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Volumn 188, Issue 24, 2006, Pages 8421-8429

Staphylococcus aureus IsdB is a hemoglobin receptor required for heme iron utilization

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 14; GENOMIC DNA; HEME; HEMOGLOBIN; HEMOPROTEIN; IRON; IRON 57; ISDB PROTEIN; MEMBRANE PROTEIN; MYOGLOBIN;

EID: 33845428586     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01335-06     Document Type: Article
Times cited : (230)

References (43)
  • 1
    • 29144482705 scopus 로고    scopus 로고
    • Allelic replacement in Staphylococcus aureus with inducible counter-selection
    • Bae, T., and O. Schneewind. 2006. Allelic replacement in Staphylococcus aureus with inducible counter-selection. Plasmid 55:58-63.
    • (2006) Plasmid , vol.55 , pp. 58-63
    • Bae, T.1    Schneewind, O.2
  • 2
    • 0037371345 scopus 로고    scopus 로고
    • Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron
    • Bates, C. S., G. E. Montanez, C. R. Woods, R. M. Vincent, and Z. Eichenbaum. 2003. Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron. Infect. Immun. 71:1042-1055.
    • (2003) Infect. Immun. , vol.71 , pp. 1042-1055
    • Bates, C.S.1    Montanez, G.E.2    Woods, C.R.3    Vincent, R.M.4    Eichenbaum, Z.5
  • 3
    • 0014322660 scopus 로고
    • Lytic effects of staphylococcal alpha-toxin and delta-hemolysin
    • Bernheimer, A. W., L. S. Avigad, and P. Grushoff. 1968. Lytic effects of staphylococcal alpha-toxin and delta-hemolysin. J. Bacteriol. 96:487-491.
    • (1968) J. Bacteriol. , vol.96 , pp. 487-491
    • Bernheimer, A.W.1    Avigad, L.S.2    Grushoff, P.3
  • 5
    • 12744254896 scopus 로고    scopus 로고
    • Newer antistaphylococcal agents
    • Bradley, J. S. 2005. Newer antistaphylococcal agents. Curr. Opin. Pediatr. 17:71-77.
    • (2005) Curr. Opin. Pediatr. , vol.17 , pp. 71-77
    • Bradley, J.S.1
  • 6
    • 0036801009 scopus 로고    scopus 로고
    • Secondary bacterial infections complicating skin lesions
    • Brook, I. 2002. Secondary bacterial infections complicating skin lesions. J. Med. Microbiol. 51:808-812.
    • (2002) J. Med. Microbiol. , vol.51 , pp. 808-812
    • Brook, I.1
  • 8
    • 33645111877 scopus 로고    scopus 로고
    • Natural resistance, iron and infection: A challenge for clinical medicine
    • Bullen, J. J., H. J. Rogers, P. B. Spalding, and C. G. Ward. 2006. Natural resistance, iron and infection: a challenge for clinical medicine. J. Med. Microbiol. 55:251-258.
    • (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
  • 10
    • 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
  • 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
    • 0020740239 scopus 로고
    • Iron metabolism in reticuloendothelial cells
    • Deiss, A. 1983. Iron metabolism in reticuloendothelial cells. Semin. Hematol. 20:81-90.
    • (1983) Semin. Hematol. , vol.20 , pp. 81-90
    • Deiss, A.1
  • 13
    • 0034128270 scopus 로고    scopus 로고
    • Corynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters
    • Drazek, E. S., C. A. Hammack, and M. P. Schmitt. 2000. Corynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters. Mol. Microbiol. 36:68-84.
    • (2000) Mol. Microbiol. , vol.36 , pp. 68-84
    • Drazek, E.S.1    Hammack, C.A.2    Schmitt, M.P.3
  • 14
    • 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
  • 15
    • 0038385189 scopus 로고    scopus 로고
    • Identification of a novel iron regulated staphylococcal surface protein with haptoglobin-haemoglobin binding activity
    • Dryla, A., D. Gelbmann, A. Von Gabain, and E. Nagy. 2003. Identification of a novel iron regulated staphylococcal surface protein with haptoglobin-haemoglobin 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
  • 16
    • 0002527348 scopus 로고
    • Staphylococcal coagulase: Mode of action and antigenicity
    • Duthie, E. S., and L. L. Lorenz. 1952. Staphylococcal coagulase: mode of action and antigenicity. J. Gen. Microbiol. 6:95-107.
    • (1952) J. Gen. Microbiol. , vol.6 , pp. 95-107
    • Duthie, E.S.1    Lorenz, L.L.2
  • 18
    • 0019752467 scopus 로고
    • Induction of hemoglobin synthesis in original K 562 cell line
