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Volumn 78, Issue 12, 2010, Pages 5178-5194

Surface immunolabeling and consensus computational framework to identify candidate rare outer membrane proteins of Treponema pallidum

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ANTIGEN; GLYCOLIPID; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN M ANTIBODY; LIPOPROTEIN; MEMBRANE ANTIGEN; OUTER MEMBRANE PROTEIN; PERIPLASMIC BINDING PROTEIN; PERIPLASMIC PROTEIN; PROTEINASE K;

EID: 78649914479     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00834-10     Document Type: Article
Times cited : (91)

References (132)
  • 1
    • 0030877543 scopus 로고    scopus 로고
    • Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane
    • Akins, D. R., E. Robinson, D. Shevchenko, C. Elkins, D. L. Cox, and J. D. Radolf. 1997. Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane. J. Bacteriol. 179:5076-5086.
    • (1997) J. Bacteriol. , vol.179 , pp. 5076-5086
    • Akins, D.R.1    Robinson, E.2    Shevchenko, D.3    Elkins, C.4    Cox, D.L.5    Radolf, J.D.6
  • 2
    • 0025270698 scopus 로고
    • Phagocytosis of opsonized Treponema pallidum subsp. pallidum proceeds slowly
    • Alder, J. D., L. Friess, M. Tengowski, and R. F. Schell. 1990. Phagocytosis of opsonized Treponema pallidum subsp. pallidum proceeds slowly. Infect. Immun. 58:1167-1173.
    • (1990) Infect. Immun. , vol.58 , pp. 1167-1173
    • Alder, J.D.1    Friess, L.2    Tengowski, M.3    Schell, R.F.4
  • 3
    • 0018717694 scopus 로고
    • Surface-associated host proteins on virulent Treponema pallidum
    • Alderete, J. F., and J. B. Baseman. 1979. Surface-associated host proteins on virulent Treponema pallidum. Infect. Immun. 26:1048-1056.
    • (1979) Infect. Immun. , vol.26 , pp. 1048-1056
    • Alderete, J.F.1    Baseman, J.B.2
  • 4
    • 13244259253 scopus 로고    scopus 로고
    • Evaluation of methods for predicting the topology of B-barrel outer membrane proteins and a consensus prediction method
    • Bagos, P. G., T. D. Liakopoulos, and S. J. Hamodrakas. 2005. Evaluation of methods for predicting the topology of B-barrel outer membrane proteins and a consensus prediction method. BMC Bioinformatics 6:7.
    • (2005) BMC Bioinformatics , vol.6 , pp. 7
    • Bagos, P.G.1    Liakopoulos, T.D.2    Hamodrakas, S.J.3
  • 5
    • 3242883431 scopus 로고    scopus 로고
    • PRED-TMBB: A web server for predicting the topology of B-barrel outer membrane proteins
    • Bagos, P. G., T. D. Liakopoulos, I. C. Spyropoulos, and S. J. Hamodrakas. 2004. PRED-TMBB: a web server for predicting the topology of B-barrel outer membrane proteins. Nucleic Acids Res. 32:W400-W404.
    • (2004) Nucleic Acids Res. , vol.32
    • Bagos, P.G.1    Liakopoulos, T.D.2    Spyropoulos, I.C.3    Hamodrakas, S.J.4
  • 6
    • 0027410540 scopus 로고
    • VDRL antibodies enhance phagocytosis of Treponema pallidum by macrophages
    • Baker-Zander, S. A., J. M. Shaffer, and S. A. Lukehart. 1993. VDRL antibodies enhance phagocytosis of Treponema pallidum by macrophages. J. Infect. Dis. 167:1100-1105.
    • (1993) J. Infect. Dis. , vol.167 , pp. 1100-1105
    • Baker-Zander, S.A.1    Shaffer, J.M.2    Lukehart, S.A.3
  • 9
    • 0028297815 scopus 로고
    • Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins
    • Belisle, J. T., M. E. Brandt, J. D. Radolf, and M. V. Norgard. 1994. Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins. J. Bacteriol. 176:2151-2157.
    • (1994) J. Bacteriol. , vol.176 , pp. 2151-2157
    • Belisle, J.T.1    Brandt, M.E.2    Radolf, J.D.3    Norgard, M.V.4
  • 11
    • 3242879514 scopus 로고    scopus 로고
    • BOMP: A program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria
    • Berven, F. S., K. Flikka, H. B. Jensen, and I. Eidhammer. 2004. BOMP: a program to predict integral beta-barrel outer membrane proteins encoded within genomes of Gram-negative bacteria. Nucleic Acids Res. 32:W394-W399.
    • (2004) Nucleic Acids Res. , vol.32
    • Berven, F.S.1    Flikka, K.2    Jensen, H.B.3    Eidhammer, I.4
  • 12
    • 0011202990 scopus 로고
    • Humoral immune mechanisms in experimental syphilis
    • R. F. Schell and D. M. Musher (ed.), Marcel Dekker, Inc., New York, NY
    • Bishop, N. H., and J. N. Miller. 1983. Humoral immune mechanisms in experimental syphilis, p. 241-270. In R. F. Schell and D. M. Musher (ed.), Pathogenesis and immunology of treponemal infection, vol. 1. Marcel Dekker, Inc., New York, NY.
    • (1983) Pathogenesis and Immunology of Treponemal Infection , vol.1 , pp. 241-270
    • Bishop, N.H.1    Miller, J.N.2
  • 16
    • 0028225554 scopus 로고
    • Isolation of integral membrane proteins by phase partitioning with Triton X-114
    • Brusca, J. S., and J. D. Radolf. 1994. Isolation of integral membrane proteins by phase partitioning with Triton X-114. Methods Enzymol. 228:182-193.
    • (1994) Methods Enzymol. , vol.228 , pp. 182-193
    • Brusca, J.S.1    Radolf, J.D.2
  • 17
    • 78649957383 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 18
    • 0032765412 scopus 로고    scopus 로고
    • The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure
    • Caimano, M. J., K. W. Bourell, T. D. Bannister, D. L. Cox, and J. D. Radolf. 1999. The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure. Infect. Immun. 67:4072-4083.
    • (1999) Infect. Immun. , vol.67 , pp. 4072-4083
    • Caimano, M.J.1    Bourell, K.W.2    Bannister, T.D.3    Cox, D.L.4    Radolf, J.D.5
  • 19
    • 0037408253 scopus 로고    scopus 로고
    • Identification of a Treponema pallidum lamininbinding protein
    • Cameron, C. E. 2003. Identification of a Treponema pallidum lamininbinding protein. Infect. Immun. 71:2525-2533.
