메뉴 건너뛰기




Volumn 188, Issue 5, 2012, Pages 2338-2349

A metalloproteinase karilysin present in the majority of Tannerella forsythia isolates inhibits all pathways of the complement system

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C4; COMPLEMENT COMPONENT C5; COMPLEMENT COMPONENT C5A; COMPLEMENT MEMBRANE ATTACK COMPLEX; FICOLIN; FICOLIN 2; FICOLIN 3; KARILYSIN; METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 84857463226     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1101240     Document Type: Article
Times cited : (76)

References (50)
  • 3
    • 20444471123 scopus 로고    scopus 로고
    • Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: The 'red complex', a prototype polybacterial pathogenic consortium in periodontitis
    • DOI 10.1111/j.1600-0757.2005.00113.x
    • Holt, S. C., and J. L. Ebersole. 2005. Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: the "red complex," a prototype polybacterial pathogenic consortium in periodontitis. Periodontol. 2000 38: 72-122. (Pubitemid 43034324)
    • (2005) Periodontology 2000 , vol.38 , pp. 72-122
    • Holt, S.C.1    Ebersole, J.L.2
  • 4
    • 33747862498 scopus 로고    scopus 로고
    • Tannerella forsythia, a periodontal pathogen entering the genomic era
    • DOI 10.1111/j.1600-0757.2006.00184.x
    • Tanner, A. C., and J. Izard. 2006. Tannerella forsythia, a periodontal pathogen entering the genomic era. Periodontol. 2000 42: 88-113. (Pubitemid 44286049)
    • (2006) Periodontology 2000 , vol.42 , Issue.1 , pp. 88-113
    • Tanner, A.C.R.1    Izard, J.2
  • 5
    • 0026840948 scopus 로고
    • Bacterial synergy of Treponema denticola and Porphyromonas gingivalis in a multinational population
    • Simonson, L. G., K. T. McMahon, D. W. Childers, and H. E. Morton. 1992. Bacterial synergy of Treponema denticola and Porphyromonas gingivalis in a multinational population. Oral Microbiol. Immunol. 7: 111-112.
    • (1992) Oral Microbiol. Immunol. , vol.7 , pp. 111-112
    • Simonson, L.G.1    McMahon, K.T.2    Childers, D.W.3    Morton, H.E.4
  • 6
    • 34249799593 scopus 로고    scopus 로고
    • Biphasic effect of gingipains from Porphyromonas gingivalis on the human complement system
    • Popadiak, K., J. Potempa, K. Riesbeck, and A. M. Blom. 2007. Biphasic effect of gingipains from Porphyromonas gingivalis on the human complement system. J. Immunol. 178: 7242-7250. (Pubitemid 46847450)
    • (2007) Journal of Immunology , vol.178 , Issue.11 , pp. 7242-7250
    • Popadiak, K.1    Potempa, J.2    Riesbeck, K.3    Blom, A.M.4
  • 7
    • 61449163214 scopus 로고    scopus 로고
    • Corruption of innate immunity by bacterial proteases
    • Potempa, J., and R. N. Pike. 2009. Corruption of innate immunity by bacterial proteases. J. Innate Immun. 1: 70-87.
    • (2009) J. Innate Immun. , vol.1 , pp. 70-87
    • Potempa, J.1    Pike, R.N.2
  • 8
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • Ricklin, D., G. Hajishengallis, K. Yang, and J. D. Lambris. 2010. Complement: a key system for immune surveillance and homeostasis. Nat. Immunol. 11: 785-797.
    • (2010) Nat. Immunol. , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 9
    • 0029013679 scopus 로고
    • Increased opsonization of a prtH-defective mutant of Porphyromonas gingivalis W83 is caused by reduced degradation of complement-derived opsonins
    • Schenkein, H. A., H. M. Fletcher, M. Bodnar, and F. L. Macrina. 1995. Increased opsonization of a prtH-defective mutant of Porphyromonas gingivalis W83 is caused by reduced degradation of complement-derived opsonins. J. Immunol. 154: 5331-5337.
    • (1995) J. Immunol. , vol.154 , pp. 5331-5337
    • Schenkein, H.A.1    Fletcher, H.M.2    Bodnar, M.3    Macrina, F.L.4
  • 11
    • 1842557722 scopus 로고    scopus 로고
    • Complement inhibitor C4b-binding protein - Friend or foe in the innate immune system?
