메뉴 건너뛰기




Volumn 34, Issue 2, 1999, Pages 238-246

The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FERRITIN; INTERLEUKIN 8; IRON BINDING PROTEIN; OLIGOMER;

EID: 0001413894     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01584.x     Document Type: Article
Times cited : (153)

References (53)
  • 1
    • 0033552961 scopus 로고    scopus 로고
    • Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori
    • Alm, R.A., Ling, L.S., Moir, D.T., King, B.L., Brown, E.D., Doig, P.C., et al. (1999) Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori. Nature 397: 176-180.
    • (1999) Nature , vol.397 , pp. 176-180
    • Alm, R.A.1    Ling, L.S.2    Moir, D.T.3    King, B.L.4    Brown, E.D.5    Doig, P.C.6
  • 2
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron, M., Link, A.J., Furlong, D., and Kolter, R. (1992) A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6: 2646-2654.
    • (1992) Genes Dev , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 6
    • 0031685512 scopus 로고    scopus 로고
    • Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori
    • Bereswill, S., Waidner, U., Odenbreit, S., Lichte, F., Fassbinder, F., Bode, G., and Kist, M. (1998) Structural, functional and mutational analysis of the pfr gene encoding a ferritin from Helicobacter pylori. Microbiology 144: 2505-2516.
    • (1998) Microbiology , vol.144 , pp. 2505-2516
    • Bereswill, S.1    Waidner, U.2    Odenbreit, S.3    Lichte, F.4    Fassbinder, F.5    Bode, G.6    Kist, M.7
  • 7
    • 0027441698 scopus 로고
    • Helicobacter pylori: Microbiology of a 'slow' bacterial infection
    • Blaser, M.J. (1993) Helicobacter pylori: microbiology of a 'slow' bacterial infection. Trends Microbiol 1: 255-259.
    • (1993) Trends Microbiol , vol.1 , pp. 255-259
    • Blaser, M.J.1
  • 8
    • 0031032646 scopus 로고    scopus 로고
    • A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua
    • Bozzi, M., Mignogna, G., Stefanini, S., Barra, D., Longhi, C., Valenti, P., and Chiancone, E. (1997) A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. J Biol Chem 272: 3259-3265.
    • (1997) J Biol Chem , vol.272 , pp. 3259-3265
    • Bozzi, M.1    Mignogna, G.2    Stefanini, S.3    Barra, D.4    Longhi, C.5    Valenti, P.6    Chiancone, E.7
  • 9
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps (PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • Chen, L., and Helmann, J.D. (1995) Bacillus subtilis MrgA is a Dps (PexB) homologue: evidence for metalloregulation of an oxidative-stress gene. Mol Microbiol 18: 295-300.
    • (1995) Mol Microbiol , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 10
    • 0030809535 scopus 로고    scopus 로고
    • Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating toxin, reveals its pattern of assembly
    • Cover, T.L., Hanson, P.I., and Heuse, J.E. (1997) Acid-induced dissociation of VacA, the Helicobacter pylori vacuolating toxin, reveals its pattern of assembly. J Cell Biol 138: 759-769.
    • (1997) J Cell Biol , vol.138 , pp. 759-769
    • Cover, T.L.1    Hanson, P.I.2    Heuse, J.E.3
  • 11
    • 0026680231 scopus 로고
    • Helicobacter pylori secretes a chemotactic factor for monocytes and neutrophils
    • Craig, P.M., Territo, M.C., Karnes, W.E., and Walsh, J.H. (1992) Helicobacter pylori secretes a chemotactic factor for monocytes and neutrophils. Gut 33: 1020-1023.
    • (1992) Gut , vol.33 , pp. 1020-1023
    • Craig, P.M.1    Territo, M.C.2    Karnes, W.E.3    Walsh, J.H.4
  • 13
    • 1842370320 scopus 로고    scopus 로고
    • Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori
    • Dhaenens, L., Szczebara, F., and Husson, O. (1997) Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori. Infect Immun 65: 514-518.