    • (2003) Infect. Immun. , vol.71 , pp. 2525-2533
    • Cameron, C.E.1
  • 20
    • 72449176516 scopus 로고    scopus 로고
    • The T. pallidum outer membrane and outer membrane proteins
    • J. D. Radolf and S. A. Lukehart (ed.), Caister Academic Press, Norwich, United Kingdom
    • Cameron, C. E. 2006. The T. pallidum outer membrane and outer membrane proteins, p. 237-266. In J. D. Radolf and S. A. Lukehart (ed.), Pathogenic treponema: molecular and cellular biology. Caister Academic Press, Norwich, United Kingdom.
    • (2006) Pathogenic Treponema: Molecular and Cellular Biology , pp. 237-266
    • Cameron, C.E.1
  • 22
    • 0034122411 scopus 로고    scopus 로고
    • Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92
    • Cameron, C. E., S. A. Lukehart, C. Castro, B. Molini, C. Godornes, and W. C. Van Voorhis. 2000. Opsonic potential, protective capacity, and sequence conservation of the Treponema pallidum subspecies pallidum Tp92. J. Infect. Dis. 181:1401-1413.
    • (2000) J. Infect. Dis. , vol.181 , pp. 1401-1413
    • Cameron, C.E.1    Lukehart, S.A.2    Castro, C.3    Molini, B.4    Godornes, C.5    Van Voorhis, W.C.6
  • 23
    • 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., C. Castro, L. Barrett, C. Cameron, M. Mostowfi, W. C. Van Voorhis, and S. A. Lukehart. 1999. 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) J. Exp. Med. , vol.189 , pp. 647-656
    • Centurion-Lara, A.1    Castro, C.2    Barrett, L.3    Cameron, C.4    Mostowfi, M.5    Van Voorhis, W.C.6    Lukehart, S.A.7
  • 24
  • 25
    • 0024323710 scopus 로고
    • Major integral membrane protein immunogens of Treponema pallidum are proteolipids
    • Chamberlain, N. R., M. E. Brandt, A. L. Erwin, J. D. Radolf, and M. V. Norgard. 1989. Major integral membrane protein immunogens of Treponema pallidum are proteolipids. Infect. Immun. 57:2872-2877.
    • (1989) Infect. Immun. , vol.57 , pp. 2872-2877
    • Chamberlain, N.R.1    Brandt, M.E.2    Erwin, A.L.3    Radolf, J.D.4    Norgard, M.V.5
  • 26
    • 34247544233 scopus 로고    scopus 로고
    • Signal-CF: A subsite-coupled and window-fusing approach for predicting signal peptides
    • Chou, K. C., and H. B. Shen. 2007. Signal-CF: a subsite-coupled and window-fusing approach for predicting signal peptides. Biochem. Biophys. Res. Commun. 357:633-640.
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 633-640
    • Chou, K.C.1    Shen, H.B.2
  • 27
    • 0006163774 scopus 로고
    • Protective layer covering pathogenic treponemata
    • Christiansen, S. 1963. Protective layer covering pathogenic treponemata. Lancet i:423-425.
    • (1963) Lancet , vol.1 , pp. 423-425
    • Christiansen, S.1
  • 28
    • 0008297169 scopus 로고
    • The Oslo study of the natural history of untreated syphilis. An epidemiologic investigation based on a restudy of the Boeck-Bruusgaard material
    • Clark, E. G., and N. Danbolt. 1955. The Oslo study of the natural history of untreated syphilis. An epidemiologic investigation based on a restudy of the Boeck-Bruusgaard material. J. Chronic Dis. 2:311-344.
    • (1955) J. Chronic Dis. , vol.2 , pp. 311-344
    • Clark, E.G.1    Danbolt, N.2
  • 29
    • 0043073264 scopus 로고    scopus 로고
    • Folding of a monomeric porin, OmpG, in detergent solution
    • Moscow
    • Conlan, S., and H. Bayley. 2003. Folding of a monomeric porin, OmpG, in detergent solution. Biochemistry (Moscow) 42:9453-9465.
    • (2003) Biochemistry , vol.42 , pp. 9453-9465
    • Conlan, S.1    Bayley, H.2
  • 30
    • 0028128859 scopus 로고
    • Culture of Treponema pallidum
    • Cox, D. L. 1994. Culture of Treponema pallidum. Methods Enzymol. 236:390-405.
    • (1994) Methods Enzymol. , vol.236 , pp. 390-405
    • Cox, D.L.1
  • 31
    • 0028956653 scopus 로고
    • Treponema pallidum in gel microdroplets: A novel strategy for investigation of treponemal molecular architecture
    • Cox, D. L., D. R. Akins, S. F. Porcella, M. V. Norgard, and J. D. Radolf. 1995. Treponema pallidum in gel microdroplets: a novel strategy for investigation of treponemal molecular architecture. Mol. Microbiol. 15:1151-1164.
    • (1995) Mol. Microbiol. , vol.15 , pp. 1151-1164
    • Cox, D.L.1    Akins, D.R.2    Porcella, S.F.3    Norgard, M.V.4    Radolf, J.D.5
  • 32
    • 0026605987 scopus 로고
    • The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum
    • Cox, D. L., P. Chang, A. W. McDowall, and J. D. Radolf. 1992. The outer membrane, not a coat of host proteins, limits antigenicity of virulent Treponema pallidum. Infect. Immun. 60:1076-1083.
    • (1992) Infect. Immun. , vol.60 , pp. 1076-1083
    • Cox, D.L.1    Chang, P.2    McDowall, A.W.3    Radolf, J.D.4
  • 33
    • 0034998230 scopus 로고    scopus 로고
    • Insertion of fluorescent fatty acid probes into the outer membranes of the pathogenic spirochaetes Treponema pallidum and Borrelia burgdorferi
    • Cox, D. L., and J. D. Radolf. 2001. Insertion of fluorescent fatty acid probes into the outer membranes of the pathogenic spirochaetes Treponema pallidum and Borrelia burgdorferi. Microbiology 147:1161-1169.
    • (2001) Microbiology , vol.147 , pp. 1161-1169
    • Cox, D.L.1    Radolf, J.D.2
  • 34
    • 37749024618 scopus 로고    scopus 로고
    • Phagocytosis of Borrelia burgdorferi, the Lyme disease spirochete, potentiates innate immune activation and induces apoptosis in human monocytes
    • Cruz, A. R., M. W. Moore, C. J. La Vake, C. H. Eggers, J. C. Salazar, and J. D. Radolf. 2008. Phagocytosis of Borrelia burgdorferi, the Lyme disease spirochete, potentiates innate immune activation and induces apoptosis in human monocytes. Infect. Immun. 76:56-70.
