chemistry of vibriobactin, a siderophore of Vibrio cholerae
    • Allred BE, Correnti C, Clifton MC, Strong RK, Raymond KN. 2013. Siderocalin outwits the coordination chemistry of vibriobactin, a siderophore of Vibrio cholerae. ACS Chem Biol 8:1882-1887. http://dx.doi.org/10.1021/cb4002552.
    • (2013) ACS Chem Biol , vol.8 , pp. 1882-1887
    • Allred, B.E.1    Correnti, C.2    Clifton, M.C.3    Strong, R.K.4    Raymond, K.N.5
  • 197
    • 0021960914 scopus 로고
    • Iron-vibriobactin transport system is not required for virulence of Vibrio cholerae
    • Sigel SP, Stoebner JA, Payne SM. 1985. Iron-vibriobactin transport system is not required for virulence of Vibrio cholerae. Infect Immun 47:360-362.
    • (1985) Infect Immun , vol.47 , pp. 360-362
    • Sigel, S.P.1    Stoebner, J.A.2    Payne, S.M.3
  • 198
    • 0027939182 scopus 로고
    • Vibrio cholerae iron transport systems: Roles of heme and siderophore iron transport in virulence and identification of a gene associated with multiple iron transport systems
    • Henderson DP, Payne SM. 1994. Vibrio cholerae iron transport systems: roles of heme and siderophore iron transport in virulence and identification of a gene associated with multiple iron transport systems. Infect Immun 62:5120-5125.
    • (1994) Infect Immun , vol.62 , pp. 5120-5125
    • Henderson, D.P.1    Payne, S.M.2
  • 199
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • Touati D. 2000. Iron and oxidative stress in bacteria. Arch Biochem Biophys 373:1-6. http://dx.doi.org/10.1006/abbi.1999.1518.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 1-6
    • Touati, D.1
  • 200
    • 0034648298 scopus 로고    scopus 로고
    • The Haber-Weiss reaction and mechanisms of toxicity
    • Kehrer JP. 2000. The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 149:43-50. http://dx.doi.org/10.1016/S0300-483X (00) 00231-6.
    • (2000) Toxicology , vol.149 , pp. 43-50
    • Kehrer, J.P.1
  • 201
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay JA, Linn S. 1988. DNA damage and oxygen radical toxicity. Science 240:1302-1309. http://dx.doi.org/10.1126/science.3287616.
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 202
    • 0030447225 scopus 로고    scopus 로고
    • Cellular and molecular physiology of Escherichia coli in the adaptation to aerobic environments
    • Iuchi S, Weiner L. 1996. Cellular and molecular physiology of Escherichia coli in the adaptation to aerobic environments. J Biochem 120:1055-1063. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021519.
    • (1996) J Biochem , vol.120 , pp. 1055-1063
    • Iuchi, S.1    Weiner, L.2
  • 203
    • 0026534389 scopus 로고
    • Cloning, sequencing, and transcriptional regulation of the Vibrio cholerae fur gene
    • Litwin CM, Boyko SA, Calderwood SB. 1992. Cloning, sequencing, and transcriptional regulation of the Vibrio cholerae fur gene. J Bacteriol 174:1897-1903.
    • (1992) J Bacteriol , vol.174 , pp. 1897-1903
    • Litwin, C.M.1    Boyko, S.A.2    Calderwood, S.B.3
  • 204
    • 0028181626 scopus 로고
    • Analysis of the complexity of gene regulation by Fur in Vibrio cholerae
    • Litwin CM, Calderwood SB. 1994. Analysis of the complexity of gene regulation by Fur in Vibrio cholerae. J Bacteriol 176:240-248.
    • (1994) J Bacteriol , vol.176 , pp. 240-248
    • Litwin, C.M.1    Calderwood, S.B.2
  • 205
    • 65949087462 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination
    • Sheikh MA, Taylor GL. 2009. Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination. Mol Microbiol 72:1208-1220. http://dx.doi.org/10.1111/j.1365-2958.2009.06718.x.
    • (2009) Mol Microbiol , vol.72 , pp. 1208-1220
    • Sheikh, M.A.1    Taylor, G.L.2
  • 206
    • 0031033529 scopus 로고    scopus 로고
    • Purification of Vibrio cholerae Fur and estimation of its intracellular abundance by antibody sandwich enzyme-linked immunosorbent assay
    • Watnick PI, Eto T, Takahashi H, Calderwood SB. 1997. Purification of Vibrio cholerae Fur and estimation of its intracellular abundance by antibody sandwich enzyme-linked immunosorbent assay. J Bacteriol 179:243-247.