    • DOI 10.1016/j.molimm.2003.12.002, PII S0161589003004085
    • Blom, A. M., B. O. Villoutreix, and B. Dahlbäck. 2004. Complement inhibitor C4b-binding protein-friend or foe in the innate immune system? Mol. Immunol. 40: 1333-1346. (Pubitemid 38456985)
    • (2004) Molecular Immunology , vol.40 , Issue.18 , pp. 1333-1346
    • Blom, A.M.1    Villoutreix, B.O.2    Dahlback, B.3
  • 12
    • 34548259156 scopus 로고    scopus 로고
    • Complement evasion of pathogens: Common strategies are shared by diverse organisms
    • DOI 10.1016/j.molimm.2007.06.149, PII S0161589007002581, XIth European meeting on Complement in Human Disease
    • Zipfel, P. F., R. Würzner, and C. Skerka. 2007. Complement evasion of pathogens: common strategies are shared by diverse organisms. Mol. Immunol. 44: 3850-3857. (Pubitemid 47332624)
    • (2007) Molecular Immunology , vol.44 , Issue.16 , pp. 3850-3857
    • Zipfel, P.F.1    Wurzner, R.2    Skerka, C.3
  • 13
    • 54049101495 scopus 로고    scopus 로고
    • Binding of complement inhibitor C4b-binding protein contributes to serum resistance of Porphyromonas gingivalis
    • Potempa, M., J. Potempa, M. Okroj, K. Popadiak, S. Eick, K. A. Nguyen, K. Riesbeck, and A. M. Blom. 2008. Binding of complement inhibitor C4b-binding protein contributes to serum resistance of Porphyromonas gingivalis. J. Immunol. 181: 5537-5544.
    • (2008) J. Immunol. , vol.181 , pp. 5537-5544
    • Potempa, M.1    Potempa, J.2    Okroj, M.3    Popadiak, K.4    Eick, S.5    Nguyen, K.A.6    Riesbeck, K.7    Blom, A.M.8
  • 14
    • 33750487181 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpes virus complement control protein: KCP - complement inhibition and more
    • DOI 10.1016/j.molimm.2006.06.018, PII S0161589006002239
    • Mark, L., O. B. Spiller, B. O. Villoutreix, and A. M. Blom. 2007. Kaposi's sarcoma-associated herpes virus complement control protein: KCP - complement inhibition and more. Mol. Immunol. 44: 11-22. (Pubitemid 44647105)
    • (2007) Molecular Immunology , vol.44 , Issue.1-3 , pp. 11-22
    • Mark, L.1    Spiller, O.B.2    Villoutreix, B.O.3    Blom, A.M.4
  • 15
    • 0022754901 scopus 로고
    • Susceptibility of Bacteroides gingivalis to bactericidal activity of human serum
    • Okuda, K., T. Kato, Y. Naito, M. Ono, Y. Kikuchi, and I. Takazoe. 1986. Susceptibility of Bacteroides gingivalis to bactericidal activity of human serum. J. Dent. Res. 65: 1024-1027.
    • (1986) J. Dent. Res. , vol.65 , pp. 1024-1027
    • Okuda, K.1    Kato, T.2    Naito, Y.3    Ono, M.4    Kikuchi, Y.5    Takazoe, I.6
  • 16
    • 0020045302 scopus 로고
    • Bactericidal effect of pooled human serum on Bacteroides melaninogenicus, Bacteroides asaccharolyticus and Actinobacillus actinomycetemcomitans
    • Sundqvist, G., and E. Johansson. 1982. Bactericidal effect of pooled human serum on Bacteroides melaninogenicus, Bacteroides asaccharolyticus and Actinobacillus actinomycetemcomitans. Scand. J. Dent. Res. 90: 29-36. (Pubitemid 12116061)
    • (1982) Scandinavian Journal of Dental Research , vol.90 , Issue.1 , pp. 29-36
    • Sundqvist, G.1    Johannson, E.2
  • 17
    • 0026725842 scopus 로고
    • Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis
    • Wingrove, J. A., R. G. DiScipio, Z. Chen, J. Potempa, J. Travis, and T. E. Hugli. 1992. Activation of complement components C3 and C5 by a cysteine proteinase (gingipain-1) from Porphyromonas (Bacteroides) gingivalis. J. Biol. Chem. 267: 18902-18907.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18902-18907
    • Wingrove, J.A.1    DiScipio, R.G.2    Chen, Z.3    Potempa, J.4    Travis, J.5    Hugli, T.E.6
  • 18
    • 0026724045 scopus 로고
    • Inactivation of human serum bactericidal activity by a tryp-sinlike protease isolated from Porphyromonas gingivalis
    • Grenier, D. 1992. Inactivation of human serum bactericidal activity by a tryp-sinlike protease isolated from Porphyromonas gingivalis. Infect. Immun. 60: 1854-1857.