    • (2008) Infect. Immun. , vol.76 , pp. 56-70
    • Cruz, A.R.1    Moore, M.W.2    La Vake, C.J.3    Eggers, C.H.4    Salazar, J.C.5    Radolf, J.D.6
  • 36
    • 33646487063 scopus 로고    scopus 로고
    • Progress towards an effective syphilis vaccine: The past, present and future
    • Cullen, P. A., and C. E. Cameron. 2006. Progress towards an effective syphilis vaccine: the past, present and future. Expert Rev. Vaccines 5:67-80.
    • (2006) Expert Rev. Vaccines , vol.5 , pp. 67-80
    • Cullen, P.A.1    Cameron, C.E.2
  • 37
    • 67649403394 scopus 로고    scopus 로고
    • Common strategies for antigenic variation by bacterial, fungal and protozoan pathogens
    • Deitsch, K. W., S. A. Lukehart, and J. R. Stringer. 2009. Common strategies for antigenic variation by bacterial, fungal and protozoan pathogens. Nat. Rev. Microbiol. 7:493-503.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 493-503
    • Deitsch, K.W.1    Lukehart, S.A.2    Stringer, J.R.3
  • 38
    • 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., C. A. Brautigam, X. F. Yang, J. S. Blevins, M. Machius, D. R. Tomchick, and M. V. Norgard. 2006. 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) J. Biol. Chem. , vol.281 , pp. 8072-8081
    • Deka, R.K.1    Brautigam, C.A.2    Yang, X.F.3    Blevins, J.S.4    Machius, M.5    Tomchick, D.R.6    Norgard, M.V.7
  • 39
    • 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., L. Neil, K. E. Hagman, M. Machius, D. R. Tomchick, C. A. Brautigam, and M. V. Norgard. 2004. Structural evidence that the 32-kilodalton lipoprotein (Tp32) of Treponema pallidum is an L-methionine-binding protein. J. Biol. Chem. 279:55644-55650.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55644-55650
    • Deka, R.K.1    Neil, L.2    Hagman, K.E.3    Machius, M.4    Tomchick, D.R.5    Brautigam, C.A.6    Norgard, M.V.7
  • 40
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot, R., and J. Vanderleyden. 1994. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol. Microbiol. 12:333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 41
    • 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., Y. C. Sun, A. A. Zaidi, C. H. Eggers, D. L. Cox, and J. D. Radolf. 2007. 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) Mol. Microbiol. , vol.65 , pp. 137-152
    • Desrosiers, D.C.1    Sun, Y.C.2    Zaidi, A.A.3    Eggers, C.H.4    Cox, D.L.5    Radolf, J.D.6
  • 42
    • 17644380678 scopus 로고    scopus 로고
    • Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405
    • Edwards, A. M., H. F. Jenkinson, M. J. Woodward, and D. Dymock. 2005. Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405. Infect. Immun. 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
  • 43
    • 1242352009 scopus 로고    scopus 로고
    • The structure of a mycobacterial outer-membrane channel
    • Faller, M., M. Niederweis, and G. E. Schulz. 2004. The structure of a mycobacterial outer-membrane channel. Science 303:1189-1192.
    • (2004) Science , vol.303 , pp. 1189-1192
    • Faller, M.1    Niederweis, M.2    Schulz, G.E.3
  • 44
    • 0029863955 scopus 로고    scopus 로고
    • Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola
    • Fenno, J. C., K. H. Muller, and B. C. McBride. 1996. Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola. J. Bacteriol. 178:2489-2497.
    • (1996) J. Bacteriol. , vol.178 , pp. 2489-2497
    • Fenno, J.C.1    Muller, K.H.2    McBride, B.C.3
  • 45
    • 0017654143 scopus 로고
    • Scanning electron microscopy of Treponema pallidum (Nichols strain) attached to cultured mammalian cells
    • Fitzgerald, T. J., P. Cleveland, R. C. Johnson, J. N. Miller, and J. A. Sykes. 1977. Scanning electron microscopy of Treponema pallidum (Nichols strain) attached to cultured mammalian cells. J. Bacteriol. 130:1333-1344.
    • (1977) J. Bacteriol. , vol.130 , pp. 1333-1344
    • Fitzgerald, T.J.1    Cleveland, P.2    Johnson, R.C.3    Miller, J.N.4    Sykes, J.A.5
  • 46
    • 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., R. C. Johnson, J. N. Miller, and J. A. Sykes. 1977. 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) Infect. Immun. , vol.18 , pp. 467-478
    • Fitzgerald, T.J.1    Johnson, R.C.2    Miller, J.N.3    Sykes, J.A.4
  • 47
    • 0016773244 scopus 로고
    • Treponema pallidum (Nichols strain) in tissue cultures: Cellular attachment, entry, and survival
    • Fitzgerald, T. J., J. N. Miller, and J. A. Sykes. 1975. Treponema pallidum (Nichols strain) in tissue cultures: cellular attachment, entry, and survival. Infect. Immun. 11:1133-1140.
    • (1975) Infect. Immun. , vol.11 , pp. 1133-1140
    • Fitzgerald, T.J.1    Miller, J.N.2    Sykes, J.A.3
  • 49
    • 0023042026 scopus 로고
    • Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12
    • Freudl, R., S. MacIntyre, M. Degen, and U. Henning. 1986. Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12. J. Mol. Biol. 188:491-494.
    • (1986) J. Mol. Biol. , vol.188 , pp. 491-494
    • Freudl, R.1    MacIntyre, S.2    Degen, M.3    Henning, U.4
  • 50
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • Gentle, I. E., L. Burri, and T. Lithgow. 2005. Molecular architecture and function of the Omp85 family of proteins. Mol. Microbiol. 58:1216-1225.
    • (2005) Mol. Microbiol. , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 51
    • 33846026029 scopus 로고    scopus 로고
    • Quantitative analysis of tpr gene expression in Treponema pallidum isolates: Differences among isolates and correlation with T-cell responsiveness in experimental syphilis
    • Giacani, L., B. Molini, C. Godornes, L. Barrett, V. W. Van, A. Centurion-Lara, and S. A. Lukehart. 2007. Quantitative analysis of tpr gene expression in Treponema pallidum isolates: differences among isolates and correlation with T-cell responsiveness in experimental syphilis. Infect. Immun. 75:104-112.
