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Volumn 14, Issue 12, 2016, Pages 744-759

Treponema pallidum, the syphilis spirochete: Making a living as a stealth pathogen

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM CULTURE; GENETIC MANIPULATION; IMMUNE EVASION; NONHUMAN; PATHOGENESIS; PATHOGENICITY; PRIORITY JOURNAL; REVIEW; SYPHILIS; TREPONEMA PALLIDUM; GENETICS; GENOMICS; HUMAN; IMMUNOLOGY; METABOLISM; MICROBIOLOGY; PHYSIOLOGY; SEQUENCE ALIGNMENT; TRANSMISSION;

EID: 84990911171     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro.2016.141     Document Type: Review
Times cited : (184)

References (158)
  • 3
    • 0017876994 scopus 로고
    • Genetics of Treponema: Relationship between Treponema pallidum and five cultivable treponemes
    • Miao, R. & Fieldsteel, A. H. Genetics of Treponema: relationship between Treponema pallidum and five cultivable treponemes. J. Bacteriol. 133, 101-107 (1978).
    • (1978) J. Bacteriol. , vol.133 , pp. 101-107
    • Miao, R.1    Fieldsteel, A.H.2
  • 4
    • 0018898587 scopus 로고
    • Genetic relationship between Treponema pallidum and Treponema pertenue, two noncultivable human pathogens
    • Miao, R. M. & Fieldsteel, A. H. Genetic relationship between Treponema pallidum and Treponema pertenue, two noncultivable human pathogens. J. Bacteriol. 141, 427-429 (1980).
    • (1980) J. Bacteriol. , vol.141 , pp. 427-429
    • Miao, R.M.1    Fieldsteel, A.H.2
  • 5
    • 84857659482 scopus 로고    scopus 로고
    • Genetic diversity in Treponema pallidum: Implications for pathogenesis, evolution and molecular diagnostics of syphilis and yaws
    • Smajs, D., Norris, S. J. & Weinstock, G. M. Genetic diversity in Treponema pallidum: implications for pathogenesis, evolution and molecular diagnostics of syphilis and yaws. Infect. Genet. Evol. 12, 191-202 (2012).
    • (2012) Infect. Genet. Evol. , vol.12 , pp. 191-202
    • Smajs, D.1    Norris, S.J.2    Weinstock, G.M.3
  • 6
    • 84875829608 scopus 로고    scopus 로고
    • Is there a difference between hare syphilis and rabbit syphilis? Cross infection experiments between rabbits and hares
    • Lumeij, J. T., Mikalova, L. & Smajs, D. Is there a difference between hare syphilis and rabbit syphilis? Cross infection experiments between rabbits and hares. Vet. Microbiol. 164, 190-194 (2013).
    • (2013) Vet. Microbiol. , vol.164 , pp. 190-194
    • Lumeij, J.T.1    Mikalova, L.2    Smajs, D.3
  • 7
    • 79957874612 scopus 로고    scopus 로고
    • Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A: The loss of infectivity to humans is associated with genome decay
    • Smajs, D. et al. Complete genome sequence of Treponema paraluiscuniculi, strain Cuniculi A: the loss of infectivity to humans is associated with genome decay. PLoS ONE 6, e20415 (2011).
    • (2011) PLoS ONE , vol.6
    • Smajs, D.1
  • 8
    • 84930333217 scopus 로고    scopus 로고
    • Global epidemiology of yaws: A systematic review
    • Mitja, O. et al. Global epidemiology of yaws: a systematic review. Lancet Glob. Health 3, e324-e331 (2015).
    • (2015) Lancet Glob. Health , vol.3 , pp. e324-e331
    • Mitja, O.1
  • 10
    • 84878445734 scopus 로고    scopus 로고
    • The sound of silence: Missing the opportunity to save lives at birth
    • Klausner, J. D. The sound of silence: missing the opportunity to save lives at birth. Bull. World Health Organ. 91, 158-158A (2013).
    • (2013) Bull. World Health Organ. , vol.91 , pp. 158-158A
    • Klausner, J.D.1
  • 15
    • 72449158825 scopus 로고    scopus 로고
    • Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirochete
    • Izard, J. et al. Cryo-electron tomography elucidates the molecular architecture of Treponema pallidum, the syphilis spirochete. J. Bacteriol. 191, 7566-7580 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 7566-7580
    • Izard, J.1
  • 16
    • 0006210009 scopus 로고
    • Treponema pallidum invades intercellular junctions of endothelial cell monolayers
    • Thomas, D. D. et al. Treponema pallidum invades intercellular junctions of endothelial cell monolayers. Proc. Natl Acad. Sci. USA 85, 3608-3612 (1988).
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 3608-3612
    • Thomas, D.D.1
  • 17
    • 84951277335 scopus 로고    scopus 로고
    • Flagellar motility of the pathogenic spirochetes
    • Wolgemuth, C. W. Flagellar motility of the pathogenic spirochetes. Semin. Cell Dev. Biol. 46, 104-112 (2015).
    • (2015) Semin. Cell Dev. Biol. , vol.46 , pp. 104-112
    • Wolgemuth, C.W.1
  • 18
    • 0032540874 scopus 로고    scopus 로고
    • Complete genome sequence of Treponema pallidum, the syphilis spirochete
    • Fraser, C. M. et al. Complete genome sequence of Treponema pallidum, the syphilis spirochete. Science 281, 375-388 (1998).
    • (1998) Science , vol.281 , pp. 375-388
    • Fraser, C.M.1
  • 20
    • 34147191555 scopus 로고    scopus 로고
    • Phagocytosis of Borrelia burgdorferi and Treponema pallidum potentiates innate immune activation and induces gamma interferon production
    • Moore, M. W. et al. Phagocytosis of Borrelia burgdorferi and Treponema pallidum potentiates innate immune activation and induces gamma interferon production. Infect. Immun. 75, 2046-2062 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 2046-2062
    • Moore, M.W.1
  • 21
    • 39649102172 scopus 로고    scopus 로고
    • Scientific monogamy: Thirty years dancing with the same bug: 2007 Thomas Parran Award Lecture
    • Lukehart, S. A. Scientific monogamy: thirty years dancing with the same bug: 2007 Thomas Parran Award Lecture. Sex. Transm. Dis. 35, 2-7 (2008).
    • (2008) Sex. Transm. Dis. , vol.35 , pp. 2-7
    • Lukehart, S.A.1
  • 22
    • 0016642480 scopus 로고
    • Secondary syphilis: A clinico-pathological review
    • Abell, E., Marks, R. & Jones, E. W. Secondary syphilis: a clinico-pathological review. Br. J. Dermatol. 93, 53-61 (1975).
    • (1975) Br. J. Dermatol. , vol.93 , pp. 53-61
    • Abell, E.1    Marks, R.2    Jones, E.W.3
  • 24
    • 33847683862 scopus 로고    scopus 로고
    • Treponema pallidum elicits innate and adaptive cellular immune responses in skin and blood during secondary syphilis: A flow-cytometric analysis
    • Salazar, J. C. et al. Treponema pallidum elicits innate and adaptive cellular immune responses in skin and blood during secondary syphilis: a flow-cytometric analysis. J. Infect. Dis. 195, 879-887 (2007).
    • (2007) J. Infect. Dis. , vol.195 , pp. 879-887
    • Salazar, J.C.1
  • 25
    • 78149304382 scopus 로고    scopus 로고
    • Host defense mechanisms in secondary syphilitic lesions: A role for IFN-κ/IL-17-producing CD8+ T cells?
    • Stary, G. et al. Host defense mechanisms in secondary syphilitic lesions: a role for IFN-κ/IL-17-producing CD8+ T cells? Am. J. Pathol. 177, 2421-2432 (2010).