    • (1997) J Bacteriol , vol.179 , pp. 243-247
    • Watnick, P.I.1    Eto, T.2    Takahashi, H.3    Calderwood, S.B.4
  • 207
    • 0024276112 scopus 로고
    • Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli
    • De Lorenzo V, Herrero M, Giovannini F, Neilands JB. 1988. Fur (ferric uptake regulation) protein and CAP (catabolite-activator protein) modulate transcription of fur gene in Escherichia coli. Eur J Biochem 173:537-546. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14032.x.
    • (1988) Eur J Biochem , vol.173 , pp. 537-546
    • De Lorenzo, V.1    Herrero, M.2    Giovannini, F.3    Neilands, J.B.4
  • 208
    • 34147151006 scopus 로고    scopus 로고
    • Positive regulation of fur gene expression via direct interaction of Fur in a pathogenic bacterium, Vibrio vulnificus
    • Lee H-J, Bang SH, Lee K-H, Park S-J. 2007. Positive regulation of fur gene expression via direct interaction of Fur in a pathogenic bacterium, Vibrio vulnificus. J Bacteriol 189:2629-2636. http://dx.doi.org/10.1128/JB.01791-06.
    • (2007) J Bacteriol , vol.189 , pp. 2629-2636
    • Lee, H.-J.1    Bang, S.H.2    Lee, K.-H.3    Park, S.-J.4
  • 209
    • 0141727572 scopus 로고    scopus 로고
    • Regulation of fur expression by RpoS and Fur in Vibrio vulnificus
    • Lee H-J, Park K-J, Lee AY, Park SG, Park BC, Lee K-H, Park S-J. 2003. Regulation of fur expression by RpoS and Fur in Vibrio vulnificus. J Bacteriol 185:5891-5896. http://dx.doi.org/10.1128/JB.185.19.5891-5896.2003.
    • (2003) J Bacteriol , vol.185 , pp. 5891-5896
    • Lee, H.-J.1    Park, K.-J.2    Lee, A.Y.3    Park, S.G.4    Park, B.C.5    Lee, K.-H.6    Park, S.-J.7
  • 210
    • 28444438519 scopus 로고    scopus 로고
    • Iron and Fur regulation in Vibrio cholerae and the role of Fur in virulence
    • Mey AR, Wyckoff EE, Kanukurthy V, Fisher CR, Payne SM. 2005. Iron and Fur regulation in Vibrio cholerae and the role of Fur in virulence. Infect Immun 73:8167-8178. http://dx.doi.org/10.1128/IAI.73.12.8167-8178.2005.
    • (2005) Infect Immun , vol.73 , pp. 8167-8178
    • Mey, A.R.1    Wyckoff, E.E.2    Kanukurthy, V.3    Fisher, C.R.4    Payne, S.M.5
  • 211
    • 84855386928 scopus 로고    scopus 로고
    • Positive regulation of the Vibrio cholerae porin OmpT by iron and Fur
    • Craig SA, Carpenter CD, Mey AR, Wyckoff EE, Payne SM. 2011. Positive regulation of the Vibrio cholerae porin OmpT by iron and Fur. J Bacteriol 193:6505-6511. http://dx.doi.org/10.1128/JB.05681-11.
    • (2011) J Bacteriol , vol.193 , pp. 6505-6511
    • Craig, S.A.1    Carpenter, C.D.2    Mey, A.R.3    Wyckoff, E.E.4    Payne, S.M.5
  • 212
    • 79961063576 scopus 로고    scopus 로고
    • Mapping the regulon of Vibrio cholerae ferric uptake regulator expands its known network of gene regulation
    • Davies BW, Bogard RW, Mekalanos JJ. 2011. Mapping the regulon of Vibrio cholerae ferric uptake regulator expands its known network of gene regulation. Proc Natl Acad Sci U S A 108:12467-12472. http://dx.doi.org/10.1073/pnas.1107894108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12467-12472
    • Davies, B.W.1    Bogard, R.W.2    Mekalanos, J.J.3
  • 213
    • 33646903239 scopus 로고    scopus 로고
    • Differences in gene expression between the classical and El Tor biotypes of Vibrio cholerae O1
    • Beyhan S, Tischler AD, Camilli A, Yildiz FH. 2006. Differences in gene expression between the classical and El Tor biotypes of Vibrio cholerae O1. Infect Immun 74:3633-3642. http://dx.doi.org/10.1128/IAI.01750-05.