    • (2007) Infect. Immun. , vol.75 , pp. 104-112
    • Giacani, L.1    Molini, B.2    Godornes, C.3    Barrett, L.4    Van, V.W.5    Centurion-Lara, A.6    Lukehart, S.A.7
  • 52
    • 77951633722 scopus 로고    scopus 로고
    • Antigenic variation in Treponema pallidum: TprK sequence diversity accumulates in response to immune pressure during experimental syphilis
    • Giacani, L., B. J. Molini, E. Y. Kim, B. C. Godornes, B. T. Leader, L. C. Tantalo, A. Centurion-Lara, and S. A. Lukehart. 2010. Antigenic variation in Treponema pallidum: TprK sequence diversity accumulates in response to immune pressure during experimental syphilis. J. Immunol. 184:3822-3829.
    • (2010) J. Immunol. , vol.184 , pp. 3822-3829
    • Giacani, L.1    Molini, B.J.2    Kim, E.Y.3    Godornes, B.C.4    Leader, B.T.5    Tantalo, L.C.6    Centurion-Lara, A.7    Lukehart, S.A.8
  • 54
    • 39349091616 scopus 로고    scopus 로고
    • Current developments on B-barrel membrane proteins: Sequence and structure analysis, discrimination and prediction
    • Gromiha, M. M., and M. Suwa. 2007. Current developments on B-barrel membrane proteins: sequence and structure analysis, discrimination and prediction. Curr. Protein Pept. Sci. 8:580-599.
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 580-599
    • Gromiha, M.M.1    Suwa, M.2
  • 55
    • 0028006525 scopus 로고
    • Identification and characterization of the Treponema pallidum tpn50 gene, an ompA homolog
    • Hardham, J. M., and L. V. Stamm. 1994. Identification and characterization of the Treponema pallidum tpn50 gene, an ompA homolog. Infect. Immun. 62:1015-1025.
    • (1994) Infect. Immun. , vol.62 , pp. 1015-1025
    • Hardham, J.M.1    Stamm, L.V.2
  • 56
    • 70449151575 scopus 로고
    • Study of the antigenic structure of Treponema pallidum by specific agglutination
    • Hardy, P. H., Jr., and E. E. Nell. 1957. Study of the antigenic structure of Treponema pallidum by specific agglutination. Am. J. Hyg. 66:160-172.
    • (1957) Am. J. Hyg. , vol.66 , pp. 160-172
    • Hardy Jr., P.H.1    Nell, E.E.2
  • 58
    • 0038081029 scopus 로고    scopus 로고
    • The Treponema pallidum tro operon encodes a multiple metal transporter, a Zndependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase
    • Hazlett, K. R., F. Rusnak, D. G. Kehres, S. W. Bearden, C. J. LaVake, M. E. LaVake, M. E. Maquire, R. D. Perry, and J. D. Radolf. 2003. The Treponema pallidum tro operon encodes a multiple metal transporter, a Zndependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase. J. Biol. Chem. 278:20687-20694.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20687-20694
    • Hazlett, K.R.1    Rusnak, F.2    Kehres, D.G.3    Bearden, S.W.4    LaVake, C.J.5    LaVake, M.E.6    Maquire, M.E.7    Perry, R.D.8    Radolf, J.D.9
  • 59
    • 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., T. J. Sellati, T. T. Nguyen, D. L. Cox, M. L. Clawson, M. J. Caimano, and J. D. Radolf. 2001. 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) J. Exp. Med. , vol.193 , pp. 1015-1026
    • Hazlett, K.R.1    Sellati, T.J.2    Nguyen, T.T.3    Cox, D.L.4    Clawson, M.L.5    Caimano, M.J.6    Radolf, J.D.7
  • 60
    • 3242878999 scopus 로고    scopus 로고
    • PrediSi: Prediction of signal peptides and their cleavage positions
    • DOI 10.1093/nar/gkh378
    • Hiller, K., A. Grote, M. Scheer, R. Munch, and D. Jahn. 2004. PrediSi: prediction of signal peptides and their cleavage positions. Nucleic Acids Res. 32:W375-W379. (Pubitemid 38997362)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS
    • Hiller, K.1    Grote, A.2    Scheer, M.3    Munch, R.4    Jahn, D.5
  • 61
    • 0027377337 scopus 로고
    • The orientation of porin OmpF in the outer membrane of Escherichia coli
    • Hoenger, A., J. M. Pages, D. Fourel, and A. Engel. 1993. The orientation of porin OmpF in the outer membrane of Escherichia coli. J. Mol. Biol. 233:400-413.
    • (1993) J. Mol. Biol. , vol.233 , pp. 400-413
    • Hoenger, A.1    Pages, J.M.2    Fourel, D.3    Engel, A.4
  • 62
    • 0018717663 scopus 로고
    • Electron microscopy of treponemes subjected to the Treponema pallidum immobilization (TPI) test. II. Immunoelectron microscopy
    • Hovind-Hougen, K., A. Birch Andersen, and H. A. Nielsen. 1979. Electron microscopy of treponemes subjected to the Treponema pallidum immobilization (TPI) test. II. Immunoelectron microscopy. Acta Pathol. Microbiol. Scand. 87C:263-268.
    • (1979) Acta Pathol. Microbiol. Scand. , vol.87 C , pp. 263-268
    • Hovind-Hougen, K.1    Andersen, A.B.2    Nielsen, H.A.3
  • 63
    • 77952479299 scopus 로고    scopus 로고
    • Two evolutionarily conserved essential beta-barrel proteins in the chloroplast outer envelope membrane
    • Hsu, S. C., and K. Inoue. 2009. Two evolutionarily conserved essential beta-barrel proteins in the chloroplast outer envelope membrane. Biosci. Trends 3:168-178.
    • (2009) Biosci. Trends , vol.3 , pp. 168-178
    • Hsu, S.C.1    Inoue, K.2
  • 66
    • 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., Y. M. Kang, H. R. Lee, S. H. Lee, and B. K. Choi. 2008. Highly conserved surface proteins of oral spirochetes as adhesins and potent inducers of proinflammatory and osteoclastogenic factors. Infect. Immun. 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
  • 67
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll, L., A. Krogh, and E. L. Sonnhammer. 2004. A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338:1027-1036.