    • (2010) Am. J. Pathol. , vol.177 , pp. 2421-2432
    • Stary, G.1
  • 26
    • 84864620354 scopus 로고    scopus 로고
    • Immune evasion and recognition of the syphilis spirochete in blood and skin of secondary syphilis patients: Two immunologically distinct compartments
    • Cruz, A. R. et al. Immune evasion and recognition of the syphilis spirochete in blood and skin of secondary syphilis patients: two immunologically distinct compartments. PLoS Negl Trop. Dis. 6, e1717 (2012).
    • (2012) PLoS Negl Trop. Dis. , vol.6
    • Cruz, A.R.1
  • 27
    • 77955293683 scopus 로고    scopus 로고
    • Secondary syphilis in Cali, Colombia: New concepts in disease pathogenesis
    • Cruz, A. R. et al. Secondary syphilis in Cali, Colombia: new concepts in disease pathogenesis. PLoS Negl Trop. Dis. 4, e690 (2010).
    • (2010) PLoS Negl Trop. Dis. , vol.4 , pp. e690
    • Cruz, A.R.1
  • 29
    • 0017081470 scopus 로고
    • Humoral immunity in experimental syphilis. I. The demonstration of resistance conferred by passive immunization
    • Bishop, N. H. & Miller, J. N. Humoral immunity in experimental syphilis. I. The demonstration of resistance conferred by passive immunization. J. Immunol. 117, 191-196 (1976).
    • (1976) J. Immunol. , vol.117 , pp. 191-196
    • Bishop, N.H.1    Miller, J.N.2
  • 30
    • 0015899571 scopus 로고
    • Immunity to syphilis. I. Passive transfer in rabbits with hyperimmune serum
    • Perine, P. L., Weiser, R. S. & Klebanoff, S. J. Immunity to syphilis. I. Passive transfer in rabbits with hyperimmune serum. Infect. Immun. 8, 787-790 (1973).
    • (1973) Infect. Immun. , vol.8 , pp. 787-790
    • Perine, P.L.1    Weiser, R.S.2    Klebanoff, S.J.3
  • 31
    • 0020646416 scopus 로고
    • The biology, pathology and immunology of syphilis
    • Sell, S. & Norris, S. J. The biology, pathology and immunology of syphilis. Int. Rev. Exp. Pathol. 24, 203-276 (1983).
    • (1983) Int. Rev. Exp. Pathol. , vol.24 , pp. 203-276
    • Sell, S.1    Norris, S.J.2
  • 32
    • 0021983454 scopus 로고
    • Reinfection of chancre-immune rabbits with Treponema pallidum. I. Light and immunofluorescence studies
    • Sell, S., Salman, J. & Norris, S. J. Reinfection of chancre-immune rabbits with Treponema pallidum. I. Light and immunofluorescence studies. Am. J. Pathol. 118, 248-255 (1985).
    • (1985) Am. J. Pathol. , vol.118 , pp. 248-255
    • Sell, S.1    Salman, J.2    Norris, S.J.3
  • 33
    • 0036753733 scopus 로고    scopus 로고
    • The immune response to infection with Treponema pallidum, the stealth pathogen
    • Salazar, J. C., Hazlett, K. R. & Radolf, J. D. The immune response to infection with Treponema pallidum, the stealth pathogen. Microbes Infect. 4, 1133-1140 (2002).
    • (2002) Microbes Infect. , vol.4 , pp. 1133-1140
    • Salazar, J.C.1    Hazlett, K.R.2    Radolf, J.D.3
  • 34
    • 84055193960 scopus 로고    scopus 로고
    • Syphilis: Using modern approaches to understand an old disease
    • Ho, E. L. & Lukehart, S. A. Syphilis: using modern approaches to understand an old disease. J. Clin. Invest. 121, 4584-4592 (2011).
    • (2011) J. Clin. Invest. , vol.121 , pp. 4584-4592
    • Ho, E.L.1    Lukehart, S.A.2
  • 35
    • 0035132533 scopus 로고    scopus 로고
    • Biology of Treponema pallidum: Correlation of functional activities with genome sequence data
    • Norris, S. J., Cox, D. L. & Weinstock, G. M. Biology of Treponema pallidum: correlation of functional activities with genome sequence data. J. Mol. Microbiol. Biotechnol. 3, 37-62 (2001).
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 37-62
    • Norris, S.J.1    Cox, D.L.2    Weinstock, G.M.3
  • 36
    • 0006220997 scopus 로고
    • Factors affecting the survival of Treponema pallidum in vitro
    • Nelson, R. A. Jr. Factors affecting the survival of Treponema pallidum in vitro. Am. J. Hyg. 48, 120-132 (1948).
    • (1948) Am. J. Hyg. , vol.48 , pp. 120-132
    • Nelson, R.A.1
  • 37
    • 0019522692 scopus 로고
    • Cultivation of virulent Treponema pallidum in tissue culture
    • Fieldsteel, A. H., Cox, D. L. & Moeckli, R. A. Cultivation of virulent Treponema pallidum in tissue culture. Infect. Immun. 32, 908-915 (1981).
    • (1981) Infect. Immun. , vol.32 , pp. 908-915
    • Fieldsteel, A.H.1    Cox, D.L.2    Moeckli, R.A.3
  • 38
    • 0020054250 scopus 로고
    • In vitro cultivation of Treponema pallidum: Independent confirmation
    • Norris, S. J. In vitro cultivation of Treponema pallidum: independent confirmation. Infect. Immun. 36, 437-439 (1982).
    • (1982) Infect. Immun. , vol.36 , pp. 437-439
    • Norris, S.J.1
  • 39
    • 0022455720 scopus 로고
    • Factors affecting the multiplication and subculture of Treponema pallidum subsp. Pallidum in a tissue culture system
    • Norris, S. J. & Edmondson, D. G. Factors affecting the multiplication and subculture of Treponema pallidum subsp. pallidum in a tissue culture system. Infect. Immun. 53, 534-539 (1986).
    • (1986) Infect. Immun. , vol.53 , pp. 534-539
    • Norris, S.J.1    Edmondson, D.G.2
  • 40
    • 84929995550 scopus 로고    scopus 로고
    • Identification of functional candidates amongst hypothetical proteins of Treponema pallidum ssp. Pallidum
    • Naqvi, A. A., Shahbaaz, M., Ahmad, F. & Hassan, M. I. Identification of functional candidates amongst hypothetical proteins of Treponema pallidum ssp. pallidum. PLoS ONE 10, e0124177 (2015).
    • (2015) PLoS ONE , vol.10
    • Naqvi, A.A.1    Shahbaaz, M.2    Ahmad, F.3    Hassan, M.I.4
  • 41
    • 84874585719 scopus 로고    scopus 로고
    • Evidence for an ABC-type riboflavin transporter system in pathogenic spirochetes
    • Deka, R. K., Brautigam, C. A., Biddy, B. A., Liu, W. Z. & Norgard, M. V. Evidence for an ABC-type riboflavin transporter system in pathogenic spirochetes. mBio 4, e00615-12 (2013).
    • (2013) MBio , vol.4 , pp. e00615-e00712
    • Deka, R.K.1    Brautigam, C.A.2    Biddy, B.A.3    Liu, W.Z.4    Norgard, M.V.5
  • 42
    • 84936929927 scopus 로고    scopus 로고
    • Evidence for posttranslational protein flavinylation in the syphilis spirochete Treponema pallidum: Structural and biochemical insights from the catalytic core of a periplasmic flavin-trafficking protein
    • Deka, R. K., Brautigam, C. A., Liu, W. Z., Tomchick, D. R. & Norgard, M. V. Evidence for posttranslational protein flavinylation in the syphilis spirochete Treponema pallidum: structural and biochemical insights from the catalytic core of a periplasmic flavin-trafficking protein. mBio 6, e00519-15 (2015).
