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Volumn 110, Issue 10, 2013, Pages 3841-3846

Molecular basis for manganese sequestration by calprotectin and roles in the innate immune response to invading bacterial pathogens

Author keywords

Antibiotic resistance; Bacterial pathogenesis; Isothermal titration calorimetry; Protein crystal structure; Staphylococcus aureus

Indexed keywords

CALGRANULIN; HETERODIMER; HISTIDINE; MANGANESE; PROTEIN S 100;

EID: 84874640244     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1220341110     Document Type: Article
Times cited : (313)

References (55)
  • 1
    • 35349019173 scopus 로고    scopus 로고
    • Active bacterial core surveillance (ABCs) MRSA investigators (2007) Invasive methicillin-resistant staphylococcus aureus infections in the United States
    • Klevens RM, et al.; Active Bacterial Core surveillance (ABCs) MRSA Investigators (2007) Invasive methicillin-resistant Staphylococcus aureus infections in the United States. JAMA 298(15):1763-1771.
    • JAMA , vol.298 , Issue.15 , pp. 1763-1771
    • Klevens, R.M.1
  • 3
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Waldron KJ, Robinson NJ (2009) How do bacterial cells ensure that metalloproteins get the correct metal? Nat Rev Microbiol 7(1):25-35.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.1 , pp. 25-35
    • Waldron, K.J.1    Robinson, N.J.2
  • 5
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg ED (2009) Iron availability and infection. Biochim Biophys Acta 1790(7): 600-605.
    • (2009) Biochim Biophys Acta , vol.1790 , Issue.7 , pp. 600-605
    • Weinberg, E.D.1
  • 6
    • 0016227934 scopus 로고
    • Iron and susceptibility to infectious disease
    • Weinberg ED (1974) Iron and susceptibility to infectious disease. Science 184(4140): 952-956.
    • (1974) Science , vol.184 , Issue.4140 , pp. 952-956
    • Weinberg, E.D.1
  • 7
    • 0019640696 scopus 로고
    • The significance of iron in infection
    • Bullen JJ (1981) The significance of iron in infection. Rev Infect Dis 3(6):1127-1138.
    • (1981) Rev Infect Dis , vol.3 , Issue.6 , pp. 1127-1138
    • Bullen, J.J.1
  • 8
    • 84863899006 scopus 로고    scopus 로고
    • Nutritional immunity: Transition metals at the pathogenhost interface
    • Hood MI, Skaar EP (2012) Nutritional immunity: Transition metals at the pathogenhost interface. Nat Rev Microbiol 10(8):525-537.
    • (2012) Nat Rev Microbiol , vol.10 , Issue.8 , pp. 525-537
    • Hood, M.I.1    Skaar, E.P.2
  • 9
    • 77949885386 scopus 로고    scopus 로고
    • Nutritional immunity beyond iron: A role for manganese and zinc
    • Kehl-Fie TE, Skaar EP (2010) Nutritional immunity beyond iron: A role for manganese and zinc. Curr Opin Chem Biol 14(2):218-224.
    • (2010) Curr Opin Chem Biol , vol.14 , Issue.2 , pp. 218-224
    • Kehl-Fie, T.E.1    Skaar, E.P.2
  • 10
    • 79955596509 scopus 로고    scopus 로고
    • Restoration of anti- Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease after gene therapy is calprotectin-dependent
    • Bianchi M, Niemiec MJ, Siler U, Urban CF, Reichenbach J (2011) Restoration of anti- Aspergillus defense by neutrophil extracellular traps in human chronic granulomatous disease after gene therapy is calprotectin- dependent. J Allergy Clin Immunol 127(5):1243-1252.