    • (2006) Infect Immun , vol.74 , pp. 3633-3642
    • Beyhan, S.1    Tischler, A.D.2    Camilli, A.3    Yildiz, F.H.4
  • 214
    • 51949096025 scopus 로고    scopus 로고
    • Global gene expression as a function of the iron status of the bacterial cell: Influence of differentially expressed genes in the virulence of the human pathogen Vibrio vulnificus
    • Alice AF, Naka H, Crosa JH. 2008. Global gene expression as a function of the iron status of the bacterial cell: influence of differentially expressed genes in the virulence of the human pathogen Vibrio vulnificus. Infect Immun 76:4019-4037. http://dx.doi.org/10.1128/IAI.00208-08.
    • (2008) Infect Immun , vol.76 , pp. 4019-4037
    • Alice, A.F.1    Naka, H.2    Crosa, J.H.3
  • 215
    • 84877797054 scopus 로고    scopus 로고
    • Regulation of haemolysin (VvhA) production by ferric uptake regulator (Fur) in Vibrio vulnificus: Repression of vvhA transcription by Fur and proteolysis of VvhA by Fur-repressive exoproteases
    • Lee H-J, Kim J-A, Lee M-A, Park S-J, Lee K-H. 2013. Regulation of haemolysin (VvhA) production by ferric uptake regulator (Fur) in Vibrio vulnificus: repression of vvhA transcription by Fur and proteolysis of VvhA by Fur-repressive exoproteases. Mol Microbiol 88:813-826. http://dx.doi.org/10.1111/mmi.12224.
    • (2013) Mol Microbiol , vol.88 , pp. 813-826
    • Lee, H.-J.1    Kim, J.-A.2    Lee, M.-A.3    Park, S.-J.4    Lee, K.-H.5
  • 216
    • 0027461550 scopus 로고
    • Cloning and genetic analysis of the Vibrio vulnificus fur gene and construction of a fur mutant by in vivo marker exchange
    • Litwin CM, Calderwood SB. 1993. Cloning and genetic analysis of the Vibrio vulnificus fur gene and construction of a fur mutant by in vivo marker exchange. J Bacteriol 175:706-715.
    • (1993) J Bacteriol , vol.175 , pp. 706-715
    • Litwin, C.M.1    Calderwood, S.B.2
  • 217
    • 0027955329 scopus 로고
    • Characterization of the Vibrio anguillarum fur gene: Role in regulation of expression of the FatA outer membrane protein and catechols
    • Tolmasky ME, Wertheimer AM, Actis LA, Crosa JH. 1994. Characterization of the Vibrio anguillarum fur gene: role in regulation of expression of the FatA outer membrane protein and catechols. J Bacteriol 176:213-220.
    • (1994) J Bacteriol , vol.176 , pp. 213-220
    • Tolmasky, M.E.1    Wertheimer, A.M.2    Actis, L.A.3    Crosa, J.H.4
  • 218
    • 0033758935 scopus 로고    scopus 로고
    • Characterization of the DNA- and metal-binding properties of Vibrio anguillarum Fur reveals conservation of a structural Zn (2+) ion
    • Zheleznova EE, Crosa JH, Brennan RG. 2000. Characterization of the DNA- and metal-binding properties of Vibrio anguillarum Fur reveals conservation of a structural Zn (2+) ion. J Bacteriol 182:6264-6267. http://dx.doi.org/10.1128/JB.182.21.6264-6267.2000.
    • (2000) J Bacteriol , vol.182 , pp. 6264-6267
    • Zheleznova, E.E.1    Crosa, J.H.2    Brennan, R.G.3
  • 220
    • 0023806512 scopus 로고
    • Iron-regulated hemolysin production and utilization of heme and hemoglobin by Vibrio cholerae
    • Stoebner JA, Payne SM. 1988. Iron-regulated hemolysin production and utilization of heme and hemoglobin by Vibrio cholerae. Infect Immun 56:2891-2895.
    • (1988) Infect Immun , vol.56 , pp. 2891-2895
    • Stoebner, J.A.1    Payne, S.M.2
  • 221
    • 0028286106 scopus 로고
    • Regulation of iron on bacterial growth and production of thermostable direct hemolysin by Vibrio parahaemolyticus in intraperitoneal infected mice
    • Wong HC, Lee YS. 1994. Regulation of iron on bacterial growth and production of thermostable direct hemolysin by Vibrio parahaemolyticus in intraperitoneal infected mice. Microbiol Immunol 38:367-371. http://dx.doi.org/10.1111/j.1348-0421.1994.tb01792.x.
    • (1994) Microbiol Immunol , vol.38 , pp. 367-371
    • Wong, H.C.1    Lee, Y.S.2
  • 222
    • 0027195778 scopus 로고
    • Regulation of proteolytic activity of Vibrio vulnificus by iron-containing compounds
    • Simpson LM, Oliver JD. 1993. Regulation of proteolytic activity of Vibrio vulnificus by iron-containing compounds. Microb Pathog 14:249-252. http://dx.doi.org/10.1006/mpat.1993.1024.