    • (2015) MBio , vol.6 , pp. e00519-e00615
    • Deka, R.K.1    Brautigam, C.A.2    Liu, W.Z.3    Tomchick, D.R.4    Norgard, M.V.5
  • 43
    • 54749084727 scopus 로고    scopus 로고
    • Isolation and laboratory maintenance of Treponema pallidum
    • Chapter 12, Unit 12A.1
    • Lukehart, S. A. & Marra, C. M. Isolation and laboratory maintenance of Treponema pallidum. Curr. Protoc. Microbiol. Chapter 12, Unit 12A.1 (2007).
    • (2007) Curr. Protoc. Microbiol
    • Lukehart, S.A.1    Marra, C.M.2
  • 44
    • 0018717694 scopus 로고
    • Surface-associated host proteins on virulent Treponema pallidum
    • Alderete, J. F. & Baseman, J. B. Surface-associated host proteins on virulent Treponema pallidum. Infect. Immun. 26, 1048-1056 (1979).
    • (1979) Infect. Immun. , vol.26 , pp. 1048-1056
    • Alderete, J.F.1    Baseman, J.B.2
  • 45
    • 0029091151 scopus 로고
    • Treponema pallidum and the quest for outer membrane proteins
    • Radolf, J. D. Treponema pallidum and the quest for outer membrane proteins. Mol. Microbiol. 16, 1067-1073 (1995).
    • (1995) Mol. Microbiol. , vol.16 , pp. 1067-1073
    • Radolf, J.D.1
  • 46
    • 84881170792 scopus 로고    scopus 로고
    • MyD88 deficiency markedly worsens tissue inflammation and bacterial clearance in mice infected with Treponema pallidum, the agent of syphilis
    • Silver, A. C. et al. MyD88 deficiency markedly worsens tissue inflammation and bacterial clearance in mice infected with Treponema pallidum, the agent of syphilis. PLoS ONE 8, e71388 (2013).
    • (2013) PLoS ONE , vol.8
    • Silver, A.C.1
  • 47
    • 84896725484 scopus 로고    scopus 로고
    • Current status of syphilis vaccine development: Need, challenges, prospects
    • Cameron, C. E. & Lukehart, S. A. Current status of syphilis vaccine development: need, challenges, prospects. Vaccine 32, 1602-1609 (2014).
    • (2014) Vaccine , vol.32 , pp. 1602-1609
    • Cameron, C.E.1    Lukehart, S.A.2
  • 49
    • 2642680890 scopus 로고
    • Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidum
    • Radolf, J. D., Norgard, M. V. & Schulz, W. W. Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidum. Proc. Natl Acad. Sci. USA 86, 2051-2055 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2051-2055
    • Radolf, J.D.1    Norgard, M.V.2    Schulz, W.W.3
  • 50
    • 0024308491 scopus 로고
    • Demonstration of rare protein in the outer membrane of Treponema pallidum subsp. Pallidum by freeze-fracture analysis
    • Walker, E. M., Zampighi, G. A., Blanco, D. R., Miller, J. N. & Lovett, M. A. Demonstration of rare protein in the outer membrane of Treponema pallidum subsp. pallidum by freeze-fracture analysis. J. Bacteriol. 171, 5005-5011 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 5005-5011
    • Walker, E.M.1    Zampighi, G.A.2    Blanco, D.R.3    Miller, J.N.4    Lovett, M.A.5
  • 51
    • 0002969806 scopus 로고
    • The minimal infectious inoculum of Spirochaeta pallida (Nichols strain) and a consideration of its rate of multiplication in vivo
    • Magnuson, H. J., Eagle, H. & Fleischman, R. The minimal infectious inoculum of Spirochaeta pallida (Nichols strain) and a consideration of its rate of multiplication in vivo. Am. J. Syph. Gonorrhea Vener. Dis. 32, 1-18 (1948).
    • (1948) Am. J. Syph. Gonorrhea Vener. Dis. , vol.32 , pp. 1-18
    • Magnuson, H.J.1    Eagle, H.2    Fleischman, R.3
  • 52
    • 0033557257 scopus 로고    scopus 로고
    • Treponema pallidum major sheath protein homologue TprK is a target of opsonic antibody and the protective immune response
    • Centurion-Lara, A. et al. Treponema pallidum major sheath protein homologue TprK is a target of opsonic antibody and the protective immune response. J. Exp. Med. 189, 647-656 (1999).
    • (1999) J. Exp. Med. , vol.189 , pp. 647-656
    • Centurion-Lara, A.1
  • 53
    • 33749567374 scopus 로고    scopus 로고
    • Molecular evolution of the tprC. D, I, K, G, and J genes in the pathogenic genus Treponema
    • Gray, R. R. et al. Molecular evolution of the tprC. D, I, K, G, and J genes in the pathogenic genus Treponema. Mol. Biol. Evol. 23, 2220-2233 (2006).
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 2220-2233
    • Gray, R.R.1
  • 55
    • 67649403394 scopus 로고    scopus 로고
    • Common strategies for antigenic variation by bacterial, fungal and protozoan pathogens
    • Deitsch, K. W., Lukehart, S. A. & Stringer, J. R. Common strategies for antigenic variation by bacterial, fungal and protozoan pathogens. Nat. Rev. Microbiol. 7, 493-503 (2009).
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 493-503
    • Deitsch, K.W.1    Lukehart, S.A.2    Stringer, J.R.3
  • 56
    • 0035821220 scopus 로고    scopus 로고
    • The TprK protein of Treponema pallidum is periplasmic and is not a target of opsonic antibody or protective immunity
    • Hazlett, K. R. et al. The TprK protein of Treponema pallidum is periplasmic and is not a target of opsonic antibody or protective immunity. J. Exp. Med. 193, 1015-1026 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 1015-1026
    • Hazlett, K.R.1
  • 57
    • 78649914479 scopus 로고    scopus 로고
    • Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum
    • Cox, D. L. et al. Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum. Infect. Immun. 78, 5178-5194 (2010).
    • (2010) Infect. Immun. , vol.78 , pp. 5178-5194
    • Cox, D.L.1
  • 58
    • 0034122411 scopus 로고    scopus 로고
    • Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92
    • Cameron, C. E. et al. Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92. J. Infect. Dis. 181, 1401-1413 (2000).
    • (2000) J. Infect. Dis. , vol.181 , pp. 1401-1413
    • Cameron, C.E.1
  • 59
    • 84929119861 scopus 로고    scopus 로고
    • Bipartite topology of Treponema pallidum repeat proteins C/D and I: Outer membrane insertion, trimerization, and porin function require a C-terminal β-barrel domain
    • Anand, A. et al. Bipartite topology of Treponema pallidum repeat proteins C/D and I: outer membrane insertion, trimerization, and porin function require a C-terminal β-barrel domain. J. Biol. Chem. 290, 12313-12331 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 12313-12331
    • Anand, A.1
  • 60
    • 84861213325 scopus 로고    scopus 로고
    • TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structure
    • Anand, A. et al. TprC/D (Tp0117/131), a trimeric, pore-forming rare outer membrane protein of Treponema pallidum, has a bipartite domain structure. J. Bacteriol. 194, 2321-2333 (2012).
    • (2012) J. Bacteriol. , vol.194 , pp. 2321-2333
    • Anand, A.1
  • 61
    • 84876178833 scopus 로고    scopus 로고
    • The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformers
    • Anand, A. et al. The major outer sheath protein (Msp) of Treponema denticola has a bipartite domain architecture and exists as periplasmic and outer membrane-spanning conformers. J. Bacteriol. 195, 2060-2071 (2013).
    • (2013) J. Bacteriol. , vol.195 , pp. 2060-2071
    • Anand, A.1
  • 62
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67, 593-656 (2003).
