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Volumn 43, Issue 2, 2005, Pages 183-190

Staphylococcus aureus siderophore-mediated iron-acquisition system plays a dominant and essential role in the utilization of transferrin-bound iron

Author keywords

Iron; Siderophore; Staphylococcus aureus; Transferrin; Transferrin binding protein

Indexed keywords

APOTRANSFERRIN; IRON; PROTEINASE; SIDEROPHORE; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 19344362794     PISSN: 12258873     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (43)
  • 2
    • 0036216270 scopus 로고    scopus 로고
    • Active transport of iron and siderophore antibiotics
    • Braun, V. and M. Barun. 2002. Active transport of iron and siderophore antibiotics. Curr. Opin. Microbiol. 5, 194-201.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 194-201
    • Braun, V.1    Barun, M.2
  • 3
    • 0025886812 scopus 로고
    • Relative availability of transferrin-bound iron and cell-driven iron to aerobactin-producing and enterochelin-producing strains of Escherichia coli and to other microorganisms
    • Brock, J.H., P.H. Williams, J. Liceaga, and K.G. Woolridge. 1991. Relative availability of transferrin-bound iron and cell-driven iron to aerobactin-producing and enterochelin-producing strains of Escherichia coli and to other microorganisms. Infect. Immun. 59, 3185-3190.
    • (1991) Infect. Immun. , vol.59 , pp. 3185-3190
    • Brock, J.H.1    Williams, P.H.2    Liceaga, J.3    Woolridge, K.G.4
  • 4
    • 0036754957 scopus 로고    scopus 로고
    • Iron acquisition by Gram-positive bacterial pathogens
    • Brown, J.S. and D.W. Holden. 2002. Iron acquisition by Gram-positive bacterial pathogens. Microbes Infect. 4, 1149-1156.
    • (2002) Microbes Infect. , vol.4 , pp. 1149-1156
    • Brown, J.S.1    Holden, D.W.2
  • 6
    • 0035143844 scopus 로고    scopus 로고
    • Molecular characterization of the iron-hydroxamate uptake system in Staphylococcus aureus
    • Cabrera, G., A. Xiong, M. Uebel, V.K. Singh, and R.K. Jayaswal. 2001. Molecular characterization of the iron-hydroxamate uptake system in Staphylococcus aureus. Appl. Environ. Microbiol. 67, 1001-1003.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1001-1003
    • Cabrera, G.1    Xiong, A.2    Uebel, M.3    Singh, V.K.4    Jayaswal, R.K.5
  • 7
    • 1542407100 scopus 로고    scopus 로고
    • IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesion
    • Clarke, S.R., M.D. Wiltshire, and S.J. Foster. 2004. IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesion. Mol. Microbiol. 51, 1509-1519.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1509-1519
    • Clarke, S.R.1    Wiltshire, M.D.2    Foster, S.J.3
  • 8
    • 0035048099 scopus 로고    scopus 로고
    • Iron: Seminal publications of the twentieth century-transferrin
    • Conrad, M.E. 2001. Iron: seminal publications of the twentieth century-transferrin. J. Tra. Ele. Exp. Med. 14, 115-117.
    • (2001) J. Tra. Ele. Exp. Med. , vol.14 , pp. 115-117
    • Conrad, M.E.1
  • 9
    • 0030969403 scopus 로고    scopus 로고
    • Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins
    • Courcol, R.J., D. Trivier, M.C. Bissinger, G.R. Martin, and M.R. Brown. 1997. Siderophore production by Staphylococcus aureus and identification of iron-regulated proteins. Infect. Immun. 65, 1944-1948.
    • (1997) Infect. Immun. , vol.65 , pp. 1944-1948
    • Courcol, R.J.1    Trivier, D.2    Bissinger, M.C.3    Martin, G.R.4    Brown, M.R.5
  • 10
    • 0031407137 scopus 로고    scopus 로고
    • Signal transduction and transcriptional and post-transcriptional control of iron-regulated genes in bacteria
    • Crosa, J.H. 1997. Signal transduction and transcriptional and post-transcriptional control of iron-regulated genes in bacteria. Microbiol Mol. Biol. Rev. 61, 319-336.
