메뉴 건너뛰기




Volumn 78, Issue 11, 2010, Pages 4779-4791

Characterization of the CpxRA regulon in Haemophilus ducreyi

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CPXA PROTEIN; CPXR PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 78049419108     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00678-10     Document Type: Article
Times cited : (34)

References (69)
  • 1
    • 0034074236 scopus 로고    scopus 로고
    • An isogenic hemoglobin receptor-deficient mutant of Haemophilus ducreyi is attenuated in the human model of experimental infection
    • Al-Tawfiq, J. A., K. R. Fortney, B. P. Katz, A. F. Hood, C. Elkins, and S. M. Spinola. 2000. An isogenic hemoglobin receptor-deficient mutant of Haemophilus ducreyi is attenuated in the human model of experimental infection. J. Infect. Dis. 181:1049-1054.
    • (2000) J. Infect. Dis. , vol.181 , pp. 1049-1054
    • Al-Tawfiq, J.A.1    Fortney, K.R.2    Katz, B.P.3    Hood, A.F.4    Elkins, C.5    Spinola, S.M.6
  • 3
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L., and C. P. Ponting. 1999. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176:111-116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 4
    • 43949133840 scopus 로고    scopus 로고
    • The enterobacterial common antigen-like gene cluster of Haemophilus ducreyi contributes to virulence in humans
    • Banks, K. E., K. R. Fortney, B. Baker, S. D. Billings, B. P. Katz, R. S. J. Munson, and S. M. Spinola. 2008. The enterobacterial common antigen-like gene cluster of Haemophilus ducreyi contributes to virulence in humans. J. Infect. Dis. 197:1531-1536.
    • (2008) J. Infect. Dis. , vol.197 , pp. 1531-1536
    • Banks, K.E.1    Fortney, K.R.2    Baker, B.3    Billings, S.D.4    Katz, B.P.5    Munson, R.S.J.6    Spinola, S.M.7
  • 5
    • 23644456999 scopus 로고    scopus 로고
    • The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins OmpF and OmpC
    • Batchelor, E., D. Walthers, L. J. Kenney, and M. Goulian. 2005. The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins OmpF and OmpC. J. Bacteriol. 187:5723-5731.
    • (2005) J. Bacteriol. , vol.187 , pp. 5723-5731
    • Batchelor, E.1    Walthers, D.2    Kenney, L.J.3    Goulian, M.4
  • 7
    • 0036754146 scopus 로고    scopus 로고
    • Haemophilus ducreyi: Clinical features, epidemiology, and prospects for disease control
    • Bong, C. T., M. E. Bauer, and S. M. Spinola. 2002. Haemophilus ducreyi: clinical features, epidemiology, and prospects for disease control. Microbes Infect. 4:1141-1148.
    • (2002) Microbes Infect. , vol.4 , pp. 1141-1148
    • Bong, C.T.1    Bauer, M.E.2    Spinola, S.M.3
  • 8
    • 0035119494 scopus 로고    scopus 로고
    • DsrA-deficient mutant of Haemophilus ducreyi is impaired in its ability to infect human volunteers
    • Bong, C. T., R. E. Throm, K. R. Fortney, B. P. Katz, A. F. Hood, C. Elkins, and S. M. Spinola. 2001. DsrA-deficient mutant of Haemophilus ducreyi is impaired in its ability to infect human volunteers. Infect. Immun. 69:1488-1491.
    • (2001) Infect. Immun. , vol.69 , pp. 1488-1491
    • Bong, C.T.1    Throm, R.E.2    Fortney, K.R.3    Katz, B.P.4    Hood, A.F.5    Elkins, C.6    Spinola, S.M.7
  • 9
    • 0030022898 scopus 로고    scopus 로고
    • Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili
    • Brentjens, R. J., M. Ketterer, M. A. Apicella, and S. M. Spinola. 1996. Fine tangled pili expressed by Haemophilus ducreyi are a novel class of pili. J. Bacteriol. 178:808-816.