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 63
    • 84878518777 scopus 로고    scopus 로고
    • Fine analysis of genetic diversity of the tpr gene family among treponemal species, subspecies and strains
    • Centurion-Lara, A. et al. Fine analysis of genetic diversity of the tpr gene family among treponemal species, subspecies and strains. PLoS Negl Trop. Dis. 7, e2222 (2013).
    • (2013) PLoS Negl Trop. Dis. , vol.7
    • Centurion-Lara, A.1
  • 64
    • 79958843998 scopus 로고    scopus 로고
    • TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein
    • Desrosiers, D. C. et al. TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein. Mol. Microbiol. 80, 1496-1515 (2011).
    • (2011) Mol. Microbiol. , vol.80 , pp. 1496-1515
    • Desrosiers, D.C.1
  • 65
    • 84929440351 scopus 로고    scopus 로고
    • A homology model reveals novel structural features and an immunodominant surface loop/opsonic target in the Treponema pallidum BamA ortholog TP-0326
    • Luthra, A. et al. A homology model reveals novel structural features and an immunodominant surface loop/opsonic target in the Treponema pallidum BamA ortholog TP-0326. J. Bacteriol. 197, 1906-1920 (2015).
    • (2015) J. Bacteriol. , vol.197 , pp. 1906-1920
    • Luthra, A.1
  • 66
    • 84902327125 scopus 로고    scopus 로고
    • Assembly of β-barrel proteins into bacterial outer membranes
    • Selkrig, J., Leyton, D. L., Webb, C. T. & Lithgow, T. Assembly of β-barrel proteins into bacterial outer membranes. Biochim. Biophys. Acta 1843, 1542-1550 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1542-1550
    • Selkrig, J.1    Leyton, D.L.2    Webb, C.T.3    Lithgow, T.4
  • 67
    • 84884419175 scopus 로고    scopus 로고
    • Structural insight into the biogenesis of β-barrel membrane proteins
    • Noinaj, N. et al. Structural insight into the biogenesis of β-barrel membrane proteins. Nature 501, 385-390 (2013).
    • (2013) Nature , vol.501 , pp. 385-390
    • Noinaj, N.1
  • 68
    • 0017648412 scopus 로고
    • Characterization of the attachment of Treponema pallidum (Nichols strain) to cultured mammalian cells and the potential relationship of attachment to pathogenicity
    • Fitzgerald, T. J., Johnson, R. C., Miller, J. N. & Sykes, J. A. Characterization of the attachment of Treponema pallidum (Nichols strain) to cultured mammalian cells and the potential relationship of attachment to pathogenicity. Infect. Immun. 18, 467-478 (1977).
    • (1977) Infect. Immun. , vol.18 , pp. 467-478
    • Fitzgerald, T.J.1    Johnson, R.C.2    Miller, J.N.3    Sykes, J.A.4
  • 69
    • 0017646146 scopus 로고
    • Parasitism by virulent Treponema pallidum of host cell surfaces
    • Hayes, N. S., Muse, K. E., Collier, A. M. & Baseman, J. B. Parasitism by virulent Treponema pallidum of host cell surfaces. Infect. Immun. 17, 174-186 (1977).
    • (1977) Infect. Immun. , vol.17 , pp. 174-186
    • Hayes, N.S.1    Muse, K.E.2    Collier, A.M.3    Baseman, J.B.4
  • 70
    • 84906417349 scopus 로고
    • Attachment of Treponema pallidum to fibronectin, laminin, collagen IV, and collagen I, and blockage of attachment by immune rabbit IgG
    • Fitzgerald, T. J., Repesh, L. A., Blanco, D. R. & Miller, J. N. Attachment of Treponema pallidum to fibronectin, laminin, collagen IV, and collagen I, and blockage of attachment by immune rabbit IgG. Br. J. Vener. Dis. 60, 357-363 (1984).
    • (1984) Br. J. Vener. Dis. , vol.60 , pp. 357-363
    • Fitzgerald, T.J.1    Repesh, L.A.2    Blanco, D.R.3    Miller, J.N.4
  • 72
    • 0037408253 scopus 로고    scopus 로고
    • Identification of a Treponema pallidum laminin-binding protein
    • Cameron, C. E. Identification of a Treponema pallidum laminin-binding protein. Infect. Immun. 71, 2525-2533 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 2525-2533
    • Cameron, C.E.1
  • 73
    • 27744587898 scopus 로고    scopus 로고
    • Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin
    • Cameron, C. E., Brouwer, N. L., Tisch, L. M. & Kuroiwa, J. M. Defining the interaction of the Treponema pallidum adhesin Tp0751 with laminin. Infect. Immun. 73, 7485-7494 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 7485-7494
    • Cameron, C.E.1    Brouwer, N.L.2    Tisch, L.M.3    Kuroiwa, J.M.4
  • 74
    • 84864626180 scopus 로고    scopus 로고
    • Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin
    • Houston, S., Hof, R., Honeyman, L., Hassler, J. & Cameron, C. E. Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin. PLoS Pathog. 8, e1002822 (2012).
    • (2012) PLoS Pathog. , vol.8
    • Houston, S.1    Hof, R.2    Honeyman, L.3    Hassler, J.4    Cameron, C.E.5
  • 75
    • 84908112563 scopus 로고    scopus 로고
    • The multifunctional role of the pallilysin-associated Treponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradation
    • Houston, S. et al. The multifunctional role of the pallilysin-associated Treponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradation. Mol. Microbiol. 91, 618-634 (2014).
    • (2014) Mol. Microbiol. , vol.91 , pp. 618-634
    • Houston, S.1
  • 76
    • 42949134430 scopus 로고    scopus 로고
    • A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectin
    • Brinkman, M. B. et al. A novel Treponema pallidum antigen, TP0136, is an outer membrane protein that binds human fibronectin. Infect. Immun. 76, 1848-1857 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 1848-1857
    • Brinkman, M.B.1
  • 77
    • 84928823058 scopus 로고    scopus 로고
    • Treponema pallidum subsp. Pallidum TP0136 protein is heterogeneous among isolates and binds cellular and plasma fibronectin via its NH2-terminal end
    • Ke, W., Molini, B. J., Lukehart, S. A. & Giacani, L. Treponema pallidum subsp. pallidum TP0136 protein is heterogeneous among isolates and binds cellular and plasma fibronectin via its NH2-terminal end. PLoS Negl Trop. Dis. 9, e0003662 (2015).
    • (2015) PLoS Negl Trop. Dis. , vol.9
    • Ke, W.1    Molini, B.J.2    Lukehart, S.A.3    Giacani, L.4
  • 78
    • 84969243999 scopus 로고    scopus 로고
    • Treponema pallidum lipoprotein TP0435 expressed in Borrelia burgdorferi produces multiple surface/periplasmic isoforms and mediates adherence
    • Chan, K. et al. Treponema pallidum lipoprotein TP0435 expressed in Borrelia burgdorferi produces multiple surface/periplasmic isoforms and mediates adherence. Sci. Rep. 6, 25593 (2016).
    • (2016) Sci. Rep. , vol.6 , pp. 25593
    • Chan, K.1
  • 79
    • 0022353755 scopus 로고
    • The outer membrane of Treponema pallidum: Biological significance and biochemical properties
    • Penn, C. W., Cockayne, A. & Bailey, M. J. The outer membrane of Treponema pallidum: biological significance and biochemical properties. J. Gen. Microbiol. 131, 2349-2357 (1985).
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2349-2357
    • Penn, C.W.1    Cockayne, A.2    Bailey, M.J.3
  • 80
    • 0026605987 scopus 로고
    • The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum
    • Cox, D. L., Chang, P., McDowall, A. W. & Radolf, J. D. The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum. Infect. Immun. 60, 1076-1083 (1992).