    • (1997) Microbiol Mol. Biol. Rev. , vol.61 , pp. 319-336
    • Crosa, J.H.1
  • 11
    • 0348141912 scopus 로고    scopus 로고
    • Role of siderophore biosynthesis in virulence of Staphylococcus aureus: Identification and characterization of genes involved in production of a siderophore
    • Dale, S.E., A. Doherty-Kirby, G. Lajoie and D.E. Heinrichs. 2004. Role of siderophore biosynthesis in virulence of Staphylococcus aureus: Identification and characterization of genes involved in production of a siderophore. Infect. Immun. 72, 29-37.
    • (2004) Infect. Immun. , vol.72 , pp. 29-37
    • Dale, S.E.1    Doherty-Kirby, A.2    Lajoie, G.3    Heinrichs, D.E.4
  • 12
    • 0027661433 scopus 로고
    • Purification and chemical characterization of staphyloferrin B, a hydrophilic siderophore from staphylococci
    • Drechsel, H., S. Freund, G. Nicholson, H. Haag, O. Jung, H. Zahner, and G. Jung. 1993. Purification and chemical characterization of staphyloferrin B, a hydrophilic siderophore from staphylococci. Biometals 6, 185-192.
    • (1993) Biometals , vol.6 , pp. 185-192
    • Drechsel, H.1    Freund, S.2    Nicholson, G.3    Haag, H.4    Jung, O.5    Zahner, H.6    Jung, G.7
  • 13
    • 0038385189 scopus 로고    scopus 로고
    • Identification of a novel iron regulated staphylococcal surface protein with haptoglobulin-hemoglobin binding activity
    • Dryla, A., D. Gelbmann, A. Von Gabain, and E. Nagy. 2003. Identification of a novel iron regulated staphylococcal surface protein with haptoglobulin-hemoglobin binding activity. Mol. Microbiol. 49, 37-53.
    • (2003) Mol. Microbiol. , vol.49 , pp. 37-53
    • Dryla, A.1    Gelbmann, D.2    Von Gabain, A.3    Nagy, E.4
  • 14
    • 0027379284 scopus 로고
    • An overview of nosocomial infections, including the role of the microbiology laboratory
    • Emori, T.G. and R.P. Gaynes. 1993. An overview of nosocomial infections, including the role of the microbiology laboratory. Clin. Microbiol. Rev. 6, 428-442.
    • (1993) Clin. Microbiol. Rev. , vol.6 , pp. 428-442
    • Emori, T.G.1    Gaynes, R.P.2
  • 15
    • 0025313285 scopus 로고
    • Staphyloferrin A: A structurally new siderophore from staphylococci
    • Konetschny-Rapp, S., G. Jung, J. Meiwes, and H. Zahner. 1990. Staphyloferrin A: a structurally new siderophore from staphylococci. Eur. J. Biochem. 191, 65-74.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 65-74
    • Konetschny-Rapp, S.1    Jung, G.2    Meiwes, J.3    Zahner, H.4
  • 16
    • 0020484025 scopus 로고
    • Siderophore production by phytopathogenic microbial species
    • Leong, S.A. and J.B. Neilands. 1982. Siderophore production by phytopathogenic microbial species. Arch. Biochem. Biophys. 218, 351-359.
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 351-359
    • Leong, S.A.1    Neilands, J.B.2
  • 17
    • 0032530002 scopus 로고    scopus 로고
    • A human transferrin-binding protein of Staphylococcus aureus is immunogenic in vivo and has an epitope in common with human transferrin receptor
    • Lim, Y., S.H. Shin, I.Y. Jang, J.H. Rhee, and I.S. Kim. 1998. A human transferrin-binding protein of Staphylococcus aureus is immunogenic in vivo and has an epitope in common with human transferrin receptor. FEMS Microbiol. Lett. 166, 225-230.
