메뉴 건너뛰기




Volumn 6, Issue 2, 2011, Pages

HmuY haemophore and gingipain proteases constitute a unique syntrophic system of haem acquisition by Porphyromonas gingivalis

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; BINDING PROTEIN; DEOXYHEMOGLOBIN; GINGIPAIN K; GINGIPAIN R; HEMATIN; METHEMOGLOBIN; OXYHEMOGLOBIN; PROTEIN HMUY; PROTEINASE; UNCLASSIFIED DRUG; ADHESIN; ARGINGIPAIN, PORPHYROMONAS GINGIVALIS; CYSTEINE PROTEINASE; HEME; HEMOGLOBIN; IRON PROTOPORPHYRIN IX; MULTIPROTEIN COMPLEX; PEPTIDE HYDROLASE; PROTOPORPHYRIN; SERUM ALBUMIN;

EID: 79951971895     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017182     Document Type: Article
Times cited : (72)

References (34)
  • 1
    • 20444471123 scopus 로고    scopus 로고
    • Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: the red complex, a prototype polybacterial pathogenic consortium in periodontitis
    • Holt SC, Ebersole JL, (2005) Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: the red complex, a prototype polybacterial pathogenic consortium in periodontitis. Periodontology 2000 38: 72-122.
    • (2005) Periodontology 2000 , vol.38 , pp. 72-122
    • Holt, S.C.1    Ebersole, J.L.2
  • 2
    • 0032080290 scopus 로고    scopus 로고
    • The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the μ-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism
    • Smalley JW, Silver J, Marsh PJ, Birss AJ, (1998) The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the μ-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism. Biochem J 331: 681-685.
    • (1998) Biochem J , vol.331 , pp. 681-685
    • Smalley, J.W.1    Silver, J.2    Marsh, P.J.3    Birss, A.J.4
  • 4
    • 0028204138 scopus 로고
    • The effect of growth rate and haemin on the virulence and proteolytic activity of Porphyromonas gingivalis W50
    • Marsh PD, McDermid AS, McKee AS, Baskerville A, (1994) The effect of growth rate and haemin on the virulence and proteolytic activity of Porphyromonas gingivalis W50. Microbiology 140: 861-865.
    • (1994) Microbiology , vol.140 , pp. 861-865
    • Marsh, P.D.1    McDermid, A.S.2    McKee, A.S.3    Baskerville, A.4
  • 5
    • 0026426028 scopus 로고
    • Haemin-restriction influences haemin-binding, haemagglutination and protease activity of cells and extracellular membrane vesicles of Porphyromonas gingivalis W50
    • Smalley JW, Birss AJ, McKee AS, Marsh PD, (1991) Haemin-restriction influences haemin-binding, haemagglutination and protease activity of cells and extracellular membrane vesicles of Porphyromonas gingivalis W50. FEMS Microbiol Lett 15: 63-67.
    • (1991) FEMS Microbiol Lett , vol.15 , pp. 63-67
    • Smalley, J.W.1    Birss, A.J.2    McKee, A.S.3    Marsh, P.D.4
  • 6
    • 11844277116 scopus 로고    scopus 로고
    • Iron and heme utilization in Porphyromonas gingivalis
    • Olczak T, Simpson W, Liu X, Genco CA, (2005) Iron and heme utilization in Porphyromonas gingivalis. FEMS Microbiol Rev 29: 119-144.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 119-144
    • Olczak, T.1    Simpson, W.2    Liu, X.3    Genco, C.A.4
  • 7
    • 43049126508 scopus 로고    scopus 로고
    • Porphyromonas gingivalis HmuY and HmuR: Further characterization of a novel mechanism of heme utilization
    • Olczak T, Sroka A, Potempa J, Olczak M, (2008) Porphyromonas gingivalis HmuY and HmuR: Further characterization of a novel mechanism of heme utilization. Arch Microbiol 189: 197-210.