    • (1993) Microb Pathog , vol.14 , pp. 249-252
    • Simpson, L.M.1    Oliver, J.D.2
  • 223
    • 0025159493 scopus 로고
    • A regulatory gene, angR, of the iron uptake system of Vibrio anguillarum: Similarity with phage P22 cro and regulation by iron
    • Farrell DH, Mikesell P, Actis LA, Crosa JH. 1990. A regulatory gene, angR, of the iron uptake system of Vibrio anguillarum: similarity with phage P22 cro and regulation by iron. Gene 86:45-51. http://dx.doi.org/10.1016/0378-1119 (90) 90112-5.
    • (1990) Gene , vol.86 , pp. 45-51
    • Farrell, D.H.1    Mikesell, P.2    Actis, L.A.3    Crosa, J.H.4
  • 224
    • 0024670217 scopus 로고
    • Regulation of the iron uptake system in Vibrio anguillarum: Evidence for a cooperative effect between two transcriptional activators
    • Salinas PC, Tolmasky ME, Crosa JH. 1989. Regulation of the iron uptake system in Vibrio anguillarum: evidence for a cooperative effect between two transcriptional activators. Proc Natl Acad Sci U S A 86:3529-3533. http://dx.doi.org/10.1073/pnas.86.10.3529.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3529-3533
    • Salinas, P.C.1    Tolmasky, M.E.2    Crosa, J.H.3
  • 226
    • 0023944783 scopus 로고
    • Genetic analysis of the iron uptake region of the Vibrio anguillarum plasmid pJM1: Molecular cloning of genetic determinants encoding a novel trans activator of siderophore biosynthesis
    • Tolmasky ME, Actis LA, Crosa JH. 1988. Genetic analysis of the iron uptake region of the Vibrio anguillarum plasmid pJM1: molecular cloning of genetic determinants encoding a novel trans activator of siderophore biosynthesis. J Bacteriol 170:1913-1919.
    • (1988) J Bacteriol , vol.170 , pp. 1913-1919
    • Tolmasky, M.E.1    Actis, L.A.2    Crosa, J.H.3
  • 227
    • 0029060567 scopus 로고
    • Regulation of angR, a gene with regulatory and biosynthetic functions in the pJM1 plasmid-mediated iron uptake system of Vibrio anguillarum
    • Salinas PC, Crosa JH. 1995. Regulation of angR, a gene with regulatory and biosynthetic functions in the pJM1 plasmid-mediated iron uptake system of Vibrio anguillarum. Gene 160:17-23. http://dx.doi.org/10.1016/0378-1119 (95) 00213-P.
    • (1995) Gene , vol.160 , pp. 17-23
    • Salinas, P.C.1    Crosa, J.H.2
  • 228
    • 0026099665 scopus 로고
    • Positive transcriptional regulation of an iron-regulated virulence gene in Vibrio cholerae
    • Goldberg MB, Boyko SA, Calderwood SB. 1991. Positive transcriptional regulation of an iron-regulated virulence gene in Vibrio cholerae. Proc Natl Acad Sci U S A 88:1125-1129. http://dx.doi.org/10.1073/pnas.88.4.1125.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 1125-1129
    • Goldberg, M.B.1    Boyko, S.A.2    Calderwood, S.B.3
  • 229
    • 0032536843 scopus 로고    scopus 로고
    • The interaction of the Vibrio cholerae transcription factors, Fur and IrgB, with the overlapping promoters of two virulence genes, irgA and irgB
    • Watnick PI, Butterton JR, Calderwood SB. 1998. The interaction of the Vibrio cholerae transcription factors, Fur and IrgB, with the overlapping promoters of two virulence genes, irgA and irgB. Gene 209:65-70. http://dx.doi.org/10.1016/S0378-1119 (98) 00018-3.
    • (1998) Gene , vol.209 , pp. 65-70
    • Watnick, P.I.1    Butterton, J.R.2    Calderwood, S.B.3
  • 230
    • 0035696699 scopus 로고    scopus 로고
    • Characterization of a Vibrio vulnificus LysR homologue, HupR, which regulates expression of the haem uptake outer membrane protein, HupA
    • Litwin CM, Quackenbush J. 2001. Characterization of a Vibrio vulnificus LysR homologue, HupR, which regulates expression of the haem uptake outer membrane protein, HupA. Microb Pathog 31:295-307. http://dx.doi.org/10.1006/mpat.2001.0472.
