메뉴 건너뛰기




Volumn 17, Issue 4, 2011, Pages 502-512

New insights into the emerging role of oral spirochaetes in periodontal disease

Author keywords

Oral; Pathogenesis; Periodontitis; Review; Spirochaete; Treponema; Virulence

Indexed keywords

ALVEOLAR BONE LOSS; BACTERIAL VIRULENCE; HUMAN; PERIODONTAL DISEASE; PRIORITY JOURNAL; REVIEW; SOFT TISSUE INJURY; SPIROCHETE; SPIROCHETE INFECTION; TREPONEMA DENTICOLA;

EID: 79952729069     PISSN: 1198743X     EISSN: 14690691     Source Type: Journal    
DOI: 10.1111/j.1469-0691.2011.03460.x     Document Type: Review
Times cited : (61)

References (154)
  • 1
  • 2
    • 72449208157 scopus 로고    scopus 로고
    • The phylogenetic diversity of the genus Treponema
    • Radolf JD, Lukehart SA, eds. Wymondham, UK: Caister Academic Press
    • Paster BJ, Dewhirst FE. The phylogenetic diversity of the genus Treponema. In: Radolf JD, Lukehart SA, eds. Pathogenic Treponema molecular and cellular biology. Wymondham, UK: Caister Academic Press, 2006; 9-18.
    • (2006) Pathogenic Treponema molecular and cellular biology , pp. 9-18
    • Paster, B.J.1    Dewhirst, F.E.2
  • 3
  • 4
    • 0027416360 scopus 로고
    • Treponema denticola (ex brumpt 1925) sp. Nov., nom. Rev., and identification of new spirochete isolates from periodontal pockets
    • Chan EC, Siboo R, Keng T et al. Treponema denticola (ex brumpt 1925) sp. Nov., nom. Rev., and identification of new spirochete isolates from periodontal pockets. Int J Syst Bacteriol 1993; 43: 196-203.
    • (1993) Int J Syst Bacteriol , vol.43 , pp. 196-203
    • Chan, E.C.1    Siboo, R.2    Keng, T.3
  • 5
    • 0021056168 scopus 로고
    • Treponema pectinovorum sp. Nov. isolated from humans with periodontitis
    • Smibert RM, Burmeister JA. Treponema pectinovorum sp. Nov. isolated from humans with periodontitis. Int J Syst Bacteriol 1983; 33: 852-856.
    • (1983) Int J Syst Bacteriol , vol.33 , pp. 852-856
    • Smibert, R.M.1    Burmeister, J.A.2
  • 6
    • 0021179551 scopus 로고
    • Treponema socranskii sp. Nov., Treponema socranskii subsp. Socranksii subsp. Nov., Treponema socranskii subsp. Buccale subsp. Nov., Treponema socranskii subsp. Paredis subsp. Nov. isolated form the human periodontia
    • Smibert RM, Johnson JL, Ranney RR. Treponema socranskii sp. Nov., Treponema socranskii subsp. Socranksii subsp. Nov., Treponema socranskii subsp. Buccale subsp. Nov., Treponema socranskii subsp. Paredis subsp. Nov. isolated form the human periodontia. Int J Syst Bacteriol 1984; 34: 457-462.
    • (1984) Int J Syst Bacteriol , vol.34 , pp. 457-462
    • Smibert, R.M.1    Johnson, J.L.2    Ranney, R.R.3
  • 7
    • 0001781079 scopus 로고
    • Genus iii. Treponema schaudinn 1905, 1728
    • Kreig N, Holt J, eds. Baltimore: Williams & Wilkins
    • Smibert RM. Genus iii. Treponema schaudinn 1905, 1728. In: Kreig N, Holt J, eds. Bergey's manual of systematic bacteriology. Baltimore: Williams & Wilkins, 1984; 49-57.
    • (1984) Bergey's manual of systematic bacteriology , pp. 49-57
    • Smibert, R.M.1
  • 8
    • 0032733070 scopus 로고    scopus 로고
    • Treponema lecithinolyticum sp. Nov., a small saccharolytic spirochaete with phospholipase a and c activities associated with periodontal diseases
    • Wyss C, Choi BK, Schupbach P, Moter A, Guggenheim B, Gobel UB. Treponema lecithinolyticum sp. Nov., a small saccharolytic spirochaete with phospholipase a and c activities associated with periodontal diseases. Int J Syst Bacteriol 1999; 4: 1329-1339.
    • (1999) Int J Syst Bacteriol , vol.4 , pp. 1329-1339
    • Wyss, C.1    Choi, B.K.2    Schupbach, P.3    Moter, A.4    Guggenheim, B.5    Gobel, U.B.6
  • 9
    • 0029680301 scopus 로고    scopus 로고
    • Treponema maltophilum sp. Nov., a small oral spirochete isolated from human periodontal lesions
    • Wyss C, Choi BK, Schupbach P, Guggenheim B, Gobel UB. Treponema maltophilum sp. Nov., a small oral spirochete isolated from human periodontal lesions. Int J Syst Bacteriol 1996; 46: 745-752.
    • (1996) Int J Syst Bacteriol , vol.46 , pp. 745-752
    • Wyss, C.1    Choi, B.K.2    Schupbach, P.3    Guggenheim, B.4    Gobel, U.B.5
  • 11
    • 0034980413 scopus 로고    scopus 로고
    • Treponema parvum sp. Nov., a small, glucoronic or galacturonic acid-dependent oral spirochaete from lesions of human periodontitis and acute necrotizing ulcerative gingivitis
    • Wyss C, Dewhirst FE, Gmur R et al. Treponema parvum sp. Nov., a small, glucoronic or galacturonic acid-dependent oral spirochaete from lesions of human periodontitis and acute necrotizing ulcerative gingivitis. Int J Syst Evol Microbiol 2001; 51: 955-962.
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 955-962
    • Wyss, C.1    Dewhirst, F.E.2    Gmur, R.3
  • 12
    • 4344629517 scopus 로고    scopus 로고
    • Treponema putidum sp. Nov., a medium-sized proteolytic spirochaete isolated from lesions of human periodontitis and acute necrotizing ulcerative gingivitis
    • Wyss C, Moter A, Choi BK et al. Treponema putidum sp. Nov., a medium-sized proteolytic spirochaete isolated from lesions of human periodontitis and acute necrotizing ulcerative gingivitis. Int J Syst Evol Microbiol 2004; 54: 1117-1122.
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 1117-1122
    • Wyss, C.1    Moter, A.2    Choi, B.K.3
  • 13
    • 0030752878 scopus 로고    scopus 로고
    • Treponema amylovorum sp. Nov., a saccharolytic spirochete of medium size isolated from an advanced human periodontal lesion
    • Wyss C, Choi BK, Schupbach P, Guggenheim B, Gobel UB. Treponema amylovorum sp. Nov., a saccharolytic spirochete of medium size isolated from an advanced human periodontal lesion. Int J Syst Bacteriol 1997; 47: 842-845.
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 842-845
    • Wyss, C.1    Choi, B.K.2    Schupbach, P.3    Guggenheim, B.4    Gobel, U.B.5
  • 15
    • 0036708328 scopus 로고    scopus 로고
    • Detection and quantification of oral treponemes in subgingival plaque by real-time PCR
    • Asai Y, Jinno T, Igarashi H, Ohyama Y, Ogawa T. Detection and quantification of oral treponemes in subgingival plaque by real-time PCR. J Clin Microbiol 2002; 40: 3334-3340.
    • (2002) J Clin Microbiol , vol.40 , pp. 3334-3340
    • Asai, Y.1    Jinno, T.2    Igarashi, H.3    Ohyama, Y.4    Ogawa, T.5
  • 16
    • 11144358038 scopus 로고    scopus 로고
    • Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes
    • Seshadri R, Myers GS, Tettelin H et al. Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes. Proc Natl Acad Sci USA 2004; 101: 5646-5651.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5646-5651
    • Seshadri, R.1    Myers, G.S.2    Tettelin, H.3
  • 18
    • 0030175169 scopus 로고    scopus 로고
    • Development of a gene transfer system in Treponema denticola by electroporation
    • Li H, Kuramitsu HK. Development of a gene transfer system in Treponema denticola by electroporation. Oral Microbiol Immunol 1996; 11: 161-165.
    • (1996) Oral Microbiol Immunol , vol.11 , pp. 161-165
    • Li, H.1    Kuramitsu, H.K.2
  • 19
    • 0030001214 scopus 로고    scopus 로고
    • Gene inactivation in the oral spirochete Treponema denticola: construction of an flge mutant
    • Li H, Ruby J, Charon N, Kuramitsu H. Gene inactivation in the oral spirochete Treponema denticola: construction of an flge mutant. J Bacteriol 1996; 178: 3664-3667.
    • (1996) J Bacteriol , vol.178 , pp. 3664-3667
    • Li, H.1    Ruby, J.2    Charon, N.3    Kuramitsu, H.4
  • 20
    • 54949096586 scopus 로고    scopus 로고
    • Development of a transposon mutagenesis system in the oral spirochete Treponema denticola
    • Yang Y, Stewart PE, Shi X, Li C. Development of a transposon mutagenesis system in the oral spirochete Treponema denticola. Appl Environ Microbiol 2008; 74: 6461-6464.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6461-6464
    • Yang, Y.1    Stewart, P.E.2    Shi, X.3    Li, C.4
  • 21
    • 79952733471 scopus 로고    scopus 로고
    • Virulence factors of the oral spirochete Treponema denticola
    • Oct 12 [Epub ahead of print]. doi: 10.1177/0022034510385242.
