메뉴 건너뛰기




Volumn 23, Issue 4, 2010, Pages 601-611

Siderophore uptake in bacteria and the battle for iron with the host; a bird's eye view

Author keywords

Hepcidin; Host defense; Iron transport; Siderocalin; Siderophore; TonB

Indexed keywords

BINDING PROTEIN; CARRIER PROTEIN; DEFERASIROX; DEFERIPRONE; DEFEROXAMINE; DEFEROXAMINE MESYLATE; ENTEROCHELIN; FERRICHROME; GRISEIN; IRON; IRON BINDING PROTEIN; LACTOFERRIN; LIPOCALIN; OUTER MEMBRANE PROTEIN; OXYGEN; SIDEROPHORE; STAPHYLOFERRIN A; UNCLASSIFIED DRUG;

EID: 78651370006     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-010-9361-x     Document Type: Review
Times cited : (273)

References (57)
  • 2
    • 0036188896 scopus 로고    scopus 로고
    • Lactoferrin and transferrin: Functional variations on a common structural framework
    • Baker EN, Baker HM, Kidd RD 2002 Lactoferrin and transferrin: functional variations on a common structural framework. Biochem Cell Biol 80:27-34
    • (2002) Biochem. Cell. Biol. , vol.80 , pp. 27-34
    • Baker, E.N.1    Baker, H.M.2    Kidd, R.D.3
  • 4
    • 34648827867 scopus 로고    scopus 로고
    • Coordination chemistry and biology of chelators for the treatment of iron overload disorders
    • Bernhardt PV 2007 Coordination chemistry and biology of chelators for the treatment of iron overload disorders. Dalton Trans 30:3214-3220
    • (2007) Dalton Trans. , vol.30 , pp. 3214-3220
    • Bernhardt, P.V.1
  • 6
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the ironsupply problem
    • Braun V, Killmann H 1999 Bacterial solutions to the ironsupply problem. Trends Biochem Sci 24:104-109
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 7
    • 40149101277 scopus 로고    scopus 로고
    • Iron overload disorders: Treatment options for patients refractory to or intolerant of phlebotomy
    • Bring P, Partovi N, Ford JE, Yoshida EM 2008 Iron overload disorders: treatment options for patients refractory to or intolerant of phlebotomy. Pharmacotherapy 28:331-342
    • (2008) Pharmacotherapy , vol.28 , pp. 331-342
    • Bring, P.1    Partovi, N.2    Ford, J.E.3    Yoshida, E.M.4
  • 9
    • 67650094768 scopus 로고    scopus 로고
    • This is not your mother's repressor: The complex role of fur in pathogenesis
    • Carpenter BM, Whitmire JM, Merrell DS 2009 This is not your mother's repressor: the complex role of fur in pathogenesis. Infect Immun 77:2590-2601
    • (2009) Infect. Immun. , vol.77 , pp. 2590-2601
    • Carpenter, B.M.1    Whitmire, J.M.2    Merrell, D.S.3
  • 11
    • 77955481009 scopus 로고    scopus 로고
    • Current understanding of fatty acid biosynthesis and the acyl carrier protein
    • press
    • Chan DI, Vogel HJ 2010 Current understanding of fatty acid biosynthesis and the acyl carrier protein. Biochem J (in press)
    • (2010) Biochem. J.
    • Chan, D.I.1    Vogel, H.J.2
  • 13
    • 34248636774 scopus 로고    scopus 로고
    • Bioinformatic analysis of the TonB protein family
    • Chu BC, Peacock RS, Vogel HJ 2007 Bioinformatic analysis of the TonB protein family. Biometals 20:467-483
    • (2007) Biometals , vol.20 , pp. 467-483
    • Chu, B.C.1    Peacock, R.S.2    Vogel, H.J.3
  • 14
    • 0034127329 scopus 로고    scopus 로고
    • The structure of the ferric siderophore binding protein FhuD complexed with gallichrome
    • Clarke TE, Ku SY, Dougan DR, Vogel HJ, Tari LW 2000 The structure of the ferric siderophore binding protein FhuD complexed with gallichrome. Nat Struct Biol 7:287-289
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 287-289
    • Clarke, T.E.1    Ku, S.Y.2    Dougan, D.R.3    Vogel, H.J.4    Tari, L.W.5
  • 15
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • Clarke TE, Braun V, Winkelmann G, Tari LW, Vogel HJ 2002 X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin. J Biol Chem 277:13966-13972
    • (2002) J. Biol. Chem. , vol.277 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 17
    • 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
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 18
    • 0027328530 scopus 로고
    • Synthesis, physicochemical properties, and biological evaluation of N-substituted 2-alkyl-3-hydroxy-4 (1H)-pyridinones: Orally active iron chelators with clinical potential