    • (2011) J Allergy Clin Immunol , vol.127 , Issue.5 , pp. 1243-1252
    • Bianchi, M.1    Niemiec, M.J.2    Siler, U.3    Urban, C.F.4    Reichenbach, J.5
  • 11
    • 39349117867 scopus 로고    scopus 로고
    • Metal chelation and inhibition of bacterial growth in tissue abscesses
    • Corbin BD, et al. (2008) Metal chelation and inhibition of bacterial growth in tissue abscesses. Science 319(5865):962-965.
    • (2008) Science , vol.319 , Issue.5865 , pp. 962-965
    • Corbin, B.D.1
  • 12
    • 73649099522 scopus 로고    scopus 로고
    • Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans
    • Urban CF, et al. (2009) Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog 5(10):e1000639.
    • (2009) PLoS Pathog , vol.5 , Issue.10
    • Urban, C.F.1
  • 13
    • 80051898476 scopus 로고    scopus 로고
    • Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus
    • Kehl-Fie TE, et al. (2011) Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus. Cell Host Microbe 10(2):158-164.
    • (2011) Cell Host Microbe , vol.10 , Issue.2 , pp. 158-164
    • Kehl-Fie, T.E.1
  • 14
    • 33750505883 scopus 로고    scopus 로고
    • S100A8 and S100A9 in inflammation and cancer
    • Gebhardt C, Németh J, Angel P, Hess J (2006) S100A8 and S100A9 in inflammation and cancer. Biochem Pharmacol 72(11):1622-1631.
    • (2006) Biochem Pharmacol , vol.72 , Issue.11 , pp. 1622-1631
    • Gebhardt, C.1    Németh, J.2    Angel, P.3    Hess, J.4
  • 16
    • 67651160306 scopus 로고    scopus 로고
    • The crystal structures of human S100A12 in apo form and in complex with zinc: New insights into S100A12 oligomerisation
    • Moroz OV, Blagova EV, Wilkinson AJ, Wilson KS, Bronstein IB (2009) The crystal structures of human S100A12 in apo form and in complex with zinc: New insights into S100A12 oligomerisation. J Mol Biol 391(3):536-551.
    • (2009) J Mol Biol , vol.391 , Issue.3 , pp. 536-551
    • Moroz, O.V.1    Blagova, E.V.2    Wilkinson, A.J.3    Wilson, K.S.4    Bronstein, I.B.5
  • 17
    • 79955645914 scopus 로고    scopus 로고
    • The crystal structures of human S100B in the zinc- and calcium-loaded state at three pH values reveal zinc ligand swapping
    • Ostendorp T, Diez J, Heizmann CW, Fritz G (2011) The crystal structures of human S100B in the zinc- and calcium-loaded state at three pH values reveal zinc ligand swapping. Biochim Biophys Acta 1813(5):1083-1091.
    • (2011) Biochim Biophys Acta , vol.1813 , Issue.5 , pp. 1083-1091
    • Ostendorp, T.1    Diez, J.2    Heizmann, C.W.3    Fritz, G.4
  • 18
    • 0033796465 scopus 로고    scopus 로고
    • Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14)
    • Sohnle PG, Hunter MJ, Hahn B, Chazin WJ (2000) Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14). J Infect Dis 182(4):1272-1275.
    • (2000) J Infect Dis , vol.182 , Issue.4 , pp. 1272-1275
    • Sohnle, P.G.1    Hunter, M.J.2    Hahn, B.3    Chazin, W.J.4
  • 19
    • 34250164654 scopus 로고    scopus 로고
    • The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EFhand proteins
    • Korndörfer IP, Brueckner F, Skerra A (2007) The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EFhand proteins. J Mol Biol 370(5):887-898.
    • (2007) J Mol Biol , vol.370 , Issue.5 , pp. 887-898
    • Korndörfer, I.P.1    Brueckner, F.2    Skerra, A.3
  • 20
    • 35449004112 scopus 로고    scopus 로고
    • Human calprotectin: Effect of calcium and zinc on its secondary and tertiary structures, and role of pH in its thermal stability
    • Yousefi R, et al. (2007) Human calprotectin: Effect of calcium and zinc on its secondary and tertiary structures, and role of pH in its thermal stability. Acta Biochim Biophys Sin (Shanghai) 39(10):795-802.