    • (2008) Arch Microbiol , vol.189 , pp. 197-210
    • Olczak, T.1    Sroka, A.2    Potempa, J.3    Olczak, M.4
  • 8
    • 33750933470 scopus 로고    scopus 로고
    • Transcriptional organization, regulation and role of the Porphyromonas gingivalis W83 hmu haemin-uptake locus
    • Lewis JP, Plata K, Yu F, Rosato A, Anaya C, (2006) Transcriptional organization, regulation and role of the Porphyromonas gingivalis W83 hmu haemin-uptake locus. Microbiology 152: 3367-3382.
    • (2006) Microbiology , vol.152 , pp. 3367-3382
    • Lewis, J.P.1    Plata, K.2    Yu, F.3    Rosato, A.4    Anaya, C.5
  • 9
    • 67249153503 scopus 로고    scopus 로고
    • Unique structure and stability of HmuY, a novel heme-binding protein of Porphyromonas gingivalis
    • Wojtowicz H, Guevara T, Tallant C, Olczak M, Sroka A, et al. (2009) Unique structure and stability of HmuY, a novel heme-binding protein of Porphyromonas gingivalis. PLoS Pathog 5 (5): e1000419.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Wojtowicz, H.1    Guevara, T.2    Tallant, C.3    Olczak, M.4    Sroka, A.5
  • 11
    • 2542570174 scopus 로고    scopus 로고
    • A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the μ-oxo bishaem-containing pigment from haemoglobin
    • Smalley JW, Thomas MF, Birss AJ, Withnall R, Silver J, (2004) A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the μ-oxo bishaem-containing pigment from haemoglobin. Biochem J 379: 833-840.
    • (2004) Biochem J , vol.379 , pp. 833-840
    • Smalley, J.W.1    Thomas, M.F.2    Birss, A.J.3    Withnall, R.4    Silver, J.5
  • 12
    • 34548022164 scopus 로고    scopus 로고
    • Sequential action of R- and K-specific gingipains of Porphyromonas gingivalis in the generation of the haem-containing pigment from oxyhaemoglobin
    • Smalley JW, Birss AJ, Szmigielski B, Potempa J, (2007) Sequential action of R- and K-specific gingipains of Porphyromonas gingivalis in the generation of the haem-containing pigment from oxyhaemoglobin. Arch Biochem Biophys 465: 44-49.
    • (2007) Arch Biochem Biophys , vol.465 , pp. 44-49
    • Smalley, J.W.1    Birss, A.J.2    Szmigielski, B.3    Potempa, J.4
  • 13
    • 54049097084 scopus 로고    scopus 로고
    • Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis
    • Smalley JW, Birss AJ, Szmigielski B, Potempa J, (2008) Mechanism of methaemoglobin breakdown by the lysine-specific gingipain of the periodontal pathogen Porphyromonas gingivalis. Biol Chem 389: 1235-1238.
    • (2008) Biol Chem , vol.389 , pp. 1235-1238
    • Smalley, J.W.1    Birss, A.J.2    Szmigielski, B.3    Potempa, J.4
  • 14
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between haemoglobin and albumin
    • Bunn HF, Jandl JH, (1968) Exchange of heme among hemoglobins and between haemoglobin and albumin. J Biol Chem 243: 465-475.
    • (1968) J Biol Chem , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 15
    • 0025122955 scopus 로고
    • The stability of the heme-globin linkage in some normal, mutant and chemically modified hemoglobins
    • Benesch RE, Kwong S, (1990) The stability of the heme-globin linkage in some normal, mutant and chemically modified hemoglobins. J Biol Chem 265: 14881-14885.
    • (1990) J Biol Chem , vol.265 , pp. 14881-14885
    • Benesch, R.E.1    Kwong, S.2
  • 16
    • 0029892404 scopus 로고    scopus 로고
    • Stability of heme-globin linkage in αβ dimers and isolated chains of human haemoglobin
    • Gattoni M, Boffi A, Sarti P, Chiancone E, (1996) Stability of heme-globin linkage in αβ dimers and isolated chains of human haemoglobin. J Biol Chem 271: 10130-10136.