    • Dashper SG, Seers CA, Tan KH, Reynolds EC. Virulence factors of the oral spirochete Treponema denticola. J Dent Res 2010; Oct 12 [Epub ahead of print]. doi: 10.1177/0022034510385242.
    • (2010) J Dent Res
    • Dashper, S.G.1    Seers, C.A.2    Tan, K.H.3    Reynolds, E.C.4
  • 22
    • 72449191874 scopus 로고    scopus 로고
    • Virulence determinants of oral treponemes
    • Radolf JD, Lukehart SA, eds. Wymondham: Caister Academic Press
    • Ellen RP. Virulence determinants of oral treponemes. In: Radolf JD, Lukehart SA, eds. Pathogenic Treponema molecular and cellular biology. Wymondham: Caister Academic Press, 2006; 359-388.
    • (2006) Pathogenic Treponema molecular and cellular biology , pp. 359-388
    • Ellen, R.P.1
  • 23
    • 77955744318 scopus 로고    scopus 로고
    • Virulence factors of Treponema denticola
    • Ishihara K. Virulence factors of Treponema denticola. Periodontol 2000 2010; 54: 117-135.
    • (2010) Periodontol 2000 , vol.54 , pp. 117-135
    • Ishihara, K.1
  • 24
    • 0034754077 scopus 로고    scopus 로고
    • Role of Treponema denticola in periodontal diseases
    • Sela MN. Role of Treponema denticola in periodontal diseases. Crit Rev Oral Biol Med 2001; 12: 399-413.
    • (2001) Crit Rev Oral Biol Med , vol.12 , pp. 399-413
    • Sela, M.N.1
  • 25
    • 0028478239 scopus 로고
    • Pathogenic mechanisms in periodontal disease
    • Smalley JW. Pathogenic mechanisms in periodontal disease. Adv Dent Res 1994; 8: 320-328.
    • (1994) Adv Dent Res , vol.8 , pp. 320-328
    • Smalley, J.W.1
  • 26
    • 77949917076 scopus 로고    scopus 로고
    • Evolution and phyletic distribution of two-component signal transduction systems
    • Wuichet K, Cantwell BJ, Zhulin IB. Evolution and phyletic distribution of two-component signal transduction systems. Curr Opin Microbiol 2010; 13: 219-225.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 219-225
    • Wuichet, K.1    Cantwell, B.J.2    Zhulin, I.B.3
  • 27
    • 51549113579 scopus 로고    scopus 로고
    • Analysis of a growth-phase-regulated two-component regulatory system in the periodontal pathogen Treponema denticola
    • Frederick JR, Rogers EA, Marconi RT. Analysis of a growth-phase-regulated two-component regulatory system in the periodontal pathogen Treponema denticola. J Bacteriol 2008; 190: 6162-6169.
    • (2008) J Bacteriol , vol.190 , pp. 6162-6169
    • Frederick, J.R.1    Rogers, E.A.2    Marconi, R.T.3
  • 28
    • 77954360266 scopus 로고    scopus 로고
    • The hpk2-rrp2 two-component regulatory system of Treponema denticola: a potential regulator of environmental and adaptive responses
    • Sarkar J, Frederick J, Marconi RT. The hpk2-rrp2 two-component regulatory system of Treponema denticola: a potential regulator of environmental and adaptive responses. Mol Oral Microbiol 2010; 25: 241-251.
    • (2010) Mol Oral Microbiol , vol.25 , pp. 241-251
    • Sarkar, J.1    Frederick, J.2    Marconi, R.T.3
  • 29
    • 42949103706 scopus 로고    scopus 로고
    • Telling bacteria: do not lyttr
    • Galperin MY. Telling bacteria: do not lyttr. Structure 2008; 16: 657-659.
    • (2008) Structure , vol.16 , pp. 657-659
    • Galperin, M.Y.1
  • 30
    • 78149442623 scopus 로고    scopus 로고
    • Transcriptional profiles of Treponema denticola in response to environmental conditions
    • McHardy I, Keegan C, Sim JH, Shi W, Lux R. Transcriptional profiles of Treponema denticola in response to environmental conditions. PLoS ONE 2010; 5: e13655.
    • (2010) PLoS ONE , vol.5
    • McHardy, I.1    Keegan, C.2    Sim, J.H.3    Shi, W.4    Lux, R.5
  • 33
    • 0027983951 scopus 로고
    • Effect of iron regulation on expression and hemin-binding function of outer-sheath proteins from Treponema denticola
    • Chu L, Song M, Holt SC. Effect of iron regulation on expression and hemin-binding function of outer-sheath proteins from Treponema denticola. Microb Pathog 1994; 16: 321-335.
    • (1994) Microb Pathog , vol.16 , pp. 321-335
    • Chu, L.1    Song, M.2    Holt, S.C.3
  • 34
    • 0029820149 scopus 로고    scopus 로고
    • Iron acquisition by oral hemolytic spirochetes: isolation of a hemin-binding protein and identification of iron reductase activity
    • Scott D, Chan EC, Siboo R. Iron acquisition by oral hemolytic spirochetes: isolation of a hemin-binding protein and identification of iron reductase activity. Can J Microbiol 1996; 42: 1072-1079.
    • (1996) Can J Microbiol , vol.42 , pp. 1072-1079
    • Scott, D.1    Chan, E.C.2    Siboo, R.3
  • 36
    • 0028361459 scopus 로고
    • Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola
    • Staggs TM, Greer MK, Baseman JB, Holt SC, Tryon VV. Identification of lactoferrin-binding proteins from Treponema pallidum subspecies pallidum and Treponema denticola. Mol Microbiol 1994; 12: 613-619.
    • (1994) Mol Microbiol , vol.12 , pp. 613-619
    • Staggs, T.M.1    Greer, M.K.2    Baseman, J.B.3    Holt, S.C.4    Tryon, V.V.5
  • 37
    • 0028113991 scopus 로고
    • Purification and characterization of a 45kDa hemolysin from Treponema denticola ATCC 35404
    • Chu L, Holt SC. Purification and characterization of a 45kDa hemolysin from Treponema denticola ATCC 35404. Microb Pathog 1994; 16: 197-212.
    • (1994) Microb Pathog , vol.16 , pp. 197-212
    • Chu, L.1    Holt, S.C.2
  • 38
    • 0030822744 scopus 로고    scopus 로고
    • Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities
    • Chu L, Ebersole JL, Kurzban GP, Holt SC. Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities. Infect Immun 1997; 65: 3231-3238.
    • (1997) Infect Immun , vol.65 , pp. 3231-3238
    • Chu, L.1    Ebersole, J.L.2    Kurzban, G.P.3    Holt, S.C.4
  • 39
    • 52649116664 scopus 로고    scopus 로고
    • Treponema denticola tror is a manganese- and iron-dependent transcriptional repressor
    • Brett PJ, Burtnick MN, Fenno JC, Gherardini FC. Treponema denticola tror is a manganese- and iron-dependent transcriptional repressor. Mol Microbiol 2008; 70: 396-409.
    • (2008) Mol Microbiol , vol.70 , pp. 396-409
    • Brett, P.J.1    Burtnick, M.N.2    Fenno, J.C.3    Gherardini, F.C.4
  • 41
    • 0034859151 scopus 로고    scopus 로고
    • Chemotaxis of oral treponemes toward sera and albumin of rabbit
    • Umemoto T, Jinno T, Taiji Y, Ogawa T. Chemotaxis of oral treponemes toward sera and albumin of rabbit. Microbiol Immunol 2001; 45: 571-577.
    • (2001) Microbiol Immunol , vol.45 , pp. 571-577
    • Umemoto, T.1    Jinno, T.2    Taiji, Y.3    Ogawa, T.4
  • 44
    • 0036010895 scopus 로고    scopus 로고
    • Genetic exchange between Treponema denticola and Streptococcus gordonii in biofilms
    • Wang BY, Chi B, Kuramitsu HK. Genetic exchange between Treponema denticola and Streptococcus gordonii in biofilms. Oral Microbiol Immunol 2002; 17: 108-112.
    • (2002) Oral Microbiol Immunol , vol.17 , pp. 108-112
    • Wang, B.Y.1    Chi, B.2    Kuramitsu, H.K.3
  • 45
    • 77749280253 scopus 로고    scopus 로고
    • Treponema denticola biofilm-induced expression of a bacteriophage, toxin-antitoxin systems and transposases
    • Mitchell HL, Dashper SG, Catmull DV et al. Treponema denticola biofilm-induced expression of a bacteriophage, toxin-antitoxin systems and transposases. Microbiology 2010; 156: 774-788.
    • (2010) Microbiology , vol.156 , pp. 774-788
    • Mitchell, H.L.1    Dashper, S.G.2    Catmull, D.V.3
  • 46
    • 77956213914 scopus 로고    scopus 로고
    • The small, slow and specialized crispr and anti-crispr of Escherichia and Salmonella
    • Touchon M, Rocha EP. The small, slow and specialized crispr and anti-crispr of Escherichia and Salmonella. PLoS ONE 2010; 5: e11126.
