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Volumn 6, Issue MAY, 2016, Pages

Characterization of Spbhp-37, a hemoglobin-binding protein of Streptococcus pneumoniae

Author keywords

Haem; Haem binding protein; Iron; Iron starvation; Streptococcus pneumoniae

Indexed keywords

HAPTOGLOBIN; HEMOGLOBIN; SPBHP 37 PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; HEME; HEMOGLOBIN-BINDING PROTEIN, BACTERIA; IRON; PROTEIN BINDING;

EID: 85006226404     PISSN: None     EISSN: 22352988     Source Type: Journal    
DOI: 10.3389/fcimb.2016.00047     Document Type: Article
Times cited : (6)

References (40)
  • 3
    • 0002229032 scopus 로고
    • Pneumococcal polysaccharide vaccines
    • Austrian, R. (1989). Pneumococcal polysaccharide vaccines. Rev. Infect. Dis. 11, 598-602. doi: 10.1093/clinids/11.Supplement_3.S598
    • (1989) Rev. Infect. Dis , vol.11 , pp. 598-602
    • Austrian, R.1
  • 4
    • 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., Montanez, G. E., Woods, C. R., Vincent, R. M., and Eichenbaum, Z. (2003). Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron. Infect. Immun. 71, 1042-1055. doi: 10.1128/IAI.71.3.1042-1055.2003
    • (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
  • 5
    • 0036226966 scopus 로고    scopus 로고
    • Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence
    • Bierne, H., Mazmanian, S. K., Trost, M., Pucciarelli, M. G., Liu, G., Dehoux, P., et al. (2002). Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring of surface proteins and affects virulence. Mol. Microbiol. 43, 869-881 doi: 10.1046/j.1365-2958.2002.02798.x
    • (2002) Mol. Microbiol , vol.43 , pp. 869-881
    • Bierne, H.1    Mazmanian, S.K.2    Trost, M.3    Pucciarelli, M.G.4    Liu, G.5    Dehoux, P.6
  • 6
    • 0035006337 scopus 로고    scopus 로고
    • A Streptococcus pneumoniae pathogenicity island encoding an ABC transporter involved in iron uptake and virulence
    • Brown, J. S., Gilliland, S. M., and Holden, D. W. (2001). A Streptococcus pneumoniae pathogenicity island encoding an ABC transporter involved in iron uptake and virulence. Mol. Microbiol. 40, 572-585. doi: 10.1046/j.1365-2958.2001.02414.x
    • (2001) Mol. Microbiol , vol.40 , pp. 572-585
    • Brown, J.S.1    Gilliland, S.M.2    Holden, D.W.3
  • 7
    • 0033399598 scopus 로고    scopus 로고
    • Epidemiology of pneumococcal infections in the elderly
    • Butler, J. C., and Schuchat, A. (1999). Epidemiology of pneumococcal infections in the elderly. Drugs Aging 15, 11-19. doi: 10.2165/00002512-199915001-00002
    • (1999) Drugs Aging , vol.15 , pp. 11-19
    • Butler, J.C.1    Schuchat, A.2
  • 8
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa, J., and Walsh, C. (2002). Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Mol. Biol. R. 66, 223-249. doi: 10.1128/MMBR.66.2.223-249.2002
    • (2002) Microbiol. Mol. Biol. R , vol.66 , pp. 223-249
    • Crosa, J.1    Walsh, C.2
  • 9
    • 0042820128 scopus 로고    scopus 로고
    • Thermodynamics of heme binding to the HasA(SM) hemophore: effect of mutations at three key residues for heme uptake
    • Deniau, C., Gilli, R., Izadi-Pruneyre, N., Letoffe, S., Delepierre, M., Wandersman, C., et al. (2003). Thermodynamics of heme binding to the HasA(SM) hemophore: effect of mutations at three key residues for heme uptake. Biochemistry 42, 10627-10633. doi: 10.1021/bi030015k
    • (2003) Biochemistry , vol.42 , pp. 10627-10633
    • Deniau, C.1    Gilli, R.2    Izadi-Pruneyre, N.3    Letoffe, S.4    Delepierre, M.5    Wandersman, C.6
  • 10
    • 84862756028 scopus 로고    scopus 로고
    • Iron trafficking system in Helicobacter pylori
    • Ge, R., and Sun, X. (2012). Iron trafficking system in Helicobacter pylori. BioMetals 25, 247-258. doi: 10.1007/s10534-011-9512-8
    • (2012) BioMetals , vol.25 , pp. 247-258
    • Ge, R.1    Sun, X.2
  • 11
    • 0035181250 scopus 로고    scopus 로고
    • Emerging strategies in microbial haem capture