    • (2007) Acta Biochim Biophys Sin (Shanghai) , vol.39 , Issue.10 , pp. 795-802
    • Yousefi, R.1
  • 22
    • 33749575659 scopus 로고    scopus 로고
    • Manganese transport and the role of manganese in virulence
    • Papp-Wallace KM, Maguire ME (2006) Manganese transport and the role of manganese in virulence. Annu Rev Microbiol 60:187-209.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 187-209
    • Papp-Wallace, K.M.1    Maguire, M.E.2
  • 23
    • 0033056490 scopus 로고    scopus 로고
    • Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity
    • Clements MO, Watson SP, Foster SJ (1999) Characterization of the major superoxide dismutase of Staphylococcus aureus and its role in starvation survival, stress resistance, and pathogenicity. J Bacteriol 181(13):3898-3903.
    • (1999) J Bacteriol , vol.181 , Issue.13 , pp. 3898-3903
    • Clements, M.O.1    Watson, S.P.2    Foster, S.J.3
  • 24
    • 0035036429 scopus 로고    scopus 로고
    • Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus
    • Valderas MW, Hart ME (2001) Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus. J Bacteriol 183(11): 3399-3407.
    • (2001) J Bacteriol , vol.183 , Issue.11 , pp. 3399-3407
    • Valderas, M.W.1    Hart, M.E.2
  • 25
    • 0142074789 scopus 로고    scopus 로고
    • Role and regulation of the superoxide dismutases of Staphylococcus aureus
    • Karavolos MH, Horsburgh MJ, Ingham E, Foster SJ (2003) Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 149(Pt 10):2749-2758.
    • (2003) Microbiology , vol.149 , Issue.PART 10 , pp. 2749-2758
    • Karavolos, M.H.1    Horsburgh, M.J.2    Ingham, E.3    Foster, S.J.4
  • 26
    • 79951789722 scopus 로고    scopus 로고
    • The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide
    • Gu M, Imlay JA (2011) The SoxRS response of Escherichia coli is directly activated by redox-cycling drugs rather than by superoxide. Mol Microbiol 79(5):1136-1150.
    • (2011) Mol Microbiol , vol.79 , Issue.5 , pp. 1136-1150
    • Gu, M.1    Imlay, J.A.2
  • 27
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical
    • Hassan HM, Fridovich I (1979) Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J Biol Chem 254(21):10846-10852.
    • (1979) J Biol Chem , vol.254 , Issue.21 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 28
    • 0032524649 scopus 로고    scopus 로고
    • High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14
    • Hunter MJ, Chazin WJ (1998) High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J Biol Chem 273(20):12427-12435.
    • (1998) J Biol Chem , vol.273 , Issue.20 , pp. 12427-12435
    • Hunter, M.J.1    Chazin, W.J.2
  • 29
    • 0242691764 scopus 로고    scopus 로고
    • High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins
    • Mäler L, Potts BCM, Chazin WJ (1999) High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins. J Biomol NMR 13(3):233-247.
    • (1999) J Biomol NMR , vol.13 , Issue.3 , pp. 233-247
    • Mäler, L.1    Potts, B.C.M.2    Chazin, W.J.3
  • 30
    • 0036290247 scopus 로고    scopus 로고
    • 2+)- dependent regulator protein in inflammatory process
    • 2+)-dependent regulator protein in inflammatory process. J Mol Biol 316(2):265-276.
    • (2002) J Mol Biol , vol.316 , Issue.2 , pp. 265-276
    • Itou, H.1
  • 31
    • 77956309711 scopus 로고    scopus 로고
    • Metal-binding sites are designed to achieve optimal mechanical and signaling properties
    • Dutta A, Bahar I (2010) Metal-binding sites are designed to achieve optimal mechanical and signaling properties. Structure 18(9):1140-1148.