    • (1992) Infect. Immun. , vol.60 , pp. 1854-1857
    • Grenier, D.1
  • 19
    • 0027135337 scopus 로고
    • Inhibition of C3 and IgG proteolysis enhances phagocytosis of Porphyromonas gingivalis
    • Cutler, C. W., R. R. Arnold, and H. A. Schenkein. 1993. Inhibition of C3 and IgG proteolysis enhances phagocytosis of Porphyromonas gingivalis. J. Immunol. 151: 7016-7029. (Pubitemid 24001076)
    • (1993) Journal of Immunology , vol.151 , Issue.12 , pp. 7016-7029
    • Cutler, C.W.1    Arnold, R.R.2    Schenkein, H.A.3
  • 21
    • 78650231500 scopus 로고    scopus 로고
    • The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases
    • Cerdà-Costa, N., T. Guevara, A. Y. Karim, M. Ksiazek, K. A. Nguyen, J. L. Arolas, J. Potempa, and F. X. Gomis-Rüth. 2011. The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases. Mol. Microbiol. 79: 119-132.
    • (2011) Mol. Microbiol. , vol.79 , pp. 119-132
    • Cerdà-Costa, N.1    Guevara, T.2    Karim, A.Y.3    Ksiazek, M.4    Nguyen, K.A.5    Arolas, J.L.6    Potempa, J.7    Gomis-Rüth, F.X.8
  • 22
    • 0024382807 scopus 로고
    • Dependence of proliferation of Bacteroides forsythus on exogenous N-acetylmuramic acid
    • Wyss, C. 1989. Dependence of proliferation of Bacteroides forsythus on exogenous N-acetylmuramic acid. Infect. Immun. 57: 1757-1759. (Pubitemid 19140139)
    • (1989) Infection and Immunity , vol.57 , Issue.6 , pp. 1757-1759
    • Wyss, C.1
  • 25
    • 40849126550 scopus 로고    scopus 로고
    • Characterization of a polymorphism in the coding sequence of FCN3 resulting in a Ficolin-3 (Hakata antigen) deficiency state
    • Munthe-Fog, L., T. Hummelshøj, Y. J. Ma, B. E. Hansen, C. Koch, H. O. Madsen, K. Skjødt, and P. Garred. 2008. Characterization of a polymorphism in the coding sequence of FCN3 resulting in a Ficolin-3 (Hakata antigen) deficiency state. Mol. Immunol. 45: 2660-2666.
    • (2008) Mol. Immunol. , vol.45 , pp. 2660-2666
    • Munthe-Fog, L.1    Hummelshøj, T.2    Ma, Y.J.3    Hansen, B.E.4    Koch, C.5    Madsen, H.O.6    Skjødt, K.7    Garred, P.8
  • 28
    • 0036721025 scopus 로고    scopus 로고
    • Essential role of the C5a receptor in E coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation
    • Mollnes, T. E., O. L. Brekke, M. Fung, H. Fure, D. Christiansen, G. Bergseth, V. Videm, K. T. Lappegård, J. Köhl, and J. D. Lambris. 2002. Essential role of the C5a receptor in E. coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation. Blood 100: 1869-1877. (Pubitemid 34925168)
    • (2002) Blood , vol.100 , Issue.5 , pp. 1869-1877
    • Mollnes, T.E.1    Brekke, O.-L.2    Fung, M.3    Fure, H.4    Christiansen, D.5    Bergseth, G.6    Videm, V.7    Lappegard, K.T.8    Kohl, J.9    Lambris, J.D.10
  • 29
    • 0030205852 scopus 로고    scopus 로고
    • Polymerase chain reaction detection of 8 putative periodontal pathogens in subgingival plaque of gingivitis and advanced periodontitis lesions
    • Ashimoto, A., C. Chen, I. Bakker, and J. Slots. 1996. Polymerase chain reaction detection of 8 putative periodontal pathogens in subgingival plaque of gingivitis and advanced periodontitis lesions. Oral Microbiol. Immunol. 11: 266-273. (Pubitemid 27324157)
    • (1996) Oral Microbiology and Immunology , vol.11 , Issue.4 , pp. 266-273
    • Ashimoto, A.1    Chen, C.2    Bakker, I.3    Slots, J.4
  • 30
    • 0017584749 scopus 로고
    • Gingival fluid and serum in periodontal diseases. I. Quantitative study of immunoglobulins, complement components, and other plasma proteins
    • Schenkein, H. A., and R. J. Genco. 1977. Gingival fluid and serum in periodontal diseases. I. Quantitative study of immunoglobulins, complement components, and other plasma proteins. J. Periodontol. 48: 772-777. (Pubitemid 8254482)
    • (1977) Journal of Periodontology , vol.48 , Issue.2 , pp. 772-777
    • Schenkein, H.A.1    Genco, R.J.2
  • 31
    • 0016639639 scopus 로고
    • Complement factors in gingival crevice material from healthy and inflamed gingiva in humans
    • Attström, R., A. B. Laurel, U. Lahsson, and A. Sjöholm. 1975. Complement factors in gingival crevice material from healthy and inflamed gingiva in humans. J. Periodontal Res. 10: 19-27.
