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Volumn 77, Issue 4, 2009, Pages 1417-1425

Analysis of a unique interaction between the complement regulatory protein factor H and the periodontal pathogen treponema denticola

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT; COMPLEMENT COMPONENT C3B; COMPLEMENT FACTOR H; COMPLEMENT FACTOR H LIKE PROTEIN 1; COMPLEMENT FACTOR I; DENTILISIN; LIPOPROTEIN; LIPOPROTEIN FHBB; UNCLASSIFIED DRUG; VIRULENCE FACTOR; BACTERIAL PROTEIN; CHYMOTRYPSIN;

EID: 63149173182     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.01544-08     Document Type: Article
Times cited : (56)

References (76)
  • 2
    • 0036784619 scopus 로고    scopus 로고
    • Complement inhibitor factor H binding to Lyme disease spirochetes is mediated by inducible expression of multiple plasmid- encoded outer surface protein E paralogs
    • Alitalo, A., T. Meri, H. Lankinen, I. Seppala, P. Lahdenne, P. S. Hefty, D. Akins, and S. Meri. 2002. Complement inhibitor factor H binding to Lyme disease spirochetes is mediated by inducible expression of multiple plasmid- encoded outer surface protein E paralogs. J. Immunol. 169:3847-3853.
    • (2002) J. Immunol , vol.169 , pp. 3847-3853
    • Alitalo, A.1    Meri, T.2    Lankinen, H.3    Seppala, I.4    Lahdenne, P.5    Hefty, P.S.6    Akins, D.7    Meri, S.8
  • 3
    • 84986656420 scopus 로고
    • Oral health of US adults: NIDR 1985 national survey
    • Anonymous
    • Anonymous. 1987. Oral health of US adults: NIDR 1985 national survey. J. Public Health Dent. 47:198-205.
    • (1987) J. Public Health Dent , vol.47 , pp. 198-205
  • 4
    • 0037066750 scopus 로고    scopus 로고
    • Streptococcal beta protein has separate binding sites for human factor H and IgA-Fc
    • Areschoug, T., M. Stalhammar-Carlemalm, I. Karlsosson, and G. Lindahl. 2002. Streptococcal beta protein has separate binding sites for human factor H and IgA-Fc. J. Biol. Chem. 277:12642-12648.
    • (2002) J. Biol. Chem , vol.277 , pp. 12642-12648
    • Areschoug, T.1    Stalhammar-Carlemalm, M.2    Karlsosson, I.3    Lindahl, G.4
  • 6
    • 34548502272 scopus 로고    scopus 로고
    • The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation
    • Bamford, C. V., J. C. Fenno, H. F. Jenkinson, and D. Dymock. 2007. The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation. Infect. Immun. 75:4364-4372.
    • (2007) Infect. Immun , vol.75 , pp. 4364-4372
    • Bamford, C.V.1    Fenno, J.C.2    Jenkinson, H.F.3    Dymock, D.4
  • 7
    • 12844278881 scopus 로고    scopus 로고
    • Mutagenesis ofa novel gene inthe prcA-prtP protease locus affects expressionof Treponema denticola membrane complexes
    • Bian, X. L., H. T. Wang, Y. Ning, S. Y. Lee, and J. C. Fenno. 2005. Mutagenesis ofa novel gene inthe prcA-prtP protease locus affects expressionof Treponema denticola membrane complexes. Infect. Immun. 73:1252-1255.
    • (2005) Infect. Immun , vol.73 , pp. 1252-1255
    • Bian, X.L.1    Wang, H.T.2    Ning, Y.3    Lee, S.Y.4    Fenno, J.C.5
  • 8
    • 0025807059 scopus 로고
    • The interaction of salivary secretions with the human complement system-a model for the study of host defense systems on inflamed mucosal surfaces
    • Boackle, R. J. 1991. The interaction of salivary secretions with the human complement system-a model for the study of host defense systems on inflamed mucosal surfaces. Crit. Rev. Oral Biol. Med. 2:355-367.
    • (1991) Crit. Rev. Oral Biol. Med , vol.2 , pp. 355-367
    • Boackle, R.J.1
  • 9
    • 0018188150 scopus 로고
    • The effects of human saliva on the hemolytic activity of complement
    • Boackle, R. J., K. M. Pruitt, M. S. Silverman, and J. L. Glymph, Jr. 1978. The effects of human saliva on the hemolytic activity of complement. J. Dent. Res. 57:103-110.
    • (1978) J. Dent. Res , vol.57 , pp. 103-110
    • Boackle, R.J.1    Pruitt, K.M.2    Silverman, M.S.3    Glymph Jr, J.L.4
  • 10
    • 0142195829 scopus 로고    scopus 로고
    • Role of dentilisin in Treponema denticola epithelial cell layer penetration
    • Chi, B., M. Qi, and H. K. Kuramitsu. 2003. Role of dentilisin in Treponema denticola epithelial cell layer penetration. Res. Microbiol. 154:637-643.