    • (2010) Structure , vol.18 , Issue.9 , pp. 1140-1148
    • Dutta, A.1    Bahar, I.2
  • 32
    • 75649096389 scopus 로고    scopus 로고
    • MIPS: Metal interactions in protein structures
    • Hemavathi K, et al. (2010) MIPS: Metal interactions in protein structures. J Appl Cryst 43:196-199.
    • (2010) J Appl Cryst , vol.43 , pp. 196-199
    • Hemavathi, K.1
  • 33
    • 84863338466 scopus 로고    scopus 로고
    • Zinc sequestration by the neutrophil protein calprotectin enhances Salmonella growth in the inflamed gut
    • Liu JZ, et al. (2012) Zinc sequestration by the neutrophil protein calprotectin enhances Salmonella growth in the inflamed gut. Cell Host Microbe 11(3):227-239.
    • (2012) Cell Host Microbe , vol.11 , Issue.3 , pp. 227-239
    • Liu, J.Z.1
  • 34
    • 84872024018 scopus 로고    scopus 로고
    • Identification of an acinetobacter baumannii zinc acquisition system that facilitates resistance to calprotectin-mediated zinc sequestration
    • Hood MI, et al. (2012) Identification of an Acinetobacter baumannii zinc acquisition system that facilitates resistance to calprotectin-mediated zinc sequestration. PLoS Pathog 8(12):e1003068.
    • (2012) PLoS Pathog , vol.8 , Issue.12
    • Hood, M.I.1
  • 35
    • 0030898101 scopus 로고    scopus 로고
    • Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulindependent pathway
    • Rammes A, et al. (1997) Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulindependent pathway. J Biol Chem 272(14):9496-9502.
    • (1997) J Biol Chem , vol.272 , Issue.14 , pp. 9496-9502
    • Rammes, A.1
  • 36
    • 77953778296 scopus 로고    scopus 로고
    • History of biological metal utilization inferred through phylogenomic analysis of protein structures
    • Dupont CL, Butcher A, Valas RE, Bourne PE, Caetano-Anollés G (2010) History of biological metal utilization inferred through phylogenomic analysis of protein structures. Proc Natl Acad Sci USA 107(23):10567-10572.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.23 , pp. 10567-10572
    • Dupont, C.L.1    Butcher, A.2    Valas, R.E.3    Bourne, P.E.4    Caetano-Anollés, G.5
  • 37
    • 33845230241 scopus 로고    scopus 로고
    • Modern proteomes contain putative imprints of ancient shifts in trace metal geochemistry
    • Dupont CL, Yang S, Palenik B, Bourne PE (2006) Modern proteomes contain putative imprints of ancient shifts in trace metal geochemistry. Proc Natl Acad Sci USA 103(47): 17822-17827.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.47 , pp. 17822-17827
    • Dupont, C.L.1    Yang, S.2    Palenik, B.3    Bourne, P.E.4
  • 38
    • 34948900275 scopus 로고    scopus 로고
    • Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock
    • Vogl T, et al. (2007) Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock. Nat Med 13(9):1042-1049.
    • (2007) Nat Med , vol.13 , Issue.9 , pp. 1042-1049
    • Vogl, T.1
  • 39
    • 77953233075 scopus 로고    scopus 로고
    • The Toll-like receptor 4 ligands Mrp8 and Mrp14 are crucial in the development of autoreactive CD8+ T cells
    • Loser K, et al. (2010) The Toll-like receptor 4 ligands Mrp8 and Mrp14 are crucial in the development of autoreactive CD8+ T cells. Nat Med 16(6):713-717.
    • (2010) Nat Med , vol.16 , Issue.6 , pp. 713-717
    • Loser, K.1
  • 40
    • 77957920876 scopus 로고    scopus 로고
    • Metals in protein structures: A review of their principal features
    • Harding MM, Nowicki MW, Walkinshaw MD (2010) Metals in protein structures: A review of their principal features. Crystallogr Rev 16(4):247-302.