    • (1992) Infect. Immun. , vol.60 , pp. 1076-1083
    • Cox, D.L.1    Chang, P.2    McDowall, A.W.3    Radolf, J.D.4
  • 81
    • 0026481983 scopus 로고
    • A subpopulation of Treponema pallidum is resistant to phagocytosis: Possible mechanism of persistence
    • Lukehart, S. A., Shaffer, J. M. & Baker-Zander, S. A. A subpopulation of Treponema pallidum is resistant to phagocytosis: possible mechanism of persistence. J. Infect. Dis. 166, 1449-1453 (1992).
    • (1992) J. Infect. Dis. , vol.166 , pp. 1449-1453
    • Lukehart, S.A.1    Shaffer, J.M.2    Baker-Zander, S.A.3
  • 82
    • 2942677762 scopus 로고    scopus 로고
    • Gene conversion: A mechanism for generation of heterogeneity in the tprK gene of Treponema pallidum during infection
    • Centurion-Lara, A. et al. Gene conversion: a mechanism for generation of heterogeneity in the tprK gene of Treponema pallidum during infection. Mol. Microbiol. 52, 1579-1596 (2004).
    • (2004) Mol. Microbiol. , vol.52 , pp. 1579-1596
    • Centurion-Lara, A.1
  • 83
    • 33750468688 scopus 로고    scopus 로고
    • Antigenic variation of TprK V regions abrogates specific antibody binding in syphilis
    • LaFond, R. E., Molini, B. J., Van Voorhis, W. C. & Lukehart, S. A. Antigenic variation of TprK V regions abrogates specific antibody binding in syphilis. Infect. Immun. 74, 6244-6251 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 6244-6251
    • LaFond, R.E.1    Molini, B.J.2    Van Voorhis, W.C.3    Lukehart, S.A.4
  • 84
    • 77951633722 scopus 로고    scopus 로고
    • Antigenic variation in Treponema pallidum: TprK sequence diversity accumulates in response to immune pressure during experimental syphilis
    • Giacani, L. et al. Antigenic variation in Treponema pallidum: TprK sequence diversity accumulates in response to immune pressure during experimental syphilis. J. Immunol. 184, 3822-3829 (2010).
    • (2010) J. Immunol. , vol.184 , pp. 3822-3829
    • Giacani, L.1
  • 85
    • 84911396352 scopus 로고    scopus 로고
    • Antigenic variation of TprK facilitates development of secondary syphilis
    • Reid, T. B., Molini, B. J., Fernandez, M. C. & Lukehart, S. A. Antigenic variation of TprK facilitates development of secondary syphilis. Infect. Immun. 82, 4959-4967 (2014).
    • (2014) Infect. Immun. , vol.82 , pp. 4959-4967
    • Reid, T.B.1    Molini, B.J.2    Fernandez, M.C.3    Lukehart, S.A.4
  • 86
    • 84866307448 scopus 로고    scopus 로고
    • Comparative investigation of the genomic regions involved in antigenic variation of the TprK antigen among treponemal species, subspecies, and strains
    • Giacani, L. et al. Comparative investigation of the genomic regions involved in antigenic variation of the TprK antigen among treponemal species, subspecies, and strains. J. Bacteriol. 194, 4208-4225 (2012).
    • (2012) J. Bacteriol. , vol.194 , pp. 4208-4225
    • Giacani, L.1
  • 87
    • 84883829562 scopus 로고    scopus 로고
    • Resequencing of Treponema pallidum ssp.pallidum strains Nichols and SS14: Correction of sequencing errors resulted in increased separation of syphilis treponeme subclusters
    • Petrosova, H. et al. Resequencing of Treponema pallidum ssp. pallidum strains Nichols and SS14: correction of sequencing errors resulted in increased separation of syphilis treponeme subclusters. PLoS ONE 8, e74319 (2013).
    • (2013) PLoS ONE , vol.8
    • Petrosova, H.1
  • 88
    • 35148814341 scopus 로고    scopus 로고
    • Length of guanosine homopolymeric repeats modulates promoter activity of subfamily II tpr genes of Treponema pallidum ssp. Pallidum
    • Giacani, L., Lukehart, S. & Centurion-Lara, A. Length of guanosine homopolymeric repeats modulates promoter activity of subfamily II tpr genes of Treponema pallidum ssp. pallidum. FEMS Immunol. Med. Microbiol. 51, 289-301 (2007).
    • (2007) FEMS Immunol. Med. Microbiol. , vol.51 , pp. 289-301
    • Giacani, L.1    Lukehart, S.2    Centurion-Lara, A.3
  • 91
    • 77957905087 scopus 로고    scopus 로고
    • Cellular architecture of Treponema pallidum: Novel flagellum, periplasmic cone, and cell envelope as revealed by cryo electron tomography
    • Liu, J. et al. Cellular architecture of Treponema pallidum: novel flagellum, periplasmic cone, and cell envelope as revealed by cryo electron tomography. J. Mol. Biol. 403, 546-561 (2010).
    • (2010) J. Mol. Biol. , vol.403 , pp. 546-561
    • Liu, J.1
  • 92
    • 84898953304 scopus 로고    scopus 로고
    • New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography
    • Briegel, A. et al. New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography. Biochemistry 53, 1575-1585 (2014).
    • (2014) Biochemistry , vol.53 , pp. 1575-1585
    • Briegel, A.1
  • 93
    • 1842454798 scopus 로고    scopus 로고
    • The Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum
    • Deka, R. K., Goldberg, M. S., Hagman, K. E. & Norgard, M. V. The Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum. J. Bacteriol. 186, 2303-2308 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 2303-2308
    • Deka, R.K.1    Goldberg, M.S.2    Hagman, K.E.3    Norgard, M.V.4
  • 94
    • 11244349700 scopus 로고    scopus 로고
    • Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an l-methionine-binding protein
    • Deka, R. K. et al. Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an l-methionine-binding protein. J. Biol. Chem. 279, 55644-55650 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 55644-55650
    • Deka, R.K.1
  • 95
    • 84924666772 scopus 로고    scopus 로고
    • Evidence that TP-0144 of Treponema pallidum is a thiamine-binding protein
    • Bian, J., Tu, Y., Wang, S. M., Wang, X. Y. & Li, C. Evidence that TP-0144 of Treponema pallidum is a thiamine-binding protein. J. Bacteriol. 197, 1164-1172 (2015).
    • (2015) J. Bacteriol. , vol.197 , pp. 1164-1172
    • Bian, J.1    Tu, Y.2    Wang, S.M.3    Wang, X.Y.4    Li, C.5
  • 96
    • 84921020525 scopus 로고    scopus 로고
    • Diversity of membrane transport proteins for vitamins in bacteria and archaea
    • Jaehme, M. & Slotboom, D. J. Diversity of membrane transport proteins for vitamins in bacteria and archaea. Biochim. Biophys. Acta 1850, 565-576 (2015).
    • (2015) Biochim. Biophys. Acta , vol.1850 , pp. 565-576
    • Jaehme, M.1    Slotboom, D.J.2
  • 97
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee, Y. H., Deka, R. K., Norgard, M. V., Radolf, J. D. & Hasemann, C. A. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nat. Struct. Biol. 6, 628-633 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 628-633
    • Lee, Y.H.1    Deka, R.K.2    Norgard, M.V.3    Radolf, J.D.4    Hasemann, C.A.5
  • 98
    • 33646363802 scopus 로고    scopus 로고
    • The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum
    • Deka, R. K. et al. The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum. J. Biol. Chem. 281, 8072-8081 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8072-8081
    • Deka, R.K.1
  • 99
    • 34848839191 scopus 로고    scopus 로고
    • Structural and biochemical basis for polyamine binding to the Tp0655 lipoprotein of Treponema pallidum: Putative role for Tp0655 (TpPotD) as a polyamine receptor
    • Machius, M. et al. Structural and biochemical basis for polyamine binding to the Tp0655 lipoprotein of Treponema pallidum: putative role for Tp0655 (TpPotD) as a polyamine receptor. J. Mol. Biol. 373, 681-694 (2007).