    • (2010) PLoS ONE , vol.5
    • Touchon, M.1    Rocha, E.P.2
  • 48
    • 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. Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia: the 'Red complex', a prototype polybacterial pathogenic consortium in periodontitis. Periodontol 2000 2005; 38: 72-122.
    • (2005) Periodontol 2000 , vol.38 , pp. 72-122
    • Holt, S.C.1    Ebersole, J.L.2
  • 49
    • 0642377572 scopus 로고    scopus 로고
    • Binding of Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin
    • Hashimoto M, Ogawa S, Asai Y, Takai Y, Ogawa T. Binding of Porphyromonas gingivalis fimbriae to Treponema denticola dentilisin. FEMS Microbiol Lett 2003; 226: 267-271.
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 267-271
    • Hashimoto, M.1    Ogawa, S.2    Asai, Y.3    Takai, Y.4    Ogawa, T.5
  • 50
    • 3342927588 scopus 로고    scopus 로고
    • Multiple functions of the leucine-rich repeat protein lrra of Treponema denticola
    • Ikegami A, Honma K, Sharma A, Kuramitsu HK. Multiple functions of the leucine-rich repeat protein lrra of Treponema denticola. Infect Immun 2004; 72: 4619-4627.
    • (2004) Infect Immun , vol.72 , pp. 4619-4627
    • Ikegami, A.1    Honma, K.2    Sharma, A.3    Kuramitsu, H.K.4
  • 51
    • 54249088503 scopus 로고    scopus 로고
    • Coaggregation of Treponema denticola with Porphyromonas gingivalis and Fusobacterium nucleatum is mediated by the major outer sheath protein of Treponema denticola
    • Rosen G, Genzler T, Sela MN. Coaggregation of Treponema denticola with Porphyromonas gingivalis and Fusobacterium nucleatum is mediated by the major outer sheath protein of Treponema denticola. FEMS Microbiol Lett 2008; 289: 59-66.
    • (2008) FEMS Microbiol Lett , vol.289 , pp. 59-66
    • Rosen, G.1    Genzler, T.2    Sela, M.N.3
  • 52
    • 0037261991 scopus 로고    scopus 로고
    • The role of gingipains in the pathogenesis of periodontal disease
    • Imamura T. The role of gingipains in the pathogenesis of periodontal disease. J Periodontol 2003; 74: 111-118.
    • (2003) J Periodontol , vol.74 , pp. 111-118
    • Imamura, T.1
  • 53
    • 78349232350 scopus 로고    scopus 로고
    • Hemagglutinin/adhesin domains of Porphyromonas gingivalis play key roles in coaggregation with Treponema denticola
    • Ito R, Ishihara K, Shoji M, Nakayama K, Okuda K. Hemagglutinin/adhesin domains of Porphyromonas gingivalis play key roles in coaggregation with Treponema denticola. FEMS Immunol Med Microbiol 2010; 60: 251-260.
    • (2010) FEMS Immunol Med Microbiol , vol.60 , pp. 251-260
    • Ito, R.1    Ishihara, K.2    Shoji, M.3    Nakayama, K.4    Okuda, K.5
  • 54
    • 0344033711 scopus 로고    scopus 로고
    • Effect of Porphyromonas gingivalis vesicles on coaggregation of Staphylococcus aureus to oral microorganisms
    • Kamaguchi A, Nakayama K, Ichiyama S et al. Effect of Porphyromonas gingivalis vesicles on coaggregation of Staphylococcus aureus to oral microorganisms. Curr Microbiol 2003; 47: 485-491.
    • (2003) Curr Microbiol , vol.47 , pp. 485-491
    • Kamaguchi, A.1    Nakayama, K.2    Ichiyama, S.3
  • 55
    • 0029116782 scopus 로고
    • Proteases of Treponema denticola outer sheath and extracellular vesicles
    • Rosen G, Naor R, Rahamim E, Yishai R, Sela MN. Proteases of Treponema denticola outer sheath and extracellular vesicles. Infect Immun 1995; 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
  • 56
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn MJ, Kesty NC. Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev 2005; 19: 2645-2655.
    • (2005) Genes Dev , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 57
    • 78651393562 scopus 로고    scopus 로고
    • Selective sorting of cargo proteins into bacterial membrane vesicles
    • Haurat MF, Aduse-Opoku J, Rangarajan M et al. Selective sorting of cargo proteins into bacterial membrane vesicles. J Biol Chem 2011; 286: 1269-1276.
    • (2011) J Biol Chem , vol.286 , pp. 1269-1276
    • Haurat, M.F.1    Aduse-Opoku, J.2    Rangarajan, M.3
  • 58
    • 0031255770 scopus 로고    scopus 로고
    • Differential attachment of oral treponemes to monolayers of epithelial cells
    • Carranza N Jr, Riviere GR, Smith KS, Adams DF, Maier T. Differential attachment of oral treponemes to monolayers of epithelial cells. J Periodontol 1997; 68: 1010-1018.
    • (1997) J Periodontol , vol.68 , pp. 1010-1018
    • Carranza Jr, N.1    Riviere, G.R.2    Smith, K.S.3    Adams, D.F.4    Maier, T.5
  • 59
    • 36549003731 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding protein of Treponema lecithinolyticum by two-dimensional gel electrophoresis and ligand binding assay
    • Lee HR, Choi BK. Identification of a fibronectin-binding protein of Treponema lecithinolyticum by two-dimensional gel electrophoresis and ligand binding assay. Can J Microbiol 2007; 53: 1185-1190.
    • (2007) Can J Microbiol , vol.53 , pp. 1185-1190
    • Lee, H.R.1    Choi, B.K.2
  • 60
    • 0030861335 scopus 로고    scopus 로고
    • Identification, isolation, and characterization of the 42-kilodalton major outer membrane protein (MOMPA) from Treponema pectinovorum ATCC 33768
    • Walker SG, Ebersole JL, Holt SC. Identification, isolation, and characterization of the 42-kilodalton major outer membrane protein (MOMPA) from Treponema pectinovorum ATCC 33768. J Bacteriol 1997; 179: 6441-6447.
    • (1997) J Bacteriol , vol.179 , pp. 6441-6447
    • Walker, S.G.1    Ebersole, J.L.2    Holt, S.C.3
  • 61
    • 0028229045 scopus 로고
    • Degradation of endogenous plasma membrane fibronectin concomitant with Treponema denticola 35405 adhesion to gingival fibroblasts
    • Ellen RP, Song M, McCulloch CA. Degradation of endogenous plasma membrane fibronectin concomitant with Treponema denticola 35405 adhesion to gingival fibroblasts. Infect Immun 1994; 62: 3033-3037.
    • (1994) Infect Immun , vol.62 , pp. 3033-3037
    • Ellen, R.P.1    Song, M.2    McCulloch, C.A.3
  • 62
    • 0025322941 scopus 로고
    • Interaction of Treponema denticola td-4, gm-1, and ms25 with human gingival fibroblasts
    • Weinberg A, Holt SC. Interaction of Treponema denticola td-4, gm-1, and ms25 with human gingival fibroblasts. Infect Immun 1990; 58: 1720-1729.
    • (1990) Infect Immun , vol.58 , pp. 1720-1729
    • Weinberg, A.1    Holt, S.C.2
  • 63
    • 0032752578 scopus 로고    scopus 로고
    • Adherence to and penetration through endothelial cells by oral treponemes
    • Peters SR, Valdez M, Riviere G, Thomas DD. Adherence to and penetration through endothelial cells by oral treponemes. Oral Microbiol Immunol 1999; 14: 379-383.
    • (1999) Oral Microbiol Immunol , vol.14 , pp. 379-383
    • Peters, S.R.1    Valdez, M.2    Riviere, G.3    Thomas, D.D.4
  • 64
    • 0030175286 scopus 로고    scopus 로고
    • Hyaluronan, a possible ligand mediating Treponema denticola binding to periodontal tissue
    • Haapasalo M, Hannam P, McBride BC, Uitto VJ. Hyaluronan, a possible ligand mediating Treponema denticola binding to periodontal tissue. Oral Microbiol Immunol 1996; 11: 156-160.
    • (1996) Oral Microbiol Immunol , vol.11 , pp. 156-160
    • Haapasalo, M.1    Hannam, P.2    McBride, B.C.3    Uitto, V.J.4
  • 65
    • 0026069890 scopus 로고
    • Sulfhydryl-dependent attachment of Treponema denticola to laminin and other proteins
    • Haapasalo M, Singh U, McBride BC, Uitto VJ. Sulfhydryl-dependent attachment of Treponema denticola to laminin and other proteins. Infect Immun 1991; 59: 4230-4237.
    • (1991) Infect Immun , vol.59 , pp. 4230-4237
    • Haapasalo, M.1    Singh, U.2    McBride, B.C.3    Uitto, V.J.4
  • 66
    • 34548502272 scopus 로고    scopus 로고
    • The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation
    • Bamford CV, Fenno JC, Jenkinson HF, Dymock D. The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation. Infect Immun 2007; 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
  • 67
    • 0029863955 scopus 로고    scopus 로고
    • Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (msp) of Treponema denticola
    • Fenno JC, Muller KH, McBride BC. Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (msp) of Treponema denticola. J Bacteriol 1996; 178: 2489-2497.