    • (2010) Crystallogr Rev , vol.16 , Issue.4 , pp. 247-302
    • Harding, M.M.1    Nowicki, M.W.2    Walkinshaw, M.D.3
  • 41
    • 0031920306 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-angstrom resolution
    • Edwards RA, et al. (1998) Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-angstrom resolution. J Biol Inorg Chem 3(2):161-171.
    • (1998) J Biol Inorg Chem , vol.3 , Issue.2 , pp. 161-171
    • Edwards, R.A.1
  • 42
    • 54549088946 scopus 로고    scopus 로고
    • Protein-folding location can regulate manganese-binding versus copper- or zinc-binding
    • Tottey S, et al. (2008) Protein-folding location can regulate manganese-binding versus copper- or zinc-binding. Nature 455(7216):1138-1142.
    • (2008) Nature , vol.455 , Issue.7216 , pp. 1138-1142
    • Tottey, S.1
  • 43
    • 35348903797 scopus 로고    scopus 로고
    • S100A15, an antimicrobial protein of the skin: Regulation by E. Coli through Toll-like receptor 4
    • Büchau AS, et al. (2007) S100A15, an antimicrobial protein of the skin: Regulation by E. coli through Toll-like receptor 4. J Invest Dermatol 127(11):2596-2604.
    • (2007) J Invest Dermatol , vol.127 , Issue.11 , pp. 2596-2604
    • Büchau, A.S.1
  • 44
    • 12344302254 scopus 로고    scopus 로고
    • Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection
    • Gläser R, et al. (2005) Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection. Nat Immunol 6(1):57-64.
    • (2005) Nat Immunol , vol.6 , Issue.1 , pp. 57-64
    • Gläser, R.1
  • 45
    • 0032743405 scopus 로고    scopus 로고
    • Calgranulin C has filariacidal and filariastatic activity
    • Gottsch JD, Eisinger SW, Liu SH, Scott AL (1999) Calgranulin C has filariacidal and filariastatic activity. Infect Immun 67(12):6631-6636.
    • (1999) Infect Immun , vol.67 , Issue.12 , pp. 6631-6636
    • Gottsch, J.D.1    Eisinger, S.W.2    Liu, S.H.3    Scott, A.L.4
  • 46
    • 49349090104 scopus 로고    scopus 로고
    • Divalent metal ion complexes of S100B in the absence and presence of pentamidine
    • Charpentier TH, et al. (2008) Divalent metal ion complexes of S100B in the absence and presence of pentamidine. J Mol Biol 382(1):56-73.
    • (2008) J Mol Biol , vol.382 , Issue.1 , pp. 56-73
    • Charpentier, T.H.1
  • 47
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and clustal X version 2.0
    • Larkin MA, et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23(21): 2947-2948.
    • (2007) Bioinformatics , vol.23 , Issue.21 , pp. 2947-2948
    • Larkin, M.A.1
  • 49
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , Issue.PART 4 , pp. 658-674
    • Mccoy, A.J.1
  • 51
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 52
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53(Pt 3): 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 53
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 1 , pp. 12-21
    • Chen, V.B.1
  • 54
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Web Server issue
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35(Web Server issue):W375-W383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1
  • 55
    • 84872564946 scopus 로고    scopus 로고
    • High-affinity manganese coordination by human calprotectin is calcium-dependent and requires the histidine-rich site formed at the dimer interface
    • Hayden JA, et al. (2013) High-affinity manganese coordination by human calprotectin is calcium-dependent and requires the histidine-rich site formed at the dimer interface. J Am Chem Soc 135(2):775-787.
    • (2013) J Am Chem Soc , vol.135 , Issue.2 , pp. 775-787
    • Hayden, J.A.1


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