메뉴 건너뛰기




Volumn 54, Issue 10, 2010, Pages 606-617

Identification and characterization of a Vibrio mimicus gene encoding the heme/hemoglobin receptor

Author keywords

Heme hemoglobin receptor gene; Iron source; Iron repressible outer membrane protein; Vibrio mimicus

Indexed keywords

BACTERIAL PROTEIN; BETA GALACTOSIDASE; HEME; HEME RECEPTOR; HEMOGLOBIN; HEMOGLOBIN RECEPTOR; IRON; OUTER MEMBRANE PROTEIN; PROTEIN LYSR; PROTEIN MHUB; UNCLASSIFIED DRUG;

EID: 77957936057     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2010.00256.x     Document Type: Article
Times cited : (7)

References (43)
  • 1
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C., Dover L.G. (2000) Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 54: 881-941.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 2
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke M., Marahiel M.A. (2007) Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol Rev 71: 413-51.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 3
    • 57649107157 scopus 로고    scopus 로고
    • Bacterial heme-transport proteins and their heme-coordination modes
    • Tong Y., Guo M. (2009) Bacterial heme-transport proteins and their heme-coordination modes. Arch Biochem Biophys 481: 1-15.
    • (2009) Arch Biochem Biophys , vol.481 , pp. 1-15
    • Tong, Y.1    Guo, M.2
  • 4
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg A., Neilands J.B. (1987) Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26: 5471-7.
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 5
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: transcriptional metalloregulation by the Fur protein
    • Escolar L., Perez-Martin J., de Lorenzo V. (1999) Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181: 6223-9.
    • (1999) J Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    de Lorenzo, V.3
  • 6
    • 0019784585 scopus 로고
    • Characterization of biochemically atypical Vibrio cholerae strains and designation of a new pathogenic species Vibrio mimicus
    • Davis B.R., Fanning G.R., Madden J.M., Steigerwalt A.G., Bradford H.B., Smith H.L., Brenner D.J. (1981) Characterization of biochemically atypical Vibrio cholerae strains and designation of a new pathogenic species, Vibrio mimicus. J Clin Microbiol 14: 631-9.
    • (1981) J Clin Microbiol , vol.14 , pp. 631-639
    • Davis, B.R.1    Fanning, G.R.2    Madden, J.M.3    Steigerwalt, A.G.4    Bradford, H.B.5    Smith, H.L.6    Brenner, D.J.7
  • 7
    • 3242755208 scopus 로고    scopus 로고
    • Distribution of virulence-associated genes in Vibrio mimicus isolates from clinical and environmental origins
    • Shinoda S., Nakagawa T., Shi L., Bi K., Kanoh Y., Tomochika K., Miyoshi S., Shimada T. (2004) Distribution of virulence-associated genes in Vibrio mimicus isolates from clinical and environmental origins. Microbiol Immunol 48: 547-51.
    • (2004) Microbiol Immunol , vol.48 , pp. 547-551
    • Shinoda, S.1    Nakagawa, T.2    Shi, L.3    Bi, K.4    Kanoh, Y.5    Tomochika, K.6    Miyoshi, S.7    Shimada, T.8
  • 9
    • 0028225597 scopus 로고
    • Identification of the siderophores from Vibrio hollisae and Vibrio mimicus as aerobactin
    • Okujo N., Yamamoto S. (1994) Identification of the siderophores from Vibrio hollisae and Vibrio mimicus as aerobactin. FEMS Microbiol Lett 118: 187-92.
    • (1994) FEMS Microbiol Lett , vol.118 , pp. 187-192
    • Okujo, N.1    Yamamoto, S.2
  • 10
    • 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.
    • (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
  • 11
    • 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 TonB-dependent proteins
    • Henderson D.P., Payne S.M. (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 TonB-dependent proteins. J Bacteriol 176: 3269-77.
    • (1994) J Bacteriol , vol.176 , pp. 3269-3277
    • Henderson, D.P.1    Payne, S.M.2
  • 12
    • 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 C.M., Byrne B.L. (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: 3134-41.
    • (1998) Infect Immun , vol.66 , pp. 3134-3141
    • Litwin, C.M.1    Byrne, B.L.2
  • 13
    • 0029005717 scopus 로고
    • Utilization of hemin and hemoglobin as iron sources by Vibrio parahaemolyticus and identification of an iron-repressible hemin-binding protein
    • Yamamoto S., Hara Y., Tomochika K., Shinoda S. (1995) Utilization of hemin and hemoglobin as iron sources by Vibrio parahaemolyticus and identification of an iron-repressible hemin-binding protein. FEMS Microbiol Lett 128: 195-200.
    • (1995) FEMS Microbiol Lett , vol.128 , pp. 195-200
    • Yamamoto, S.1    Hara, Y.2    Tomochika, K.3    Shinoda, S.4
  • 14
    • 0028327173 scopus 로고