    • Dobbin PS, Hider RC, Hall AD, Taylor PD, Sarpong P, Porter JB, Xiao G, van der Helm D 1993 Synthesis, physicochemical properties, and biological evaluation of N-substituted 2-alkyl-3-hydroxy-4 (1H)-pyridinones: orally active iron chelators with clinical potential. J Med Chem 36:2448-2458
    • (1993) J. Med. Chem. , vol.36 , pp. 2448-2458
    • Dobbin, P.S.1    Hider, R.C.2    Hall, A.D.3    Taylor, P.D.4    Sarpong, P.5    Porter, J.B.6    Xiao, G.7    Van Der Helm, D.8
  • 19
    • 0036500658 scopus 로고    scopus 로고
    • Structural basis of gating by the outer membrane transporter FecA
    • DOI 10.1126/science.1067313
    • Ferguson AD, Chakraborty R, Smith BS, Esser L, van der Helm D, Deisenhofer J 2002 Structural basis of gating by the outer membrane transporter FecA. Science 295:1715-1719 (Pubitemid 34202907)
    • (2002) Science , vol.295 , Issue.5560 , pp. 1715-1719
    • Ferguson, A.D.1    Chakraborty, R.2    Smith, B.S.3    Esser, L.4    Van Der Helm, D.5    Deisenhofer, J.6
  • 20
    • 33646593180 scopus 로고    scopus 로고
    • How pathogenic bacteria evade mammalian sabotage in the battle for iron
    • Fischbach MA, Lin H, Liu DR, Walsh CT 2006 How pathogenic bacteria evade mammalian sabotage in the battle for iron. Nat Chem Biol 2:132-138
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 132-138
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 21
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Fleming A 1922 On a remarkable bacteriolytic element found in tissues and secretions. Proc R Soc Lond B 93:306-317
    • (1922) Proc. R Soc. Lond. B. , vol.93 , pp. 306-317
    • Fleming, A.1
  • 24
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • Ganz T 2003 Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 102:783-788
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 25
    • 33748102856 scopus 로고    scopus 로고
    • Hepcidin-a peptide hormone at the interface of innate immunity and iron metabolism
    • Ganz T 2006 Hepcidin-a peptide hormone at the interface of innate immunity and iron metabolism. Curr Top Microbiol Immunol 306:183-198
    • (2006) Curr. Top Microbiol. Immunol. , vol.306 , pp. 183-198
    • Ganz, T.1
  • 26
    • 35748976227 scopus 로고    scopus 로고
    • The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins
    • Garcia-Herrero A, Peacock RS, Howard SP, Vogel HJ 2007 The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins. Mol Microbiol 66:872-889
    • (2007) Mol. Microbiol. , vol.66 , pp. 872-889
    • Garcia-Herrero, A.1    Peacock, R.S.2    Howard, S.P.3    Vogel, H.J.4
  • 27
    • 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
    • (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
  • 28
    • 77951234543 scopus 로고    scopus 로고
    • The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket
    • Grigg JC, Cooper JD, Cheung J, Heinrichs DE, Murphy ME 2010 The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket. J Biol Chem 285:11162-11171
    • (2010) J. Biol. Chem. , vol.285 , pp. 11162-11171
    • Grigg, J.C.1    Cooper, J.D.2    Cheung, J.3    Heinrichs, D.E.4    Murphy, M.E.5
  • 29
    • 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 USA 100:3677-3682
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3677-3682
    • Hantke, K.1    Nicholson, G.2    Rabsch, W.3    Winkelmann, G.4
  • 30
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P 1996 The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275:161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 31
    • 77951981537 scopus 로고    scopus 로고
    • Chemistry and biology of siderophores
    • Hider RC, Kong X 2010 Chemistry and biology of siderophores. Nat Prod Rep 27:637-657
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 637-657
    • Hider, R.C.1    Kong, X.2
  • 32
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • Hunter HN, Fulton DB, Ganz T, Vogel HJ 2002 The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J Biol Chem 277:37597-37603
    • (2002) J. Biol. Chem. , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 34
    • 50049089034 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake
    • Krewulak KD, Vogel HJ 2008 Structural biology of bacterial iron uptake. Biochim Biophys Acta 1778:1781-1804
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1781-1804
    • Krewulak, K.D.1    Vogel, H.J.2
  • 35
    • 24744433447 scopus 로고    scopus 로고