    • (2003) Res. Microbiol , vol.154 , pp. 637-643
    • Chi, B.1    Qi, M.2    Kuramitsu, H.K.3
  • 12
  • 13
    • 2942724425 scopus 로고    scopus 로고
    • Dual roles of PspC, a surface protein of Streptococcus pneumoniae, in binding human secretory IgA and factor H
    • Dave, S., S. Carmicle, S. Hammerschmidt, M. K. Pangburn, and L. S. McDaniel. 2004. Dual roles of PspC, a surface protein of Streptococcus pneumoniae, in binding human secretory IgA and factor H. J. Immunol. 173:471-477.
    • (2004) J. Immunol , vol.173 , pp. 471-477
    • Dave, S.1    Carmicle, S.2    Hammerschmidt, S.3    Pangburn, M.K.4    McDaniel, L.S.5
  • 14
    • 0036786488 scopus 로고    scopus 로고
    • The human complement regulator factor H binds pneumococcal surface protein PspC via short consensus repeats 13 to 15
    • Duthy, T. G., R. J. Ormsby, E. Giannakis, A. D. Ogunniyi, U. H. Stroeher, J. C. Paton, and D. L. Gordon. 2002. The human complement regulator factor H binds pneumococcal surface protein PspC via short consensus repeats 13 to 15. Infect. Immun. 70:5604-5611.
    • (2002) Infect. Immun , vol.70 , pp. 5604-5611
    • Duthy, T.G.1    Ormsby, R.J.2    Giannakis, E.3    Ogunniyi, A.D.4    Stroeher, U.H.5    Paton, J.C.6    Gordon, D.L.7
  • 15
    • 20444440319 scopus 로고    scopus 로고
    • Spirochetes at the forefront of periodontal infections
    • Ellen, R. P., and V. B. Galimanas. 2005. Spirochetes at the forefront of periodontal infections. Periodontol. 2000 38:13-32.
    • (2005) Periodontol. 2000 , vol.38 , pp. 13-32
    • Ellen, R.P.1    Galimanas, V.B.2
  • 16
    • 0033764688 scopus 로고    scopus 로고
    • Insertional inactivation of the prtP gene of Treponema denticola confirms dentilisin's disruption of epithelial junctions
    • Ellen, R. P., K. S. Ko, C. M. Lo, D. A. Grove, and K. Ishihara. 2000. Insertional inactivation of the prtP gene of Treponema denticola confirms dentilisin's disruption of epithelial junctions. J. Mol. Microbiol. Biotech. 2:581-586.
    • (2000) J. Mol. Microbiol. Biotech , vol.2 , pp. 581-586
    • Ellen, R.P.1    Ko, K.S.2    Lo, C.M.3    Grove, D.A.4    Ishihara, K.5
  • 17
    • 0031900968 scopus 로고    scopus 로고
    • Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola
    • Fenno, J. C., P. M. Hannam, W. K. Leung, M. Tamura, V. J. Uitto, and B. C. McBride. 1998. Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola. Infect. Immun. 66:1869-1877.
    • (1998) Infect. Immun , vol.66 , pp. 1869-1877
    • Fenno, J.C.1    Hannam, P.M.2    Leung, W.K.3    Tamura, M.4    Uitto, V.J.5    McBride, B.C.6
  • 18
    • 0034832886 scopus 로고    scopus 로고
    • The opdB locus encodes the trypsin-like peptidase activity of Treponema denticola
    • Fenno, J. C., S. Y. Lee, C. H. Bayer, and Y. Ning. 2001. The opdB locus encodes the trypsin-like peptidase activity of Treponema denticola. Infect. Immun. 69:6193-6200.
    • (2001) Infect. Immun , vol.69 , pp. 6193-6200
    • Fenno, J.C.1    Lee, S.Y.2    Bayer, C.H.3    Ning, Y.4
  • 19
    • 0032526403 scopus 로고    scopus 로고
    • 19. Fenno, J. C., G. W. Wong, P. M. Hannam, and B. C. McBride. 1998. Mutagenesis of outer membrane virulence determinants of the oral spirochete reponema denticola. FEMS Microbiol. Lett. 163:209-215.
    • 19. Fenno, J. C., G. W. Wong, P. M. Hannam, and B. C. McBride. 1998. Mutagenesis of outer membrane virulence determinants of the oral spirochete reponema denticola. FEMS Microbiol. Lett. 163:209-215.
  • 20
    • 0028804370 scopus 로고    scopus 로고
    • 20. Fischetti, V. A., R. D. Horstmann, and V. Pancholi. 1995. Location of the complement factor H binding site on streptococcal M6 protein. Infect. Immun 63:149-154.
    • 20. Fischetti, V. A., R. D. Horstmann, and V. Pancholi. 1995. Location of the complement factor H binding site on streptococcal M6 protein. Infect. Immun 63:149-154.
  • 22
    • 0025117758 scopus 로고
    • Cellular location of a Treponema denticola chymotrypsinlike protease and importance of the protease in migration through the basement membrane
    • Grenier, D., V. J. Uitto, and B. C. McBride. 1990. Cellular location of a Treponema denticola chymotrypsinlike protease and importance of the protease in migration through the basement membrane. Infect. Immun. 58:347-351.