    • (1997) Infect Immun , vol.65 , pp. 514-518
    • Dhaenens, L.1    Szczebara, F.2    Husson, O.3
  • 15
    • 0028843199 scopus 로고
    • Identification of four new prokaryotic bacterio-ferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences
    • Evans, Jr, D.J., Evans, D.G., Lampert, H.C., and Nakano, H. (1995b) Identification of four new prokaryotic bacterio-ferritins, from Helicobacter pylori, Anabaena variabilis, Bacillus subtilis and Treponema pallidum, by analysis of gene sequences. Gene 153: 123-127.
    • (1995) Gene , vol.153 , pp. 123-127
    • Evans D.J. Jr1    Evans, D.G.2    Lampert, H.C.3    Nakano, H.4
  • 16
    • 0026717475 scopus 로고
    • Helicobacter colonization and histopatological profile of chronic gastritis in patients with or without dyspepsia, mucosal erosion and peptic ulcer: A morphological approach to the study of ulcerogenesis in man
    • Fiocca, R., Villani, L, Luinetti, O., Gianotti, A., Perego, M., Alvisi, C., et al. (1992) Helicobacter colonization and histopatological profile of chronic gastritis in patients with or without dyspepsia, mucosal erosion and peptic ulcer: a morphological approach to the study of ulcerogenesis in man. Virchows Arch Pathol Anat Histol 420: 489-492.
    • (1992) Virchows Arch Pathol Anat Histol , vol.420 , pp. 489-492
    • Fiocca, R.1    Villani, L.2    Luinetti, O.3    Gianotti, A.4    Perego, M.5    Alvisi, C.6
  • 17
    • 0028117801 scopus 로고
    • Epithelial cytoxicity, immune response, and inflammatory components of Helicobacter pylori gastritis
    • Fiocca, R., Luinetti, O., Villani, L., Chiaravalli, A.M., Capella, C., and Solcia, E. (1994) Epithelial cytoxicity, immune response, and inflammatory components of Helicobacter pylori gastritis. Scand J Gastroenterol 205: 11-21.
    • (1994) Scand J Gastroenterol , vol.205 , pp. 11-21
    • Fiocca, R.1    Luinetti, O.2    Villani, L.3    Chiaravalli, A.M.4    Capella, C.5    Solcia, E.6
  • 18
    • 0031470826 scopus 로고    scopus 로고
    • Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi
    • Fraser, C.M., Casjens, S., Huang, W.M., Sutton, G.G., Clayton, R., Lathigra, R., et al. (1997) Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390: 580-586.
    • (1997) Nature , vol.390 , pp. 580-586
    • Fraser, C.M.1    Casjens, S.2    Huang, W.M.3    Sutton, G.G.4    Clayton, R.5    Lathigra, R.6
  • 19
    • 0027462566 scopus 로고
    • Paracrystalline inclusions of a novel ferritin containing nonheme iron, produced by the human gastric pathogen Helicobacter pylori: Evidence for a third class of ferritins
    • Frazier, B.A., Pfeifer, J.D., Russell, D.G., Falk, P., Olsen, A.N., Hammar, M., et al. (1993) Paracrystalline inclusions of a novel ferritin containing nonheme iron, produced by the human gastric pathogen Helicobacter pylori: evidence for a third class of ferritins. J Bacteriol 175: 966-972.
    • (1993) J Bacteriol , vol.175 , pp. 966-972
    • Frazier, B.A.1    Pfeifer, J.D.2    Russell, D.G.3    Falk, P.4    Olsen, A.N.5    Hammar, M.6
  • 20
    • 0028467772 scopus 로고
    • Structure of a unique two fold symmetric haem-binding site
    • Frolow, F., Kalb, A.J., and Yariv, J. (1994) Structure of a unique two fold symmetric haem-binding site. Nature Struct Biol 1: 453-460.