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 225-230
    • Lim, Y.1    Shin, S.H.2    Jang, I.Y.3    Rhee, J.H.4    Kim, I.S.5
  • 18
    • 0032103015 scopus 로고    scopus 로고
    • Iron-repressibility of siderophore and transferrin-binding protein in Staphylococccus aureus
    • Lim, Y., S.H. Shin, S.I. Lee, I.S. Kim, and J.H. Rhee. 1998. Iron-repressibility of siderophore and transferrin-binding protein in Staphylococccus aureus. FEMS Microbiol. Lett. 163, 19-24.
    • (1998) FEMS Microbiol. Lett. , vol.163 , pp. 19-24
    • Lim, Y.1    Shin, S.H.2    Lee, S.I.3    Kim, I.S.4    Rhee, J.H.5
  • 19
    • 19344369579 scopus 로고    scopus 로고
    • Oxygen stimulates the expression of iron-repressible high-affinity iron-uptake systems of Staphylococcus aureus-Application of CAS agar diffusion assay
    • Lim, Y., S.Y. Cho, N.S. Cho, S.I. Lee, J.Y. Chung, C.H. Chung, and S.H. Shin. 2004. Oxygen stimulates the expression of iron-repressible high-affinity iron-uptake systems of Staphylococcus aureus-Application of CAS agar diffusion assay. Infection and Chemotherapy 36, 32-39.
    • (2004) Infection and Chemotherapy , vol.36 , pp. 32-39
    • Lim, Y.1    Cho, S.Y.2    Cho, N.S.3    Lee, S.I.4    Chung, J.Y.5    Chung, C.H.6    Shin, S.H.7
  • 20
    • 0028284677 scopus 로고
    • Staphylococcal iron requirements, siderophore production, and iron-regulated protein expression
    • Lindsay, J.A. and T.V. Riley. 1994. Staphylococcal iron requirements, siderophore production, and iron-regulated protein expression. Infect. Immun. 62, 2309-2314.
    • (1994) Infect. Immun. , vol.62 , pp. 2309-2314
    • Lindsay, J.A.1    Riley, T.V.2
  • 21
    • 0028847890 scopus 로고
    • Staphylococcus aureus but not Staphylococcus epidermidis can acquire iron from transferrin
    • Lindsay, J.A., T.V. Riley, and B.J. Mee. 1995. Staphylococcus aureus but not Staphylococcus epidermidis can acquire iron from transferrin. Microbiology 141, 197-203.
    • (1995) Microbiology , vol.141 , pp. 197-203
    • Lindsay, J.A.1    Riley, T.V.2    Mee, B.J.3
  • 22
    • 0017100245 scopus 로고
    • The detection of four molecular forms of human transferrin during the iron binding process
    • Makey, D.G. and U.S. Seal. 1988. The detection of four molecular forms of human transferrin during the iron binding process. Biochem. Biophys. Acta 453, 250-256.
    • (1988) Biochem. Biophys. Acta , vol.453 , pp. 250-256
    • Makey, D.G.1    Seal, U.S.2
  • 25
    • 0031955933 scopus 로고    scopus 로고
    • The Staphylococcus aureus and Staphylococcus epidermidis transferrin-binding proteins are expressed in vivo during infection
    • Modun, B.J., A. Cockayne, R. Finch, and P. Williams. 1998. The Staphylococcus aureus and Staphylococcus epidermidis transferrin-binding proteins are expressed in vivo during infection. Microbiology 144, 1005-1012.
    • (1998) Microbiology , vol.144 , pp. 1005-1012
    • Modun, B.J.1    Cockayne, A.2    Finch, R.3    Williams, P.4
  • 26
    • 0028133393 scopus 로고
    • Staphylococci express a receptor for human transferrin: Identification of a 42-kilodalton cell wall transferrin-binding protein
    • Modun, B., D. Kendall, and P. Williams. 1994. Staphylococci express a receptor for human transferrin: Identification of a 42-kilodalton cell wall transferrin-binding protein. Infect. Immun. 62, 3850-3858.
    • (1994) Infect. Immun. , vol.62 , pp. 3850-3858
    • Modun, B.1    Kendall, D.2    Williams, P.3
  • 27
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehydes-3-phosphate dehydrogenase
    • Modun, B. and P. Williams. 1999. The staphylococcal transferrin-binding protein is a cell wall glyceraldehydes-3-phosphate dehydrogenase. Infect. Immun. 67, 1086-1092.