    • (1996) J Bacteriol , vol.178 , pp. 2489-2497
    • Fenno, J.C.1    Muller, K.H.2    McBride, B.C.3
  • 68
    • 0034064780 scopus 로고    scopus 로고
    • Identification of a Treponema denticola oppa homologue that binds host proteins present in the subgingival environment
    • Fenno JC, Tamura M, Hannam PM, Wong GW, Chan RA, McBride BC. Identification of a Treponema denticola oppa homologue that binds host proteins present in the subgingival environment. Infect Immun 2000; 68: 1884-1892.
    • (2000) Infect Immun , vol.68 , pp. 1884-1892
    • Fenno, J.C.1    Tamura, M.2    Hannam, P.M.3    Wong, G.W.4    Chan, R.A.5    McBride, B.C.6
  • 69
    • 78049431143 scopus 로고    scopus 로고
    • Characterization of a novel family of fibronectin-binding proteins with m23 peptidase domains from Treponema denticola
    • Bamford CV, Francescutti T, Cameron CE, Jenkinson HF, Dymock D. Characterization of a novel family of fibronectin-binding proteins with m23 peptidase domains from Treponema denticola. Mol Oral Microbiol 2010; 25: 369-383.
    • (2010) Mol Oral Microbiol , vol.25 , pp. 369-383
    • Bamford, C.V.1    Francescutti, T.2    Cameron, C.E.3    Jenkinson, H.F.4    Dymock, D.5
  • 70
    • 0030017433 scopus 로고    scopus 로고
    • The major surface protein complex of Treponema denticola depolarizes and induces ion channels in hela cell membranes
    • Mathers DA, Leung WK, Fenno JC, Hong Y, McBride BC. The major surface protein complex of Treponema denticola depolarizes and induces ion channels in hela cell membranes. Infect Immun 1996; 64: 2904-2910.
    • (1996) Infect Immun , vol.64 , pp. 2904-2910
    • Mathers, D.A.1    Leung, W.K.2    Fenno, J.C.3    Hong, Y.4    McBride, B.C.5
  • 71
    • 17644380678 scopus 로고    scopus 로고
    • Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405
    • Edwards AM, Jenkinson HF, Woodward MJ, Dymock D. Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405. Infect Immun 2005; 73: 2891-2898.
    • (2005) Infect Immun , vol.73 , pp. 2891-2898
    • Edwards, A.M.1    Jenkinson, H.F.2    Woodward, M.J.3    Dymock, D.4
  • 72
    • 0031054308 scopus 로고    scopus 로고
    • Conservation of msp, the gene encoding the major outer membrane protein of oral Treponema spp
    • Fenno JC, Wong GW, Hannam PM, Muller KH, Leung WK, McBride BC. Conservation of msp, the gene encoding the major outer membrane protein of oral Treponema spp. J Bacteriol 1997; 179: 1082-1089.
    • (1997) J Bacteriol , vol.179 , pp. 1082-1089
    • Fenno, J.C.1    Wong, G.W.2    Hannam, P.M.3    Muller, K.H.4    Leung, W.K.5    McBride, B.C.6
  • 73
    • 0032917054 scopus 로고    scopus 로고
    • Cloning and characterization of a gene (mspa) encoding the major sheath protein of Treponema maltophilum ATCC 51939(t)
    • Heuner K, Choi BK, Schade R, Moter A, Otto A, Gobel UB. Cloning and characterization of a gene (mspa) encoding the major sheath protein of Treponema maltophilum ATCC 51939(t). J Bacteriol 1999; 181: 1025-1029.
    • (1999) J Bacteriol , vol.181 , pp. 1025-1029
    • Heuner, K.1    Choi, B.K.2    Schade, R.3    Moter, A.4    Otto, A.5    Gobel, U.B.6
  • 74
    • 0037022419 scopus 로고    scopus 로고
    • Cloning and characterization of a major surface protein (msptl) of Treponema lecithinolyticum associated with rapidly progressive periodontitis
    • Park KK, Heuner K, Gobel UB, Yoo YJ, Kim CK, Choi BK. Cloning and characterization of a major surface protein (msptl) of Treponema lecithinolyticum associated with rapidly progressive periodontitis. FEMS Microbiol Lett 2002; 207: 185-192.
    • (2002) FEMS Microbiol Lett , vol.207 , pp. 185-192
    • Park, K.K.1    Heuner, K.2    Gobel, U.B.3    Yoo, Y.J.4    Kim, C.K.5    Choi, B.K.6
  • 75
    • 0027210973 scopus 로고
    • Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola
    • Egli C, Leung WK, Muller KH, Hancock RE, McBride BC. Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola. Infect Immun 1993; 61: 1694-1699.
    • (1993) Infect Immun , vol.61 , pp. 1694-1699
    • Egli, C.1    Leung, W.K.2    Muller, K.H.3    Hancock, R.E.4    McBride, B.C.5
  • 76
    • 0035853474 scopus 로고    scopus 로고
    • Outer sheath associated proteins of the oral spirochete Treponema maltophilum
    • Heuner K, Meltzer U, Choi BK, Gobel UB. Outer sheath associated proteins of the oral spirochete Treponema maltophilum. FEMS Microbiol Lett 2001; 197: 187-193.
    • (2001) FEMS Microbiol Lett , vol.197 , pp. 187-193
    • Heuner, K.1    Meltzer, U.2    Choi, B.K.3    Gobel, U.B.4
  • 77
    • 0344393469 scopus 로고    scopus 로고
    • Two paralogous families of a two-gene subtilisin operon are widely distributed in oral treponemes
    • Correia FF, Plummer AR, Ellen RP et al. Two paralogous families of a two-gene subtilisin operon are widely distributed in oral treponemes. J Bacteriol 2003; 185: 6860-6869.
    • (2003) J Bacteriol , vol.185 , pp. 6860-6869
    • Correia, F.F.1    Plummer, A.R.2    Ellen, R.P.3
  • 78
    • 0035943117 scopus 로고    scopus 로고
    • Proteolytic activity among various oral Treponema species and cloning of a prtp-like gene of Treponema socranskii subsp. Socranskii
    • Heuner K, Bergmann I, Heckenbach K, Gobel UB. Proteolytic activity among various oral Treponema species and cloning of a prtp-like gene of Treponema socranskii subsp. Socranskii. FEMS Microbiol Lett 2001; 201: 169-176.
    • (2001) FEMS Microbiol Lett , vol.201 , pp. 169-176
    • Heuner, K.1    Bergmann, I.2    Heckenbach, K.3    Gobel, U.B.4
  • 79
    • 0029162741 scopus 로고
    • Role of the chymotrypsin-like membrane-associated proteinase from Treponema denticola ATCC 35405 in inactivation of bioactive peptides
    • Makinen PL, Makinen KK, Syed SA. Role of the chymotrypsin-like membrane-associated proteinase from Treponema denticola ATCC 35405 in inactivation of bioactive peptides. Infect Immun 1995; 63: 3567-3575.
    • (1995) Infect Immun , vol.63 , pp. 3567-3575
    • Makinen, P.L.1    Makinen, K.K.2    Syed, S.A.3
  • 80
    • 33645520537 scopus 로고    scopus 로고
    • The Treponema denticola surface protease dentilisin degrades interleukin-1 beta (IL-1 beta), IL-6, and tumor necrosis factor alpha
    • Miyamoto M, Ishihara K, Okuda K. The Treponema denticola surface protease dentilisin degrades interleukin-1 beta (IL-1 beta), IL-6, and tumor necrosis factor alpha. Infect Immun 2006; 74: 2462-2467.
    • (2006) Infect Immun , vol.74 , pp. 2462-2467
    • Miyamoto, M.1    Ishihara, K.2    Okuda, K.3
  • 81
    • 0023791265 scopus 로고
    • Isolation of a chymotrypsin-like enzyme from Treponema denticola
    • Uitto VJ, Grenier D, Chan EC, McBride BC. Isolation of a chymotrypsin-like enzyme from Treponema denticola. Infect Immun 1988; 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
  • 82
    • 33746395470 scopus 로고    scopus 로고
    • Surface protease of Treponema denticola hydrolyzes c3 and influences function of polymorphonuclear leukocytes
    • Yamazaki T, Miyamoto M, Yamada S, Okuda K, Ishihara K. Surface protease of Treponema denticola hydrolyzes c3 and influences function of polymorphonuclear leukocytes. Microbes Infect 2006; 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
  • 83
    • 79251519933 scopus 로고    scopus 로고
    • Treponema denticola chymotrypsin-like protease (dentilisin) induces mmp-2-dependent fibronectin fragmentation in periodontal ligament cells
    • Miao D, Fenno JC, Timm JC, Joo NE, Kapila YL. Treponema denticola chymotrypsin-like protease (dentilisin) induces mmp-2-dependent fibronectin fragmentation in periodontal ligament cells. Infect Immun 2011; 79: 806-811.
    • (2011) Infect Immun , vol.79 , pp. 806-811
    • Miao, D.1    Fenno, J.C.2    Timm, J.C.3    Joo, N.E.4    Kapila, Y.L.5
  • 84
    • 0032769654 scopus 로고    scopus 로고
    • Phylogenetic analysis of saccharolytic oral treponemes isolated from human subgingival plaque
    • Sakamoto M, Koseki T, Umeda M, Ishikawa I, Benno Y, Nakase T. Phylogenetic analysis of saccharolytic oral treponemes isolated from human subgingival plaque. Microbiol Immunol 1999; 43: 711-716.