    • (1975) J. Periodontal Res. , vol.10 , pp. 19-27
    • Attström, R.1    Laurel, A.B.2    Lahsson, U.3    Sjöholm, A.4
  • 32
    • 0017605530 scopus 로고
    • Gingival fluid and serum in periodontal diseases. II. Evidence for cleavage of complement components C3, C3 proactivator (factor B) and C4 in gingival fluid
    • Schenkein, H. A., and R. J. Genco. 1977. Gingival fluid and serum in periodontal diseases. II. Evidence for cleavage of complement components C3, C3 proactivator (factor B) and C4 in gingival fluid. J. Periodontol. 48: 778-784. (Pubitemid 8254483)
    • (1977) Journal of Periodontology , vol.48 , Issue.2 , pp. 778-784
    • Schenkein, H.A.1    Genco, R.J.2
  • 33
    • 0038498113 scopus 로고    scopus 로고
    • The benzoyl-DL arginine-naphthylamide (BANA) test and polymerase chain reaction measurement of pathogenic bacteria can assess the severity of periodontal disease
    • Takaishi, Y., H. Morii, and T. Miki. 2003. The benzoyl-DL argininenaphthylamide (BANA) test and polymerase chain reaction measurement of pathogenic bacteria can assess the severity of periodontal disease. Int. J. Tissue React. 25: 19-24. (Pubitemid 36805755)
    • (2003) International Journal of Tissue Reactions , vol.25 , Issue.1 , pp. 19-24
    • Takaishi, Y.1    Morii, H.2    Miki, T.3
  • 34
    • 0030781216 scopus 로고    scopus 로고
    • Cloning, expression, and sequencing of a protease gene from bacteroides forsythus ATCC 43037 in Escherichia coli
    • Saito, T., K. Ishihara, T. Kato, and K. Okuda. 1997. Cloning, expression, and sequencing of a protease gene from Bacteroides forsythus ATCC 43037 in Escherichia coli. Infect. Immun. 65: 4888-4891. (Pubitemid 27463275)
    • (1997) Infection and Immunity , vol.65 , Issue.11 , pp. 4888-4891
    • Saito, T.1    Ishihara, K.2    Kato, T.3    Okuda, K.4
  • 36
    • 65949094575 scopus 로고    scopus 로고
    • Prediction of a caspase-like fold in Tannerella forsythia virulence factor PrtH
    • Pei, J., and N. V. Grishin. 2009. Prediction of a caspase-like fold in Tannerella forsythia virulence factor PrtH. Cell Cycle 8: 1453-1455.
    • (2009) Cell Cycle , vol.8 , pp. 1453-1455
    • Pei, J.1    Grishin, N.V.2
  • 38
    • 79960476334 scopus 로고    scopus 로고
    • Comparison of gingival crevicular fluid sampling methods in patients with severe chronic periodontitis
    • Guentsch, A., M. Kramesberger, A. Sroka, W. Pfister, J. Potempa, and S. Eick. 2011. Comparison of gingival crevicular fluid sampling methods in patients with severe chronic periodontitis. J. Periodontol. 82: 1051-1060.
    • (2011) J. Periodontol. , vol.82 , pp. 1051-1060
    • Guentsch, A.1    Kramesberger, M.2    Sroka, A.3    Pfister, W.4    Potempa, J.5    Eick, S.6
  • 39
    • 78649945617 scopus 로고    scopus 로고
    • Comparison of real-time polymerase chain reaction and DNA-strip technology in microbiological evaluation of periodontitis treatment
    • Eick, S., A. Straube, A. Guentsch,W. Pfister, and H. Jentsch. 2011. Comparison of real-time polymerase chain reaction and DNA-strip technology in microbiological evaluation of periodontitis treatment. Diagn. Microbiol. Infect. Dis. 69: 12-20.