    • (1990) Infect. Immun , vol.58 , pp. 347-351
    • Grenier, D.1    Uitto, V.J.2    McBride, B.C.3
  • 23
    • 34247573934 scopus 로고    scopus 로고
    • The host immune regulator factor H interacts via two contact sites with the PspC protein of Streptococcus pneumoniae and mediates adhesion to host epithelial cells
    • Hammerschmidt, S., V. Agarwal, A. Kunert, S. Haelbich, C. Skerka, and P. Zipfel. 2007. The host immune regulator factor H interacts via two contact sites with the PspC protein of Streptococcus pneumoniae and mediates adhesion to host epithelial cells. J. Immunol. 178:5848-5858.
    • (2007) J. Immunol , vol.178 , pp. 5848-5858
    • Hammerschmidt, S.1    Agarwal, V.2    Kunert, A.3    Haelbich, S.4    Skerka, C.5    Zipfel, P.6
  • 24
    • 33747057122 scopus 로고    scopus 로고
    • 24. Hartmann, K., C. Corvey, C. Skerka, M. Kirschfink, M. Karas, V. Brade, J. C. Miller, B. Stevenson, R. Wallich, P. F. Zipfel, and P. Kraiczy. 2006. Functional characterization of BbCRASP-2, a distinct outer membrane protein of Borrelia burgdorferi that binds host complement regulators factor H and FHL-1. Mol. Microbiol. 61:1220-1236.
    • 24. Hartmann, K., C. Corvey, C. Skerka, M. Kirschfink, M. Karas, V. Brade, J. C. Miller, B. Stevenson, R. Wallich, P. F. Zipfel, and P. Kraiczy. 2006. Functional characterization of BbCRASP-2, a distinct outer membrane protein of Borrelia burgdorferi that binds host complement regulators factor H and FHL-1. Mol. Microbiol. 61:1220-1236.
  • 25
    • 0642377572 scopus 로고    scopus 로고
    • 25. Hashimoto, M., S. Ogawa, Y. Asai, Y. Takai, and T. Ogawa. 2003. Bindingof Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin. FEMS Microbiol. Lett. 226:267-271.
    • 25. Hashimoto, M., S. Ogawa, Y. Asai, Y. Takai, and T. Ogawa. 2003. Bindingof Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin. FEMS Microbiol. Lett. 226:267-271.
  • 28
    • 0343017792 scopus 로고    scopus 로고
    • 28. Horstmann, R. D., H. J. Sievertsen, J. Knobloch, and V. A. Fischetti. 1988. Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc. Natl. Acad. Sci. USA 85:1657-1661.
    • 28. Horstmann, R. D., H. J. Sievertsen, J. Knobloch, and V. A. Fischetti. 1988. Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc. Natl. Acad. Sci. USA 85:1657-1661.
  • 29
    • 42949116992 scopus 로고    scopus 로고
    • 29. Hovis, K. M., J. C. Freedman, H. Zhang, J. L. Forbes, and R. T. Marconi. 2008. Identification of an antiparallel coiled-coil/loop domain required for ligand binding by the Borrelia hermsii FhbA protein: additional evidence for the role of FhbA in the host-pathogen interaction. Infect. Immun. 76:2113-2122.
    • 29. Hovis, K. M., J. C. Freedman, H. Zhang, J. L. Forbes, and R. T. Marconi. 2008. Identification of an antiparallel coiled-coil/loop domain required for ligand binding by the Borrelia hermsii FhbA protein: additional evidence for the role of FhbA in the host-pathogen interaction. Infect. Immun. 76:2113-2122.
  • 30
    • 33645509329 scopus 로고    scopus 로고
    • Molecular analyses of the interaction of Borrelia hermsii FhbA with the complement regulatory proteins factor H and factor H-like protein 1
    • Hovis, K. M., J. P. Jones, T. Sadlon, G. Raval, D. L. Gordon, and R. T. Marconi. 2006. Molecular analyses of the interaction of Borrelia hermsii FhbA with the complement regulatory proteins factor H and factor H-like protein 1. Infect. Immun. 74:2007-2014.
    • (2006) Infect. Immun , vol.74 , pp. 2007-2014
    • Hovis, K.M.1    Jones, J.P.2    Sadlon, T.3    Raval, G.4    Gordon, D.L.5    Marconi, R.T.6
  • 31
    • 1942508082 scopus 로고    scopus 로고
    • Identification and characterization of a linear-plasmid-encoded factor H-binding protein (FhbA) of the relapsing fever spirochete Borrelia hermsii
    • Hovis, K. M., J. V. McDowell, L. Griffin, and R. T. Marconi. 2004. Identification and characterization of a linear-plasmid-encoded factor H-binding protein (FhbA) of the relapsing fever spirochete Borrelia hermsii. J. Bacteriol. 186:2612-2618.