    • (1996) J. Bacteriol. , vol.178 , pp. 808-816
    • Brentjens, R.J.1    Ketterer, M.2    Apicella, M.A.3    Spinola, S.M.4
  • 10
    • 34548495145 scopus 로고    scopus 로고
    • Influence of the Cpx extracytoplasmic-stress-responsive pathway on Yersinia sp.-eukaryotic cell contact
    • Carlsson, K. E., J. Liu, P. J. Edqvist, and M. S. Francis. 2007. Influence of the Cpx extracytoplasmic-stress-responsive pathway on Yersinia sp.-eukaryotic cell contact. Infect. Immun. 75:4386-4399.
    • (2007) Infect. Immun. , vol.75 , pp. 4386-4399
    • Carlsson, K.E.1    Liu, J.2    Edqvist, P.J.3    Francis, M.S.4
  • 11
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino, P., V. Rubio, and A. Marina. 2009. Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139:325-336.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 12
    • 0031020834 scopus 로고    scopus 로고
    • Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter
    • Dahl, J. L., B. Y. Wei, and R. J. Kadner. 1997. Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter. J. Biol. Chem. 272:1910-1919.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1910-1919
    • Dahl, J.L.1    Wei, B.Y.2    Kadner, R.J.3
  • 13
    • 0028951033 scopus 로고
    • The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP
    • Danese, P. N., W. B. Snyder, C. L. Cosma, L. J. B. Davis, and T. J. Silhavy. 1995. The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 9:387-398.
    • (1995) Genes Dev. , vol.9 , pp. 387-398
    • Danese, P.N.1    Snyder, W.B.2    Cosma, C.L.3    Davis, L.J.B.4    Silhavy, T.J.5
  • 14
    • 0037135593 scopus 로고    scopus 로고
    • Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli
    • De Wulf, P., A. M. McGuire, X. Liu, and E. C. Lin. 2002. Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli. J. Biol. Chem. 277:26652-26661.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26652-26661
    • De Wulf, P.1    McGuire, A.M.2    Liu, X.3    Lin, E.C.4
  • 15
    • 0033962665 scopus 로고    scopus 로고
    • Cpx two-component signal transduction in Escherichia coli: Excessive CpxR-P levels underlie CpxA* phenotypes
    • De Wulf, P., and E. C. C. Lin. 2000. Cpx two-component signal transduction in Escherichia coli: excessive CpxR-P levels underlie CpxA* phenotypes. J. Bacteriol. 182:1423-1426.
    • (2000) J. Bacteriol. , vol.182 , pp. 1423-1426
    • De Wulf, P.1    Lin, E.C.C.2
  • 16
    • 0027968079 scopus 로고
    • An analysis of the complete nucleotide sequence of the Haemophilus ducreyi broad-host-range plasmid pLS88
    • Dixon, L. G., W. L. Albritton, and P. J. Willson. 1994. An analysis of the complete nucleotide sequence of the Haemophilus ducreyi broad-host-range plasmid pLS88. Plasmid 32:228-232.
    • (1994) Plasmid , vol.32 , pp. 228-232
    • Dixon, L.G.1    Albritton, W.L.2    Willson, P.J.3
  • 17
    • 33646072467 scopus 로고    scopus 로고
    • The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities?
    • Dorel, C., P. Lejeune, and A. Rodrigue. 2006. The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities? Res. Microbiol. 157:306-314.
    • (2006) Res. Microbiol. , vol.157 , pp. 306-314
    • Dorel, C.1    Lejeune, P.2    Rodrigue, A.3
  • 18
    • 0028905674 scopus 로고
    • Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi
    • Elkins, C. 1995. Identification and purification of a conserved heme-regulated hemoglobin-binding outer membrane protein from Haemophilus ducreyi. Infect. Immun. 63:1241-1245.
    • (1995) Infect. Immun. , vol.63 , pp. 1241-1245
    • Elkins, C.1
  • 19
    • 0033963479 scopus 로고    scopus 로고
    • Serum resistance in Haemophilus ducreyi requires outer membrane protein DsrA
    • Elkins, C., K. J. Morrow, Jr., and B. Olsen. 2000. Serum resistance in Haemophilus ducreyi requires outer membrane protein DsrA. Infect. Immun. 68:1608-1619.