    • (1994) Nature Struct Biol , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 21
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple method for predicting the secondary structure of globular proteins
    • Gamier, J., Osguthorphe, D.J., and Robson, B. (1978) Analysis of the accuracy and implications of simple method for predicting the secondary structure of globular proteins. J Mol Biol 120: 97-120.
    • (1978) J Mol Biol , vol.120 , pp. 97-120
    • Gamier, J.1    Osguthorphe, D.J.2    Robson, B.3
  • 22
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acids sequence data
    • Gill, S.C., and von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acids sequence data. Anal Biochem 182: 319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 23
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R.A., Filman, D.J., Finkel, S.E., Kolter, R., and Hogle, J.M. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nature Struct Biol 5: 294-303.
    • (1998) Nature Struct Biol , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 24
    • 0032984042 scopus 로고    scopus 로고
    • Proinflammatory activation of neutrophils and monocytes by Helicobacter pylori in patients with different clinical presentations
    • Hansen, P.S., Go, M.F., Varming, K., Andersen, L.P., Genta, R.M., Graham, D.Y., and Nielsen, H. (1999) Proinflammatory activation of neutrophils and monocytes by Helicobacter pylori in patients with different clinical presentations. Infect Immun 67: 3171-3174.
    • (1999) Infect Immun , vol.67 , pp. 3171-3174
    • Hansen, P.S.1    Go, M.F.2    Varming, K.3    Andersen, L.P.4    Genta, R.M.5    Graham, D.Y.6    Nielsen, H.7
  • 25
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M., and 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
  • 26
    • 0031599683 scopus 로고    scopus 로고
    • Structure-function relationships in the ferritins
    • Astrid, S., and Helmut, S. (eds). New York: Marcel Dekker
    • Harrison, P.M., Hempstead, P.C., Artymiuk, P.J., and Andrews, S.C. (1998) Structure-function relationships in the ferritins. In Metal Ions in Biological Systems, vol. 35. Astrid, S., and Helmut, S. (eds). New York: Marcel Dekker, pp. 435-478.
    • (1998) Metal Ions in Biological Systems , vol.35 , pp. 435-478
    • Harrison, P.M.1    Hempstead, P.C.2    Artymiuk, P.J.3    Andrews, S.C.4
  • 27
    • 0027276444 scopus 로고
    • Iron acquisition by Helicobacter pylori: Importance of human lactoferrin
    • Housson, M.-O., Legrand, D., Spik, G., and LeClerc, H. (1993) Iron acquisition by Helicobacter pylori: importance of human lactoferrin. Infect Immun 61: 2694-2697.
    • (1993) Infect Immun , vol.61 , pp. 2694-2697
    • Housson, M.-O.1    Legrand, D.2    Spik, G.3    LeClerc, H.4
  • 29
    • 0033081590 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the unusual ferritin from Listeria innocua
    • Ilari, A., Savino, C., Stefanini, S., Chiancone, E., and Tsernoglou, D. (1999) Crystallization and preliminary X-ray crystallographic analysis of the unusual ferritin from Listeria innocua. Acta Crystallogr D Biol Crystallogr 55: 552-553.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 552-553
    • Ilari, A.1    Savino, C.2    Stefanini, S.3    Chiancone, E.4    Tsernoglou, D.5
  • 31
    • 0027397858 scopus 로고
    • A neutrophil chemotactic factor present in Helicobacter pylori but absent in Helicobacter mustelae
    • Kozol, R., McCurdy, B., and Czanko, R. (1993) A neutrophil chemotactic factor present in Helicobacter pylori but absent in Helicobacter mustelae. Dig Dis Sci 38: 137-141.
    • (1993) Dig Dis Sci , vol.38 , pp. 137-141
    • Kozol, R.1    McCurdy, B.2    Czanko, R.3
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0026570302 scopus 로고
    • Surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism
    • Mai, U.E., Perez-Perez, G.I., Allen, J.B., Wahl, S.M., Blaser, M.J., and Smith, P.D. (1992) Surface proteins from Helicobacter pylori activate monocytes/macrophages by lipopolysaccharide-independent mechanism. J Exp Med 175: 517-525.