    • (1999) Infect. Immun. , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 28
    • 0031824078 scopus 로고    scopus 로고
    • Receptor-mediated recognition and uptake of iron from human transferrin by Staphylococcus aureus and Staphylococcus epidermidis
    • Modun, B., R.W. Evans, C.L. Joannou, and P. Williams. 1998. Receptor-mediated recognition and uptake of iron from human transferrin by Staphylococcus aureus and Staphylococcus epidermidis. Infect. Immun. 66, 3591-3596.
    • (1998) Infect. Immun. , vol.66 , pp. 3591-3596
    • Modun, B.1    Evans, R.W.2    Joannou, C.L.3    Williams, P.4
  • 29
    • 0033789579 scopus 로고    scopus 로고
    • Molecular cloning and analysis of a putative siderophore ABC transporter from Staphylococcus aureus
    • Morrissey, J.A., A. Cockayne, P.J. Hill, and P. Williams. 2000. Molecular cloning and analysis of a putative siderophore ABC transporter from Staphylococcus aureus. Infect. Immun. 68, 6281-6288.
    • (2000) Infect. Immun. , vol.68 , pp. 6281-6288
    • Morrissey, J.A.1    Cockayne, A.2    Hill, P.J.3    Williams, P.4
  • 30
    • 0029787281 scopus 로고    scopus 로고
    • Involvement of vulnibactin and exocellular protease in utilization of transferrin-and lactoferrin-bound iron by Vibrio vulnificus
    • Okuzo, N., T. Akiyama, S. Miyoshi, S. Shinoda, and S. Yamamoto. 1996. Involvement of vulnibactin and exocellular protease in utilization of transferrin-and lactoferrin-bound iron by Vibrio vulnificus. Microbiol Immunol. 40, 595-598.
    • (1996) Microbiol Immunol. , vol.40 , pp. 595-598
    • Okuzo, N.1    Akiyama, T.2    Miyoshi, S.3    Shinoda, S.4    Yamamoto, S.5
  • 31
    • 15944394697 scopus 로고    scopus 로고
    • Growth of Staphylococcus aureus with defective siderophore production in human peritoneal dialysate solution
    • Park, R.Y., H.Y. Sun, M.H. Choi, Y.H. Bae, and S.H. Shin. 2005. Growth of Staphylococcus aureus with defective siderophore production in human peritoneal dialysate solution. J. Microbiol. 43, 54-61.
    • (2005) J. Microbiol. , vol.43 , pp. 54-61
    • Park, R.Y.1    Sun, H.Y.2    Choi, M.H.3    Bae, Y.H.4    Shin, S.H.5
  • 32
    • 0023833788 scopus 로고
    • Degradation of elastin by a cysteine proteinase from Staphylococcus aureus
    • Potempa, J., A. Dubin, G. Korzus, and J. Travis. 1988. Degradation of elastin by a cysteine proteinase from Staphylococcus aureus. J. Biol. Chem. 263, 2664-2667.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2664-2667
    • Potempa, J.1    Dubin, A.2    Korzus, G.3    Travis, J.4
  • 33
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C. and L. Dover. 2000. Iron metabolism in pathogenic bacteria, Ann. Rev. Microbiol. 54, 881-941.
    • (2000) Ann. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.2
  • 34
    • 0035132479 scopus 로고    scopus 로고
    • Emergence of methicillin-resistant Staphylococcus aureus with intermediate glycopeptide resistance: Clinical significance and treatment options
    • Rybak, M.J. and R.L. Akins. 2001. Emergence of methicillin-resistant Staphylococcus aureus with intermediate glycopeptide resistance: clinical significance and treatment options. Drugs 61, 1-7.
    • (2001) Drugs , vol.61 , pp. 1-7
    • Rybak, M.J.1    Akins, R.L.2
  • 35
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn, B. and J.B. Neilands. 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
  • 36
    • 0034885056 scopus 로고    scopus 로고
    • Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus
    • Sebulsky, M.T. and D.E. Heinrichs. 2001. Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus. J. Bacteriol. 183, 4994-5000.