    • (2001) Microb Pathog , vol.31 , pp. 295-307
    • Litwin, C.M.1    Quackenbush, J.2
  • 231
    • 26444505976 scopus 로고    scopus 로고
    • Effect of RyhB small RNA on global iron use in Escherichia coli
    • Masse E, Vanderpool CK, Gottesman S. 2005. Effect of RyhB small RNA on global iron use in Escherichia coli. J Bacteriol 187:6962-6971. http://dx.doi.org/10.1128/JB.187.20.6962-6971.2005.
    • (2005) J Bacteriol , vol.187 , pp. 6962-6971
    • Masse, E.1    Vanderpool, C.K.2    Gottesman, S.3
  • 232
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Massé E, Gottesman S. 2002. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci U S A 99:4620-4625. http://dx.doi.org/10.1073/pnas.032066599.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4620-4625
    • Massé, E.1    Gottesman, S.2
  • 233
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Masse E, Escorcia FE, Gottesman S. 2003. Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev 17:2374-2383. http://dx.doi.org/10.1101/gad.1127103.
    • (2003) Genes Dev , vol.17 , pp. 2374-2383
    • Masse, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 234
    • 0038352109 scopus 로고    scopus 로고
    • Regulatory roles for small RNAs in bacteria
    • Masse E, Majdalani N, Gottesman S. 2003. Regulatory roles for small RNAs in bacteria. Curr Opin Microbiol 6:120-124. http://dx.doi.org/10.1016/S1369-5274 (03) 00027-4.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 120-124
    • Masse, E.1    Majdalani, N.2    Gottesman, S.3
  • 235
    • 33847206046 scopus 로고    scopus 로고
    • Control of Fur synthesis by the non-coding RNA RyhB and iron-responsive decoding
    • Vecerek B, Moll I, Bläsi U. 2007. Control of Fur synthesis by the non-coding RNA RyhB and iron-responsive decoding. EMBO J 26:965-975. http://dx.doi.org/10.1038/sj.emboj.7601553.
    • (2007) EMBO J , vol.26 , pp. 965-975
    • Vecerek, B.1    Moll, I.2    Bläsi, U.3
  • 236
    • 20444473805 scopus 로고    scopus 로고
    • Characterization of the small untranslated RNA RyhB and its regulon in Vibrio cholerae
    • Davis BM, Quinones M, Pratt J, Ding Y, Waldor MK. 2005. Characterization of the small untranslated RNA RyhB and its regulon in Vibrio cholerae. J Bacteriol 187:4005-4014. http://dx.doi.org/10.1128/JB.187.12.4005-4014.2005.
    • (2005) J Bacteriol , vol.187 , pp. 4005-4014
    • Davis, B.M.1    Quinones, M.2    Pratt, J.3    Ding, Y.4    Waldor, M.K.5
  • 237
    • 84880999526 scopus 로고    scopus 로고
    • The Vibrio parahaemolyticus small RNA RyhB promotes production of the siderophore vibrioferrin by stabilizing the polycistronic mRNA
    • Tanabe T, Funahashi T, Nakao H, Maki J, Yamamoto S. 2013. The Vibrio parahaemolyticus small RNA RyhB promotes production of the siderophore vibrioferrin by stabilizing the polycistronic mRNA. J Bacteriol 195:3692-3703. http://dx.doi.org/10.1128/JB.00162-13.
    • (2013) J Bacteriol , vol.195 , pp. 3692-3703
    • Tanabe, T.1    Funahashi, T.2    Nakao, H.3    Maki, J.4    Yamamoto, S.5
  • 238
    • 0029744688 scopus 로고    scopus 로고
    • Antisense RNA, Fur, iron, and the regulation of iron transport genes in Vibrio anguillarum
    • Chen Q, Crosa JH. 1996. Antisense RNA, Fur, iron, and the regulation of iron transport genes in Vibrio anguillarum. J Biol Chem 271:18885-18891. http://dx.doi.org/10.1074/jbc.271.31.18885.
    • (1996) J Biol Chem , vol.271 , pp. 18885-18891
    • Chen, Q.1    Crosa, J.H.2
  • 239
    • 0029050239 scopus 로고
    • Antisense RNA regulation of the fatB iron transport protein gene in Vibrio anguillarum
    • Waldbeser LS, Chen Q, Crosa JH. 1995. Antisense RNA regulation of the fatB iron transport protein gene in Vibrio anguillarum. Mol Microbiol 17:747-756. http://dx.doi.org/10.1111/j.1365-2958.1995.mmi-17040747.x.
    • (1995) Mol Microbiol , vol.17 , pp. 747-756
    • Waldbeser, L.S.1    Chen, Q.2    Crosa, J.H.3
  • 240
    • 84897114148 scopus 로고    scopus 로고
    • Regulation of iron transport systems in Enterobacteriaceae in response to oxygen and iron availability
    • Carpenter C, Payne SM. 2014. Regulation of iron transport systems in Enterobacteriaceae in response to oxygen and iron availability. J Inorg Biochem 133:110-117. http://dx.doi.org/10.1016/j.jinorgbio.2014.01.007.