    • (1992) J Exp Med , vol.175 , pp. 517-525
    • Mai, U.E.1    Perez-Perez, G.I.2    Allen, J.B.3    Wahl, S.M.4    Blaser, M.J.5    Smith, P.D.6
  • 34
    • 0028902758 scopus 로고
    • Development of a mouse model of Helicobacter pylori infection that mimics human disease
    • Marchetti, M., Arico, B., Burroni, D., Figura, N., Rappuoli, R., and Ghiara, P. (1995) Development of a mouse model of Helicobacter pylori infection that mimics human disease. Science 267: 1655-1658.
    • (1995) Science , vol.267 , pp. 1655-1658
    • Marchetti, M.1    Arico, B.2    Burroni, D.3    Figura, N.4    Rappuoli, R.5    Ghiara, P.6
  • 35
    • 0022363305 scopus 로고
    • Attempt to fulfill Koch's postulates for pyloric Campylobacter
    • Marshall, B.J., Armstrong, J.A., McGechie, D.B., and Glancy, R.J. (1985) Attempt to fulfill Koch's postulates for pyloric Campylobacter. Med J Aust 142: 436-439.
    • (1985) Med J Aust , vol.142 , pp. 436-439
    • Marshall, B.J.1    Armstrong, J.A.2    McGechie, D.B.3    Glancy, R.J.4
  • 36
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez, A., and Kolter, R. (1997) Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J Bacteriol 179: 5188-5194.
    • (1997) J Bacteriol , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 37
    • 0025964262 scopus 로고
    • Oxidation of homovanillic acid as a selective assay for eosinophil peroxidase in eosinophil peroxidase-myeloperoxidase mixtures and its use in the detection of human eosinophil peroxidase deficiency
    • Menegazzi, R., Zabucchi, G., Zuccato, P., Cramer, R., Piccinini, C., and Patriarca, P. (1991) Oxidation of homovanillic acid as a selective assay for eosinophil peroxidase in eosinophil peroxidase-myeloperoxidase mixtures and its use in the detection of human eosinophil peroxidase deficiency. J Immunol Methods 137: 55-63.
    • (1991) J Immunol Methods , vol.137 , pp. 55-63
    • Menegazzi, R.1    Zabucchi, G.2    Zuccato, P.3    Cramer, R.4    Piccinini, C.5    Patriarca, P.6
  • 38
    • 0031883873 scopus 로고    scopus 로고
    • Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin
    • Namavar, F., Sparrius, M., Veerman, E.C., Appelmelk, B.J., and Vandenbroucke-Grauls, C.M. (1998) Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin. Infect Immun 66: 444-447.
    • (1998) Infect Immun , vol.66 , pp. 444-447
    • Namavar, F.1    Sparrius, M.2    Veerman, E.C.3    Appelmelk, B.J.4    Vandenbroucke-Grauls, C.M.5
  • 39
    • 0026452890 scopus 로고
    • Activation of human phagocyte oxidative metabolism by Helicobacter pylori
    • Nielsen, H., and Andersen, L.P. (1992a) Activation of human phagocyte oxidative metabolism by Helicobacter pylori. Gastroenterology 103: 1747-1753.
    • (1992) Gastroenterology , vol.103 , pp. 1747-1753
    • Nielsen, H.1    Andersen, L.P.2
  • 40
    • 0026590361 scopus 로고
    • Chemotactic activity of Helicobacter pylori sonicate for human polymorpho-nuclear leucocytes and monocytes
    • Nielsen, H., and Andersen, L.P. (1992b) Chemotactic activity of Helicobacter pylori sonicate for human polymorpho-nuclear leucocytes and monocytes. Gut 33: 738-742.