    • (2000) Infect. Immun. , vol.68 , pp. 1608-1619
    • Elkins, C.1    Morrow Jr., K.J.2    Olsen, B.3
  • 20
    • 0033017798 scopus 로고    scopus 로고
    • From epidemiological synergy to public health policy and practice: The contribution of other sexually transmitted diseases to sexual transmission of HIV infection
    • Fleming, D. T., and J. N. Wasserheit. 1999. From epidemiological synergy to public health policy and practice: the contribution of other sexually transmitted diseases to sexual transmission of HIV infection. Sex. Transm. Infect. 75:3-17.
    • (1999) Sex. Transm. Infect. , vol.75 , pp. 3-17
    • Fleming, D.T.1    Wasserheit, J.N.2
  • 21
    • 0033784127 scopus 로고    scopus 로고
    • Expression of peptidoglycan-associated lipoprotein is required for virulence in the human model of Haemophilus ducreyi infection
    • Fortney, K. R., R. S. Young, M. E. Bauer, B. P. Katz, A. F. Hood, R. S. Munson, Jr., and S. M. Spinola. 2000. Expression of peptidoglycan-associated lipoprotein is required for virulence in the human model of Haemophilus ducreyi infection. Infect. Immun. 68:6441-6448.
    • (2000) Infect. Immun. , vol.68 , pp. 6441-6448
    • Fortney, K.R.1    Young, R.S.2    Bauer, M.E.3    Katz, B.P.4    Hood, A.F.5    Munson Jr., R.S.6    Spinola, S.M.7
  • 22
    • 33646350248 scopus 로고    scopus 로고
    • Expression of Haemophilus ducreyi collagen binding outer membrane protein NcaA is required for virulence in swine and human challenge models of chancroid
    • Fulcher, R. A., L. E. Cole, D. M. Janowicz, K. L. Toffer, K. R. Fortney, B. P. Katz, P. E. Orndorff, S. M. Spinola, and T. H. Kawula. 2006. Expression of Haemophilus ducreyi collagen binding outer membrane protein NcaA is required for virulence in swine and human challenge models of chancroid. Infect. Immun. 74:2651-2658.
    • (2006) Infect. Immun. , vol.74 , pp. 2651-2658
    • Fulcher, R.A.1    Cole, L.E.2    Janowicz, D.M.3    Toffer, K.L.4    Fortney, K.R.5    Katz, B.P.6    Orndorff, P.E.7    Spinola, S.M.8    Kawula, T.H.9
  • 23
    • 0032994480 scopus 로고    scopus 로고
    • Molecular characterization of Haemophilus ducreyi strains from Jackson, Mississippi and New Orleans, Louisiana
    • Haydock, A. K., D. H. Martin, S. A. Morse, C. Cammarata, K. J. Mertz, and P. A. Totten. 1999. Molecular characterization of Haemophilus ducreyi strains from Jackson, Mississippi and New Orleans, Louisiana. J. Infect. Dis. 179:1423-1432.
    • (1999) J. Infect. Dis. , vol.179 , pp. 1423-1432
    • Haydock, A.K.1    Martin, D.H.2    Morse, S.A.3    Cammarata, C.4    Mertz, K.J.5    Totten, P.A.6
  • 24
    • 8844275981 scopus 로고    scopus 로고
    • Regulation of the Pap epigenetic switch by CpxAR: Phosphorylated CpxR inhibits transition to the phase on state by competition with Lrp
    • Hernday, A. D., B. A. Braaten, G. Broitman-Maduro, P. Engelberts, and D. A. Low. 2004. Regulation of the Pap epigenetic switch by CpxAR: Phosphorylated CpxR inhibits transition to the phase ON state by competition with Lrp. Mol. Cell 16:537-547.
    • (2004) Mol. Cell , vol.16 , pp. 537-547
    • Hernday, A.D.1    Braaten, B.A.2    Broitman-Maduro, G.3    Engelberts, P.4    Low, D.A.5
  • 25
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., H. D. Hunt, S. N. Ho, J. K. Pullen, and L. R. Pease. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 27
    • 69949145154 scopus 로고    scopus 로고
    • A two-component system is required for colonization of host cells by meningococcus
    • Jamet, A., C. Rousseau, J. B. Monfort, E. Frapy, X. Nassif, and P. Martin. 2009. A two-component system is required for colonization of host cells by meningococcus. Microbiology 155:2288-2295.