    • (2004) J. Bacteriol , vol.186 , pp. 2612-2618
    • Hovis, K.M.1    McDowell, J.V.2    Griffin, L.3    Marconi, R.T.4
  • 32
    • 33746585279 scopus 로고    scopus 로고
    • Immunological and molecular analyses of the Borrelia hermsii factor H and factor H-like protein 1 binding protein, FhbA: Demonstration of its utility as a diagnostic marker and epidemiological tool for tick-borne relapsing fever
    • Hovis, K. M., M. E. Schriefer, S. Bahlani, and R. T. Marconi. 2006. Immunological and molecular analyses of the Borrelia hermsii factor H and factor H-like protein 1 binding protein, FhbA: demonstration of its utility as a diagnostic marker and epidemiological tool for tick-borne relapsing fever. Infect. Immun. 74:4519-4529.
    • (2006) Infect. Immun , vol.74 , pp. 4519-4529
    • Hovis, K.M.1    Schriefer, M.E.2    Bahlani, S.3    Marconi, R.T.4
  • 33
    • 1842524063 scopus 로고    scopus 로고
    • A 43-kDa protein of Treponema denticola is essential for dentilisin activity
    • Ishihara, K., H. Kuramitsu, and K. Okuda. 2004. A 43-kDa protein of Treponema denticola is essential for dentilisin activity. FEMS Microbiol. Lett. 232:181-188.
    • (2004) FEMS Microbiol. Lett , vol.232 , pp. 181-188
    • Ishihara, K.1    Kuramitsu, H.2    Okuda, K.3
  • 34
    • 0029833178 scopus 로고    scopus 로고
    • Characterization of the Treponema denticola prtP gene encoding a prolyl-phenylala- nine-specific protease (dentilisin)
    • Ishihara, K., T. Miura, H. K. Kuramitsu, and K. Okuda. 1996. Characterization of the Treponema denticola prtP gene encoding a prolyl-phenylala- nine-specific protease (dentilisin). Infect. Immun. 64:5178-5186.
    • (1996) Infect. Immun , vol.64 , pp. 5178-5186
    • Ishihara, K.1    Miura, T.2    Kuramitsu, H.K.3    Okuda, K.4
  • 35
    • 47749126514 scopus 로고    scopus 로고
    • Factor H family proteins and human diseases
    • Jozsi, M., and P. F. Zipfel. 2008. Factor H family proteins and human diseases. Trends Immunol. 29:380-387.
    • (2008) Trends Immunol , vol.29 , pp. 380-387
    • Jozsi, M.1    Zipfel, P.F.2
  • 36
    • 1642535449 scopus 로고    scopus 로고
    • Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins
    • Kraiczy, P., J. Hellwage, C. Skerka, H. Becker, M. Kirschfink, M. S. Simon, V. Brade, P. F. Zipfel, and R. Wallich. 2004. Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins. J. Biol. Chem. 279:2421-2429.
    • (2004) J. Biol. Chem , vol.279 , pp. 2421-2429
    • Kraiczy, P.1    Hellwage, J.2    Skerka, C.3    Becker, H.4    Kirschfink, M.5    Simon, M.S.6    Brade, V.7    Zipfel, P.F.8    Wallich, R.9
  • 37
    • 22644433305 scopus 로고    scopus 로고
    • Complement escape of human pathogenic bacteria by acquisition of complement regulators
    • Kraiczy, P., and R. Wurzner. 2006. Complement escape of human pathogenic bacteria by acquisition of complement regulators. Mol. Immunol. 43:31-44.
    • (2006) Mol. Immunol , vol.43 , pp. 31-44
    • Kraiczy, P.1    Wurzner, R.2
  • 38
    • 0036302650 scopus 로고    scopus 로고
    • Cleavage of Treponema denticola PrcA polypeptide to yield protease complex-associated proteins Prca1 and Prca2 is dependent on PrtP
    • Lee, S. Y., X. L. Bian, G. W. Wong, P. M. Hannam, B. C. McBride, and J. C. Fenno. 2002. Cleavage of Treponema denticola PrcA polypeptide to yield protease complex-associated proteins Prca1 and Prca2 is dependent on PrtP. J. Bacteriol. 184:3864-3870.
    • (2002) J. Bacteriol , vol.184 , pp. 3864-3870
    • Lee, S.Y.1    Bian, X.L.2    Wong, G.W.3    Hannam, P.M.4    McBride, B.C.5    Fenno, J.C.6
  • 39
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science 252:1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 40
    • 0030000004 scopus 로고    scopus 로고
    • The peptidolytic capacity of the spirochete system
    • Muakinen, K. K., and P. L. Muakinen. 1996. The peptidolytic capacity of the spirochete system. Med. Microbiol. Immunol. 185:1-10.
    • (1996) Med. Microbiol. Immunol , vol.185 , pp. 1-10
    • Muakinen, K.K.1    Muakinen, P.L.2
  • 41
    • 0026629301 scopus 로고
    • Purification and substrate specificity of an endopeptidase from the human oral spirochete Treponema denticola ATCC 35405, active on furylacryloyl-Leu-Gly-Pro-Ala and bradykinin
    • MUkinen, K. K., P. L. MUkinen, and S. A. Syed. 1992. Purification and substrate specificity of an endopeptidase from the human oral spirochete Treponema denticola ATCC 35405, active on furylacryloyl-Leu-Gly-Pro-Ala and bradykinin. J. Biol. Chem. 267:14285-14293.