    • (2014) J Inorg Biochem , vol.133 , pp. 110-117
    • Carpenter, C.1    Payne, S.M.2
  • 241
    • 62449186797 scopus 로고    scopus 로고
    • Regulation of the Vibrio vulnificus hupA gene by temperature alteration and cyclic AMP receptor protein and evaluation of its role in virulence
    • Oh MH, Lee SM, Lee DH, Choi SH. 2009. Regulation of the Vibrio vulnificus hupA gene by temperature alteration and cyclic AMP receptor protein and evaluation of its role in virulence. Infect Immun 77:1208-1215. http://dx.doi.org/10.1128/IAI.01006-08.
    • (2009) Infect Immun , vol.77 , pp. 1208-1215
    • Oh, M.H.1    Lee, S.M.2    Lee, D.H.3    Choi, S.H.4
  • 242
    • 0035183674 scopus 로고    scopus 로고
    • Temperature dependent siderophore production in Vibrio salmonicida
    • Colquhoun DJ, Sørum H. 2001. Temperature dependent siderophore production in Vibrio salmonicida. Microb Pathog 31:213-219. http://dx.doi.org/10.1006/mpat.2001.0464.
    • (2001) Microb Pathog , vol.31 , pp. 213-219
    • Colquhoun, D.J.1    Sørum, H.2
  • 243
    • 84860369015 scopus 로고    scopus 로고
    • Cyclic AMP-receptor protein activates aerobactin receptor IutA expression in Vibrio vulnificus
    • Kim C-M, Kim S-J, Shin S-H. 2012. Cyclic AMP-receptor protein activates aerobactin receptor IutA expression in Vibrio vulnificus. J Microbiol 50:320-325. http://dx.doi.org/10.1007/s12275-012-2056-y.
    • (2012) J Microbiol , vol.50 , pp. 320-325
    • Kim, C.-M.1    Kim, S.-J.2    Shin, S.-H.3
  • 244
    • 84903896000 scopus 로고    scopus 로고
    • Physiological and proteomic analysis of Escherichia coli iron-limited chemostat growth
    • Folsom JP, Parker AE, Carlson RP. 2014. Physiological and proteomic analysis of Escherichia coli iron-limited chemostat growth. J Bacteriol 196:2748-2761. http://dx.doi.org/10.1128/JB.01606-14.
    • (2014) J Bacteriol , vol.196 , pp. 2748-2761
    • Folsom, J.P.1    Parker, A.E.2    Carlson, R.P.3
  • 245
    • 84864541698 scopus 로고    scopus 로고
    • Iron and quorum sensing coordinately regulate the expression of vulnibactin biosynthesis in Vibrio vulnificus
    • Wen Y, Kim IH, Son J-S, Lee B-H, Kim K-S. 2012. Iron and quorum sensing coordinately regulate the expression of vulnibactin biosynthesis in Vibrio vulnificus. J Biol Chem 287:26727-26739. http://dx.doi.org/10.1074/jbc. M112.374165.
    • (2012) J Biol Chem , vol.287 , pp. 26727-26739
    • Wen, Y.1    Kim, I.H.2    Son, J.-S.3    Lee, B.-H.4    Kim, K.-S.5
  • 246
    • 79955652929 scopus 로고    scopus 로고
    • Modulation of iron-uptake systems by a mutation of luxS encoding an autoinducer-2 synthase in Vibrio vulnificus
    • Kim CM, Shin SH. 2011. Modulation of iron-uptake systems by a mutation of luxS encoding an autoinducer-2 synthase in Vibrio vulnificus. Biol Pharm Bull 34:632-637. http://dx.doi.org/10.1248/bpb.34.632.
    • (2011) Biol Pharm Bull , vol.34 , pp. 632-637
    • Kim, C.M.1    Shin, S.H.2
  • 247
    • 84880694914 scopus 로고    scopus 로고
    • The Fur-iron complex modulates expression of the quorum-sensing master regulator, SmcR, to control expression of virulence factors in Vibrio vulnificus
    • Kim IH, Wen Y, Son J-S, Lee K-H, Kim K-S. 2013. The Fur-iron complex modulates expression of the quorum-sensing master regulator, SmcR, to control expression of virulence factors in Vibrio vulnificus. Infect Immun 81:2888-2898. http://dx.doi.org/10.1128/IAI.00375-13.