    • Fur regulon in Gram-negative bacteria Identification and characterization of new iron-regulated Escherichia coli genes by a Fur titration assay
    • Stojiljkovic I., Baumler A.J., Hantke K. (1994) Fur regulon in Gram-negative bacteria. Identification and characterization of new iron-regulated Escherichia coli genes by a Fur titration assay. J Mol Biol 236: 531-45.
    • (1994) J Mol Biol , vol.236 , pp. 531-545
    • Stojiljkovic, I.1    Baumler, A.J.2    Hantke, K.3
  • 15
    • 0034035345 scopus 로고    scopus 로고
    • Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein
    • Belyaeva T.A.,Wade J.T.,Webster C.L., Howard V.J., Thomas M.S., Hyde E.I., Busby S.J. (2000) Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein. Mol Microbiol 36: 211-22.
    • (2000) Mol Microbiol , vol.36 , pp. 211-222
    • Belyaeva, T.A.1    Wade, J.T.2    Webster, C.L.3    Howard, V.J.4    Thomas, M.S.5    Hyde, E.I.6    Busby, S.J.7
  • 16
    • 14644386907 scopus 로고    scopus 로고
    • A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPalpha) conjugative machineries and their cognate Escherichia coli host strains
    • Demarre G., Guerout A.M., Matsumoto-Mashimo C., Rowe-Magnus D.A., Marliere P., Mazel D. (2005) A new family of mobilizable suicide plasmids based on broad host range R388 plasmid (IncW) and RP4 plasmid (IncPalpha) conjugative machineries and their cognate Escherichia coli host strains. Res Microbiol 156: 245-55.
    • (2005) Res Microbiol , vol.156 , pp. 245-255
    • Demarre, G.1    Guerout, A.M.2    Matsumoto-Mashimo, C.3    Rowe-Magnus, D.A.4    Marliere, P.5    Mazel, D.6
  • 17
    • 0029812447 scopus 로고    scopus 로고
    • Location of essential sequence elements at the Escherichia coli melAB promoter
    • Keen J.,Williams J., Busby S. (1996) Location of essential sequence elements at the Escherichia coli melAB promoter. Biochem J 318: 443-9.
    • (1996) Biochem J , vol.318 , pp. 443-449
    • Keen, J.1    Williams, J.2    Busby, S.3
  • 19
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria
    • Keen N.T., Tamaki S., Kobayashi D., Trollinger D. (1988) Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria. Gene 70: 191-7.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 21
    • 0035110351 scopus 로고    scopus 로고
    • Identification and characterization of the sodA genes encoding manganese superoxide dismutases in Vibrio parahaemolyticus, Vibrio mimicus, and Vibrio vulnificus
    • Kimoto R., Funahashi T., Yamamoto N., Miyoshi S., Narimatsu S., Yamamoto S. (2001) Identification and characterization of the sodA genes encoding manganese superoxide dismutases in Vibrio parahaemolyticus, Vibrio mimicus, and Vibrio vulnificus. Microbiol Immunol 45: 135-42.
    • (2001) Microbiol Immunol , vol.45 , pp. 135-142
    • Kimoto, R.1    Funahashi, T.2    Yamamoto, N.3    Miyoshi, S.4    Narimatsu, S.5    Yamamoto, S.6
  • 22
    • 0003785155 scopus 로고
    • Cold Spring Harbor NY: Cold Spring Harbor Laboratory Press
    • Miller J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 352-3.
    • (1972) Experiments in Molecular Genetics , pp. 352-353
    • Miller, J.H.1
  • 23
    • 34248669292 scopus 로고    scopus 로고
    • Iron acquisition in Vibrio cholerae
    • Wyckoff E.E., Mey A.R., Payne S.M. (2007) Iron acquisition in Vibrio cholerae. Biometals 20: 405-16.
    • (2007) Biometals , vol.20 , pp. 405-416
    • Wyckoff, E.E.1    Mey, A.R.2    Payne, S.M.3
  • 24
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo V.,Wee S., Herrero M., Neilands J.B. (1987) Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J Bacteriol 169: 2624-30.
    • (1987) J Bacteriol , vol.169 , pp. 2624-2630
    • de Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 25
    • 0023886015 scopus 로고
    • Posttranscriptional regulatory mechanisms in Escherichia coli
    • Gold L. (1988) Posttranscriptional regulatory mechanisms in Escherichia coli. Annu Rev Biochem 57: 199-233.
    • (1988) Annu Rev Biochem , vol.57 , pp. 199-233
    • Gold, L.1
  • 26
    • 0037952996 scopus 로고    scopus 로고
    • Isolation of mutants of Vibrio anguillarum defective in heme utilisation and cloning of huvA, a gene coding for an outer membrane protein involved in the use of heme as iron source
    • Mazoy R., Osorio C.R., Toranzo A.E., Lemos M.L. (2003) Isolation of mutants of Vibrio anguillarum defective in heme utilisation and cloning of huvA, a gene coding for an outer membrane protein involved in the use of heme as iron source. Arch Microbiol 179: 329-38.
    • (2003) Arch Microbiol , vol.179 , pp. 329-338
    • Mazoy, R.1    Osorio, C.R.2    Toranzo, A.E.3    Lemos, M.L.4
  • 27
    • 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: 722-9.
    • (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