    • Fuhr, J. E., E. G. Bamberger, C. B. Lozzio, and B. B. Lozzio. 1981. Induction of hemoglobin synthesis in original K 562 cell line. Blood Cells 7:389-399.
    • (1981) Blood Cells , vol.7 , pp. 389-399
    • Fuhr, J.E.1    Bamberger, E.G.2    Lozzio, C.B.3    Lozzio, B.B.4
  • 19
    • 0035181250 scopus 로고    scopus 로고
    • Emerging strategies in microbial haem capture
    • Genco, C. A., and D. W. Dixon. 2001. Emerging strategies in microbial haem capture. Mol. Microbiol. 39:1-11.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1-11
    • Genco, C.A.1    Dixon, D.W.2
  • 20
    • 0035150765 scopus 로고    scopus 로고
    • In Staphylococcus aureus, fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis
    • Horsburgh, M. J., E. Ingham, and S. J. Foster. 2001. In Staphylococcus aureus, Fur is an interactive regulator with PerR, contributes to virulence, and is necessary for oxidative stress resistance through positive regulation of catalase and iron homeostasis. J. Bacteriol. 183:468-475.
    • (2001) J. Bacteriol. , vol.183 , pp. 468-475
    • Horsburgh, M.J.1    Ingham, E.2    Foster, S.J.3
  • 22
    • 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
  • 24
    • 0141668997 scopus 로고    scopus 로고
    • Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes
    • Lei, B., M. Liu, J. M. Voyich, C. I. Prater, S. V. Kala, F. R. DeLeo, and J. M. Musser. 2003. Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes. Infect. Immun. 71:5962-5969.
    • (2003) Infect. Immun. , vol.71 , pp. 5962-5969
    • Lei, B.1    Liu, M.2    Voyich, J.M.3    Prater, C.I.4    Kala, S.V.5    DeLeo, F.R.6    Musser, J.M.7
  • 25
    • 0036070707 scopus 로고    scopus 로고
    • Identification and characterization of a novel heme-associated cell surface protein made by Streptococcus pyogenes
    • Lei, B., L. M. Smoot, H. M. Menning, J. M. Voyich, S. V. Kala, F. R. Deleo, S. D. Reid, and J. M. Musser. 2002. Identification and characterization of a novel heme-associated cell surface protein made by Streptococcus pyogenes. Infect. Immun. 70:4494-4500.
    • (2002) Infect. Immun. , vol.70 , pp. 4494-4500
    • Lei, B.1    Smoot, L.M.2    Menning, H.M.3    Voyich, J.M.4    Kala, S.V.5    Deleo, F.R.6    Reid, S.D.7    Musser, J.M.8
  • 26
    • 0031734518 scopus 로고    scopus 로고
    • Transport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin utilization system of Neisseria meningitidis
    • Lewis, L. A., M. H. Sung, M. Gipson, K. Hartman, and D. W. Dyer. 1998. Transport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin utilization system of Neisseria meningitidis. J. Bacteriol. 180:6043-6047.
    • (1998) J. Bacteriol. , vol.180 , pp. 6043-6047
    • Lewis, L.A.1    Sung, M.H.2    Gipson, M.3    Hartman, K.4    Dyer, D.W.5
  • 27
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria
    • Marraffini, L. A., A. C. Dedent, and O. Schneewind. 2006. Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria. Microbiol. Mol. Biol. Rev. 70:192-221.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 28
    • 0034625174 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections
    • Mazmanian, S. K., G. Liu, E. R. Jensen, E. Lenoy, and O. Schneewind. 2000. Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections. Proc. Natl. Acad. Sci. USA 97:5510-5515.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5510-5515
    • Mazmanian, S.K.1    Liu, G.2    Jensen, E.R.3    Lenoy, E.4    Schneewind, O.5
  • 29
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S. K., G. Liu, H. Ton-That, and O. Schneewind. 1999. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285:760-763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 31
    • 0037133213 scopus 로고    scopus 로고
    • An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis
    • Mazmanian, S. K., H. Ton-That, K. Su, and O. Schneewind. 2002. An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc. Natl. Acad. Sci. USA 99:2293-2298.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2293-2298
    • Mazmanian, S.K.1    Ton-That, H.2    Su, K.3    Schneewind, O.4
  • 32
    • 0034741104 scopus 로고    scopus 로고
    • Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins, and metalloporphyrins