    • (1999) Microbiol Immunol , vol.43 , pp. 711-716
    • Sakamoto, M.1    Koseki, T.2    Umeda, M.3    Ishikawa, I.4    Benno, Y.5    Nakase, T.6
  • 85
    • 0034832886 scopus 로고    scopus 로고
    • The opdb locus encodes the trypsin-like peptidase activity of Treponema denticola
    • Fenno JC, Lee SY, Bayer CH, Ning Y. The opdb locus encodes the trypsin-like peptidase activity of Treponema denticola. Infect Immun 2001; 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
  • 86
    • 0030021821 scopus 로고    scopus 로고
    • Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405
    • Makinen KK, Chen CY, Makinen PL. Proline iminopeptidase from the outer cell envelope of the human oral spirochete Treponema denticola ATCC 35405. Infect Immun 1996; 64: 702-708.
    • (1996) Infect Immun , vol.64 , pp. 702-708
    • Makinen, K.K.1    Chen, C.Y.2    Makinen, P.L.3
  • 87
    • 0028911526 scopus 로고
    • Purification and general properties of an oligopeptidase from Treponema denticola ATCC 35405-a human oral spirochete
    • Makinen KK, Makinen PL, Loesche WJ, Syed SA. Purification and general properties of an oligopeptidase from Treponema denticola ATCC 35405-a human oral spirochete. Arch Biochem Biophys 1995; 316: 689-698.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 689-698
    • Makinen, K.K.1    Makinen, P.L.2    Loesche, W.J.3    Syed, S.A.4
  • 88
    • 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
    • Makinen KK, Makinen PL, Syed SA. 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 1992; 267: 14285-14293.
    • (1992) J Biol Chem , vol.267 , pp. 14285-14293
    • Makinen, K.K.1    Makinen, P.L.2    Syed, S.A.3
  • 89
    • 0026057131 scopus 로고
    • Comparison of peptidase, glycosidase and esterase activities of oral and non-oral Treponema species
    • Mikx FH. Comparison of peptidase, glycosidase and esterase activities of oral and non-oral Treponema species. J Gen Microbiol 1991; 137: 63-68.
    • (1991) J Gen Microbiol , vol.137 , pp. 63-68
    • Mikx, F.H.1
  • 90
    • 0022477095 scopus 로고
    • Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates
    • Ohta K, Makinen KK, Loesche WJ. Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates. Infect Immun 1986; 53: 213-220.
    • (1986) Infect Immun , vol.53 , pp. 213-220
    • Ohta, K.1    Makinen, K.K.2    Loesche, W.J.3
  • 91
    • 77957574501 scopus 로고    scopus 로고
    • Dentipain, a Streptococcus pyogenes ides protease homolog, is a novel virulence factor of Treponema denticola
    • Ishihara K, Wawrzonek K, Shaw LN, Inagaki S, Miyamoto M, Potempa J. Dentipain, a Streptococcus pyogenes ides protease homolog, is a novel virulence factor of Treponema denticola. Biol Chem 2010; 391: 1047-1055.
    • (2010) Biol Chem , vol.391 , pp. 1047-1055
    • Ishihara, K.1    Wawrzonek, K.2    Shaw, L.N.3    Inagaki, S.4    Miyamoto, M.5    Potempa, J.6
  • 92
    • 0031900968 scopus 로고    scopus 로고
    • Cytopathic effects of the major surface protein and the chymotrypsin-like protease of Treponema denticola
    • Fenno JC, Hannam PM, Leung WK, Tamura M, Uitto VJ, McBride BC. Cytopathic effects of the major surface protein and the chymotrypsin-like protease of Treponema denticola. Infect Immun. 1998; 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
  • 93
    • 2542524720 scopus 로고    scopus 로고
    • Induction of de novo subcortical actin filament assembly by Treponema denticola major outer sheath protein
    • Amin M, Ho AC, Lin JY, Batista da Silva AP, Glogauer M, Ellen RP. Induction of de novo subcortical actin filament assembly by Treponema denticola major outer sheath protein. Infect Immun 2004; 72: 3650-3654.
    • (2004) Infect Immun , vol.72 , pp. 3650-3654
    • Amin, M.1    Ho, A.C.2    Lin, J.Y.3    Batista da Silva, A.P.4    Glogauer, M.5    Ellen, R.P.6
  • 94
    • 1842829136 scopus 로고    scopus 로고
    • The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts
    • Batista da Silva AP, Lee W, Bajenova E, McCulloch CA, Ellen RP. The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts. Cell Microbiol 2004; 6: 485-498.
    • (2004) Cell Microbiol , vol.6 , pp. 485-498
    • Batista da Silva, A.P.1    Lee, W.2    Bajenova, E.3    McCulloch, C.A.4    Ellen, R.P.5
  • 95
    • 0032749022 scopus 로고    scopus 로고
    • Perturbation and exploitation of host cell cytoskeleton by periodontal pathogens
    • Ellen RP. Perturbation and exploitation of host cell cytoskeleton by periodontal pathogens. Microbes Infect 1999; 1: 621-632.
    • (1999) Microbes Infect , vol.1 , pp. 621-632
    • Ellen, R.P.1
  • 96
    • 0029112596 scopus 로고
    • Cytopathic effects of Treponema denticola chymotrypsin-like proteinase on migrating and stratified epithelial cells
    • Uitto VJ, Pan YM, Leung WK et al. Cytopathic effects of Treponema denticola chymotrypsin-like proteinase on migrating and stratified epithelial cells. Infect Immun 1995; 63: 3401-3410.
    • (1995) Infect Immun , vol.63 , pp. 3401-3410
    • Uitto, V.J.1    Pan, Y.M.2    Leung, W.K.3
  • 97
    • 0035933886 scopus 로고    scopus 로고
    • A spirochete surface protein uncouples store-operated calcium channels in fibroblasts: a novel cytotoxic mechanism
    • Wang Q, Ko KS, Kapus A, McCulloch CA, Ellen RP. A spirochete surface protein uncouples store-operated calcium channels in fibroblasts: a novel cytotoxic mechanism. J Biol Chem 2001; 276: 23056-23064.
    • (2001) J Biol Chem , vol.276 , pp. 23056-23064
    • Wang, Q.1    Ko, K.S.2    Kapus, A.3    McCulloch, C.A.4    Ellen, R.P.5
  • 98
    • 0242436150 scopus 로고    scopus 로고
    • Filamentous actin disruption and diminished inositol phosphate response in gingival fibroblasts caused by Treponema denticola
    • Yang PF, Song M, Grove DA, Ellen RP. Filamentous actin disruption and diminished inositol phosphate response in gingival fibroblasts caused by Treponema denticola. Infect Immun 1998; 66: 696-702.
    • (1998) Infect Immun , vol.66 , pp. 696-702
    • Yang, P.F.1    Song, M.2    Grove, D.A.3    Ellen, R.P.4
  • 99
    • 0142195829 scopus 로고    scopus 로고
    • Role of dentilisin in Treponema denticola epithelial cell layer penetration
    • Chi B, Qi M, Kuramitsu HK. Role of dentilisin in Treponema denticola epithelial cell layer penetration. Res Microbiol 2003; 154: 637-643.
    • (2003) Res Microbiol , vol.154 , pp. 637-643
    • Chi, B.1    Qi, M.2    Kuramitsu, H.K.3
  • 100
    • 0033764688 scopus 로고    scopus 로고
    • Insertional inactivation of the prtp gene of Treponema denticola confirms dentilisin's disruption of epithelial junctions
    • Ellen RP, Ko KS, Lo CM, Grove DA, Ishihara K. Insertional inactivation of the prtp gene of Treponema denticola confirms dentilisin's disruption of epithelial junctions. J Mol Microbiol Biotechnol 2000; 2: 581-586.
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 581-586
    • Ellen, R.P.1    Ko, K.S.2    Lo, C.M.3    Grove, D.A.4    Ishihara, K.5
  • 101
    • 0034819849 scopus 로고    scopus 로고
    • Motility and chemotaxis in tissue penetration of oral epithelial cell layers by Treponema denticola
    • Lux R, Miller JN, Park N-H, Shi W. Motility and chemotaxis in tissue penetration of oral epithelial cell layers by Treponema denticola. Infect Immun 2001; 69: 6276-6283.
    • (2001) Infect Immun , vol.69 , pp. 6276-6283
    • Lux, R.1    Miller, J.N.2    Park, N.-H.3    Shi, W.4
  • 102
    • 38349032541 scopus 로고    scopus 로고
    • Possible requirement of intercellular adhesion molecule-1 for invasion of gingival epithelial cells by Treponema medium
    • Tamai R, Asai Y, Kawabata A, Akisaka T, Ogawa T. Possible requirement of intercellular adhesion molecule-1 for invasion of gingival epithelial cells by Treponema medium. Can J Microbiol 2007; 53: 1232-1238.
    • (2007) Can J Microbiol , vol.53 , pp. 1232-1238
    • Tamai, R.1    Asai, Y.2    Kawabata, A.3    Akisaka, T.4    Ogawa, T.5
  • 103
    • 0036948288 scopus 로고    scopus 로고
    • Genetics of motility and chemotaxis of a fascinating group of bacteria: the spirochetes
    • Charon NW, Goldstein SF. Genetics of motility and chemotaxis of a fascinating group of bacteria: the spirochetes. Annu Rev Genet 2002; 36: 47-73.