    • (1992) J. Biol. Chem , vol.267 , pp. 14285-14293
    • MUkinen, K.K.1    MUkinen, P.L.2    Syed, S.A.3
  • 42
    • 0027959709 scopus 로고
    • An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: Evidence of hydrolysis of human bioactive peptides
    • MUkinen, P. L., K. K. MUkinen, and S. A. Syed. 1994. An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides. Infect. Immun. 62:4938-4947.
    • (1994) Infect. Immun , vol.62 , pp. 4938-4947
    • MUkinen, P.L.1    MUkinen, K.K.2    Syed, S.A.3
  • 43
    • 33846816479 scopus 로고    scopus 로고
    • Identification of the gene encoding the FhbB protein of Treponema denticola,a highly unique factor H-like protein 1 binding protein
    • McDowell, J. V., J. Frederick, L. Stamm, and R. T. Marconi. 2007. Identification of the gene encoding the FhbB protein of Treponema denticola,a highly unique factor H-like protein 1 binding protein. Infect. Immun. 75:1050-1054.
    • (2007) Infect. Immun , vol.75 , pp. 1050-1054
    • McDowell, J.V.1    Frederick, J.2    Stamm, L.3    Marconi, R.T.4
  • 44
    • 14544300067 scopus 로고    scopus 로고
    • Putative coiled-coil structural elements of the BBA68 protein of Lyme disease spirochetes are required for formation of its factor H binding site
    • McDowell, J. V., M. E. Harlin, E. A. Rogers, and R. T. Marconi. 2005. Putative coiled-coil structural elements of the BBA68 protein of Lyme disease spirochetes are required for formation of its factor H binding site. J. Bacteriol. 187:1317-1323.
    • (2005) J. Bacteriol , vol.187 , pp. 1317-1323
    • McDowell, J.V.1    Harlin, M.E.2    Rogers, E.A.3    Marconi, R.T.4
  • 45
    • 33646370724 scopus 로고    scopus 로고
    • Evidencethat the BBA68 protein (BbCRASP-1) of the Lyme disease spirochetes does not contribute to factor H-mediated immune evasion in humans and other animals
    • McDowell, J. V., K. M. Hovis, H. Zhang, E. Tran, J. Lankford, and R. T. Marconi. 2006. Evidencethat the BBA68 protein (BbCRASP-1) of the Lyme disease spirochetes does not contribute to factor H-mediated immune evasion in humans and other animals. Infect. Immun. 74:3030-3034.
    • (2006) Infect. Immun , vol.74 , pp. 3030-3034
    • McDowell, J.V.1    Hovis, K.M.2    Zhang, H.3    Tran, E.4    Lankford, J.5    Marconi, R.T.6
  • 46
    • 0042023209 scopus 로고    scopus 로고
    • Analysis of the ability of spirochete species associated with relapsing fever, avian borreliosis, and epizootic bovine abortion to bind factor H and cleave c3b
    • McDowell, J. V., E. Tran, D. Hamilton, J. Wolfgang, K. Miller, and R. T. Marconi. 2003. Analysis of the ability of spirochete species associated with relapsing fever, avian borreliosis, and epizootic bovine abortion to bind factor H and cleave c3b. J. Clin. Microbiol. 41:3905-3910.
    • (2003) J. Clin. Microbiol , vol.41 , pp. 3905-3910
    • McDowell, J.V.1    Tran, E.2    Hamilton, D.3    Wolfgang, J.4    Miller, K.5    Marconi, R.T.6
  • 47
    • 10344228235 scopus 로고    scopus 로고
    • Demonstration of the involvement of outer surface protein E coiled coil structural domains and higher order structural elements in the binding of infection-induced antibody and the complement-regulatory protein, factor H
    • McDowell, J. V., J. Wolfgang, L. Senty, C. M. Sundy, M. J. Noto, and R. T. Marconi. 2004. Demonstration of the involvement of outer surface protein E coiled coil structural domains and higher order structural elements in the binding of infection-induced antibody and the complement-regulatory protein, factor H. J. Immunol. 173:7471-7480.
    • (2004) J. Immunol , vol.173 , pp. 7471-7480
    • McDowell, J.V.1    Wolfgang, J.2    Senty, L.3    Sundy, C.M.4    Noto, M.J.5    Marconi, R.T.6
  • 48
    • 0037512361 scopus 로고    scopus 로고
    • Comprehensive analysis of the factor H binding capabilities of Borrelia species associated with Lyme disease: Delineation of two distinct classes of factor H binding proteins
    • McDowell, J. V., J. Wolfgang, E. Tran, M. S. Metts, D. Hamilton, and R. T. Marconi. 2003. Comprehensive analysis of the factor H binding capabilities of Borrelia species associated with Lyme disease: delineation of two distinct classes of factor H binding proteins. Infect. Immun. 71:3597-3602.