    • (2007) J. Mol. Biol. , vol.373 , pp. 681-694
    • Machius, M.1
  • 100
    • 84876560419 scopus 로고    scopus 로고
    • The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis
    • Deka, R. K., Brautigam, C. A., Liu, W. Z., Tomchick, D. R. & Norgard, M. V. The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis. J. Biol. Chem. 288, 11106-11121 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 11106-11121
    • Deka, R.K.1    Brautigam, C.A.2    Liu, W.Z.3    Tomchick, D.R.4    Norgard, M.V.5
  • 101
    • 84861818260 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the interaction between two periplasmic Treponema pallidum lipoproteins that are components of a TPR-protein-associated TRAP transporter (TPAT)
    • Brautigam, C. A., Deka, R. K., Schuck, P., Tomchick, D. R. & Norgard, M. V. Structural and thermodynamic characterization of the interaction between two periplasmic Treponema pallidum lipoproteins that are components of a TPR-protein-associated TRAP transporter (TPAT). J. Mol. Biol. 420, 70-86 (2012).
    • (2012) J. Mol. Biol. , vol.420 , pp. 70-86
    • Brautigam, C.A.1    Deka, R.K.2    Schuck, P.3    Tomchick, D.R.4    Norgard, M.V.5
  • 102
    • 84857598413 scopus 로고    scopus 로고
    • Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter
    • Deka, R. K. et al. Structural, bioinformatic, and in vivo analyses of two Treponema pallidum lipoproteins reveal a unique TRAP transporter. J. Mol. Biol. 416, 678-696 (2012).
    • (2012) J. Mol. Biol. , vol.416 , pp. 678-696
    • Deka, R.K.1
  • 103
    • 34250122582 scopus 로고
    • Lactate oxidation by Treponema pallidum
    • Austin, F. E. & Cox, C. D. Lactate oxidation by Treponema pallidum. Curr. Microbiol. 13, 123-128 (1986).
    • (1986) Curr. Microbiol. , vol.13 , pp. 123-128
    • Austin, F.E.1    Cox, C.D.2
  • 104
    • 0031470826 scopus 로고    scopus 로고
    • Genomic sequence of a Lyme disease spirochaete
    • Fraser, C. M. et al. Genomic sequence of a Lyme disease spirochaete. Borrelia burgdorferi. Nature 390, 580-586 (1997).
    • (1997) Borrelia Burgdorferi. Nature , vol.390 , pp. 580-586
    • Fraser, C.M.1
  • 105
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • Gorke, B. & Stulke, J. Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat. Rev. Microbiol. 6, 613-624 (2008).
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 613-624
    • Gorke, B.1    Stulke, J.2
  • 106
    • 0031940026 scopus 로고    scopus 로고
    • Illuminating the agent of syphilis: The Treponema pallidum genome project
    • Norris, S. J., Fraser, C. M. & Weinstock, G. M. Illuminating the agent of syphilis: the Treponema pallidum genome project. Electrophoresis 19, 551-553 (1998).
    • (1998) Electrophoresis , vol.19 , pp. 551-553
    • Norris, S.J.1    Fraser, C.M.2    Weinstock, G.M.3
  • 107
    • 0035862448 scopus 로고    scopus 로고
    • Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum
    • Roberson, R. S., Ronimus, R. S., Gephard, S. & Morgan, H. W. Biochemical characterization of an active pyrophosphate-dependent phosphofructokinase from Treponema pallidum. FEMS Microbiol. Lett. 194, 257-260 (2001).
    • (2001) FEMS Microbiol. Lett. , vol.194 , pp. 257-260
    • Roberson, R.S.1    Ronimus, R.S.2    Gephard, S.3    Morgan, H.W.4
  • 108
    • 0036094071 scopus 로고    scopus 로고
    • The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi
    • Moore, S. A., Ronimus, R. S., Roberson, R. S. & Morgan, H. W. The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure 10, 659-671 (2002).
    • (2002) Structure , vol.10 , pp. 659-671
    • Moore, S.A.1    Ronimus, R.S.2    Roberson, R.S.3    Morgan, H.W.4
  • 110
    • 0027412292 scopus 로고
    • ATP versus pyrophosphate: Glycolysis revisited in parasitic protists
    • Mertens, E. ATP versus pyrophosphate: glycolysis revisited in parasitic protists. Parasitol. Today 9, 122-126 (1993).
    • (1993) Parasitol. Today , vol.9 , pp. 122-126
    • Mertens, E.1
  • 111
    • 0034319185 scopus 로고    scopus 로고
    • Molecular biology of oxygen tolerance in lactic acid bacteria: Functions of NADH oxidases and Dpr in oxidative stress
    • Higuchi, M., Yamamoto, Y. & Kamio, Y. Molecular biology of oxygen tolerance in lactic acid bacteria: functions of NADH oxidases and Dpr in oxidative stress. J. Biosci. Bioeng. 90, 484-493 (2000).
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 484-493
    • Higuchi, M.1    Yamamoto, Y.2    Kamio, Y.3
  • 112
    • 84946201626 scopus 로고    scopus 로고
    • Loss of NADH oxidase activity in Streptococcus mutans leads to Rex-mediated overcompensation of NAD+ regeneration by lactate dehydrogenase
    • Baker, J. L., Derr, A. D., Faustoferri, R. C. & Quivey, R. G. Jr. Loss of NADH oxidase activity in Streptococcus mutans leads to Rex-mediated overcompensation of NAD+ regeneration by lactate dehydrogenase. J. Bacteriol. 197, 3645-3657 (2015).
    • (2015) J. Bacteriol. , vol.197 , pp. 3645-3657
    • Baker, J.L.1    Derr, A.D.2    Faustoferri, R.C.3    Quivey, R.G.4
  • 113
    • 0025113556 scopus 로고
    • Effects of molecular oxygen, oxidation-reduction potential, and antioxidants upon in vitro replication of Treponema pallidum subsp. Pallidum
    • Cox, D. L. et al. Effects of molecular oxygen, oxidation-reduction potential, and antioxidants upon in vitro replication of Treponema pallidum subsp. pallidum. Appl. Environ. Microbiol. 56, 3063-3072 (1990).
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3063-3072
    • Cox, D.L.1
  • 114
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz, E. G., Ghosh, M. C. & Rouault, T. A. Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306, 2087-2090 (2004).
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 115
    • 84899913081 scopus 로고    scopus 로고
    • Adaptations of anaerobic archaea to life under extreme energy limitation
    • Mayer, F. & Muller, V. Adaptations of anaerobic archaea to life under extreme energy limitation. FEMS Microbiol. Rev. 38, 449-472 (2014).
    • (2014) FEMS Microbiol. Rev. , vol.38 , pp. 449-472
    • Mayer, F.1    Muller, V.2
  • 116
    • 0038081029 scopus 로고    scopus 로고
    • The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase
    • Hazlett, K. R. et al. The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase. J. Biol. Chem. 278, 20687-20694 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 20687-20694
    • Hazlett, K.R.1
  • 118
    • 84906417853 scopus 로고
    • Affinities of Treponema pallidum for human lactoferrin and transferrin
    • Alderete, J. F., Peterson, K. M. & Baseman, J. B. Affinities of Treponema pallidum for human lactoferrin and transferrin. Genitourin. Med. 64, 359-363 (1988).