    • (2002) Annu Rev Genet , vol.36 , pp. 47-73
    • Charon, N.W.1    Goldstein, S.F.2
  • 104
    • 33748768733 scopus 로고    scopus 로고
    • Cytoskeletal cytoplasmic filament ribbon of Treponema: a member of an intermediate-like filament protein family
    • Izard J. Cytoskeletal cytoplasmic filament ribbon of Treponema: a member of an intermediate-like filament protein family. J Mol Microbiol Biotechnol 2006; 11: 159-166.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 159-166
    • Izard, J.1
  • 105
    • 62449087425 scopus 로고    scopus 로고
    • Structural and genomic features of treponemal architecture
    • Radolf JD, Lukehart SA, eds. Wymondham: Caister Academic Press
    • Izard J, Limberger RJ. Structural and genomic features of treponemal architecture. In: Radolf JD, Lukehart SA, eds. Pathogenic Treponema molecular and cellular biology. Wymondham: Caister Academic Press, 2006; 39-59.
    • (2006) Pathogenic Treponema molecular and cellular biology , pp. 39-59
    • Izard, J.1    Limberger, R.J.2
  • 106
    • 1242277740 scopus 로고    scopus 로고
    • Tomographic reconstruction of treponemal cytoplasmic filaments reveals novel bridging and anchoring components
    • Izard J, McEwen BF, Barnard RM, Portuese T, Samsonoff WA, Limberger RJ. Tomographic reconstruction of treponemal cytoplasmic filaments reveals novel bridging and anchoring components. Mol Microbiol 2004; 51: 609-618.
    • (2004) Mol Microbiol , vol.51 , pp. 609-618
    • Izard, J.1    McEwen, B.F.2    Barnard, R.M.3    Portuese, T.4    Samsonoff, W.A.5    Limberger, R.J.6
  • 107
    • 4344600506 scopus 로고    scopus 로고
    • Genetic analysis of Treponema denticola ATCC 35405 biofilm formation
    • Vesey PM, Kuramitsu HK. Genetic analysis of Treponema denticola ATCC 35405 biofilm formation. Microbiology 2004; 150: 2401-2407.
    • (2004) Microbiology , vol.150 , pp. 2401-2407
    • Vesey, P.M.1    Kuramitsu, H.K.2
  • 108
    • 72449158825 scopus 로고    scopus 로고
    • Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirochete
    • Izard J, Renken C, Hsieh CE et al. Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirochete. J Bacteriol 2009; 191: 7566-7580.
    • (2009) J Bacteriol , vol.191 , pp. 7566-7580
    • Izard, J.1    Renken, C.2    Hsieh, C.E.3
  • 109
    • 45549101208 scopus 로고    scopus 로고
    • Native cellular architecture of Treponema denticola revealed by cryo-electron tomography
    • Izard J, Hsieh CE, Limberger RJ, Mannella CA, Marko M. Native cellular architecture of Treponema denticola revealed by cryo-electron tomography. J Struct Biol 2008; 163: 10-17.
    • (2008) J Struct Biol , vol.163 , pp. 10-17
    • Izard, J.1    Hsieh, C.E.2    Limberger, R.J.3    Mannella, C.A.4    Marko, M.5
  • 110
    • 39849105856 scopus 로고    scopus 로고
    • Novel ultrastructures of Treponema primitia and their implications for motility
    • Murphy GE, Matson EG, Leadbetter JR, Berg HC, Jensen GJ. Novel ultrastructures of Treponema primitia and their implications for motility. Mol Microbiol 2008; 67: 1184-1195.
    • (2008) Mol Microbiol , vol.67 , pp. 1184-1195
    • Murphy, G.E.1    Matson, E.G.2    Leadbetter, J.R.3    Berg, H.C.4    Jensen, G.J.5
  • 111
    • 0025151971 scopus 로고
    • Systemic humoral immune responses in periodontal disease
    • Ebersole JL. Systemic humoral immune responses in periodontal disease. Crit Rev Oral Biol Med 1990; 1: 283-331.
    • (1990) Crit Rev Oral Biol Med , vol.1 , pp. 283-331
    • Ebersole, J.L.1
  • 112
    • 77953156509 scopus 로고    scopus 로고
    • Major surface protein complex of Treponema denticola induces the production of tumor necrosis factor alpha, interleukin-1 beta, interleukin-6 and matrix metalloproteinase 9 by primary human peripheral blood monocytes
    • Gaibani P, Caroli F, Nucci C, Sambri V. Major surface protein complex of Treponema denticola induces the production of tumor necrosis factor alpha, interleukin-1 beta, interleukin-6 and matrix metalloproteinase 9 by primary human peripheral blood monocytes. J Periodontal Res 2010; 45: 361-366.
    • (2010) J Periodontal Res , vol.45 , pp. 361-366
    • Gaibani, P.1    Caroli, F.2    Nucci, C.3    Sambri, V.4
  • 113
    • 66949135023 scopus 로고    scopus 로고
    • The major outer membrane protein of a periodontopathogen induces IFN-{beta} and IFN-stimulated genes in monocytes via lipid raft and tank-binding kinase 1/IFN regulatory factor-3
    • Lee S-H, Kim JS, Jun H-K, Lee H-R, Lee D, Choi B-K. The major outer membrane protein of a periodontopathogen induces IFN-{beta} and IFN-stimulated genes in monocytes via lipid raft and tank-binding kinase 1/IFN regulatory factor-3. J Immunol 2009; 182: 5823-5835.
    • (2009) J Immunol , vol.182 , pp. 5823-5835
    • Lee, S.-H.1    Kim, J.S.2    Jun, H.-K.3    Lee, H.-R.4    Lee, D.5    Choi, B.-K.6
  • 114
    • 11144312370 scopus 로고    scopus 로고
    • Upregulation of intercellular adhesion molecule 1 and proinflammatory cytokines by the major surface proteins of Treponema maltophilum and Treponema lecithinolyticum, the phylogenetic group iv oral spirochetes associated with periodontitis and endodontic infections
    • Lee SH, Kim KK, Choi BK. Upregulation of intercellular adhesion molecule 1 and proinflammatory cytokines by the major surface proteins of Treponema maltophilum and Treponema lecithinolyticum, the phylogenetic group iv oral spirochetes associated with periodontitis and endodontic infections. Infect Immun 2005; 73: 268-276.
    • (2005) Infect Immun , vol.73 , pp. 268-276
    • Lee, S.H.1    Kim, K.K.2    Choi, B.K.3
  • 115
    • 69049092753 scopus 로고    scopus 로고
    • Involvement of toll-like receptors 2 and 4 in the innate immune response to Treponema denticola and its outer sheath components
    • Nussbaum G, Ben-Adi S, Genzler T, Sela M, Rosen G. Involvement of toll-like receptors 2 and 4 in the innate immune response to Treponema denticola and its outer sheath components. Infect Immun 2009; 77: 3939-3947.
    • (2009) Infect Immun , vol.77 , pp. 3939-3947
    • Nussbaum, G.1    Ben-Adi, S.2    Genzler, T.3    Sela, M.4    Rosen, G.5
  • 116
    • 0001701294 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates Treponema glycolipid and lipoteichoic acid-induced NF-kappaB translocation
    • Opitz B, Schröder NWJ, Spreitzer I et al. Toll-like receptor-2 mediates Treponema glycolipid and lipoteichoic acid-induced NF-kappaB translocation. J Biol Chem. 2001; 276: 22041-22047.
    • (2001) J Biol Chem , vol.276 , pp. 22041-22047
    • Opitz, B.1    Schröder, N.W.J.2    Spreitzer, I.3
  • 117
    • 0033014671 scopus 로고    scopus 로고
    • Activation of murine macrophages by lipoprotein and lipooligosaccharide of Treponema denticola
    • Rosen G, Sela MN, Naor R, Halabi A, Barak V, Shapira L. Activation of murine macrophages by lipoprotein and lipooligosaccharide of Treponema denticola. Infect Immun 1999; 67: 1180-1186.
    • (1999) Infect Immun , vol.67 , pp. 1180-1186
    • Rosen, G.1    Sela, M.N.2    Naor, R.3    Halabi, A.4    Barak, V.5    Shapira, L.6
  • 118
    • 41649095188 scopus 로고    scopus 로고
    • Immune responses induced by spirochetal outer membrane lipoproteins and glycolipids
    • Schroder NWJ, Eckert J, Stubs G, Schumann RR. Immune responses induced by spirochetal outer membrane lipoproteins and glycolipids. Immunobiology 2008; 213: 329-340.
    • (2008) Immunobiology , vol.213 , pp. 329-340
    • Schroder, N.W.J.1    Eckert, J.2    Stubs, G.3    Schumann, R.R.4
  • 119
    • 46249109086 scopus 로고    scopus 로고
    • Highly conserved surface proteins of oral spirochetes as adhesins and potent inducers of proinflammatory and osteoclastogenic factors
    • Jun H-K, Kang Y-M, Lee H-R, Lee S-H, Choi B-K. Highly conserved surface proteins of oral spirochetes as adhesins and potent inducers of proinflammatory and osteoclastogenic factors. Infect Immun 2008; 76: 2428-2438.
    • (2008) Infect Immun , vol.76 , pp. 2428-2438
    • Jun, H.-K.1    Kang, Y.-M.2    Lee, H.-R.3    Lee, S.-H.4    Choi, B.-K.5
  • 120
    • 0037305076 scopus 로고    scopus 로고
    • Oral treponemes and their outer membrane extracts activate human gingival epithelial cells through toll-like receptor 2
    • Asai Y, Jinno T, Ogawa T. Oral treponemes and their outer membrane extracts activate human gingival epithelial cells through toll-like receptor 2. Infect Immun 2003; 71: 717-725.
