메뉴 건너뛰기




Volumn 77, Issue 10, 2009, Pages 4414-4420

Identification of a gingipain-sensitive surface ligand of Porphyromonas gingivalis that induces Toll-like receptor 2- and 4-independent NF-κB activation in CHO cells

Author keywords

[No Author keywords available]

Indexed keywords

ANTISERUM; BACTERIAL PROTEIN; GINGIPAIN R; GINGIPAIN SENSITIVE LIGAND A; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; RECOMBINANT PROTEIN; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 70349436039     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00140-09     Document Type: Article
Times cited : (12)

References (25)
  • 1
    • 0033546749 scopus 로고    scopus 로고
    • Rapid and efficient inactivation of IL-6 gingipains, lysine- And arginine-specific proteinases from Porphyromonas gingivalis
    • Banbula, A., M. Bugno, A. Kuster, P. C. Heinrich, J. Travis, and J. Potempa. 1999. Rapid and efficient inactivation of IL-6 gingipains, lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Biochem. Biophys. Res. Commun. 261:598-602.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 598-602
    • Banbula, A.1    Bugno, M.2    Kuster, A.3    Heinrich, P.C.4    Travis, J.5    Potempa, J.6
  • 2
    • 0032549590 scopus 로고    scopus 로고
    • Inactivation of tumor necrosis factor-α by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. Implications of immune evasion
    • Calkins, C. C., K. Platt, J. Potempa, and J. Travis. 1998. Inactivation of tumor necrosis factor-α by proteinases (gingipains) from the periodontal pathogen, Porphyromonas gingivalis. Implications of immune evasion. J. Biol. Chem. 273:6611-6614.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6611-6614
    • Calkins, C.C.1    Platt, K.2    Potempa, J.3    Travis, J.4
  • 3
    • 0032530613 scopus 로고    scopus 로고
    • Construction of a lipopolysaccharide reporter cell line and its use in identifying mutants defective in endotoxin, but not TNF-α, signal transduction
    • Delude, R. L., A. Yoshimura, R. R. Ingalls, and D. T. Golenbock. 1998. Construction of a lipopolysaccharide reporter cell line and its use in identifying mutants defective in endotoxin, but not TNF-α, signal transduction. J. Immunol. 161:3001-3009.
    • (1998) J. Immunol. , vol.161 , pp. 3001-3009
    • Delude, R.L.1    Yoshimura, A.2    Ingalls, R.R.3    Golenbock, D.T.4
  • 4
    • 0026101229 scopus 로고
    • A novel mouse model to study the virulence of and host response to Porphyromonas (Bacteroides) gingivalis
    • Genco, C. A., C. W. Cutler, D. Kapczynski, K. Maloney, and R. R. Arnold. 1991. A novel mouse model to study the virulence of and host response to Porphyromonas (Bacteroides) gingivalis. Infect. Immun. 59:1255-1263.
    • (1991) Infect. Immun. , vol.59 , pp. 1255-1263
    • Genco, C.A.1    Cutler, C.W.2    Kapczynski, D.3    Maloney, K.4    Arnold, R.R.5
  • 5
    • 0032582491 scopus 로고    scopus 로고
    • Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis
    • Kadowaki, T., K. Nakayama, F. Yoshimura, K. Okamoto, N. Abe, and K. Yamamoto. 1998. Arg-gingipain acts as a major processing enzyme for various cell surface proteins in Porphyromonas gingivalis. J. Biol. Chem. 273:29072-29076.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29072-29076
    • Kadowaki, T.1    Nakayama, K.2    Yoshimura, F.3    Okamoto, K.4    Abe, N.5    Yamamoto, K.6
  • 6
    • 0030262825 scopus 로고    scopus 로고
    • Effect of host responses on the pathogenicity of strains of Porphyromonas gingivalis
    • Katz, J., D. C. Ward, and S. M. Michalek. 1996. Effect of host responses on the pathogenicity of strains of Porphyromonas gingivalis. Oral Microbiol. Immunol. 11:309-318.
    • (1996) Oral Microbiol. Immunol. , vol.11 , pp. 309-318
    • Katz, J.1    Ward, D.C.2    Michalek, S.M.3
  • 7
    • 4544334599 scopus 로고    scopus 로고
    • Prevalence of Porphyromonas gingivalis in relation to periodontal status assessed by real-time PCR