    • Genco, C. A., and Dixon, D. W. (2001). Emerging strategies in microbial haem capture. Mol. Microbiol. 39, 1-11. doi: 10.1046/j.1365-2958.2001.02231.x
    • (2001) Mol. Microbiol , vol.39 , pp. 1-11
    • Genco, C.A.1    Dixon, D.W.2
  • 12
    • 1842326840 scopus 로고    scopus 로고
    • A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
    • Ghigo, J. M., Letoffe, S., and Wandersman, C. (1997). A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli. J. Bacteriol. 179, 3572-3579.
    • (1997) J. Bacteriol , vol.179 , pp. 3572-3579
    • Ghigo, J.M.1    Letoffe, S.2    Wandersman, C.3
  • 13
    • 0018630784 scopus 로고
    • Serotypes of Streptococcus pneumoniae causing disease
    • Gray, B. M., Converse, J., and Dillon, H. (1979). Serotypes of Streptococcus pneumoniae causing disease. J. Infect. Dis. 140, 979-983. doi: 10.1093/infdis/140.6.979
    • (1979) J. Infect. Dis , vol.140 , pp. 979-983
    • Gray, B.M.1    Converse, J.2    Dillon, H.3
  • 14
    • 0027945605 scopus 로고
    • Microbial iron transport
    • Guerinot, M. L. (1994). Microbial iron transport. Annu. Rev. Microbiol. 48, 743-772. doi: 10.1146/annurev.mi.48.100194.003523
    • (1994) Annu. Rev. Microbiol , vol.48 , pp. 743-772
    • Guerinot, M.L.1
  • 15
    • 0020046909 scopus 로고
    • Kinetics of biosynthesis of iron-regulated membrane proteins in Escherichia coli
    • Klebba, P. E., McIntosh, M. A., and Neilands, J. B. (1982). Kinetics of biosynthesis of iron-regulated membrane proteins in Escherichia coli. J. Bacteriol. 149, 880-888.
    • (1982) J. Bacteriol , vol.149 , pp. 880-888
    • Klebba, P.E.1    McIntosh, M.A.2    Neilands, J.B.3
  • 16
    • 0141668997 scopus 로고    scopus 로고
    • Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes
    • Lei, B., Liu, M., Voyich, J. M., Prater, C. I., Kala, S. V., DeLeo, F. R., et al. (2003). Identification and characterization of HtsA, a second heme-binding protein made by Streptococcus pyogenes. Infect. Immun. 71, 5962-5969. doi: 10.1128/iai.71.10.5962-5969.2003
    • (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
  • 17
    • 0036070707 scopus 로고    scopus 로고
    • Identification and characterization of a novel heme-associated cell surface protein made by Streptococcus pyogenes
    • Lei, B., Smoot, L. M., Menning, H. M., Voyich, J. M., Kala, S. V., Deleo, F. R., et al. (2002). Identification and characterization of a novel heme-associated cell surface protein made by Streptococcus pyogenes. Infect. Immun. 70, 4494-4500. doi: 10.1128/IAI.70.8.4494-4500.2002
    • (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
  • 18
    • 0031734518 scopus 로고    scopus 로고
    • Transport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin utilization system of Neisseria meningitidis
    • Lewis, L. A., Sung, M. H., Gipson, M., Hartman, K., and Dyer, D. W. (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
  • 19
    • 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., Liu, G., Jensen, E. R., Lenoy, E., and Schneewind, O. (2000). Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections. Proc. Natl. Acad. Sci. U.S.A. 97, 5510-5515. doi: 10.1073/pnas.080520697
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 5510-5515
    • Mazmanian, S.K.1    Liu, G.2    Jensen, E.R.3    Lenoy, E.4    Schneewind, O.5
  • 20
    • 0037423231 scopus 로고    scopus 로고
    • Passage of heme-iron across the envelope of Staphylococcus aureus
    • Mazmanian, S. K., Skaar, E. P., Gaspar, A. H., Humayun, M., Gornicki, P., Jelenska, J., et al. (2003). Passage of heme-iron across the envelope of Staphylococcus aureus. Science 299, 906-909. doi: 10.1126/science.1081147
    • (2003) Science , vol.299 , pp. 906-909
    • Mazmanian, S.K.1    Skaar, E.P.2    Gaspar, A.H.3    Humayun, M.4    Gornicki, P.5    Jelenska, J.6
  • 21
    • 0037133213 scopus 로고    scopus 로고
    • An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis
    • Mazmanian, S. K., Ton-That, H., Su, K., and Schneewind, O. (2002). An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proc. Natl. Acad. Sci. U.S.A. 99, 2293-2298. doi: 10.1073/pnas.032523999
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 2293-2298
    • Mazmanian, S.K.1    Ton-That, H.2    Su, K.3    Schneewind, O.4
  • 22
    • 0026604355 scopus 로고
    • Infections caused by Streptococcus pneumoniae: clinical spectrum, pathogenesis, immunity, and treatment
    • Musher, D. M. (1992). Infections caused by Streptococcus pneumoniae: clinical spectrum, pathogenesis, immunity, and treatment. Clin. Infect. Dis. 14, 801-807. doi: 10.1093/clinids/14.4.801
    • (1992) Clin. Infect. Dis , vol.14 , pp. 801-807
    • Musher, D.M.1
  • 23
    • 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., Dixon, D. W., and Genco, C. A. (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. doi: 10.1128/JB.183.19.5599-5608.2001
    • (2001) J. Bacteriol , vol.183 , pp. 5599-5608
    • Olczak, T.1    Dixon, D.W.2    Genco, C.A.3
  • 24
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C., and Dover, L. (2000). Iron metabolism in pathogenic bacteria. Annu. Rev. Microbiol. 54, 881-941. doi: 10.1146/annurev.micro.54.1.881
    • (2000) Annu. Rev. Microbiol , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.2
  • 25
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: an archetype for microbial iron transport
    • Raymond, K. N., Dertz, E. A., and Kim, S. S. (2003). Enterobactin: an archetype for microbial iron transport. Proc. Natl. Acad. Sci. U.S.A. 100, 3584-3588. doi: 10.1073/pnas.0630018100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 26
    • 84879557888 scopus 로고    scopus 로고
    • Streptococcus pneumoniae requires iron for its viability and expresses two membrane proteins that bind haemoglobin and haem
    • Romero-Espejel, M. E., González-López, M. A., and Olivares-Trejo, J. J. (2013). Streptococcus pneumoniae requires iron for its viability and expresses two membrane proteins that bind haemoglobin and haem. Metallomics 5, 384-389. doi: 10.1039/c3mt20244e
    • (2013) Metallomics , vol.5 , pp. 384-389
    • Romero-Espejel, M.E.1    González-López, M.A.2    Olivares-Trejo, J.J.3
  • 27
    • 0027468111 scopus 로고
    • Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of a binding protein dependent transport system
    • Schneider, R., and Hantke, K. (1993). Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of a binding protein dependent transport system. Mol. Microbiol. 8, 111-121. doi: 10.1111/j.1365-2958.1993.tb01208.x
    • (1993) Mol. Microbiol , vol.8 , pp. 111-121
    • Schneider, R.1    Hantke, K.2
  • 28
    • 0033819377 scopus 로고    scopus 로고
    • Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis
    • Simpson, W., Olczak, T., and Genco, C. A. (2000). Characterization and expression of HmuR, a TonB-dependent hemoglobin receptor of Porphyromonas gingivalis. J. Bacteriol. 182, 5737-5748. doi: 10.1128/JB.182.20.5737-5748.2000
    • (2000) J. Bacteriol , vol.182 , pp. 5737-5748
    • Simpson, W.1    Olczak, T.2    Genco, C.A.3
  • 29
    • 0345791519 scopus 로고    scopus 로고
    • IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus
    • Skaar, E. P., Gaspar, A. H., and Schneewind, O. (2004). IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus. J. Biol. Chem. 279, 436-443. doi: 10.1074/jbc.m307952200
    • (2004) J. Biol. Chem , vol.279 , pp. 436-443
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 30
    • 1642283048 scopus 로고    scopus 로고
    • Iron-regulated surface determinants (Isd) of Staphylococcus aureus: stealing iron from heme
    • Skaar, E. P., and Schneewind, O. (2004). Iron-regulated surface determinants (Isd) of Staphylococcus aureus: stealing iron from heme. Microbes Infect. 6, 390-397. doi: 10.1016/j.micinf.2003.12.008
    • (2004) Microbes Infect , vol.6 , pp. 390-397
    • Skaar, E.P.1    Schneewind, O.2
  • 31