    • (1992) Gut , vol.33 , pp. 738-742
    • Nielsen, H.1    Andersen, L.P.2
  • 41
    • 0024559452 scopus 로고
    • Treponema pallidum subspecies pallidum (Nichols) and Treponema pallidum subspecies pertenue (CDC 2575) differ in at least one nucleotide: Comparison of two homologous antigens
    • Noordhoek, G.T., Hermans, P.W., Paul, A.N., Schouls, L.M., van der Sluis, J.J., and van Embden, J.D. (1989) Treponema pallidum subspecies pallidum (Nichols) and Treponema pallidum subspecies pertenue (CDC 2575) differ in at least one nucleotide: comparison of two homologous antigens. Microb Pathog 6: 29-42.
    • (1989) Microb Pathog , vol.6 , pp. 29-42
    • Noordhoek, G.T.1    Hermans, P.W.2    Paul, A.N.3    Schouls, L.M.4    Van Der Sluis, J.J.5    Van Embden, J.D.6
  • 42
    • 0028983855 scopus 로고
    • The Swiss-3D image collection and PDB-browser on the world-wide web
    • Peitsch, M.C., Wells, T.N., Stampf, D.R., and Sussman, J.L. (1995) The Swiss-3D image collection and PDB-browser on the world-wide web. Trends Biochem Sci 20: 82-84.
    • (1995) Trends Biochem Sci , vol.20 , pp. 82-84
    • Peitsch, M.C.1    Wells, T.N.2    Stampf, D.R.3    Sussman, J.L.4
  • 43
    • 0029082683 scopus 로고
    • The DpsA protein of Synechococcus sp. strain PCC7942 is a DNA-binding hemoprotein
    • Pen̄a, M.O., and Bullerjahn, G.S. (1995) The DpsA protein of Synechococcus sp. strain PCC7942 is a DNA-binding hemoprotein. J Biol Chem 270: 22478-22482.
    • (1995) J Biol Chem , vol.270 , pp. 22478-22482
    • Pena, M.O.1    Bullerjahn, G.S.2
  • 44
    • 0027238874 scopus 로고
    • Incidence of Helicobacter pylori strains activating neutrophils in patients with peptic ulcer disease
    • Rautelin, H., Blomberg, B., Fredlund, H., Jarnerot, G., and Danielsson, D. (1993) Incidence of Helicobacter pylori strains activating neutrophils in patients with peptic ulcer disease. Gut 34: 599-563.
    • (1993) Gut , vol.34 , pp. 599-1563
    • Rautelin, H.1    Blomberg, B.2    Fredlund, H.3    Jarnerot, G.4    Danielsson, D.5
  • 46
    • 0033558219 scopus 로고    scopus 로고
    • Incorporation of iron by the unusual dodecameric ferritin from Listeria innocua
    • Stefanini, S., Cavallo, S., Montagnini, B., and Chiancone, E. (1999) Incorporation of iron by the unusual dodecameric ferritin from Listeria innocua. Biochem J 338: 71-75.
    • (1999) Biochem J , vol.338 , pp. 71-75
    • Stefanini, S.1    Cavallo, S.2    Montagnini, B.3    Chiancone, E.4
  • 49
    • 0017812024 scopus 로고
    • Incorporation and release of inorganic phosphate in horse spleen ferritin
    • Trefry, A., and Harrison, P.M. (1978) Incorporation and release of inorganic phosphate in horse spleen ferritin. Biochem J 171: 313-320.
    • (1978) Biochem J , vol.171 , pp. 313-320
    • Trefry, A.1    Harrison, P.M.2
  • 50
    • 84920247287 scopus 로고
    • Unidentified curved bacilli on gastric epithelium in active chronic gastritis
    • Warren, J.D., and Marshall, B.J. (1983) Unidentified curved bacilli on gastric epithelium in active chronic gastritis. Lancet 1: 1273-1275.
    • (1983) Lancet , vol.1 , pp. 1273-1275
    • Warren, J.D.1    Marshall, B.J.2
  • 52
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J.T., Wu, C.-S., and Martinez, H.M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol 130: 208-269.
    • (1986) Methods Enzymol , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.2    Martinez, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.