  • 28
    • 0032862457 scopus 로고    scopus 로고
    • Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: histidine residues are essential for receptor function
    • Bracken C.S., Baer M.T., Abdur-Rashid A., HelmsW., Stojiljkovic I. (1999) Use of heme-protein complexes by the Yersinia enterocolitica HemR receptor: histidine residues are essential for receptor function. J Bacteriol 181: 6063-72.
    • (1999) J Bacteriol , vol.181 , pp. 6063-6072
    • Bracken, C.S.1    Baer, M.T.2    Abdur-Rashid, A.3    Helms, W.4    Stojiljkovic, I.5
  • 29
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell M.A. (1993) Molecular biology of the LysR family of transcriptional regulators. Annu Rev Microbiol 47: 597-626.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 30
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks S.E., Oyston P.C. (2008) Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154: 3609-23.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 31
    • 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 C.M., 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.
    • (2001) Microb Pathog , vol.31 , pp. 295-307
    • Litwin, C.M.1    Quackenbush, J.2
  • 32
    • 0023806512 scopus 로고
    • Iron-regulated hemolysin production and utilization of heme and hemoglobin by Vibrio cholerae
    • Stoebner J.A., Payne S.M. (1988) Iron-regulated hemolysin production and utilization of heme and hemoglobin by Vibrio cholerae. Infect Immun 56: 2891-5.
    • (1988) Infect Immun , vol.56 , pp. 2891-2895
    • Stoebner, J.A.1    Payne, S.M.2
  • 33
    • 0026710561 scopus 로고
    • Effects of iron limitation on production of a siderophore, outer membrane proteins, and hemolysin and on hydrophobicity, cell adherence, and lethality for mice of Vibrio parahaemolyticus
    • Dai J.H., Lee Y.S.,Wong H.C. (1992) Effects of iron limitation on production of a siderophore, outer membrane proteins, and hemolysin and on hydrophobicity, cell adherence, and lethality for mice of Vibrio parahaemolyticus. Infect Immun 60: 2952-6.
    • (1992) Infect Immun , vol.60 , pp. 2952-2956
    • Dai, J.H.1    Lee, Y.S.2    Wong, H.C.3
  • 34
    • 69149110336 scopus 로고    scopus 로고
    • Iron differentially regulates gene expression and extracellular secretion of Vibrio vulnificus cytolysin-hemolysin
    • Kim C.M., Chung Y.Y., Shin S.H. (2009) Iron differentially regulates gene expression and extracellular secretion of Vibrio vulnificus cytolysin-hemolysin. J Infect Dis 200: 582-9.
    • (2009) J Infect Dis , vol.200 , pp. 582-589
    • Kim, C.M.1    Chung, Y.Y.2    Shin, S.H.3
  • 36
    • 0026043552 scopus 로고
    • Purification and characterization of a hemolysin of Vibrio mimicus that relates to the thermostable direct hemolysin of Vibrio parahaemolyticus
    • Yoshida H., Honda T., Miwatani T. (1991) Purification and characterization of a hemolysin of Vibrio mimicus that relates to the thermostable direct hemolysin of Vibrio parahaemolyticus. FEMS Microbiol Lett 84: 249-54.
    • (1991) FEMS Microbiol Lett , vol.84 , pp. 249-254
    • Yoshida, H.1    Honda, T.2    Miwatani, T.3
  • 37
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn B., Neilands J.B. (1987) Universal chemical assay for the detection and determination of siderophores. Anal Biochem 160: 47-56.
    • (1987) Anal Biochem , vol.160 , pp. 47-56
    • Schwyn, B.1    Neilands, J.B.2
  • 38
    • 34248647591 scopus 로고    scopus 로고
    • Heme, an iron supply for vibrios pathogenic for fish
    • Lemos M.L., Osorio C.R. (2007) Heme, an iron supply for vibrios pathogenic for fish. Biometals 20: 615-26.
    • (2007) Biometals , vol.20 , pp. 615-626
    • Lemos, M.L.1    Osorio, C.R.2
  • 39
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-25.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 41
    • 38949158464 scopus 로고    scopus 로고
    • Binding site determinants for the LysR-type transcriptional regulator PcaQ in the legume endosymbiont Sinorhizobium meliloti
    • MacLean A.M., Anstey M.I., Finan T.M. (2008) Binding site determinants for the LysR-type transcriptional regulator PcaQ in the legume endosymbiont Sinorhizobium meliloti. J Bacteriol 190: 1237-46.
    • (2008) J Bacteriol , vol.190 , pp. 1237-1246
    • MacLean, A.M.1    Anstey, M.I.2    Finan, T.M.3
  • 43
    • 0035168497 scopus 로고    scopus 로고
    • Haem utilization in Vibrio cholerae involves multiple TonB-dependent haem receptors
    • Mey A.R., Payne S.M. (2001) Haem utilization in Vibrio cholerae involves multiple TonB-dependent haem receptors. Mol Microbiol 42: 835-49.
    • (2001) Mol Microbiol , vol.42 , pp. 835-849
    • Mey, A.R.1    Payne, S.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.