    • (2009) Microbiology , vol.155 , pp. 2288-2295
    • Jamet, A.1    Rousseau, C.2    Monfort, J.B.3    Frapy, E.4    Nassif, X.5    Martin, P.6
  • 28
    • 31844454118 scopus 로고    scopus 로고
    • A DltA mutant of Haemophilus ducreyi Is partially attenuated in its ability to cause pustules in human volunteers
    • Janowicz, D., I. Leduc, K. R. Fortney, B. P. Katz, C. Elkins, and S. M. Spinola. 2006. A DltA mutant of Haemophilus ducreyi Is partially attenuated in its ability to cause pustules in human volunteers. Infect. Immun. 74:1394-1397.
    • (2006) Infect. Immun. , vol.74 , pp. 1394-1397
    • Janowicz, D.1    Leduc, I.2    Fortney, K.R.3    Katz, B.P.4    Elkins, C.5    Spinola, S.M.6
  • 29
    • 3343010273 scopus 로고    scopus 로고
    • Expression of the LspA1 and LspA2 proteins by Haemophilus ducreyi is required for virulence in human volunteers
    • Janowicz, D. M., K. R. Fortney, B. P. Katz, J. L. Latimer, K. Deng, E. J. Hansen, and S. M. Spinola. 2004. Expression of the LspA1 and LspA2 proteins by Haemophilus ducreyi is required for virulence in human volunteers. Infect. Immun. 72:4528-4533.
    • (2004) Infect. Immun. , vol.72 , pp. 4528-4533
    • Janowicz, D.M.1    Fortney, K.R.2    Katz, B.P.3    Latimer, J.L.4    Deng, K.5    Hansen, E.J.6    Spinola, S.M.7
  • 31
    • 67650691783 scopus 로고    scopus 로고
    • Experimental infection of human volunteers with Haemophilus ducreyi: Fifteen years of clinical data and experience
    • Janowicz, D. M., S. Ofner, B. P. Katz, and S. M. Spinola. 2009. Experimental infection of human volunteers with Haemophilus ducreyi: fifteen years of clinical data and experience. J. Infect. Dis. 199:1671-1679.
    • (2009) J. Infect. Dis. , vol.199 , pp. 1671-1679
    • Janowicz, D.M.1    Ofner, S.2    Katz, B.P.3    Spinola, S.M.4
  • 32
    • 34547614468 scopus 로고    scopus 로고
    • The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators
    • Klein, A. H., A. Shulla, S. A. Reimann, D. H. Keating, and A. J. Wolfe. 2007. The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators. J. Bacteriol. 189:5574-5581.
    • (2007) J. Bacteriol. , vol.189 , pp. 5574-5581
    • Klein, A.H.1    Shulla, A.2    Reimann, S.A.3    Keating, D.H.4    Wolfe, A.J.5
  • 35
    • 67651227355 scopus 로고    scopus 로고
    • Regulation of expression of the Haemophilus ducreyi LspB and LspA2 proteins by CpxR
    • Labandeira-Rey, M., J. R. Mock, and E. J. Hansen. 2009. Regulation of expression of the Haemophilus ducreyi LspB and LspA2 proteins by CpxR. Infect. Immun. 77:3402-3411.
    • (2009) Infect. Immun. , vol.77 , pp. 3402-3411
    • Labandeira-Rey, M.1    Mock, J.R.2    Hansen, E.J.3
  • 36
    • 0037327268 scopus 로고    scopus 로고
    • Chancroid: Clinical manifestations, diagnosis, and management
    • Lewis, D. A. 2003. Chancroid: clinical manifestations, diagnosis, and management. Sex. Transm. Infect. 79:68-71.
    • (2003) Sex. Transm. Infect. , vol.79 , pp. 68-71
    • Lewis, D.A.1
  • 37
    • 0030052359 scopus 로고    scopus 로고
    • Identification of the O antigen polymerase (rfc) gene in Escherichia coli O4 by insertional mutagenesis using a nonpolar chloramphenicol resistance cassette
    • Lukomski, S., R. A. Hull, and S. I. Hull. 1996. Identification of the O antigen polymerase (rfc) gene in Escherichia coli O4 by insertional mutagenesis using a nonpolar chloramphenicol resistance cassette. J. Bacteriol. 178:240-247.