    • Kawada, M., A. Yoshida, N. Suzuki, Y. Nakano, T. Saito, T. Oho, and T. Koga. 2004. Prevalence of Porphyromonas gingivalis in relation to periodontal status assessed by real-time PCR. Oral Microbiol. Immunol. 19:289-292.
    • (2004) Oral Microbiol. Immunol. , vol.19 , pp. 289-292
    • Kawada, M.1    Yoshida, A.2    Suzuki, N.3    Nakano, Y.4    Saito, T.5    Oho, T.6    Koga, T.7
  • 9
    • 33646564974 scopus 로고    scopus 로고
    • Effects of various growth conditions in a chemostat on expression of virulence factors in Porphyromonas gingivalis
    • Masuda, T., Y. Murakami, T. Noguchi, and F. Yoshimura. 2006. Effects of various growth conditions in a chemostat on expression of virulence factors in Porphyromonas gingivalis. Appl. Environ. Microbiol. 72:3458-3467.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3458-3467
    • Masuda, T.1    Murakami, Y.2    Noguchi, T.3    Yoshimura, F.4
  • 11
    • 0032407820 scopus 로고    scopus 로고
    • Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: Implications for pathogenicity of periodontal disease
    • Mikolajczyk-Pawlinska, J., J. Travis, and J. Potempa. 1998. Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: implications for pathogenicity of periodontal disease. FEBS Lett. 440:282-286.
    • (1998) FEBS Lett. , vol.440 , pp. 282-286
    • Mikolajczyk-Pawlinska, J.1    Travis, J.2    Potempa, J.3
  • 12
    • 0036550867 scopus 로고    scopus 로고
    • Separation of the outer membrane and identification of major outer membrane proteins from Porphyromonas gingivalis
    • Murakami, Y., M. Imai, H. Nakamura, and F. Yoshimura. 2002. Separation of the outer membrane and identification of major outer membrane proteins from Porphyromonas gingivalis. Eur. J. Oral Sci. 110:157-162.
    • (2002) Eur. J. Oral Sci. , vol.110 , pp. 157-162
    • Murakami, Y.1    Imai, M.2    Nakamura, H.3    Yoshimura, F.4
  • 13
    • 13244289808 scopus 로고    scopus 로고
    • Trimeric structure of major outer membrane proteins homologous to OmpA in Porphyromonas gingivalis
    • Nagano, K., E. K. Read, Y. Murakami, T. Masuda, T. Noguchi, and F. Yoshimura. 2005. Trimeric structure of major outer membrane proteins homologous to OmpA in Porphyromonas gingivalis. J. Bacteriol. 187:902-911.
    • (2005) J. Bacteriol. , vol.187 , pp. 902-911
    • Nagano, K.1    Read, E.K.2    Murakami, Y.3    Masuda, T.4    Noguchi, T.5    Yoshimura, F.6
  • 14
  • 15
    • 0031962568 scopus 로고    scopus 로고
    • Haemoglobin receptor protein is intragenically encoded by the cysteine proteinase-encoding genes and the haemagglutinin-encoding gene of Porphyromonas gingivalis
    • DOI 10.1046/j.1365-2958.1998.00656.x
    • Nakayama, K., D. B. Ratnayake, T. Tsukuba, T. Kadowaki, K. Yamamoto, and S. Fujimura. 1998. Haemoglobin receptor protein is intragenically encoded encoded by the cysteine proteinase-encoding genes and the haemagglutinin- encoding gene of Porphyromonas gingivalis. Mol. Microbiol. 27:51-61. (Pubitemid 28022576)
    • (1998) Molecular Microbiology , vol.27 , Issue.1 , pp. 51-61
    • Nakayama, K.1    Ratnayake, D.B.2    Tsukuba, T.3    Kadowaki, T.4    Yamamoto, K.5    Fujimura, S.6
  • 17
    • 0036302162 scopus 로고    scopus 로고
    • Proteolysis of interleukin-6 receptor (IL-6R) by Porphyromonas gingivalis cysteine proteinases (gingipains) inhibits interleukin-6-mediated cell activation
    • Oleksy, A., A. Banbula, M. Bugno, J. Travis, and J. Potempa. 2002. Proteolysis of interleukin-6 receptor (IL-6R) by Porphyromonas gingivalis cysteine proteinases (gingipains) inhibits interleukin-6-mediated cell activation. Microb. Pathog. 32:173-181.
    • (2002) Microb. Pathog. , vol.32 , pp. 173-181
    • Oleksy, A.1    Banbula, A.2    Bugno, M.3    Travis, J.4    Potempa, J.5
  • 18
    • 0035796406 scopus 로고    scopus 로고
    • Molecular genetic analysis of an endotoxin nonresponder mutant cell line: A point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling
    • Schromm, A. B., E. Lien, P. Henneke, J. C. Chow, A. Yoshimura, H. Heine, E. Latz, B. G. Monks, D. A. Schwartz, K. Miyake, and D. T. Golenbock. 2001. Molecular genetic analysis of an endotoxin nonresponder mutant cell line: a point mutation in a conserved region of MD-2 abolishes endotoxin-induced signaling. J. Exp. Med. 194:79-88.
    • (2001) J. Exp. Med. , vol.194 , pp. 79-88
    • Schromm, A.B.1    Lien, E.2    Henneke, P.3    Chow, J.C.4    Yoshimura, A.5    Heine, H.6    Latz, E.7    Monks, B.G.8    Schwartz, D.A.9    Miyake, K.10    Golenbock, D.T.11
  • 19
    • 0033580821 scopus 로고    scopus 로고
    • Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis: Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA
    • Shi, Y., D. B. Ratnayake, K. Okamoto, N. Abe, K. Yamamoto, and K. Nakayama. 1999. Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA. J. Biol. Chem. 274:17955-17960. (Pubitemid 129519157)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.25 , pp. 17955-17960
    • Shi, Y.1    Ratnayake, D.B.2    Okamoto, K.3    Abe, N.4    Yamamoto, K.5    Nakayama, K.6
  • 21
    • 0034235313 scopus 로고    scopus 로고
    • Proteolysis of human monocyte CD14 by cysteine proteinases (gingipains) from Porphyromonas gingivalis leading to lipopolysaccharide hyporesponsiveness
    • Sugawara, S., E. Nemoto, H. Tada, K. Miyake, T. Imamura, and H. Takada. 2000. Proteolysis of human monocyte CD14 by cysteine proteinases (gingipains) from Porphyromonas gingivalis leading to lipopolysaccharide hyporesponsiveness. J. Immunol. 165:411-418.
    • (2000) J. Immunol. , vol.165 , pp. 411-418
    • Sugawara, S.1    Nemoto, E.2    Tada, H.3    Miyake, K.4    Imamura, T.5    Takada, H.6
  • 22
    • 0021924980 scopus 로고
    • Degradation of human immunoglobulins G and M and complement factors C3 and C5 by black-pigmented bacteroides
    • Sundqvist, G., J. Carlsson, B. Herrmann, and A. Tarnvik. 1985. Degradation of human immunoglobulins G and M and complement factors C3 and C5 by black-pigmented Bacteroides. J. Med. Microbiol. 19:85-94. (Pubitemid 15165235)
    • (1985) Journal of Medical Microbiology , vol.19 , Issue.1 , pp. 85-94
    • Sundqvist, G.1    Carlsson, J.2    Herrmann, B.3    Tarnvik, A.4
  • 23
    • 0036259850 scopus 로고    scopus 로고
    • Proteolysis of CD14 on human gingival fibroblasts by arginine-specific cysteine proteinases from Porphyromonas gingivalis leading to down-regulation of lipopolysaccharide-induced interleukin-8 production
    • Tada, H., S. Sugawara, E. Nemoto, N. Takahashi, T. Imamura, J. Potempa, J. Travis, H. Shimauchi, and H. Takada. 2002. Proteolysis of CD14 on human gingival fibroblasts by arginine-specific cysteine proteinases from Porphyromonas gingivalis leading to down-regulation of lipopolysaccharide- induced interleukin-8 production. Infect. Immun. 70:3304-3307.
    • (2002) Infect. Immun. , vol.70 , pp. 3304-3307
    • Tada, H.1    Sugawara, S.2    Nemoto, E.3    Takahashi, N.4    Imamura, T.5    Potempa, J.6    Travis, J.7    Shimauchi, H.8    Takada, H.9
  • 24
    • 0036533761 scopus 로고    scopus 로고
    • Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50
    • Veith, P. D., G. H. Talbo, N. Slakeski, S. G. Dashper, C. Moore, R. A. Paolini, and E. C. Reynolds. 2002. Major outer membrane proteins and proteolytic processing of RgpA and Kgp of Porphyromonas gingivalis W50. Biochem. J. 363:105-115.
    • (2002) Biochem. J. , vol.363 , pp. 105-115
    • Veith, P.D.1    Talbo, G.H.2    Slakeski, N.3    Dashper, S.G.4    Moore, C.5    Paolini, R.A.6    Reynolds, E.C.7
  • 25
    • 4644245420 scopus 로고    scopus 로고
    • Occurrence of Porphyromonas gingivalis and Tannerella forsythensis in periodontally diseased and healthy subjects
    • Yang, H. W., Y. F. Huang, and M. Y. Chou. 2004. Occurrence of Porphyromonas gingivalis and Tannerella forsythensis in periodontally diseased and healthy subjects. J. Periodontol. 75:1077-1083.
    • (2004) J. Periodontol. , vol.75 , pp. 1077-1083
    • Yang, H.W.1    Huang, Y.F.2    Chou, M.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.