    • (2013) Infect Immun , vol.81 , pp. 2888-2898
    • Kim, I.H.1    Wen, Y.2    Son, J.-S.3    Lee, K.-H.4    Kim, K.-S.5
  • 248
    • 84874798275 scopus 로고    scopus 로고
    • The iron-dependent regulator Fur controls pheromone signaling systems and luminescence in the squid symbiont Vibrio fischeri ES114
    • Septer AN, Lyell NL, Stabb EV. 2013. The iron-dependent regulator Fur controls pheromone signaling systems and luminescence in the squid symbiont Vibrio fischeri ES114. Appl Environ Microbiol 79:1826-1834. http://dx.doi.org/10.1128/AEM.03079-12.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 1826-1834
    • Septer, A.N.1    Lyell, N.L.2    Stabb, E.V.3
  • 249
    • 84919684451 scopus 로고    scopus 로고
    • The Vibrio cholerae Cpx envelope stress response senses and mediates adaptation to low iron
    • Acosta N, Pukatzki S, Raivio TL. 2015. The Vibrio cholerae Cpx envelope stress response senses and mediates adaptation to low iron. J Bacteriol 197:262-276. http://dx.doi.org/10.1128/JB.01957-14.
    • (2015) J Bacteriol , vol.197 , pp. 262-276
    • Acosta, N.1    Pukatzki, S.2    Raivio, T.L.3
  • 250
    • 78049426115 scopus 로고    scopus 로고
    • Calcium and iron regulate swarming and type III secretion in Vibrio parahaemolyticus
    • Gode-Potratz CJ, Chodur DM, McCarter LL. 2010. Calcium and iron regulate swarming and type III secretion in Vibrio parahaemolyticus. J Bacteriol 192:6025-6038. http://dx.doi.org/10.1128/JB.00654-10.
    • (2010) J Bacteriol , vol.192 , pp. 6025-6038
    • Gode-Potratz, C.J.1    Chodur, D.M.2    McCarter, L.L.3
  • 251
    • 0024505398 scopus 로고
    • Iron regulation of swarmer cell differentiation of Vibrio parahaemolyticus
    • McCarter L, Silverman M. 1989. Iron regulation of swarmer cell differentiation of Vibrio parahaemolyticus. J Bacteriol 171:731-736.
    • (1989) J Bacteriol , vol.171 , pp. 731-736
    • McCarter, L.1    Silverman, M.2
  • 252
    • 0001398811 scopus 로고
    • Studies in diphtheria toxin production. I. The effect of iron and copper
    • Pappenheimer AM, Johnson SJ. 1936. Studies in diphtheria toxin production. I. The effect of iron and copper. Br J Exp Pathol 17:335-341.
    • (1936) Br J Exp Pathol , vol.17 , pp. 335-341
    • Pappenheimer, A.M.1    Johnson, S.J.2
  • 253
    • 0000475753 scopus 로고
    • Preparation and properties of Shiga toxin and toxoid
    • Dubos RJ, Geiger JW. 1946. Preparation and properties of Shiga toxin and toxoid. J Exp Med 84:143-156. http://dx.doi.org/10.1084/jem.84.2.143.
    • (1946) J Exp Med , vol.84 , pp. 143-156
    • Dubos, R.J.1    Geiger, J.W.2
  • 254
    • 0025300518 scopus 로고
    • Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae
    • Boyd J, Oza MN, Murphy JR. 1990. Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae. Proc Natl Acad Sci U S A 87:5968-5972. http://dx.doi.org/10.1073/pnas.87.15.5968.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5968-5972
    • Boyd, J.1    Oza, M.N.2    Murphy, J.R.3
  • 255
    • 0023631217 scopus 로고
    • Iron regulation of Shiga-like toxin expression in Escherichia coli is mediated by the fur locus
    • Calderwood SB, Mekalanos JJ. 1987. Iron regulation of Shiga-like toxin expression in Escherichia coli is mediated by the fur locus. J Bacteriol 169:4759-4764.
    • (1987) J Bacteriol , vol.169 , pp. 4759-4764
    • Calderwood, S.B.1    Mekalanos, J.J.2
  • 256
    • 0026666051 scopus 로고
    • Purification and characterization of the diphtheria toxin repressor
    • Schmitt MP, Twiddy EM, Holmes RK. 1992. Purification and characterization of the diphtheria toxin repressor. Proc Natl Acad Sci U S A 89:7576-7580. http://dx.doi.org/10.1073/pnas.89.16.7576.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 7576-7580
    • Schmitt, M.P.1    Twiddy, E.M.2    Holmes, R.K.3
  • 257
    • 25444488281 scopus 로고    scopus 로고
    • A novel aerobactin utilization cluster in Vibrio vulnificus with a gene involved in the transcription regulation of the iutA homologue
    • Tanabe T, Naka A, Aso H, Nakao H, Narimatsu S, Inoue Y, Ono T, Yamamoto S. 2005. A novel aerobactin utilization cluster in Vibrio vulnificus with a gene involved in the transcription regulation of the iutA homologue. Microbiol Immunol 49:823-834. http://dx.doi.org/10.1111/j.1348-0421.2005.tb03671.x.