    • 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., Larson, J., Hwa, V., Anic, S., and So, M. (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
  • 32
    • 0027363322 scopus 로고
    • Hemin utilization is related to virulence of Streptococcus pneumoniae
    • Tai, S. S., Lee, C. J., and Winter, R. E. (1993). Hemin utilization is related to virulence of Streptococcus pneumoniae. Infect. Immun. 61, 5401-5405.
    • (1993) Infect. Immun , vol.61 , pp. 5401-5405
    • Tai, S.S.1    Lee, C.J.2    Winter, R.E.3
  • 33
    • 77951205837 scopus 로고    scopus 로고
    • Pneumococcal pathogenesis: "innate invasion" yet organ-specific damage
    • Thornton, J., Durick-Eder, K., and Tuomanen, E. (2010). Pneumococcal pathogenesis: "innate invasion" yet organ-specific damage. J. Mol. Med. 88, 103-107. doi: 10.1007/s00109-009-0578-5
    • (2010) J. Mol. Med , vol.88 , pp. 103-107
    • Thornton, J.1    Durick-Eder, K.2    Tuomanen, E.3
  • 34
    • 0037187447 scopus 로고    scopus 로고
    • Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli
    • Vallejo, L., Brokelman, M., Marten, S., Trappe, S., Cabrera, J., Hoffmann, A., et al. (2002). Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli. J. Bacteriol. 94, 185-194. doi: 10.1016/s0168-1656(01)00425-4
    • (2002) J. Bacteriol , vol.94 , pp. 185-194
    • Vallejo, L.1    Brokelman, M.2    Marten, S.3    Trappe, S.4    Cabrera, J.5    Hoffmann, A.6
  • 35
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to haemophores
    • Wandersman, C., and Delepelaire, P. (2004). Bacterial iron sources: from siderophores to haemophores. Annu. Rev. Microbiol. 58, 611-647. doi: 10.1146/annurev.micro.58.030603.123811
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 36
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: the role of heme, hemoprotein receptors and haemophores
    • Wandersman, C., and Stojiljkovic, I. (2000). Bacterial heme sources: the role of heme, hemoprotein receptors and haemophores. Curr. Opin. Microbiol. 3, 215-220. doi: 10.1016/S1369-5274(00)00078-3
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 215-220
    • Wandersman, C.1    Stojiljkovic, I.2
  • 37
    • 0027435537 scopus 로고
    • Iron uptake mechanisms of pathogenic bacteria
    • Wooldridge, K. G., and Williams, P. H. (1993). Iron uptake mechanisms of pathogenic bacteria. FEMS Microbiol. Rev. 12, 325-348 doi: 10.1111/j.1574-6976.1993.tb00026.x
    • (1993) FEMS Microbiol. Rev , vol.12 , pp. 325-348
    • Wooldridge, K.G.1    Williams, P.H.2
  • 38
    • 13244296905 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases
    • Wu, R., Skaar, E. P., Zhang, R., Joachimiak, G., Gornicki, P., Schneewind, O., et al. (2005). Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases. J. Biol. Chem. 280, 2840-2846. doi: 10.1074/jbc.M409526200
    • (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
  • 39
    • 33748286755 scopus 로고    scopus 로고
    • Epidemiological and molecular characteristics of a highly lethal pneumococcal meningitis epidemic in Burkina Faso
    • Yaro, S., Lourd, M., Traoré, Y., Njanpop-Lafourcade, B. M., Sawadogo, A., Sangare, L., et al. (2006). Epidemiological and molecular characteristics of a highly lethal pneumococcal meningitis epidemic in Burkina Faso. Clin. Infect. Dis. 43, 693-700. doi: 10.1086/506940
    • (2006) Clin. Infect. Dis , vol.43 , pp. 693-700
    • Yaro, S.1    Lourd, M.2    Traoré, Y.3    Njanpop-Lafourcade, B.M.4    Sawadogo, A.5    Sangare, L.6
  • 40
    • 40549124374 scopus 로고    scopus 로고
    • The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp
    • Zhu, H., Liu, M., and Lei, B. (2008). The surface protein Shr of Streptococcus pyogenes binds heme and transfers it to the streptococcal heme-binding protein Shp. BMC Microbiol. 8:15. doi: 10.1186/1471-2180-8-15
    • (2008) BMC Microbiol , vol.8 , pp. 15
    • Zhu, H.1    Liu, M.2    Lei, B.3


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