    • (2003) Infect. Immun , vol.71 , pp. 3597-3602
    • McDowell, J.V.1    Wolfgang, J.2    Tran, E.3    Metts, M.S.4    Hamilton, D.5    Marconi, R.T.6
  • 49
    • 33745596147 scopus 로고    scopus 로고
    • Relapsing fever spirochetes Borrelia recurrentis and B. duttonii acquire complement regulators C4b-binding protein and factor H
    • Meri, T., S. J. Cutler, A. M. Blom, S. Meri, and T. S. Jokiranta. 2006. Relapsing fever spirochetes Borrelia recurrentis and B. duttonii acquire complement regulators C4b-binding protein and factor H. Infect. Immun. 74: 4157-4163.
    • (2006) Infect. Immun , vol.74 , pp. 4157-4163
    • Meri, T.1    Cutler, S.J.2    Blom, A.M.3    Meri, S.4    Jokiranta, T.S.5
  • 51
    • 0037097649 scopus 로고    scopus 로고
    • nchocerca volvulus microfilariae avoid complement attack by direct inding of factor H
    • Meri, T., T. S. Jokiranta, J. Hellwage, A. Bialonski, P. F. Zipfel, and S. Meri. 2002. nchocerca volvulus microfilariae avoid complement attack by direct inding of factor H. J. Infect. Dis. 185:1786-1793.
    • (2002) J. Infect. Dis , vol.185 , pp. 1786-1793
    • Meri, T.1    Jokiranta, T.S.2    Hellwage, J.3    Bialonski, A.4    Zipfel, P.F.5    Meri, S.6
  • 52
    • 0037512362 scopus 로고    scopus 로고
    • nalysis of the Osp Edeterminantsin volvedin binding of factor Hand OspE-targeting antibodies elicited during Borrelia burgdorferi infection in ice
    • Metts, M. S., J. V. McDowell, M. Theisen, P. R. Hansen, and R. T. Marconi. 2003. nalysis of the Osp Edeterminantsin volvedin binding of factor Hand OspE-targeting antibodies elicited during Borrelia burgdorferi infection in ice. Infect. Immun. 71:3587-3596.
    • (2003) Infect. Immun , vol.71 , pp. 3587-3596
    • Metts, M.S.1    McDowell, J.V.2    Theisen, M.3    Hansen, P.R.4    Marconi, R.T.5
  • 53
    • 33645520537 scopus 로고    scopus 로고
    • Miyamoto, M., K. Ishihara, and K. Okuda. 2006. The Treponema denticola surface protease dentilisin degrades interleukin-1|3 (IL-1|3), IL-6, and tumor necrosis factor alpha. Infect. Immun. 74:2462-2467.
    • Miyamoto, M., K. Ishihara, and K. Okuda. 2006. The Treponema denticola surface protease dentilisin degrades interleukin-1|3 (IL-1|3), IL-6, and tumor necrosis factor alpha. Infect. Immun. 74:2462-2467.
  • 54
    • 0022477095 scopus 로고
    • Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates
    • Ohta, K., K. K. MUkinen, and W. J. Loesche. 1986. Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates. Infect. Immun. 53:213-220.
    • (1986) Infect. Immun , vol.53 , pp. 213-220
    • Ohta, K.1    MUkinen, K.K.2    Loesche, W.J.3
  • 55
    • 0345714694 scopus 로고    scopus 로고
    • Recruitment of complement factor H-like protein 1 promotes intracellular invasion by group A streptococci
    • Pandiripally, V., L. Wei, C. Skerka, P. F. Zipfel, and D. Cue. 2003. Recruitment of complement factor H-like protein 1 promotes intracellular invasion by group A streptococci. Infect. Immun. 71:7119-7128.
    • (2003) Infect. Immun , vol.71 , pp. 7119-7128
    • Pandiripally, V.1    Wei, L.2    Skerka, C.3    Zipfel, P.F.4    Cue, D.5
  • 56
    • 0017704496 scopus 로고    scopus 로고
    • Pangburn, M. K., R. D. Schreiber, and H. J. Muller-Eberhard. 1977. Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein |31H for cleavage of C3b nd C4b in solution. J. Exp. Med. 146:257-270.
    • Pangburn, M. K., R. D. Schreiber, and H. J. Muller-Eberhard. 1977. Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein |31H for cleavage of C3b nd C4b in solution. J. Exp. Med. 146:257-270.
  • 58
    • 33747853795 scopus 로고    scopus 로고
    • The breadth of bacterial diversity in the human periodontal pocket and other oral sites
    • Paster, B. J., I. Olsen, J. A. Aas, and F. E. Dewhirst. 2006. The breadth of bacterial diversity in the human periodontal pocket and other oral sites. Periodontol. 2000 42:80-87.
    • (2006) Periodontol. 2000 , vol.42 , pp. 80-87
    • Paster, B.J.1    Olsen, I.2    Aas, J.A.3    Dewhirst, F.E.4
  • 59
    • 38049134765 scopus 로고    scopus 로고
    • Gpm1p is a factor H, FHL-1 and plasminogen-binding surface protein of Candida albicans
    • Poltermann, S., A. Kunert, M. von der Heide, R. Eck, A. Hartmann, and P. F. Zipfel. 2007. Gpm1p is a factor H, FHL-1 and plasminogen-binding surface protein of Candida albicans. J. Biol. Chem. 282:37537- 37544.