    • (2005) Microbiol Immunol , vol.49 , pp. 823-834
    • Tanabe, T.1    Naka, A.2    Aso, H.3    Nakao, H.4    Narimatsu, S.5    Inoue, Y.6    Ono, T.7    Yamamoto, S.8
  • 258
    • 84865646771 scopus 로고    scopus 로고
    • Characterization of Vibrio parahaemolyticus genes encoding the systems for utilization of enterobactin as a xenosiderophore
    • Tanabe T, Funahashi T, Shiuchi K, Okajima N, Nakao H, Miyamoto K, Tsujibo H, Yamamoto S. 2012. Characterization of Vibrio parahaemolyticus genes encoding the systems for utilization of enterobactin as a xenosiderophore. Microbiology 158:2039-2049. http://dx.doi.org/10.1099/mic.0.059568-0.
    • (2012) Microbiology , vol.158 , pp. 2039-2049
    • Tanabe, T.1    Funahashi, T.2    Shiuchi, K.3    Okajima, N.4    Nakao, H.5    Miyamoto, K.6    Tsujibo, H.7    Yamamoto, S.8
  • 259
    • 84938879879 scopus 로고    scopus 로고
    • Regulation of the expression of the Vibrio parahaemolyticus peuA gene encoding an alternative ferric enterobactin receptor
    • Tanabe T, Kato A, Shiuchi K, Miyamoto K, Tsujibo H, Maki J, Yamamoto S, Funahashi T. 2014. Regulation of the expression of the Vibrio parahaemolyticus peuA gene encoding an alternative ferric enterobactin receptor. PLoS One 9:e105749. http://dx.doi.org/10.1371/journal.pone.0105749.
    • (2014) PLoS One , vol.9 , pp. e105749
    • Tanabe, T.1    Kato, A.2    Shiuchi, K.3    Miyamoto, K.4    Tsujibo, H.5    Maki, J.6    Yamamoto, S.7    Funahashi, T.8
  • 260
    • 84860543897 scopus 로고    scopus 로고
    • Identification and characterization of a novel outer membrane protein receptor FetA for ferric enterobactin transport in Vibrio anguillarum 775 (pJM1)
    • Naka H, Crosa JH. 2012. Identification and characterization of a novel outer membrane protein receptor FetA for ferric enterobactin transport in Vibrio anguillarum 775 (pJM1). Biometals 25:125-133. http://dx.doi.org/10.1007/s10534-011-9488-4.
    • (2012) Biometals , vol.25 , pp. 125-133
    • Naka, H.1    Crosa, J.H.2
  • 261
    • 77952480350 scopus 로고    scopus 로고
    • Iron uptake in Vibrio and Aeromonas
    • Cornelis P, Andrews SC ed, Caister Academic Press, Norfolk, United Kingdom
    • Lemos ML, Osorio CR. 2010. Iron uptake in Vibrio and Aeromonas, p 117-141. In Cornelis P, Andrews SC (ed), Iron uptake and homeostasis in microorganisms. Caister Academic Press, Norfolk, United Kingdom.
    • (2010) Iron Uptake and Homeostasis in Microorganisms , pp. 117-141
    • Lemos, M.L.1    Osorio, C.R.2
  • 262
    • 0030952623 scopus 로고    scopus 로고
    • Iron uptake from ferric citrate by Vibrio anguillarum
    • Mazoy R, Botana LM, Lemos ML. 1997. Iron uptake from ferric citrate by Vibrio anguillarum. FEMS Microbiol Lett 154:145-150. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12636.x.
    • (1997) FEMS Microbiol Lett , vol.154 , pp. 145-150
    • Mazoy, R.1    Botana, L.M.2    Lemos, M.L.3
  • 263
    • 0035113720 scopus 로고    scopus 로고
    • VibD and VibH are required for late steps in vibriobactin biosynthesis in Vibrio cholerae
    • Wyckoff EE, Smith SL, Payne SM. 2001. VibD and VibH are required for late steps in vibriobactin biosynthesis in Vibrio cholerae. J Bacteriol 183:1830-1834. http://dx.doi.org/10.1128/JB.183.5.1830-1834.2001.
    • (2001) J Bacteriol , vol.183 , pp. 1830-1834
    • Wyckoff, E.E.1    Smith, S.L.2    Payne, S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.