    • (2004) J. Mol. Biol. , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 68
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: The role of the BAM complex in outer membrane protein assembly
    • Knowles, T. J., A. Scott-Tucker, M. Overduin, and I. R. Henderson. 2009. Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat. Rev. Microbiol. 7:206-214.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 69
    • 0022459151 scopus 로고
    • Electron microscopy of Treponema pallidum (Nichols) cultivated in tissue cultures of Sf1Ep cells
    • Konishi, H., Z. Yoshii, and D. L. Cox. 1986. Electron microscopy of Treponema pallidum (Nichols) cultivated in tissue cultures of Sf1Ep cells. Infect. Immun. 53:32-37.
    • (1986) Infect. Immun. , vol.53 , pp. 32-37
    • Konishi, H.1    Yoshii, Z.2    Cox, D.L.3
  • 70
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., B. Larsson, G. von Heijne, and E. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 71
    • 0142183493 scopus 로고    scopus 로고
    • Sequence diversity of Treponema pallidum subsp. pallidum tprK in human syphilis lesions and rabbit-propagated isolates
    • LaFond, R. E., A. Centurion-Lara, C. Godornes, A. M. Rompalo, W. C. Van Voorhis, and S. A. Lukehart. 2003. Sequence diversity of Treponema pallidum subsp. pallidum tprK in human syphilis lesions and rabbit-propagated isolates. J. Bacteriol. 185:6262-6268.
    • (2003) J. Bacteriol. , vol.185 , pp. 6262-6268
    • LaFond, R.E.1    Centurion-Lara, A.2    Godornes, C.3    Rompalo, A.M.4    Van Voorhis, W.C.5    Lukehart, S.A.6
  • 72
    • 33644767982 scopus 로고    scopus 로고
    • TprK sequence diversity accumulates during infection of rabbits with Treponema pallidum subsp. pallidum Nichols strain
    • LaFond, R. E., A. Centurion-Lara, C. Godornes, W. C. Van Voorhis, and S. A. Lukehart. 2006. TprK sequence diversity accumulates during infection of rabbits with Treponema pallidum subsp. pallidum Nichols strain. Infect. Immun. 74:1896-1906.
    • (2006) Infect. Immun. , vol.74 , pp. 1896-1906
    • LaFond, R.E.1    Centurion-Lara, A.2    Godornes, C.3    Van Voorhis, W.C.4    Lukehart, S.A.5
  • 74
    • 0028894512 scopus 로고
    • Laboratory diagnosis and interpretation of tests for syphilis
    • Larsen, S. A., B. M. Steiner, and A. H. Rudolph. 1995. Laboratory diagnosis and interpretation of tests for syphilis. Clin. Microbiol. Rev. 8:1-21.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 1-21
    • Larsen, S.A.1    Steiner, B.M.2    Rudolph, A.H.3
  • 76
    • 0032984288 scopus 로고    scopus 로고
    • Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone
    • Lee, Y. H., R. K. Deka, M. V. Norgard, J. D. Radolf, and C. A. Hasemann. 1999. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nat. Struct. Biol. 6:628-633.
    • (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
  • 77
    • 0036209769 scopus 로고    scopus 로고
    • The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation
    • Lee, Y. H., M. R. Dorwart, K. R. O. Hazlett, R. K. Deka, M. V. Norgard, J. D. Radolf, and C. A. Hasemann. 2002. The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation. J. Bacteriol. 184:2300-2304.
    • (2002) J. Bacteriol. , vol.184 , pp. 2300-2304
    • Lee, Y.H.1    Dorwart, M.R.2    Hazlett, K.R.O.3    Deka, R.K.4    Norgard, M.V.5    Radolf, J.D.6    Hasemann, C.A.7
  • 78
    • 75149192610 scopus 로고    scopus 로고
    • Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins
    • Lenhart, T. R., and D. R. Akins. 2010. Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins. Mol. Microbiol. 75:692-709.
    • (2010) Mol. Microbiol. , vol.75 , pp. 692-709
    • Lenhart, T.R.1    Akins, D.R.2
  • 79
    • 77957905087 scopus 로고    scopus 로고
    • Cellular architecture of Treponema pallidum: Novel flagellum, periplasmic cone, and cell envelope as revealed by cryo electron tomography
    • Lui, J., J. K. Howell, S. D. Bradley, Y. Zheng, Z. H. Zhou, and S. J. Norris. 2010. 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) J. Mol. Biol. , vol.403 , pp. 546-561
    • Lui, J.1    Howell, J.K.2    Bradley, S.D.3    Zheng, Y.4    Zhou, Z.H.5    Norris, S.J.6
  • 80
    • 39649102172 scopus 로고    scopus 로고
    • Scientific monogamy: Thirty years dancing with the same bug. 2007 Thomas Parran Award Lecture
    • Lukehart, S. A. 2008. Scientific monogamy: thirty years dancing with the same bug. 2007 Thomas Parran Award Lecture. Sex. Transm. Dis. 35:2-7.
    • (2008) Sex. Transm. Dis. , vol.35 , pp. 2-7
    • Lukehart, S.A.1
  • 81
    • 78649921625 scopus 로고    scopus 로고
    • Syphilis
    • A. S. Fauci, E. Braunwald, D. L. Kasper, S. J. Hauser, D. L. Longo, and J. L. Jameson (ed.), McGraw Hill, New York, NY
    • Lukehart, S. A. 2008. Syphilis, p. 1038-1046. In A. S. Fauci, E. Braunwald, D. L. Kasper, S. J. Hauser, D. L. Longo, and J. L. Jameson (ed.), Harrison's principles of internal medicine, vol. 17. McGraw Hill, New York, NY.
    • (2008) Harrison's Principles of Internal Medicine , vol.17 , pp. 1038-1046
    • Lukehart, S.A.1
  • 82
    • 0018141476 scopus 로고
    • Demonstration of the in vitro phagocytosis of Treponema pallidum by rabbit peritoneal macrophages
    • Lukehart, S. A., and J. N. Miller. 1978. Demonstration of the in vitro phagocytosis of Treponema pallidum by rabbit peritoneal macrophages. J. Immunol. 121:2014-2024.
    • (1978) J. Immunol. , vol.121 , pp. 2014-2024
    • Lukehart, S.A.1    Miller, J.N.2
  • 83
    • 0026481983 scopus 로고
    • A subpopulation of Treponema pallidum is resistant to phagocytosis: Possible mechanisms of persistence
    • Lukehart, S. A., J. M. Shaffer, and S. A. Baker-Zander. 1992. A subpopulation of Treponema pallidum is resistant to phagocytosis: possible mechanisms of persistence. J. Infect. Dis. 166:1449-1453.