    • (2007) J. Biol. Chem , vol.282 , pp. 37537-37544
    • Poltermann, S.1    Kunert, A.2    von der Heide, M.3    Eck, R.4    Hartmann, A.5    Zipfel, P.F.6
  • 60
    • 34547620337 scopus 로고    scopus 로고
    • Factor H binding to PspC of Streptococcus pneumoniae increases adherence to human cell lines in vitro and enhances invasion of mouse lungs in vivo
    • Quin, L. R., C. Onwubiko, Q. C. Moore, M. F. Mills, L. S. McDaniel, and S. Carmicle. 2007. Factor H binding to PspC of Streptococcus pneumoniae increases adherence to human cell lines in vitro and enhances invasion of mouse lungs in vivo. Infect. Immun. 75:4082-4087.
    • (2007) Infect. Immun , vol.75 , pp. 4082-4087
    • Quin, L.R.1    Onwubiko, C.2    Moore, Q.C.3    Mills, M.F.4    McDaniel, L.S.5    Carmicle, S.6
  • 61
    • 0032541390 scopus 로고    scopus 로고
    • Binding of complement factor H to loop 5 of porin protein 1A: A molecular mechanism of serum resistance of nonsialylated Neisseria gonorrhoeae
    • Ram, S., D. P. McQuillen, S. Gulati, C. Elkins, M. K. Pangburn, and P. A. Rice. 1998. Binding of complement factor H to loop 5 of porin protein 1A: a molecular mechanism of serum resistance of nonsialylated Neisseria gonorrhoeae. J. Exp. Med. 188:671-680.
    • (1998) J. Exp. Med , vol.188 , pp. 671-680
    • Ram, S.1    McQuillen, D.P.2    Gulati, S.3    Elkins, C.4    Pangburn, M.K.5    Rice, P.A.6
  • 62
    • 0032473556 scopus 로고    scopus 로고
    • A novel sialic acid binding site on factor H mediates serum resistance of non-sialylated Neisseria gonorrhoeae
    • Ram, S., A. K. Sharma, and S. D. Simpson. 1998. A novel sialic acid binding site on factor H mediates serum resistance of non-sialylated Neisseria gonorrhoeae. J. Exp. Med. 187:743-752.
    • (1998) J. Exp. Med , vol.187 , pp. 743-752
    • Ram, S.1    Sharma, A.K.2    Simpson, S.D.3
  • 63
    • 35648980024 scopus 로고    scopus 로고
    • Delineation of species-specific binding properties of the CspZ protein (BBH06) of Lyme disease spiro- chetes: Evidence for new contributions to the pathogenesis of Borrelia spp
    • Rogers, E. A., and R. T. Marconi. 2007. Delineation of species-specific binding properties of the CspZ protein (BBH06) of Lyme disease spiro- chetes: evidence for new contributions to the pathogenesis of Borrelia spp. Infect. Immun. 75:5272-5281.
    • (2007) Infect. Immun , vol.75 , pp. 5272-5281
    • Rogers, E.A.1    Marconi, R.T.2
  • 64
    • 0029116782 scopus 로고
    • Proteases of Treponema denticola outer sheath and extracellular vesicles
    • Rosen, G., R. Naor, E. Rahamim, R. Yishai, and M. N. Sela. 1995. Proteases of Treponema denticola outer sheath and extracellular vesicles. Infect. Immun. 63:3973-3979.
    • (1995) Infect. Immun , vol.63 , pp. 3973-3979
    • Rosen, G.1    Naor, R.2    Rahamim, E.3    Yishai, R.4    Sela, M.N.5
  • 65
    • 34249797276 scopus 로고    scopus 로고
    • Dual binding specificity of a Borrelia hermsii-associated complement regulator-acquiring surface protein for factor H and plasminogen discloses a putative virulence factor of relapsing fever spirochetes
    • Rossmann, E., P. Kraiczy, P. Herzberger, C. Skerka, M. Kirschfink, M. M. Simon, P. F. Zipfel, and R. Wallich. 2007. Dual binding specificity of a Borrelia hermsii-associated complement regulator-acquiring surface protein for factor H and plasminogen discloses a putative virulence factor of relapsing fever spirochetes. J. Immunol. 178:7292-7301.
    • (2007) J. Immunol , vol.178 , pp. 7292-7301
    • Rossmann, E.1    Kraiczy, P.2    Herzberger, P.3    Skerka, C.4    Kirschfink, M.5    Simon, M.M.6    Zipfel, P.F.7    Wallich, R.8
  • 66
    • 0014477569 scopus 로고
    • C3 inactivator of man. I. Hemolytic measurement by the inactivation of cell-bound C3
    • Ruddy, S., and K. F. Austen. 1969. C3 inactivator of man. I. Hemolytic measurement by the inactivation of cell-bound C3. J. Immunol. 102:533-543.