    • (1988) Genitourin. Med. , vol.64 , pp. 359-363
    • Alderete, J.F.1    Peterson, K.M.2    Baseman, J.B.3
  • 119
    • 34247170432 scopus 로고    scopus 로고
    • Crystal structure of the Tp34 (TP0971) lipoprotein of Treponema pallidum: Implications of its metal-bound state and affinity for human lactoferrin
    • Deka, R. K. et al. Crystal structure of the Tp34 (TP0971) lipoprotein of Treponema pallidum: implications of its metal-bound state and affinity for human lactoferrin. J. Biol. Chem. 282, 5944-5958 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 5944-5958
    • Deka, R.K.1
  • 120
    • 84857783784 scopus 로고    scopus 로고
    • Structural basis for iron piracy by pathogenic Neisseria
    • Noinaj, N. et al. Structural basis for iron piracy by pathogenic Neisseria. Nature 483, 53-58 (2012).
    • (2012) Nature , vol.483 , pp. 53-58
    • Noinaj, N.1
  • 121
    • 84864308938 scopus 로고    scopus 로고
    • Ferroportin-mediated iron transport: Expression and regulation
    • Ward, D. M. & Kaplan, J. Ferroportin-mediated iron transport: expression and regulation. Biochim. Biophys. Acta 1823, 1426-1433 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1426-1433
    • Ward, D.M.1    Kaplan, J.2
  • 122
    • 34250634316 scopus 로고    scopus 로고
    • The general transition metal (Tro) and Zn2+ (Znu) transporters in Treponema pallidum: Analysis of metal specificities and expression profiles
    • Desrosiers, D. C. et al. The general transition metal (Tro) and Zn2+ (Znu) transporters in Treponema pallidum: analysis of metal specificities and expression profiles. Mol. Microbiol. 65, 137-152 (2007).
    • (2007) Mol. Microbiol. , vol.65 , pp. 137-152
    • Desrosiers, D.C.1
  • 123
    • 84870818863 scopus 로고    scopus 로고
    • Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasis
    • Brautigam, C. A. et al. Biophysical and bioinformatic analyses implicate the Treponema pallidum Tp34 lipoprotein (Tp0971) in transition metal homeostasis. J. Bacteriol. 194, 6771-6781 (2012).
    • (2012) J. Bacteriol. , vol.194 , pp. 6771-6781
    • Brautigam, C.A.1
  • 124
    • 79960149723 scopus 로고    scopus 로고
    • Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11
    • Koch, D. et al. Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11. J. Biol. Chem. 286, 25317-25330 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 25317-25330
    • Koch, D.1
  • 125
    • 0032851843 scopus 로고    scopus 로고
    • Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum
    • Posey, J. E., Hardham, J. M., Norris, S. J. & Gherardini, F. C. Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum. Proc. Natl Acad. Sci. USA 96, 10887-10892 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10887-10892
    • Posey, J.E.1    Hardham, J.M.2    Norris, S.J.3    Gherardini, F.C.4
  • 126
    • 0036285278 scopus 로고    scopus 로고
    • Contribution of neelaredoxin to oxygen tolerance by Treponema pallidum
    • Hazlett, K. R. et al. Contribution of neelaredoxin to oxygen tolerance by Treponema pallidum. Methods Enzymol. 353, 140-156 (2002).
    • (2002) Methods Enzymol. , vol.353 , pp. 140-156
    • Hazlett, K.R.1
  • 127
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney, F. E. Jr., Verhagen, M. F., Cui, X. & Adams, M. W. Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286, 306-309 (1999).
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney, F.E.1    Verhagen, M.F.2    Cui, X.3    Adams, M.W.4
  • 128
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 77, 755-776 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 129
    • 31944447259 scopus 로고    scopus 로고
    • Crystal structure of antigen TpF1 from Treponema pallidum
    • Thumiger, A. et al. Crystal structure of antigen TpF1 from Treponema pallidum. Proteins 62, 827-830 (2006).
    • (2006) Proteins , vol.62 , pp. 827-830
    • Thumiger, A.1
  • 130
    • 77950870461 scopus 로고    scopus 로고
    • Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum
    • Parsonage, D. et al. Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum. Proc. Natl Acad. Sci. USA 107, 6240-6245 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 6240-6245
    • Parsonage, D.1
  • 131
    • 0023184441 scopus 로고
    • Role of disulfide bonds in the oligomeric structure and protease resistance of recombinant and native Treponema pallidum surface antigen 4D
    • Radolf, J. D., Borenstein, L. A., Kim, J. Y., Fehniger, T. E. & Lovett, M. A. Role of disulfide bonds in the oligomeric structure and protease resistance of recombinant and native Treponema pallidum surface antigen 4D. J. Bacteriol. 169, 1365-1371 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 1365-1371
    • Radolf, J.D.1    Borenstein, L.A.2    Kim, J.Y.3    Fehniger, T.E.4    Lovett, M.A.5
  • 132
    • 84928883790 scopus 로고    scopus 로고
    • Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analyses
    • Brautigam, C. A., Deka, R. K., Liu, W. Z. & Norgard, M. V. Insights into the potential function and membrane organization of the TP0435 (Tp17) lipoprotein from Treponema pallidum derived from structural and biophysical analyses. Protein Sci. 24, 11-19 (2015).
    • (2015) Protein Sci. , vol.24 , pp. 11-19
    • Brautigam, C.A.1    Deka, R.K.2    Liu, W.Z.3    Norgard, M.V.4
  • 133
    • 78649658931 scopus 로고    scopus 로고
    • The mechanism of signal transduction by two-component systems
    • Casino, P., Rubio, V. & Marina, A. The mechanism of signal transduction by two-component systems. Curr. Opin. Struct. Biol. 20, 763-771 (2010).
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 763-771
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 134
    • 72949124219 scopus 로고    scopus 로고
    • Sense and sensibility: Flagellum-mediated gene regulation
    • Anderson, J. K., Smith, T. G. & Hoover, T. R. Sense and sensibility: flagellum-mediated gene regulation. Trends Microbiol. 18, 30-37 (2010).
    • (2010) Trends Microbiol. , vol.18 , pp. 30-37
    • Anderson, J.K.1    Smith, T.G.2    Hoover, T.R.3
  • 136
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: The first 25 years of a universal bacterial second messenger
    • Romling, U., Galperin, M. Y. & Gomelsky, M. Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol. Mol. Biol. Rev. 77, 1-52 (2013).
    • (2013) Microbiol. Mol. Biol. Rev. , vol.77 , pp. 1-52
    • Romling, U.1    Galperin, M.Y.2    Gomelsky, M.3
  • 137
    • 84901006261 scopus 로고    scopus 로고
    • Stress-induced remodeling of the bacterial proteome
    • Guo, M. S. & Gross, C. A. Stress-induced remodeling of the bacterial proteome. Curr. Biol. 24, R424-R434 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. R424-R434
    • Guo, M.S.1    Gross, C.A.2
  • 138
    • 84873557818 scopus 로고    scopus 로고
    • Identification of the Treponema pallidum subsp.pallidum TP0092 (RpoE) regulon and its implications for pathogen persistence in the host and syphilis pathogenesis
    • Giacani, L., Denisenko, O., Tompa, M. & Centurion-Lara, A. Identification of the Treponema pallidum subsp. pallidum TP0092 (RpoE) regulon and its implications for pathogen persistence in the host and syphilis pathogenesis. J. Bacteriol. 195, 896-907 (2013).
    • (2013) J. Bacteriol. , vol.195 , pp. 896-907
    • Giacani, L.1    Denisenko, O.2    Tompa, M.3    Centurion-Lara, A.4
  • 139
    • 0034192966 scopus 로고    scopus 로고
    • The biology of enhancer-dependent transcriptional regulation in bacteria: Insights from genome sequences
    • Studholme, D. J. & Buck, M. The biology of enhancer-dependent transcriptional regulation in bacteria: insights from genome sequences. FEMS Microbiol. Lett. 186, 1-9 (2000).
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 1-9
    • Studholme, D.J.1    Buck, M.2
  • 140
    • 84865733572 scopus 로고    scopus 로고
    • The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcription
    • Bush, M. & Dixon, R. The role of bacterial enhancer binding proteins as specialized activators of σ54-dependent transcription. Microbiol. Mol. Biol. Rev. 76, 497-529 (2012).