    • (1992) J. Infect. Dis. , vol.166 , pp. 1449-1453
    • Lukehart, S.A.1    Shaffer, J.M.2    Baker-Zander, S.A.3
  • 84
    • 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., C. A. Brautigam, D. R. Tomchick, P. Ward, Z. Otwinowski, J. S. Blevins, R. K. Deka, and M. V. Norgard. 2007. 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) J. Mol. Biol. , vol.373 , pp. 681-694
    • Machius, M.1    Brautigam, C.A.2    Tomchick, D.R.3    Ward, P.4    Otwinowski, Z.5    Blevins, J.S.6    Deka, R.K.7    Norgard, M.V.8
  • 85
    • 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., H. Eagle, and R. Fleischman. 1948. 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. 32:1-19.
    • (1948) Am. J. Syph. Gonorrhea Vener. Dis. , vol.32 , pp. 1-19
    • Magnuson, H.J.1    Eagle, H.2    Fleischman, R.3
  • 88
    • 8544264167 scopus 로고
    • Influence of lysozyme upon the treponeme immobilization reaction
    • Metzger, M., P. H. Hardy, Jr., and E. E. Nell. 1961. Influence of lysozyme upon the treponeme immobilization reaction. Am. J. Hyg. 73:236-244.
    • (1961) Am. J. Hyg. , vol.73 , pp. 236-244
    • Metzger, M.1    Hardy Jr., P.H.2    Nell, E.E.3
  • 89
    • 34147191555 scopus 로고    scopus 로고
    • Phagocytosis of Borrelia burgdorferi and Treponema pallidum potentiates innate immune activation and induces gamma interferon production
    • Moore, M. W., A. R. Cruz, C. J. LaVake, A. L. Marzo, C. H. Eggers, J. C. Salazar, and J. D. Radolf. 2007. Phagocytosis of Borrelia burgdorferi and Treponema pallidum potentiates innate immune activation and induces gamma interferon production. Infect. Immun. 75:2046-2062.
    • (2007) Infect. Immun. , vol.75 , pp. 2046-2062
    • Moore, M.W.1    Cruz, A.R.2    LaVake, C.J.3    Marzo, A.L.4    Eggers, C.H.5    Salazar, J.C.6    Radolf, J.D.7
  • 90
    • 0141446129 scopus 로고    scopus 로고
    • Protection against syphilis correlates with specificity of antibodies to the variable regions of Treponema pallidum repeat protein K
    • Morgan, C. A., S. A. Lukehart, and W. C. Van Voorhis. 2003. Protection against syphilis correlates with specificity of antibodies to the variable regions of Treponema pallidum repeat protein K. Infect. Immun. 71:5605-5612.
    • (2003) Infect. Immun. , vol.71 , pp. 5605-5612
    • Morgan, C.A.1    Lukehart, S.A.2    Van Voorhis, W.C.3
  • 91
    • 84873790495 scopus 로고
    • Immobilization of Treponema pallidum in vitro by antibody produced in syphilitic infection
    • Nelson, R. A., Jr., and M. M. Mayer. 1949. Immobilization of Treponema pallidum in vitro by antibody produced in syphilitic infection. J. Exp. Med. 89:369-393.
    • (1949) J. Exp. Med. , vol.89 , pp. 369-393
    • Nelson Jr., R.A.1    Mayer, M.M.2
  • 92
    • 42949135614 scopus 로고    scopus 로고
    • Nutrient acquisition by mycobacteria
    • Niederweis, M. 2008. Nutrient acquisition by mycobacteria. Microbiology 154:679-692.
    • (2008) Microbiology , vol.154 , pp. 679-692
    • Niederweis, M.1
  • 94
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 95
    • 43249097732 scopus 로고    scopus 로고
    • TMBETADISC-RBF: Discrimination of B-barrel membrane proteins using RBF networks and PSSM profiles
    • Ou, Y. Y., M. M. Gromiha, S. A. Chen, and M. Suwa. 2008. TMBETADISC-RBF: discrimination of B-barrel membrane proteins using RBF networks and PSSM profiles. Comput. Biol. Chem. 32:227-231.
    • (2008) Comput. Biol. Chem. , vol.32 , pp. 227-231
    • Ou, Y.Y.1    Gromiha, M.M.2    Chen, S.A.3    Suwa, M.4
  • 97
    • 0019619565 scopus 로고
    • Avoidance of host defences by Treponema pallidum in situ and on extraction from infected rabbit testes
    • Penn, C. W. 1981. Avoidance of host defences by Treponema pallidum in situ and on extraction from infected rabbit testes. J. Gen. Microbiol. 126:69-75.
    • (1981) J. Gen. Microbiol. , vol.126 , pp. 69-75
    • Penn, C.W.1
  • 98
    • 0020051256 scopus 로고
    • Surface-associated antigens of Treponema pallidum concealed by an inert outer layer
    • Penn, C. W., and J. G. Rhodes. 1982. Surface-associated antigens of Treponema pallidum concealed by an inert outer layer. Immunology 46:9-16.
    • (1982) Immunology , vol.46 , pp. 9-16
    • Penn, C.W.1    Rhodes, J.G.2
  • 99
    • 0015899571 scopus 로고
    • Immunity to syphilis. I. Passive transfer in rabbits with hyperimmune serum
    • Perine, P. L., R. S. Weiser, and S. J. Klebanoff. 1973. Immunity to syphilis. I. Passive transfer in rabbits with hyperimmune serum. Infect. Immun. 8:787-790.
    • (1973) Infect. Immun. , vol.8 , pp. 787-790
    • Perine, P.L.1    Weiser, R.S.2    Klebanoff, S.J.3
  • 100
    • 67650694036 scopus 로고    scopus 로고
    • A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans
    • Pinne, M., and D. A. Haake. 2009. A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans. PLoS One 4:e6071.
    • (2009) PLoS One , vol.4
    • Pinne, M.1    Haake, D.A.2
  • 101
    • 0033623839 scopus 로고    scopus 로고
    • TolC, a macromolecular periplasmic 'chunnel'
    • Postle, K., and H. Vakharia. 2000. TolC, a macromolecular periplasmic 'chunnel.' Nat. Struct. Biol. 7:527-530.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 527-530
    • Postle, K.1    Vakharia, H.2
  • 102
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gramnegative bacteria
    • Pugsley, A. P. 1993. The complete general secretory pathway in gramnegative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 103
    • 35348966245 scopus 로고    scopus 로고
    • The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions
    • Qu, J., C. Mayer, S. Behrens, O. Holst, and J. H. Kleinschmidt. 2007. The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions. J. Mol. Biol. 374:91-105.