    • (1996) J. Bacteriol. , vol.178 , pp. 240-247
    • Lukomski, S.1    Hull, R.A.2    Hull, S.I.3
  • 38
    • 55949113873 scopus 로고    scopus 로고
    • Two-component signaling and gram negative envelope stress response systems
    • MacRitchie, D. M., D. R. Buelow, N. L. Price, and T. L. Raivio. 2008. Two-component signaling and gram negative envelope stress response systems. Adv. Exp. Med. Biol. 631:80-110.
    • (2008) Adv. Exp. Med. Biol. , vol.631 , pp. 80-110
    • MacRitchie, D.M.1    Buelow, D.R.2    Price, N.L.3    Raivio, T.L.4
  • 39
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • Marina, A., C. D. Waldburger, and W. A. Hendrickson. 2005. Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J. 24:4247-4259.
    • (2005) EMBO J. , vol.24 , pp. 4247-4259
    • Marina, A.1    Waldburger, C.D.2    Hendrickson, W.A.3
  • 42
    • 33845924731 scopus 로고    scopus 로고
    • Coordinated regulation of the Neisseria gonorrhoeae-truncated denitrification pathway by the nitric oxide-sensitive repressor, NsrR, and nitrite-insensitive NarQ-NarP
    • Overton, T. W., R. Whitehead, Y. Li, L. A. Snyder, N. J. Saunders, H. Smith, and J. A. Cole. 2006. Coordinated regulation of the Neisseria gonorrhoeae-truncated denitrification pathway by the nitric oxide-sensitive repressor, NsrR, and nitrite-insensitive NarQ-NarP. J. Biol. Chem. 281:33115-33126.
    • (2006) J. Biol. Chem. , vol.281 , pp. 33115-33126
    • Overton, T.W.1    Whitehead, R.2    Li, Y.3    Snyder, L.A.4    Saunders, N.J.5    Smith, H.6    Cole, J.A.7
  • 43
    • 0029616070 scopus 로고
    • Cloning and characterization of the genes encoding the haemolysin of Haemophilus ducreyi
    • Palmer, K. L., and R. S. Munson, Jr. 1995. Cloning and characterization of the genes encoding the haemolysin of Haemophilus ducreyi. Mol. Microbiol. 18:821-830.
    • (1995) Mol. Microbiol. , vol.18 , pp. 821-830
    • Palmer, K.L.1    Munson Jr., R.S.2
  • 44
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei, J., B. H. Kim, and N. V. Grishin. 2008. PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36:2295-2300.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 45
    • 34748904302 scopus 로고    scopus 로고
    • Proposed second class of Haemophilus ducreyi strains show altered protein and lipooligosaccharide profiles
    • Post, D. M., and B. W. Gibson. 2007. Proposed second class of Haemophilus ducreyi strains show altered protein and lipooligosaccharide profiles. Proteomics 7:3131-3142.
    • (2007) Proteomics , vol.7 , pp. 3131-3142
    • Post, D.M.1    Gibson, B.W.2
  • 47
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price, N. L., and T. L. Raivio. 2009. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 191:1798-1815.
    • (2009) J. Bacteriol. , vol.191 , pp. 1798-1815
    • Price, N.L.1    Raivio, T.L.2
  • 48
    • 0035205423 scopus 로고    scopus 로고
    • Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene
    • DOI 10.1128/JB.183.24.7213-7223.2001
    • Prigent-Combaret, C., E. Brombacher, O. Vidal, A. Ambert, P. Lejeune, P. Landini, and C. Dorel. 2001. Complex regulatory network controls initial adhesion and biofilm formation in Escherichia coli via regulation of the csgD gene. J. Bacteriol. 183:7213-7223. (Pubitemid 33121856)
    • (2001) Journal of Bacteriology , vol.183 , Issue.24 , pp. 7213-7223
    • Prigent-Combaret, C.1    Brombacher, E.2    Vidal, O.3    Ambert, A.4    Lejeune, P.5    Landini, P.6    Dorel, C.7
  • 49
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio, T. L. 2005. Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56:1119-1128.