    • Olczak, T., D. W. Dixon, and C. A. Genco. 2001. Binding specificity of the Porphyromonas gingivalis heme and hemoglobin receptor HmuR, gingipain K, and gingipain R1 for heme, porphyrins, and metalloporphyrins. J. Bacteriol. 183:5599-5608.
    • (2001) J. Bacteriol. , vol.183 , pp. 5599-5608
    • Olczak, T.1    Dixon, D.W.2    Genco, C.A.3
  • 33
    • 0035132479 scopus 로고    scopus 로고
    • Emergence of methicillin-resistant Staphylococcus aureus with intermediate glycopeptide resistance: Clinical significance and treatment options
    • Ryhak, 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
    • Ryhak, M.J.1    Akins, R.L.2
  • 34
    • 0026638608 scopus 로고
    • Sorting of protein a to the staphylococcal cell wall
    • Schneewind, O., P. Model, and V. A. Fischetti. 1992. Sorting of protein A to the staphylococcal cell wall. Cell 70:267-281.
    • (1992) Cell , vol.70 , pp. 267-281
    • Schneewind, O.1    Model, P.2    Fischetti, V.A.3
  • 35
    • 31344432103 scopus 로고    scopus 로고
    • Bacillus anthracis IsdG, a heme-degrading monooxygenase
    • Skaar, E. P., A. H. Gaspar, and O. Schneewind. 2006. Bacillus anthracis IsdG, a heme-degrading monooxygenase. J. Bacteriol. 188:1071-1080.
    • (2006) J. Bacteriol. , vol.188 , pp. 1071-1080
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 36
    • 0345791519 scopus 로고    scopus 로고
    • IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus
    • Skaar, E. P., A. H. Gaspar, and O. Schneewind. 2004. IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus. J. Biol. Chem. 279:436-443.
    • (2004) J. Biol. Chem. , vol.279 , pp. 436-443
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 37
    • 4644310922 scopus 로고    scopus 로고
    • Iron-source preference of Staphylococcus aureus infections
    • Skaar, E. P., M. Humayun, T. Bae, K. L. DeBord, and O. Schneewind. 2004. Iron-source preference of Staphylococcus aureus infections. Science 305:1626-1628.
    • (2004) Science , vol.305 , pp. 1626-1628
    • Skaar, E.P.1    Humayun, M.2    Bae, T.3    DeBord, K.L.4    Schneewind, O.5
  • 38
    • 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
  • 39
    • 0029765788 scopus 로고    scopus 로고
    • HmbR outer membrane receptors of pathogenic Neisseria spp.: Iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation
    • Stojiljkovic, I., J. Larson, V. Hwa, S. Anic, and M. So. 1996. HmbR outer membrane receptors of pathogenic Neisseria spp.: iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation. J. Bacteriol. 178:4670-4678.
    • (1996) J. Bacteriol. , vol.178 , pp. 4670-4678
    • Stojiljkovic, I.1    Larson, J.2    Hwa, V.3    Anic, S.4    So, M.5
  • 40
    • 0033607265 scopus 로고    scopus 로고
    • Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
    • Ton-That, H., G. Liu, S. K. Mazmanian, K. F. Faull, and O. Schneewind. 1999. Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc. Natl. Acad. Sci. USA 96:12424-12429.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12424-12429
    • Ton-That, H.1    Liu, G.2    Mazmanian, S.K.3    Faull, K.F.4    Schneewind, O.5
  • 41
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: The role of heme, hemoprotein receptors and hemophores
    • Wandersraan, C., and I. Stojiljkovic. 2000. Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr. Opin. Microbiol. 3:215-220.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 215-220
    • Wandersraan, C.1    Stojiljkovic, I.2
  • 42
    • 13244296905 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases
    • Wu, R., E. P. Skaar, R. Zhang, G. Joachimiak, P. Gornicki, O. Schneewind, and A. Joachimiak. 2005. Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases. J. Biol. Chem. 280:2840-2846.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2840-2846
    • Wu, R.1    Skaar, E.P.2    Zhang, R.3    Joachimiak, G.4    Gornicki, P.5    Schneewind, O.6    Joachimiak, A.7
  • 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(Pt. 3):659-668.
    • (2000) Microbiology , vol.146 , Issue.PART 3 , pp. 659-668
    • Xiong, A.1    Singh, V.K.2    Cabrera, G.3    Jayaswal, R.K.4


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