    • (2007) J. Mol. Biol. , vol.374 , pp. 91-105
    • Qu, J.1    Mayer, C.2    Behrens, S.3    Holst, O.4    Kleinschmidt, J.H.5
  • 104
    • 0029091151 scopus 로고
    • Treponema pallidum and the quest for outer membrane proteins
    • Radolf, J. D. 1995. Treponema pallidum and the quest for outer membrane proteins. Mol. Microbiol. 16:1067-1073.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1067-1073
    • Radolf, J.D.1
  • 105
    • 0022652804 scopus 로고
    • The surface of virulent Treponema pallidum: Resistance to antibody binding in the absence of complement and surface association of recombinant antigen 4D
    • Radolf, J. D., T. E. Fehniger, F. J. Silverblatt, J. N. Miller, and M. A. Lovett. 1986. The surface of virulent Treponema pallidum: resistance to antibody binding in the absence of complement and surface association of recombinant antigen 4D. Infect. Immun. 52:579-585.
    • (1986) Infect. Immun. , vol.52 , pp. 579-585
    • Radolf, J.D.1    Fehniger, T.E.2    Silverblatt, F.J.3    Miller, J.N.4    Lovett, M.A.5
  • 106
    • 34147146865 scopus 로고    scopus 로고
    • Pathogenesis of syphilis
    • J. D. Radolf and S. A. Lukehart (ed.), Caister Academic Press, Norfolk, United Kingdom
    • Radolf, J. D., K. R. O. Hazlett, and S. A. Lukehart. 2006. Pathogenesis of syphilis, p. 197-236. In J. D. Radolf and S. A. Lukehart (ed.), Pathogenic treponemes: cellular and molecular biology. Caister Academic Press, Norfolk, United Kingdom.
    • (2006) Pathogenic Treponemes: Cellular and Molecular Biology , pp. 197-236
    • Radolf, J.D.1    Hazlett, K.R.O.2    Lukehart, S.A.3
  • 107
    • 33847670013 scopus 로고    scopus 로고
    • Immunology of syphilis
    • J. D. Radolf and S. A. Lukehart (ed.), Caister Academic Press, Norfolk, United Kingdom
    • Radolf, J. D., and S. A. Lukehart. 2006. Immunology of syphilis, p. 285-322. In J. D. Radolf and S. A. Lukehart (ed.), Pathogenic treponemes: cellular and molecular biology. Caister Academic Press, Norfolk, United Kingdom.
    • (2006) Pathogenic Treponemes: Cellular and Molecular Biology , pp. 285-322
    • Radolf, J.D.1    Lukehart, S.A.2
  • 109
    • 0032972602 scopus 로고    scopus 로고
    • Treponema pallidum: Doing a remarkable job with what it's got
    • Radolf, J. D., B. Steiner, and D. Shevchenko. 1999. Treponema pallidum: doing a remarkable job with what it's got. Trends Microbiol. 7:7-9.
    • (1999) Trends Microbiol. , vol.7 , pp. 7-9
    • Radolf, J.D.1    Steiner, B.2    Shevchenko, D.3
  • 110
    • 39149140433 scopus 로고    scopus 로고
    • TMBpro: Secondary structure, beta-contact and tertiary structure prediction of transmembrane beta-barrel proteins
    • DOI 10.1093/bioinformatics/btm548
    • Randall, A., J. Cheng, M. Sweredoski, and P. Baldi. 2008. TMBpro: secondary structure, beta-contact and tertiary structure prediction of transmembrane beta-barrel proteins. Bioinformatics 24:513-520. (Pubitemid 351256295)
    • (2008) Bioinformatics , vol.24 , Issue.4 , pp. 513-520
    • Randall, A.1    Cheng, J.2    Sweredoski, M.3    Baldi, P.4
  • 111
    • 67849103758 scopus 로고    scopus 로고
    • HHomp - Prediction and classification of outer membrane proteins
    • Remmert, M., D. Linke, A. N. Lupas, and J. Soding. 2009. HHomp - prediction and classification of outer membrane proteins. Nucleic Acids Res. 37:W446-W451.
    • (2009) Nucleic Acids Res. , vol.37
    • Remmert, M.1    Linke, D.2    Lupas, A.N.3    Soding, J.4
  • 112
    • 0022338027 scopus 로고
    • Immune immobilization of Treponema pallidum: Antibody and complement interactions revisited
    • Rice, M., and T. J. Fitzgerald. 1985. Immune immobilization of Treponema pallidum: antibody and complement interactions revisited. Can. J. Microbiol. 31:1147-1151.
    • (1985) Can. J. Microbiol. , vol.31 , pp. 1147-1151
    • Rice, M.1    Fitzgerald, T.J.2
  • 113
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz, N., D. Kahne, and T. J. Silhavy. 2006. Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. 4:57-66.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 114
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz, G. E. 2002. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta 1565:308-317.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 115
    • 0020646416 scopus 로고
    • The biology, pathology, and immunology of syphilis
    • Sell, S., and S. J. Norris. 1983. The biology, pathology, and immunology of syphilis. Int. Rev. Exp. Pathol. 24:203-276.
    • (1983) Int. Rev. Exp. Pathol. , vol.24 , pp. 203-276
    • Sell, S.1    Norris, S.J.2
  • 116
    • 30744477217 scopus 로고    scopus 로고
    • Lipoprotein computational prediction in spirochaetal genomes
    • Setubal, J. C., M. Reis, J. Matsunaga, and D. A. Haake. 2006. Lipoprotein computational prediction in spirochaetal genomes. Microbiology 152:113-121.
    • (2006) Microbiology , vol.152 , pp. 113-121
    • Setubal, J.C.1    Reis, M.2    Matsunaga, J.3    Haake, D.A.4
  • 117
    • 0030821179 scopus 로고    scopus 로고
    • Identification of homologs for thioredoxin, peptidyl prolyl cis-trans isomerase, and glycerophosphodiester phosphodiesterase in outer membrane fractions from Treponema pallidum, the syphilis spirochete
    • Shevchenko, D. V., D. R. Akins, E. J. Robinson, M. Li, O. V. Shevchenko, and J. D. Radolf. 1997. Identification of homologs for thioredoxin, peptidyl prolyl cis-trans isomerase, and glycerophosphodiester phosphodiesterase in outer membrane fractions from Treponema pallidum, the syphilis spirochete. Infect. Immun. 65:4179-4189.