    • (2005) Mol. Microbiol. , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 50
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio, T. L., and T. J. Silhavy. 1997. Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J. Bacteriol. 179:7724-7733.
    • (1997) J. Bacteriol. , vol.179 , pp. 7724-7733
    • Raivio, T.L.1    Silhavy, T.J.2
  • 52
    • 0027128763 scopus 로고
    • Chancroid in the United States, 1981-1990: Evidence for underreporting of cases
    • Schulte, J. M., F. A. Martich, and G. P. Schmid. 1992. Chancroid in the United States, 1981-1990: evidence for underreporting of cases. MMWR Surveill. Summ. 41:57-61.
    • (1992) MMWR Surveill. Summ. , vol.41 , pp. 57-61
    • Schulte, J.M.1    Martich, F.A.2    Schmid, G.P.3
  • 53
    • 0035021498 scopus 로고    scopus 로고
    • The virulence factors of Bordetella pertussis: A matter of control
    • Smith, A. M., C. A. Guzman, and M. J. Walker. 2001. The virulence factors of Bordetella pertussis: a matter of control. FEMS Microbiol. Rev. 25:309-333.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 309-333
    • Smith, A.M.1    Guzman, C.A.2    Walker, M.J.3
  • 54
    • 0036128720 scopus 로고    scopus 로고
    • Immunopathogenesis of Haemophilus ducreyi infection (chancroid)
    • Spinola, S. M., M. E. Bauer, and R. S. Munson, Jr. 2002. Immunopathogenesis of Haemophilus ducreyi infection (chancroid). Infect. Immun. 70:1667-1676.
    • (2002) Infect. Immun. , vol.70 , pp. 1667-1676
    • Spinola, S.M.1    Bauer, M.E.2    Munson Jr., R.S.3
  • 56
    • 0030010928 scopus 로고    scopus 로고
    • The conserved 18,000-molecular-weight outer membrane protein of Haemophilus ducreyi has homology to PAL
    • Spinola, S. M., T. J. Hiltke, K. R. Fortney, and K. L. Shanks. 1996. The conserved 18,000-molecular-weight outer membrane protein of Haemophilus ducreyi has homology to PAL. Infect. Immun. 64:1950-1955.
    • (1996) Infect. Immun. , vol.64 , pp. 1950-1955
    • Spinola, S.M.1    Hiltke, T.J.2    Fortney, K.R.3    Shanks, K.L.4
  • 59
    • 0028981507 scopus 로고
    • Chancroid and Haemophilus ducreyi: An update
    • Trees, D. L., and S. A. Morse. 1995. Chancroid and Haemophilus ducreyi: an update. Clin. Microbiol. Rev. 8:357-375.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 357-375
    • Trees, D.L.1    Morse, S.A.2
  • 60
    • 0141668993 scopus 로고    scopus 로고
    • Inhibition of phagocytosis by Haemophilus ducreyi requires expression of the LspA1 and LspA2 proteins
    • Vakevainen, M., S. Greenberg, and E. J. Hansen. 2003. Inhibition of phagocytosis by Haemophilus ducreyi requires expression of the LspA1 and LspA2 proteins. Infect. Immun. 71:5994-6003.
    • (2003) Infect. Immun. , vol.71 , pp. 5994-6003
    • Vakevainen, M.1    Greenberg, S.2    Hansen, E.J.3
  • 61
    • 0037407498 scopus 로고    scopus 로고
    • Mutations in the lspA1 and lspA2 genes of Haemophilus ducreyi affect the virulence of this pathogen in an animal model system
    • Ward, C. K., J. L. Latimer, J. R. Nika, M. Vakevainen, J. R. Mock, K. Deng, R. J. Blick, and E. H. Hansen. 2003. Mutations in the lspA1 and lspA2 genes of Haemophilus ducreyi affect the virulence of this pathogen in an animal model system. Infect. Immun. 71:2478-2486.