    • (2003) Infect Immun , vol.71 , pp. 717-725
    • Asai, Y.1    Jinno, T.2    Ogawa, T.3
  • 121
    • 21744432872 scopus 로고    scopus 로고
    • Treponema medium glycoconjugate inhibits activation of human gingival fibroblasts stimulated with phenol-water extracts of periodontopathic bacteria
    • Asai Y, Ohyama Y, Taiji Y et al. Treponema medium glycoconjugate inhibits activation of human gingival fibroblasts stimulated with phenol-water extracts of periodontopathic bacteria. J Dent Res 2005; 84: 456-461.
    • (2005) J Dent Res , vol.84 , pp. 456-461
    • Asai, Y.1    Ohyama, Y.2    Taiji, Y.3
  • 122
    • 34547914561 scopus 로고    scopus 로고
    • Mapping of the proinflammatory domains of msptl of Treponema lecithinolyticum
    • Jun HK, Lee HR, Lee SH, Choi BK. Mapping of the proinflammatory domains of msptl of Treponema lecithinolyticum. Microbiology 2007; 153: 2386-2392.
    • (2007) Microbiology , vol.153 , pp. 2386-2392
    • Jun, H.K.1    Lee, H.R.2    Lee, S.H.3    Choi, B.K.4
  • 123
    • 0033865074 scopus 로고    scopus 로고
    • Cytokine responses to Treponema pectinovorum and Treponema denticola in human gingival fibroblasts
    • Nixon CS, Steffen MJ, Ebersole JL. Cytokine responses to Treponema pectinovorum and Treponema denticola in human gingival fibroblasts. Infect Immun 2000; 68: 5284-5292.
    • (2000) Infect Immun , vol.68 , pp. 5284-5292
    • Nixon, C.S.1    Steffen, M.J.2    Ebersole, J.L.3
  • 124
    • 48749122977 scopus 로고    scopus 로고
    • Treponema denticola lipooligosaccharide activates gingival fibroblasts and upregulates inflammatory mediator production
    • Tanabe S, Bodet C, Grenier D. Treponema denticola lipooligosaccharide activates gingival fibroblasts and upregulates inflammatory mediator production. J Cell Physiol 2008; 216: 727-731.
    • (2008) J Cell Physiol , vol.216 , pp. 727-731
    • Tanabe, S.1    Bodet, C.2    Grenier, D.3
  • 125
    • 0242391973 scopus 로고    scopus 로고
    • Treponemal glycoconjugate inhibits toll-like receptor ligand-induced cell activation by blocking lps-binding protein and cd14 functions
    • Asai Y, Hashimoto M, Ogawa T. Treponemal glycoconjugate inhibits toll-like receptor ligand-induced cell activation by blocking lps-binding protein and cd14 functions. Eur J Immunol 2003; 33: 3196-3204.
    • (2003) Eur J Immunol , vol.33 , pp. 3196-3204
    • Asai, Y.1    Hashimoto, M.2    Ogawa, T.3
  • 126
    • 32244448558 scopus 로고    scopus 로고
    • Phenol/water extract of Treponema socranskii subsp. Socranskii as an antagonist of toll-like receptor 4 signalling
    • Lee S-H, Kim K-K, Rhyu I-C, Koh S, Lee D-S, Choi B-K. Phenol/water extract of Treponema socranskii subsp. Socranskii as an antagonist of toll-like receptor 4 signalling. Microbiology 2006; 152: 535-546.
    • (2006) Microbiology , vol.152 , pp. 535-546
    • Lee, S.-H.1    Kim, K.-K.2    Rhyu, I.-C.3    Koh, S.4    Lee, D.-S.5    Choi, B.-K.6
  • 127
    • 0023851346 scopus 로고
    • Inhibition of superoxide production in human polymorphonuclear leukocytes by oral treponemal factors
    • Sela MN, Weinberg A, Borinsky R, Holt SC, Dishon T. Inhibition of superoxide production in human polymorphonuclear leukocytes by oral treponemal factors. Infect Immun 1988; 56: 589-594.
    • (1988) Infect Immun , vol.56 , pp. 589-594
    • Sela, M.N.1    Weinberg, A.2    Borinsky, R.3    Holt, S.C.4    Dishon, T.5
  • 128
    • 38049112697 scopus 로고    scopus 로고
    • The major outer sheath protein of Treponema denticola selectively inhibits rac1 activation in murine neutrophils
    • Magalhaes MA, Sun CX, Glogauer M, Ellen RP. The major outer sheath protein of Treponema denticola selectively inhibits rac1 activation in murine neutrophils. Cell Microbiol 2008; 10: 344-354.
    • (2008) Cell Microbiol , vol.10 , pp. 344-354
    • Magalhaes, M.A.1    Sun, C.X.2    Glogauer, M.3    Ellen, R.P.4
  • 129
    • 33644780745 scopus 로고    scopus 로고
    • Modulation of human neutrophil functions in vitro by Treponema denticola major outer sheath protein
    • Puthengady Thomas B, Sun CX, Bajenova E, Ellen RP, Glogauer M. Modulation of human neutrophil functions in vitro by Treponema denticola major outer sheath protein. Infect Immun 2006; 74: 1954-1957.
    • (2006) Infect Immun , vol.74 , pp. 1954-1957
    • Puthengady Thomas, B.1    Sun, C.X.2    Bajenova, E.3    Ellen, R.P.4    Glogauer, M.5
  • 130
    • 2942600174 scopus 로고    scopus 로고
    • Modulation of the innate immune response within the periodontium
    • Dixon DR, Bainbridge BW, Darveau RP. Modulation of the innate immune response within the periodontium. Periodontol 2000 2004; 35: 53-74.
    • (2004) Periodontol 2000 , vol.35 , pp. 53-74
    • Dixon, D.R.1    Bainbridge, B.W.2    Darveau, R.P.3
  • 131
    • 33747847417 scopus 로고    scopus 로고
    • Treponema denticola in disseminating endodontic infections
    • Foschi F, Izard J, Sasaki H et al. Treponema denticola in disseminating endodontic infections. J Dent Res 2006; 85: 761-765.
    • (2006) J Dent Res , vol.85 , pp. 761-765
    • Foschi, F.1    Izard, J.2    Sasaki, H.3
  • 132
    • 77955711214 scopus 로고    scopus 로고
    • Treponema denticola alters cell vitality and induces ho-1 and hsp70 expression in porcine aortic endothelial cells
    • Bernardini C, Gaibani P, Zannoni A et al. Treponema denticola alters cell vitality and induces ho-1 and hsp70 expression in porcine aortic endothelial cells. Cell Stress Chaperones 2009; 15: 509-516.
    • (2009) Cell Stress Chaperones , vol.15 , pp. 509-516
    • Bernardini, C.1    Gaibani, P.2    Zannoni, A.3
  • 134
    • 34147159390 scopus 로고    scopus 로고
    • Rat model of polymicrobial infection, immunity, and alveolar bone resorption in periodontal disease
    • Kesavalu L, Sathishkumar S, Bakthavatchalu V et al. Rat model of polymicrobial infection, immunity, and alveolar bone resorption in periodontal disease. Infect Immun 2007; 75: 1704-1712.
    • (2007) Infect Immun , vol.75 , pp. 1704-1712
    • Kesavalu, L.1    Sathishkumar, S.2    Bakthavatchalu, V.3
  • 135
    • 60549112363 scopus 로고    scopus 로고
    • Immune response and alveolar bone resorption in a mouse model of Treponema denticola infection
    • Lee SF, Andrian E, Rowland E, Marquez IC. Immune response and alveolar bone resorption in a mouse model of Treponema denticola infection. Infect Immun 2009; 77: 694-698.
    • (2009) Infect Immun , vol.77 , pp. 694-698
    • Lee, S.F.1    Andrian, E.2    Rowland, E.3    Marquez, I.C.4
  • 136
    • 77954353275 scopus 로고    scopus 로고
    • Molecular characterization of Treponema denticola infection-induced bone and soft tissue transcriptional profiles
    • Bakthavatchalu V, Meka A, Sathishkumar S et al. Molecular characterization of Treponema denticola infection-induced bone and soft tissue transcriptional profiles. Mol Oral Microbiol 2010; 25: 260-274.
    • (2010) Mol Oral Microbiol , vol.25 , pp. 260-274
    • Bakthavatchalu, V.1    Meka, A.2    Sathishkumar, S.3
  • 137
    • 0027531601 scopus 로고
    • Fibronectin-binding proteins of a human oral spirochete Treponema denticola
    • Umemoto T, Nakatani Y, Nakamura Y, Namikawa I. Fibronectin-binding proteins of a human oral spirochete Treponema denticola. Microbiol Immunol 1993; 37: 75-78.
    • (1993) Microbiol Immunol , vol.37 , pp. 75-78
    • Umemoto, T.1    Nakatani, Y.2    Nakamura, Y.3    Namikawa, I.4
  • 138
    • 27744492254 scopus 로고    scopus 로고
    • Demonstration of factor h-like protein 1 binding to Treponema denticola, a pathogen associated with periodontal disease in humans
    • McDowell JV, Lankford J, Stamm L, Sadlon T, Gordon DL, Marconi RT. Demonstration of factor h-like protein 1 binding to Treponema denticola, a pathogen associated with periodontal disease in humans. Infect Immun 2005; 73: 7126-7132.