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 497-529
    • Bush, M.1    Dixon, R.2
  • 141
    • 0035940482 scopus 로고    scopus 로고
    • Expression of Borrelia burgdorferi OspC and DbpA is controlled by a RpoN-RpoS regulatory pathway
    • Hubner, A. et al. Expression of Borrelia burgdorferi OspC and DbpA is controlled by a RpoN-RpoS regulatory pathway. Proc. Natl Acad. Sci. USA 98, 12724-12729 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12724-12729
    • Hubner, A.1
  • 142
    • 0141814623 scopus 로고    scopus 로고
    • The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in Borrelia burgdorferi
    • Yang, X. F., Alani, S. M. & Norgard, M. V. The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in Borrelia burgdorferi. Proc. Natl Acad. Sci. USA 100, 11001-11006 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11001-11006
    • Yang, X.F.1    Alani, S.M.2    Norgard, M.V.3
  • 143
    • 84856566939 scopus 로고    scopus 로고
    • Whole genome sequences of three Treponema pallidum ssp.pertenue strains: Yaws and syphilis treponemes differ in less than 0.2% of the genome sequence
    • Cejkova, D. et al. Whole genome sequences of three Treponema pallidum ssp. pertenue strains: yaws and syphilis treponemes differ in less than 0.2% of the genome sequence. PLoS Negl Trop. Dis. 6, e1471 (2012).
    • (2012) PLoS Negl Trop. Dis. , vol.6
    • Cejkova, D.1
  • 144
    • 84920465676 scopus 로고    scopus 로고
    • Whole genome sequence of the Treponema pallidum subsp. Endemicum strain Bosnia A: The genome is related to yaws treponemes but contains few loci similar to syphilis treponemes
    • Staudova, B. et al. Whole genome sequence of the Treponema pallidum subsp. endemicum strain Bosnia A: the genome is related to yaws treponemes but contains few loci similar to syphilis treponemes. PLoS Negl Trop. Dis. 8, e3261 (2014).
    • (2014) PLoS Negl Trop. Dis. , vol.8
    • Staudova, B.1
  • 145
    • 84998694529 scopus 로고    scopus 로고
    • Complete genome sequence of the Treponema pallidum subsp.pallidum Sea81-4 strain
    • Giacani, L. et al. Complete genome sequence of the Treponema pallidum subsp. pallidum Sea81-4 strain. Genome Announc. 2, e00333-14 (2014).
    • (2014) Genome Announc. , vol.2 , pp. e00333-e00414
    • Giacani, L.1
  • 146
    • 84866945465 scopus 로고    scopus 로고
    • Whole genome sequence of Treponema pallidum ssp. Pallidum, strain Mexico A, suggests recombination between yaws and syphilis strains
    • Petrosova, H. et al. Whole genome sequence of Treponema pallidum ssp. pallidum, strain Mexico A, suggests recombination between yaws and syphilis strains. PLoS Negl Trop. Dis. 6, e1832 (2012).
    • (2012) PLoS Negl Trop. Dis. , vol.6
    • Petrosova, H.1
  • 148
    • 77952552068 scopus 로고    scopus 로고
    • Regulatory roles of the bacterial nitrogen-related phosphotransferase system
    • Pfluger-Grau, K. & Gorke, B. Regulatory roles of the bacterial nitrogen-related phosphotransferase system. Trends Microbiol. 18, 205-214 (2010).
    • (2010) Trends Microbiol. , vol.18 , pp. 205-214
    • Pfluger-Grau, K.1    Gorke, B.2
  • 149
    • 0021211416 scopus 로고
    • Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system
    • Reizer, J., Novotny, M. J., Hengstenberg, W. & Saier, M. H. Jr. Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system. J. Bacteriol. 160, 333-340 (1984).
    • (1984) J. Bacteriol. , vol.160 , pp. 333-340
    • Reizer, J.1    Novotny, M.J.2    Hengstenberg, W.3    Saier, M.H.4
  • 150
    • 0021924835 scopus 로고
    • Streptococcal phosphoenolpyruvate: Sugar phosphotransferase system: Purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein
    • Deutscher, J., Kessler, U. & Hengstenberg, W. Streptococcal phosphoenolpyruvate: sugar phosphotransferase system: purification and characterization of a phosphoprotein phosphatase which hydrolyzes the phosphoryl bond in seryl-phosphorylated histidine-containing protein. J. Bacteriol. 163, 1203-1209 (1985).
    • (1985) J. Bacteriol. , vol.163 , pp. 1203-1209
    • Deutscher, J.1    Kessler, U.2    Hengstenberg, W.3
  • 151
    • 12144278799 scopus 로고    scopus 로고
    • Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases
    • Gonzalez, C. F., Stonestrom, A. J., Lorca, G. L. & Saier, M. H. Jr. Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases. Biochemistry 44, 598-608 (2005).
    • (2005) Biochemistry , vol.44 , pp. 598-608
    • Gonzalez, C.F.1    Stonestrom, A.J.2    Lorca, G.L.3    Saier, M.H.4
  • 153
    • 84901013706 scopus 로고    scopus 로고
    • The bacterial phosphoenolpyruvate: Carbohydrate phosphotransferase system: Regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions
    • Deutscher, J. et al. The bacterial phosphoenolpyruvate: carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions. Microbiol. Mol. Biol. Rev. 78, 231-256 (2014).
    • (2014) Microbiol. Mol. Biol. Rev. , vol.78 , pp. 231-256
    • Deutscher, J.1
  • 154
    • 83855165675 scopus 로고    scopus 로고
    • The myriad roles of cyclic AMP in microbial pathogens: From signal to sword
    • McDonough, K. A. & Rodriguez, A. The myriad roles of cyclic AMP in microbial pathogens: from signal to sword. Nat. Rev. Microbiol. 10, 27-38 (2012).
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 27-38
    • McDonough, K.A.1    Rodriguez, A.2
  • 155
    • 0028057599 scopus 로고
    • Analysis of Borrelia burgdorferi membrane architecture by freeze-fracture electron microscopy
    • Radolf, J. D., Bourell, K. W., Akins, D. R., Brusca, J. S. & Norgard, M. V. Analysis of Borrelia burgdorferi membrane architecture by freeze-fracture electron microscopy. J. Bacteriol. 176, 21-31 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 21-31
    • Radolf, J.D.1    Bourell, K.W.2    Akins, D.R.3    Brusca, J.S.4    Norgard, M.V.5
  • 156
    • 82355171892 scopus 로고    scopus 로고
    • The transition from closed to open conformation of Treponema pallidum outer membrane-associated lipoprotein TP0453 involves membrane sensing and integration by two amphipathic helices
    • Luthra, A. et al. The transition from closed to open conformation of Treponema pallidum outer membrane-associated lipoprotein TP0453 involves membrane sensing and integration by two amphipathic helices. J. Biol. Chem. 286, 41656-41668 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 41656-41668
    • Luthra, A.1
  • 157
    • 21544456659 scopus 로고    scopus 로고
    • Genome scale identification of Treponema pallidum antigens
    • McKevitt, M. et al. Genome scale identification of Treponema pallidum antigens. Infect. Immun. 73, 4445-4450 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 4445-4450
    • McKevitt, M.1
  • 158
    • 33644930898 scopus 로고    scopus 로고
    • Reactivity of antibodies from syphilis patients to a protein array representing the Treponema pallidum proteome
    • Brinkman, M. B. et al. Reactivity of antibodies from syphilis patients to a protein array representing the Treponema pallidum proteome. J. Clin. Microbiol. 44, 888-891 (2006).
    • (2006) J. Clin. Microbiol. , vol.44 , pp. 888-891
    • Brinkman, M.B.1


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