    • (2003) Infect. Immun. , vol.71 , pp. 2478-2486
    • Ward, C.K.1    Latimer, J.L.2    Nika, J.R.3    Vakevainen, M.4    Mock, J.R.5    Deng, K.6    Blick, R.J.7    Hansen, E.H.8
  • 62
    • 0031733742 scopus 로고    scopus 로고
    • Haemophilus ducreyi secretes a filamentous hemagglutinin-like protein
    • Ward, C. K., S. R. Lumbley, J. L. Latimer, L. D. Cope, and E. J. Hansen. 1998. Haemophilus ducreyi secretes a filamentous hemagglutinin-like protein. J. Bacteriol. 180:6013-6022.
    • (1998) J. Bacteriol. , vol.180 , pp. 6013-6022
    • Ward, C.K.1    Lumbley, S.R.2    Latimer, J.L.3    Cope, L.D.4    Hansen, E.J.5
  • 63
    • 1842536416 scopus 로고    scopus 로고
    • The LspB Protein Is Involved in the Secretion of the LspA1 and LspA2 Proteins by Haemophilus ducreyi
    • Ward, C. K., J. R. Mock, and E. J. Hansen. 2004. The LspB Protein Is Involved in the Secretion of the LspA1 and LspA2 Proteins by Haemophilus ducreyi. Infect. Immun. 72:1874-1884.
    • (2004) Infect. Immun. , vol.72 , pp. 1874-1884
    • Ward, C.K.1    Mock, J.R.2    Hansen, E.J.3
  • 64
    • 16244384155 scopus 로고    scopus 로고
    • Haemophilus ducreyi Outer membrane determinants, including DsrA, define two clonal populations
    • White, C. D., I. Leduc, B. Olsen, C. Jeter, C. Harris, and C. Elkins. 2005. Haemophilus ducreyi Outer membrane determinants, including DsrA, define two clonal populations. Infect. Immun. 73:2387-2399.
    • (2005) Infect. Immun. , vol.73 , pp. 2387-2399
    • White, C.D.1    Leduc, I.2    Olsen, B.3    Jeter, C.4    Harris, C.5    Elkins, C.6
  • 65
    • 69249240168 scopus 로고    scopus 로고
    • Evolution of prokaryotic twocomponent systems: Insights from comparative genomics
    • Whitworth, D. E., and P. J. Cock. 2009. Evolution of prokaryotic twocomponent systems: insights from comparative genomics. Amino Acids 37:459-466.
    • (2009) Amino Acids , vol.37 , pp. 459-466
    • Whitworth, D.E.1    Cock, P.J.2
  • 66
    • 0024465906 scopus 로고
    • Characterization of a multiple antibiotic resistance plasmid from Haemophilus ducreyi
    • Willson, P. J., W. L. Albritton, L. Slaney, and J. K. Setlow. 1989. Characterization of a multiple antibiotic resistance plasmid from Haemophilus ducreyi. Antimicrob. Agents Chemother. 33:1627-1630.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1627-1630
    • Willson, P.J.1    Albritton, W.L.2    Slaney, L.3    Setlow, J.K.4
  • 67
    • 77949914858 scopus 로고    scopus 로고
    • Physiologically relevant small phosphodonors link metabolism to signal transduction
    • Wolfe, A. J. 2010. Physiologically relevant small phosphodonors link metabolism to signal transduction. Curr. Opin. Microbiol. 13:204-209.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 204-209
    • Wolfe, A.J.1
  • 68
    • 41549102957 scopus 로고    scopus 로고
    • Signal integration by the two-component signal transduction response regulator CpxR
    • Wolfe, A. J., N. Parikh, B. P. Lima, and B. Zemaitaitis. 2008. Signal integration by the two-component signal transduction response regulator CpxR. J. Bacteriol. 190:2314-2322.
    • (2008) J. Bacteriol. , vol.190 , pp. 2314-2322
    • Wolfe, A.J.1    Parikh, N.2    Lima, B.P.3    Zemaitaitis, B.4
  • 69
    • 55949135533 scopus 로고    scopus 로고
    • Structural basis of the signal transduction in the two-component system
    • Yamada, S., and Y. Shiro. 2008. Structural basis of the signal transduction in the two-component system. Adv. Exp. Med. Biol. 631:22-39.
    • (2008) Adv. Exp. Med. Biol. , vol.631 , pp. 22-39
    • Yamada, S.1    Shiro, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.