    • (1997) Infect. Immun. , vol.65 , pp. 4179-4189
    • Shevchenko, D.V.1    Akins, D.R.2    Robinson, E.J.3    Li, M.4    Shevchenko, O.V.5    Radolf, J.D.6
  • 118
    • 0032899373 scopus 로고    scopus 로고
    • Membrane topology and cellular location of the Treponema pallidum glycerophosphodiester phosphodiesterase (GlpQ) ortholog
    • Shevchenko, D. V., T. J. Sellati, D. L. Cox, O. V. Shevchenko, E. J. Robinson, and J. D. Radolf. 1999. Membrane topology and cellular location of the Treponema pallidum glycerophosphodiester phosphodiesterase (GlpQ) ortholog. Infect. Immun. 67:2266-2276.
    • (1999) Infect. Immun. , vol.67 , pp. 2266-2276
    • Shevchenko, D.V.1    Sellati, T.J.2    Cox, D.L.3    Shevchenko, O.V.4    Robinson, E.J.5    Radolf, J.D.6
  • 120
    • 0023198299 scopus 로고
    • Changes in the cell surface properties of Treponema pallidum that occur during in vitro incubation of freshly extracted organisms
    • Stamm, L. V., R. L. Hodinka, P. B. Wyrick, and P. J. Bassford, Jr. 1987. Changes in the cell surface properties of Treponema pallidum that occur during in vitro incubation of freshly extracted organisms. Infect. Immun. 55:2255-2261.
    • (1987) Infect. Immun. , vol.55 , pp. 2255-2261
    • Stamm, L.V.1    Hodinka, R.L.2    Wyrick, P.B.3    Bassford Jr., P.J.4
  • 121
    • 33750287565 scopus 로고    scopus 로고
    • Characterization of pores formed by YaeT (Omp85) from Escherichia coli
    • Stegmeier, J. F., and C. Andersen. 2006. Characterization of pores formed by YaeT (Omp85) from Escherichia coli. J. Biochem. 140:275-283.
    • (2006) J. Biochem. , vol.140 , pp. 275-283
    • Stegmeier, J.F.1    Andersen, C.2
  • 122
    • 33745727012 scopus 로고    scopus 로고
    • Crystal structure of the monomeric porin OmpG
    • Subbarao, G. V., and B. van den Berg. 2006. Crystal structure of the monomeric porin OmpG. J. Mol. Biol. 360:750-759.
    • (2006) J. Mol. Biol. , vol.360 , pp. 750-759
    • Subbarao, G.V.1    Van Den Berg, B.2
  • 123
    • 0024421758 scopus 로고
    • Molecular characterization of the pathogen-specific, 34-kilodalton membrane immunogen of Treponema pallidum
    • Swancutt, M. A., B. S. Riley, J. D. Radolf, and M. V. Norgard. 1989. Molecular characterization of the pathogen-specific, 34-kilodalton membrane immunogen of Treponema pallidum. Infect. Immun. 57:3314-3323.
    • (1989) Infect. Immun. , vol.57 , pp. 3314-3323
    • Swancutt, M.A.1    Riley, B.S.2    Radolf, J.D.3    Norgard, M.V.4
  • 124
    • 0016032534 scopus 로고
    • Treponema pallidum within cells of a primary chancre from a human female
    • Sykes, J. A., J. N. Miller, and A. J. Kalan. 1974. Treponema pallidum within cells of a primary chancre from a human female. Br. J. Vener. Dis. 50:40-44.
    • (1974) Br. J. Vener. Dis. , vol.50 , pp. 40-44
    • Sykes, J.A.1    Miller, J.N.2    Kalan, A.J.3
  • 126
    • 0033570111 scopus 로고    scopus 로고
    • The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence
    • Vogt, J., and G. E. Schulz. 1999. The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure 7:1301-1309.
    • (1999) Structure , vol.7 , pp. 1301-1309
    • Vogt, J.1    Schulz, G.E.2
  • 127
    • 0017080426 scopus 로고
    • Immunity to syphilis: Passive transfer in rabbits using serial doses of immune serum
    • Weiser, R. S., D. Erickson, P. L. Perine, and N. N. Pearsall. 1976. Immunity to syphilis: passive transfer in rabbits using serial doses of immune serum. Infect. Immun. 13:1402-1407.
    • (1976) Infect. Immun. , vol.13 , pp. 1402-1407
    • Weiser, R.S.1    Erickson, D.2    Perine, P.L.3    Pearsall, N.N.4
  • 128
    • 0242490833 scopus 로고    scopus 로고
    • Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12
    • Werner, J., A. M. Augustus, and R. Misra. 2003. Assembly of TolC, a structurally unique and multifunctional outer membrane protein of Escherichia coli K-12. J. Bacteriol. 185:6540-6547.
    • (2003) J. Bacteriol. , vol.185 , pp. 6540-6547
    • Werner, J.1    Augustus, A.M.2    Misra, R.3
  • 129
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • Wimley, W. C. 2003. The versatile beta-barrel membrane protein. Curr. Opin. Struct. Biol. 13:404-411.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 130
    • 1942505330 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions
    • Yu, C. S., C. J. Lin, and J. K. Hwang. 2004. Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions. Protein Sci. 13:1402-1406.
    • (2004) Protein Sci. , vol.13 , pp. 1402-1406
    • Yu, C.S.1    Lin, C.J.2    Hwang, J.K.3
  • 131
    • 77954199597 scopus 로고    scopus 로고
    • PSORTb 3.0: Improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes
    • Yu, N. Y., J. R. Wagner, M. R. Laird, G. Melli, S. Rey, R. Lo, P. Dao, S. C. Sahinalp, M. Ester, L. J. Foster, and F. S. Brinkman. 2010. PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26:1608-1615.
    • (2010) Bioinformatics , vol.26 , pp. 1608-1615
    • Yu, N.Y.1    Wagner, J.R.2    Laird, M.R.3    Melli, G.4    Rey, S.5    Lo, R.6    Dao, P.7    Sahinalp, S.C.8    Ester, M.9    Foster, L.J.10    Brinkman, F.S.11
  • 132
    • 77953811604 scopus 로고    scopus 로고
    • Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology
    • Zeth, K. 2010. Structure and evolution of mitochondrial outer membrane proteins of beta-barrel topology. Biochim. Biophys. Acta 1797:1292-1299.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1292-1299
    • Zeth, K.1


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