    • (1969) J. Immunol , vol.102 , pp. 533-543
    • Ruddy, S.1    Austen, K.F.2
  • 67
    • 0015123385 scopus 로고
    • C3b inactivator of man. II. Fragments produced by C3b inactivator cleavage of cell-bound or fluid phase C3b
    • Ruddy, S., and K. F. Austen. 1971. C3b inactivator of man. II. Fragments produced by C3b inactivator cleavage of cell-bound or fluid phase C3b. J. Immunol. 107:742-750.
    • (1971) J. Immunol , vol.107 , pp. 742-750
    • Ruddy, S.1    Austen, K.F.2
  • 68
    • 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.
    • (1977) J. Periodontol , vol.48 , pp. 772-777
    • Schenkein, H.A.1    Genco, R.J.2
  • 69
    • 58449121716 scopus 로고    scopus 로고
    • Factor H-binding protein is important for meningococcal survival in human whole blood and serum, and in the presence of the antimicrobial peptide LL-37
    • Seib, K. L., D. Serruto, F. Oriente, I. Delany, J. Adu-Bobie, D. Veggi, B. Arico, R. Rappuoli, and M. Pizza. 2009. Factor H-binding protein is important for meningococcal survival in human whole blood and serum, and in the presence of the antimicrobial peptide LL-37. Infect. Immun. 77:292-299.
    • (2009) Infect. Immun , vol.77 , pp. 292-299
    • Seib, K.L.1    Serruto, D.2    Oriente, F.3    Delany, I.4    Adu-Bobie, J.5    Veggi, D.6    Arico, B.7    Rappuoli, R.8    Pizza, M.9
  • 70
    • 58049216337 scopus 로고    scopus 로고
    • Deciphering the ligand-binding sites in the Borrelia burgdorferi complement regulator- acquiring surface protein 2 (BbCRASP-2) required for interactions with the human immune regulators factor H and factor H-Like protein 1
    • Siegel, C., J. Schreiber, K. Haupt, C. Skerka, V. Brade, M. M. Simon, B. Stevenson, R. Wallich, P. F. Zipfel, and P. Kraiczy. 2008. Deciphering the ligand-binding sites in the Borrelia burgdorferi complement regulator- acquiring surface protein 2 (BbCRASP-2) required for interactions with the human immune regulators factor H and factor H-Like protein 1. J. Biol. Chem. 283:34855-34863.
    • (2008) J. Biol. Chem , vol.283 , pp. 34855-34863
    • Siegel, C.1    Schreiber, J.2    Haupt, K.3    Skerka, C.4    Brade, V.5    Simon, M.M.6    Stevenson, B.7    Wallich, R.8    Zipfel, P.F.9    Kraiczy, P.10
  • 71
    • 35348980673 scopus 로고    scopus 로고
    • Trouw, L. A., A. A. Bengtsson, K. A. Gelderman, B. Dahlback, G. Sturfelt, andA.M.Blom. 2007. C4b-bindingprotein and factor Hcompensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack. J. Biol. Chem. 282:28540-28548.
    • Trouw, L. A., A. A. Bengtsson, K. A. Gelderman, B. Dahlback, G. Sturfelt, andA.M.Blom. 2007. C4b-bindingprotein and factor Hcompensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack. J. Biol. Chem. 282:28540-28548.
  • 72
    • 0023791265 scopus 로고
    • Isolation of a chymotrypsinlike enzyme from Treponema denticola
    • Uitto, V. J., D. Grenier, E. C. Chan, and B. C. McBride. 1988. Isolation of a chymotrypsinlike enzyme from Treponema denticola. Infect. Immun. 56:2717-2722.
    • (1988) Infect. Immun , vol.56 , pp. 2717-2722
    • Uitto, V.J.1    Grenier, D.2    Chan, E.C.3    McBride, B.C.4
  • 73
    • 0037315708 scopus 로고    scopus 로고
    • Resolution of inflammation: A new paradigm for the pathogenesis of periodontal diseases
    • Van Dyke, T. E., and C. N. Serhan. 2003. Resolution of inflammation: a new paradigm for the pathogenesis of periodontal diseases. J. Dent. Res. 82:82-90.
    • (2003) J. Dent. Res , vol.82 , pp. 82-90
    • Van Dyke, T.E.1    Serhan, C.N.2
  • 74
    • 0017139872 scopus 로고
    • Modulation of the alternative complement pathways by β1H globulin
    • Whaley, K., and S. Ruddy. 1976. Modulation of the alternative complement pathways by β1H globulin. J. Exp. Med. 144:1147-1163.
    • (1976) J. Exp. Med , vol.144 , pp. 1147-1163
    • Whaley, K.1    Ruddy, S.2
  • 75
    • 33746395470 scopus 로고    scopus 로고
    • Surface protease of Treponema denticola hydrolyzes C3 and influences function of polymorphonuclear leukocytes
    • Yamazaki, T., M. Miyamoto, S. Yamada, K. Okuda, and K. Ishihara. 2006. Surface protease of Treponema denticola hydrolyzes C3 and influences function of polymorphonuclear leukocytes. Microbes Infect. 8:1758-1763.
    • (2006) Microbes Infect , vol.8 , pp. 1758-1763
    • Yamazaki, T.1    Miyamoto, M.2    Yamada, S.3    Okuda, K.4    Ishihara, K.5


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