    • (1996) J Biol Chem , vol.271 , pp. 10130-10136
    • Gattoni, M.1    Boffi, A.2    Sarti, P.3    Chiancone, E.4
  • 17
    • 72449195888 scopus 로고    scopus 로고
    • Role of the cysteine protease interpain A of Prevotella intermedia in breakdown and release of haem from haemoglobin
    • Byrne DP, Wawrzonek K, Jaworska A, Birss AJ, Potempa J, et al. (2009) Role of the cysteine protease interpain A of Prevotella intermedia in breakdown and release of haem from haemoglobin. Biochem J 425: 257-264.
    • (2009) Biochem J , vol.425 , pp. 257-264
    • Byrne, D.P.1    Wawrzonek, K.2    Jaworska, A.3    Birss, A.J.4    Potempa, J.5
  • 18
    • 0027358741 scopus 로고
    • Haemin-binding proteins of Porphyromonas gingivalis W50 grown in a chemostat under haemin-limitation
    • Smalley JW, Birss AJ, McKee AS, Marsh PD, (1993) Haemin-binding proteins of Porphyromonas gingivalis W50 grown in a chemostat under haemin-limitation. J Gen Microbiol 139: 2145-2150.
    • (1993) J Gen Microbiol , vol.139 , pp. 2145-2150
    • Smalley, J.W.1    Birss, A.J.2    McKee, A.S.3    Marsh, P.D.4
  • 19
    • 0037084219 scopus 로고    scopus 로고
    • Interactions of Porphyromonas gingivalis with oxyhaemoglobin and deoxyhaemoglobin
    • Smalley JW, Birss AJ, Withnall R, Silver J, (2002) Interactions of Porphyromonas gingivalis with oxyhaemoglobin and deoxyhaemoglobin. Biochem J 362: 239-245.
    • (2002) Biochem J , vol.362 , pp. 239-245
    • Smalley, J.W.1    Birss, A.J.2    Withnall, R.3    Silver, J.4
  • 20
    • 0019073710 scopus 로고
    • Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin
    • Adams P, Berman MC, (1980) Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin. Biochem J 191: 95-102.
    • (1980) Biochem J , vol.191 , pp. 95-102
    • Adams, P.1    Berman, M.C.2
  • 21
    • 0015980699 scopus 로고
    • Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin
    • Hrkal Z, Vodrzka Z, Kalousek I, (1974) Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. Eur J Biochem 43: 73-78.
    • (1974) Eur J Biochem , vol.43 , pp. 73-78
    • Hrkal, Z.1    Vodrzka, Z.2    Kalousek, I.3
  • 22
    • 77952850229 scopus 로고    scopus 로고
    • Species specificity, surface exposure, protein expression, immunogenicity, and participation in biofilm formation of Porphyromonas gingivalis HmuY
    • Olczak T, Wojtowicz H, Ciuraszkiewicz J, Olczak M, (2010) Species specificity, surface exposure, protein expression, immunogenicity, and participation in biofilm formation of Porphyromonas gingivalis HmuY. BMC Microbiol 10: 134.
    • (2010) BMC Microbiol , vol.10 , pp. 134
    • Olczak, T.1    Wojtowicz, H.2    Ciuraszkiewicz, J.3    Olczak, M.4
  • 23
    • 0025993552 scopus 로고
    • The pH of gingival crevices and periodontal pockets in children, teenagers and adults
    • Eggert FM, Drewell L, Bigelow JA, Speck JE, Goldner M, (1991) The pH of gingival crevices and periodontal pockets in children, teenagers and adults. Archs Oral Biol 36: 233-238.
    • (1991) Archs Oral Biol , vol.36 , pp. 233-238
    • Eggert, F.M.1    Drewell, L.2    Bigelow, J.A.3    Speck, J.E.4    Goldner, M.5
  • 24
    • 0021905838 scopus 로고
    • The pH of human crevicular fluid measured by a new microanalytical technique
    • Bickel M, Cimasoni G, (1985) The pH of human crevicular fluid measured by a new microanalytical technique. J Periodont Res 20: 35-40.