    • (2011) Diagn. Microbiol. Infect. Dis. , vol.69 , pp. 12-20
    • Eick, S.1    Straube, A.2    Guentsch, A.3    Pfister, W.4    Jentsch, H.5
  • 41
    • 0037264098 scopus 로고    scopus 로고
    • Origin and function of the cellular components in gingival crevice fluid
    • DOI 10.1034/j.1600-0757.2003.03105.x
    • Delima, A. J., and T. E. Van Dyke. 2003. Origin and function of the cellular components in gingival crevice fluid. Periodontol. 2000 31: 55-76. (Pubitemid 37487410)
    • (2003) Periodontology 2000 , vol.31 , pp. 55-76
    • Delima, A.J.1    Van Dyke, T.E.2
  • 42
    • 17644388462 scopus 로고    scopus 로고
    • Role of C5a in inflammatory responses
    • Guo, R. F., and P. A. Ward. 2005. Role of C5a in inflammatory responses. Annu. Rev. Immunol. 23: 821-852.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 821-852
    • Guo, R.F.1    Ward, P.A.2
  • 44
    • 77956057326 scopus 로고    scopus 로고
    • The harmful role of c5a on innate immunity in sepsis
    • Ward, P. A. 2010. The harmful role of c5a on innate immunity in sepsis. J. Innate Immun. 2: 439-445.
    • (2010) J. Innate Immun. , vol.2 , pp. 439-445
    • Ward, P.A.1
  • 45
    • 56149086187 scopus 로고    scopus 로고
    • Importance of TLR2 in early innate immune response to acute pulmonary infection with Porphyromonas gingivalis in mice
    • Hajishengallis, G., M. Wang, G. J. Bagby, and S. Nelson. 2008. Importance of TLR2 in early innate immune response to acute pulmonary infection with Porphyromonas gingivalis in mice. J. Immunol. 181: 4141-4149.
    • (2008) J. Immunol. , vol.181 , pp. 4141-4149
    • Hajishengallis, G.1    Wang, M.2    Bagby, G.J.3    Nelson, S.4
  • 47
    • 33646596865 scopus 로고    scopus 로고
    • C5a mediates secretion and activation of matrix metalloproteinase 9 from human eosinophils and neutrophils
    • DOI 10.1016/j.intimp.2006.02.006, PII S1567576906000579
    • DiScipio, R. G., I. U. Schraufstatter, L. Sikora, B. L. Zuraw, and P. Sriramarao. 2006. C5a mediates secretion and activation of matrix metalloproteinase 9 from human eosinophils and neutrophils. Int. Immunopharmacol. 6: 1109-1118. (Pubitemid 43728165)
    • (2006) International Immunopharmacology , vol.6 , Issue.7 , pp. 1109-1118
    • DiScipio, R.G.1    Schraufstatter, I.U.2    Sikora, L.3    Zuraw, B.L.4    Sriramarao, P.5
  • 48
    • 45849131697 scopus 로고    scopus 로고
    • Biomarkers of periodontitis in oral fluids
    • Rai, B., S. Kharb, R. Jain, and S. C. Anand. 2008. Biomarkers of periodontitis in oral fluids. J. Oral Sci. 50: 53-56.
    • (2008) J. Oral Sci. , vol.50 , pp. 53-56
    • Rai, B.1    Kharb, S.2    Jain, R.3    Anand, S.C.4
  • 49
    • 0037124041 scopus 로고    scopus 로고
    • Mannose-binding lectin (MBL) mutants are susceptible to matrix metalloproteinase proteolysis. Potential role in human MBL deficiency
    • DOI 10.1074/jbc.M201461200
    • Butler, G. S., D. Sim, E. Tam, D. Devine, and C. M. Overall. 2002. Mannose-binding lectin (MBL) mutants are susceptible to matrix metalloproteinase proteolysis: potential role in human MBL deficiency. J. Biol. Chem. 277: 17511-17519. (Pubitemid 34967551)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 17511-17519
    • Butler, G.S.1    Sim, D.2    Tam, E.3    Devine, D.4    Overall, C.M.5
  • 50
    • 38949154873 scopus 로고    scopus 로고
    • Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen)
    • DOI 10.1016/j.molimm.2007.10.006, PII S0161589007008000
    • Hummelshoj, T., L. M. Fog, H. O. Madsen, R. B. Sim, and P. Garred. 2008. Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen). Mol. Immunol. 45: 1623-1632. (Pubitemid 351221142)
    • (2008) Molecular Immunology , vol.45 , Issue.6 , pp. 1623-1632
    • Hummelshoj, T.1    Fog, L.M.2    Madsen, H.O.3    Sim, R.B.4    Garred, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.