    • Periplasmic binding proteins involved in bacterial iron uptake
    • ASM Press, Washington, DC
    • Krewulak KD, Peacock RS, Vogel HJ (2004) Periplasmic binding proteins involved in bacterial iron uptake. In: Iron transport in bacteria. ASM Press, Washington, DC
    • (2004) Iron Transport in Bacteria
    • Krewulak, K.D.1    Peacock, R.S.2    Vogel, H.J.3
  • 38
    • 77949263042 scopus 로고    scopus 로고
    • A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation
    • Lewinson O, Lee AT, Locher KP, Rees DC 2010 A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation. Nat Struct Mol Biol 17:332-338
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 332-338
    • Lewinson, O.1    Lee, A.T.2    Locher, K.P.3    Rees, D.C.4
  • 39
    • 59849094863 scopus 로고    scopus 로고
    • Molecular characterization of the TonB2 protein from the fish pathogen Vibrio anguillarum
    • Lopez CS, Peacock RS, Crosa JH, Vogel HJ 2009 Molecular characterization of the TonB2 protein from the fish pathogen Vibrio anguillarum. Biochem J 418:49-59
    • (2009) Biochem. J. , vol.418 , pp. 49-59
    • Lopez, C.S.1    Peacock, R.S.2    Crosa, J.H.3    Vogel, H.J.4
  • 42
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands JB 1995 Siderophores: structure and function of microbial iron transport compounds. J Biol Chem 270:26723-26726
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 44
    • 30144432585 scopus 로고    scopus 로고
    • The N-terminus of hepcidin is essential for its interaction with ferroportin: Structure-function study
    • Nemeth E, Preza GC, Jung CL, Kaplan J, Waring AJ, Ganz T 2005 The N-terminus of hepcidin is essential for its interaction with ferroportin: structure-function study. Blood 107:328-333
    • (2005) Blood , vol.107 , pp. 328-333
    • Nemeth, E.1    Preza, G.C.2    Jung, C.L.3    Kaplan, J.4    Waring, A.J.5    Ganz, T.6
  • 45
    • 33646391919 scopus 로고    scopus 로고
    • Oral chelators deferasirox and deferiprone for transfusional iron overload in thalassemia major: New data, new questions
    • Neufeld EJ 2006 Oral chelators deferasirox and deferiprone for transfusional iron overload in thalassemia major: new data, new questions. Blood 107:3436-3441
    • (2006) Blood , vol.107 , pp. 3436-3441
    • Neufeld, E.J.1
  • 46
    • 77956505672 scopus 로고    scopus 로고
    • TonB-dependent transporters: Regulation, structure, and function
    • in press, doi:10.1146/annurev. micro.112408.134247
    • Noinaj N, Guillier M, Barnard TJ, Buchanan SK 2010 TonB-dependent transporters: regulation, structure, and function. Annu Rev Microbiol 64 (in press). doi:10.1146/annurev. micro.112408.134247
    • (2010) Annu. Rev. Microbiol. , vol.64
    • Noinaj, N.1    Guillier, M.2    Barnard, T.J.3    Buchanan, S.K.4
  • 48
    • 11844269327 scopus 로고    scopus 로고
    • The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides
    • Peacock RS, Weljie AM, Howard PS, Price FD, Vogel HJ 2005 The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. J Mol Biol 345:1185-1197
    • (2005) J. Mol. Biol. , vol.345 , pp. 1185-1197
    • Peacock, R.S.1    Weljie, A.M.2    Howard, P.S.3    Price, F.D.4    Vogel, H.J.5
  • 49
    • 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
    • (2007) Biometals , vol.20 , pp. 453-465
    • Postle, K.1    Larsen, R.A.2
  • 52
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • Singh PK, Parsak MR, Greenberg EP, Welsh MJ 2002 A component of innate immunity prevents bacterial biofilm development. Nature 417:552-555
    • (2002) Nature , vol.417 , pp. 552-555
    • Singh, P.K.1    Parsak, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 54
    • 28344457682 scopus 로고    scopus 로고
    • Lactoferrin: An important host defence against microbial and viral attack
    • Valenti P, Antonini G 2005 Lactoferrin: an important host defence against microbial and viral attack. Cell Mol Life Sci 62:2576-2587
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2576-2587
    • Valenti, P.1    Antonini, G.2
  • 56
    • 0021356806 scopus 로고
    • Iron withholding: A defense against infection and neoplasia
    • Weinberg ED 1984 Iron withholding: a defense against infection and neoplasia. Physiol Rev 64:65-102
    • (1984) Physiol. Rev. , vol.64 , pp. 65-102
    • Weinberg, E.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.