    • (1985) J Periodont Res , vol.20 , pp. 35-40
    • Bickel, M.1    Cimasoni, G.2
  • 25
    • 0032502724 scopus 로고    scopus 로고
    • The molecular mechanism of autoxidation for human oxyhemoglobin: tilting of the distal histidine causes nonequivalent oxidation in the b chain
    • Tsuruga M, Matsuoka A, Hachimori A, Sugawara Y, Shikama K, (1998) The molecular mechanism of autoxidation for human oxyhemoglobin: tilting of the distal histidine causes nonequivalent oxidation in the b chain. J Biol Chem 273: 8607-8615.
    • (1998) J Biol Chem , vol.273 , pp. 8607-8615
    • Tsuruga, M.1    Matsuoka, A.2    Hachimori, A.3    Sugawara, Y.4    Shikama, K.5
  • 26
    • 0028013159 scopus 로고
    • Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins
    • Pike R, McGraw W, Potempa J, Travis J, (1994) Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins. J Biol Chem 269: 406-411.
    • (1994) J Biol Chem , vol.269 , pp. 406-411
    • Pike, R.1    McGraw, W.2    Potempa, J.3    Travis, J.4
  • 27
    • 0032555656 scopus 로고    scopus 로고
    • Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis
    • Potempa J, Mikolajczyk-Pawlinska J, Brassell D, Nelson D, Thøgersen IB, et al. (1998) Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis. J Biol Chem 273: 21648-21657.
    • (1998) J Biol Chem , vol.273 , pp. 21648-21657
    • Potempa, J.1    Mikolajczyk-Pawlinska, J.2    Brassell, D.3    Nelson, D.4    Thøgersen, I.B.5
  • 28
    • 0024114133 scopus 로고
    • The total protein concentration of gingival crevicular fluid. Variation with sampling time and gingival inflammation
    • Curtis MA, Griffiths GS, Price SJ, Coulthurst SK, Johnson NW, (1988) The total protein concentration of gingival crevicular fluid. Variation with sampling time and gingival inflammation. J Clin Periodontol 15: 628-632.
    • (1988) J Clin Periodontol , vol.15 , pp. 628-632
    • Curtis, M.A.1    Griffiths, G.S.2    Price, S.J.3    Coulthurst, S.K.4    Johnson, N.W.5
  • 29
    • 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 DW, Genco CA, (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
  • 30
    • 0028170732 scopus 로고
    • Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein
    • Letoffe S, Ghigo JM, Wandersman C, (1994) Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein. Proc Natl Acad Sci U S A 91: 9876-9880.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9876-9880
    • Letoffe, S.1    Ghigo, J.M.2    Wandersman, C.3
  • 31
    • 50849124753 scopus 로고    scopus 로고
    • Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin
    • Maresso AW, Garufi G, Schneewind O, (2008) Bacillus anthracis secretes proteins that mediate heme acquisition from hemoglobin. PLoS Pathog 4: e1000132.
    • (2008) PLoS Pathog , vol.4
    • Maresso, A.W.1    Garufi, G.2    Schneewind, O.3
  • 32
    • 33745251643 scopus 로고    scopus 로고
    • The HA2 haemagglutinin domain of the lysine-specific gingipain (Kgp) of Porphyromonas gingivalis promotes μ-oxo bishaem formation from monomeric iron(III) protoporphyrin IX
    • Smalley JW, Birss AJ, Szmigielski B, Potempa J, (2006) The HA2 haemagglutinin domain of the lysine-specific gingipain (Kgp) of Porphyromonas gingivalis promotes μ-oxo bishaem formation from monomeric iron(III) protoporphyrin IX. Microbiology 152: 1839-1845.
    • (2006) Microbiology , vol.152 , pp. 1839-1845
    • Smalley, J.W.1    Birss, A.J.2    Szmigielski, B.3    Potempa, J.4
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (5259): 680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.