    • (2005) Infect Immun , vol.73 , pp. 7126-7132
    • McDowell, J.V.1    Lankford, J.2    Stamm, L.3    Sadlon, T.4    Gordon, D.L.5    Marconi, R.T.6
  • 139
    • 0031444004 scopus 로고    scopus 로고
    • Adherence of human oral spirochetes by collagen-binding proteins
    • Umemoto T, Li M, Namikawa I. Adherence of human oral spirochetes by collagen-binding proteins. Microbiol Immunol 1997; 41: 917-923.
    • (1997) Microbiol Immunol , vol.41 , pp. 917-923
    • Umemoto, T.1    Li, M.2    Namikawa, I.3
  • 140
    • 0029833178 scopus 로고    scopus 로고
    • Characterization of the Treponema denticola prtp gene encoding a prolyl-phenylalanine-specific protease (dentilisin)
    • Ishihara K, Miura T, Kuramitsu HK, Okuda K. Characterization of the Treponema denticola prtp gene encoding a prolyl-phenylalanine-specific protease (dentilisin). Infect Immun 1996; 64: 5178-5186.
    • (1996) Infect Immun , vol.64 , pp. 5178-5186
    • Ishihara, K.1    Miura, T.2    Kuramitsu, H.K.3    Okuda, K.4
  • 141
    • 0027959709 scopus 로고
    • An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides
    • Makinen PL, Makinen KK, Syed SA. An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides. Infect Immun 1994; 62: 4938-4947.
    • (1994) Infect Immun , vol.62 , pp. 4938-4947
    • Makinen, P.L.1    Makinen, K.K.2    Syed, S.A.3
  • 142
    • 0027997362 scopus 로고
    • Characterization of hemolysis and hemoxidation activities by Treponema denticola
    • Chu L, Kennell W, Holt SC. Characterization of hemolysis and hemoxidation activities by Treponema denticola. Microb Pathog 1994; 16: 183-195.
    • (1994) Microb Pathog , vol.16 , pp. 183-195
    • Chu, L.1    Kennell, W.2    Holt, S.C.3
  • 143
    • 0032956139 scopus 로고    scopus 로고
    • Characterization of a novel methyl-accepting chemotaxis gene, dmcb, from the oral spirochete Treponema denticola
    • Li H, Arakawa S, Deng QD, Kuramitsu H. Characterization of a novel methyl-accepting chemotaxis gene, dmcb, from the oral spirochete Treponema denticola. Infect Immun 1999; 67: 694-699.
    • (1999) Infect Immun , vol.67 , pp. 694-699
    • Li, H.1    Arakawa, S.2    Deng, Q.D.3    Kuramitsu, H.4
  • 144
    • 0033014008 scopus 로고    scopus 로고
    • Insertional inactivation of Treponema denticola tap1 results in a non-motile mutant with elongated flagellar hooks
    • Limberger RJ, Slivienski LL, Izard J, Samsonoff WA. Insertional inactivation of Treponema denticola tap1 results in a non-motile mutant with elongated flagellar hooks. J Bacteriol 1999; 181: 3743-3750.
    • (1999) J Bacteriol , vol.181 , pp. 3743-3750
    • Limberger, R.J.1    Slivienski, L.L.2    Izard, J.3    Samsonoff, W.A.4
  • 145
    • 67650823087 scopus 로고    scopus 로고
    • Treponema denticola peptidoglycan induces the production of inflammatory mediators and matrix metalloproteinase 9 in macrophage-like cells
    • Tanabe SI, Bodet C, Grenier D. Treponema denticola peptidoglycan induces the production of inflammatory mediators and matrix metalloproteinase 9 in macrophage-like cells. J Periodont Res 2009; 44: 503-510.
    • (2009) J Periodont Res , vol.44 , pp. 503-510
    • Tanabe, S.I.1    Bodet, C.2    Grenier, D.3
  • 146
    • 77956039738 scopus 로고    scopus 로고
    • Treponema denticola suppresses expression of human beta-defensin-2 in gingival epithelial cells through inhibition of tnfalpha production and tlr2 activation
    • Shin JE, Choi Y. Treponema denticola suppresses expression of human beta-defensin-2 in gingival epithelial cells through inhibition of tnfalpha production and tlr2 activation. Mol Cells 2010; 29: 407-412.
    • (2010) Mol Cells , vol.29 , pp. 407-412
    • Shin, J.E.1    Choi, Y.2
  • 147
    • 76749122413 scopus 로고    scopus 로고
    • Treponema denticola suppresses expression of human {beta}-defensin-3 in gingival epithelial cells through inhibition of the toll-like receptor 2 axis
    • Shin JE, Kim YS, Oh J-E, Min B-M, Choi Y. Treponema denticola suppresses expression of human {beta}-defensin-3 in gingival epithelial cells through inhibition of the toll-like receptor 2 axis. Infect Immun 2010; 78: 672-679.
    • (2010) Infect Immun , vol.78 , pp. 672-679
    • Shin, J.E.1    Kim, Y.S.2    Oh, J.-E.3    Min, B.-M.4    Choi, Y.5
  • 148
    • 0036086590 scopus 로고    scopus 로고
    • Treponema denticola is resistant to human beta-defensins
    • Brissette CA, Lukehart SA. Treponema denticola is resistant to human beta-defensins. Infect Immun 2002; 70: 3982-3984.
    • (2002) Infect Immun , vol.70 , pp. 3982-3984
    • Brissette, C.A.1    Lukehart, S.A.2
  • 149
    • 0034283666 scopus 로고    scopus 로고
    • Involvement of lipopolysaccharide binding protein, cd14, and toll-like receptors in the initiation of innate immune responses by Treponema glycolipids
    • Schroder NWJ, Opitz B, Lamping N et al. Involvement of lipopolysaccharide binding protein, cd14, and toll-like receptors in the initiation of innate immune responses by Treponema glycolipids. J Immunol 2000; 165: 2683-2693.
    • (2000) J Immunol , vol.165 , pp. 2683-2693
    • Schroder, N.W.J.1    Opitz, B.2    Lamping, N.3
  • 150
    • 77958527926 scopus 로고    scopus 로고
    • Td92, an outer membrane protein of Treponema denticola, induces osteoclastogenesis via prostaglandin e-mediated rankl/osteoprotegerin regulation
    • Kim M, Jun HK, Choi BK, Cha JH, Yoo YJ. Td92, an outer membrane protein of Treponema denticola, induces osteoclastogenesis via prostaglandin e-mediated rankl/osteoprotegerin regulation. J Periodontal Res 2010; 45: 772-779.
    • (2010) J Periodontal Res , vol.45 , pp. 772-779
    • Kim, M.1    Jun, H.K.2    Choi, B.K.3    Cha, J.H.4    Yoo, Y.J.5
  • 151
    • 0037222693 scopus 로고    scopus 로고
    • Induction of osteoclastogenesis and matrix metalloproteinase expression by the lipooligosaccharide of Treponema denticola
    • Choi BK, Lee HJ, Kang JH, Jeong GJ, Min CK, Yoo YJ. Induction of osteoclastogenesis and matrix metalloproteinase expression by the lipooligosaccharide of Treponema denticola. Infect Immun 2003; 71: 226-233.
    • (2003) Infect Immun , vol.71 , pp. 226-233
    • Choi, B.K.1    Lee, H.J.2    Kang, J.H.3    Jeong, G.J.4    Min, C.K.5    Yoo, Y.J.6
  • 152
    • 0036839963 scopus 로고    scopus 로고
    • Construction and analysis of hemin binding protein mutants in the oral pathogen Treponema denticola
    • Xu X, Kolodrubetz D. Construction and analysis of hemin binding protein mutants in the oral pathogen Treponema denticola. Res Microbiol 2002; 153: 569-577.
    • (2002) Res Microbiol , vol.153 , pp. 569-577
    • Xu, X.1    Kolodrubetz, D.2
  • 153
    • 0031111719 scopus 로고    scopus 로고
    • Release and activation of human neutrophil matrix metallo- and serine proteinases during phagocytosis of Fusobacterium nucleatum, Porphyromonas gingivalis and Treponema denticola
    • Ding Y, Haapasalo M, Kerosuo E, Lounatmaa K, Kotiranta A, Sorsa T. Release and activation of human neutrophil matrix metallo- and serine proteinases during phagocytosis of Fusobacterium nucleatum, Porphyromonas gingivalis and Treponema denticola. J Clin Periodontol 1997; 24: 237-248.
    • (1997) J Clin Periodontol , vol.24 , pp. 237-248
    • Ding, Y.1    Haapasalo, M.2    Kerosuo, E.3    Lounatmaa, K.4    Kotiranta, A.5    Sorsa, T.6
  • 154
    • 33947142352 scopus 로고    scopus 로고
    • Activation of mapk in fibroblasts by Treponema denticola major outer sheath protein
    • Jobin MC, Virdee I, McCulloch CA, Ellen RP. Activation of mapk in fibroblasts by Treponema denticola major outer sheath protein. Biochem Biophys Res Commun 2007; 356: 213-218.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 213-218
    • Jobin, M.C.1    Virdee, I.2    McCulloch, C.A.3    Ellen, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.