    • (2001) J. Bacteriol. , vol.183 , pp. 4994-5000
    • Sebulsky, M.T.1    Heinrichs, D.E.2
  • 37
    • 0033907955 scopus 로고    scopus 로고
    • Identification and characterization of a membrane permease involved in iron-hydroxamate transport in Staphylococcus aureus
    • Sebulsky, M.T., D. Hohnstein, M.D. Hunter, and D.E. Heinrichs. 2000. Identification and characterization of a membrane permease involved in iron-hydroxamate transport in Staphylococcus aureus. J. Bacteriol. 182, 4394-4400.
    • (2000) J. Bacteriol. , vol.182 , pp. 4394-4400
    • Sebulsky, M.T.1    Hohnstein, D.2    Hunter, M.D.3    Heinrichs, D.E.4
  • 38
    • 0035125397 scopus 로고    scopus 로고
    • CAS agar diffusion assay for the measurement of siderophores in biological fluids
    • Shin, S.H., Y. Lim, S.E. Lee, N.W. Yang, and J.H. Rhee. 2001. CAS agar diffusion assay for the measurement of siderophores in biological fluids. J. Microbiol. Methods 44, 89-95.
    • (2001) J. Microbiol. Methods , vol.44 , pp. 89-95
    • Shin, S.H.1    Lim, Y.2    Lee, S.E.3    Yang, N.W.4    Rhee, J.H.5
  • 39
    • 0033580211 scopus 로고    scopus 로고
    • The development of vancomycin resistance in a patient with methicillin-resistant Staphylococcus aureus infection
    • Sieradzki, K., R.B. Roberts, S.W. Haber, and A.Tomasz. 1999. The development of vancomycin resistance in a patient with methicillin-resistant Staphylococcus aureus infection. N. Engl. J. Med. 340, 517-523.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 517-523
    • Sieradzki, K.1    Roberts, R.B.2    Haber, S.W.3    Tomasz, A.4
  • 40
    • 1642283048 scopus 로고    scopus 로고
    • Iron-regulated surface determinants (Isd) of Staphylococcus aureus: Stealing iron from heme
    • Skaar, E.P. and O. Schneewind. 2004. Iron-regulated surface determinants (Isd) of Staphylococcus aureus: stealing iron from heme. Microbes Infect. 6, 390-397.
    • (2004) Microbes Infect. , vol.6 , pp. 390-397
    • Skaar, E.P.1    Schneewind, O.2
  • 41
    • 0036275173 scopus 로고    scopus 로고
    • Transferrin binding in Staphylococcus aureus: Involvement of a cell wall-anchored protein
    • Taylor, J.M. and Heinrichs, D.E. (2002) Transferrin binding in Staphylococcus aureus: involvement of a cell wall-anchored protein. Mol. Microbiol. 43, 1603-1614.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1603-1614
    • Taylor, J.M.1    Heinrichs, D.E.2
  • 42
    • 0030222101 scopus 로고    scopus 로고
    • Iron depletion and virulence in Staphylococcus aureus
    • Trivier, D. and R.J. Courcol. 1996. Iron depletion and virulence in Staphylococcus aureus. FEMS Microbiol. Lett. 141, 117-127.
    • (1996) FEMS Microbiol. Lett. , vol.141 , pp. 117-127
    • Trivier, D.1    Courcol, R.J.2
  • 43
    • 0034113354 scopus 로고    scopus 로고
    • Molecular characterization of the ferric-uptake regulator, Fur, from Staphylococcus aureus
    • Xiong, A., V.K. Singh, G. Cabrera, and R.K. Jayaswal. 2000. Molecular characterization of the ferric-uptake regulator, Fur, from Staphylococcus aureus. Microbiology 146, 659-668.
    • (2000) Microbiology , vol.146 , pp. 659-668
    • Xiong, A.1    Singh, V.K.2    Cabrera, G.3    Jayaswal, R.K.4


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