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Volumn 88, Issue 3, 2013, Pages 619-633

The HtrA protease of Borrelia burgdorferi degrades outer membrane protein BmpD and chemotaxis phosphatase CheX

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE ANTIGEN; BASIC MEMBRANE PROTEIN D; CASEIN; CHEMOTAXIS PHOSPHATASE; ESCHERICHIA COLI PROTEIN; HTRABB PROTEIN; LIPOPROTEIN; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; PHOSPHATASE; RECOMBINANT PROTEIN; SERINE; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 84876702079     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12213     Document Type: Article
Times cited : (46)

References (80)
  • 1
    • 34548694325 scopus 로고    scopus 로고
    • Borrelia burgdorferi adhesins identified using in vivo phage display
    • Antonara, S., Chafel, R.M., LaFrance, M., and Coburn, J. (2007) Borrelia burgdorferi adhesins identified using in vivo phage display. Mol Microbiol 66: 262-276.
    • (2007) Mol Microbiol , vol.66 , pp. 262-276
    • Antonara, S.1    Chafel, R.M.2    LaFrance, M.3    Coburn, J.4
  • 2
    • 17044389822 scopus 로고    scopus 로고
    • Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry
    • Backert, S., Kwok, T., Schmid, M., Selbach, M., Moese, S., Peek, R.M., Jr., etal. (2005) Subproteomes of soluble and structure-bound Helicobacter pylori proteins analyzed by two-dimensional gel electrophoresis and mass spectrometry. Proteomics 5: 1331-1345.
    • (2005) Proteomics , vol.5 , pp. 1331-1345
    • Backert, S.1    Kwok, T.2    Schmid, M.3    Selbach, M.4    Moese, S.5    Peek R.M., Jr.6
  • 3
    • 79958784499 scopus 로고    scopus 로고
    • Membrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein
    • Baud, C., Gutsche, I., Willery, E., de Paepe, D., Drobecq, H., Gilleron, M., etal. (2011) Membrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein. Mol Microbiol 80: 1625-1636.
    • (2011) Mol Microbiol , vol.80 , pp. 1625-1636
    • Baud, C.1    Gutsche, I.2    Willery, E.3    de Paepe, D.4    Drobecq, H.5    Gilleron, M.6
  • 4
    • 0028215784 scopus 로고
    • Salmonella typhimurium loci involved in survival within macrophages
    • Baumler, A.J., Kusters, J.G., Stojiljkovic, I., and Heffron, F. (1994) Salmonella typhimurium loci involved in survival within macrophages. Infect Immun 62: 1623-1630.
    • (1994) Infect Immun , vol.62 , pp. 1623-1630
    • Baumler, A.J.1    Kusters, J.G.2    Stojiljkovic, I.3    Heffron, F.4
  • 5
    • 58449096795 scopus 로고    scopus 로고
    • Borrelia burgdorferi infection-associated surface proteins ErpP, ErpA, and ErpC bind human plasminogen
    • Brissette, C.A., Haupt, K., Barthel, D., Cooley, A.E., Bowman, A., Skerka, C., etal. (2009) Borrelia burgdorferi infection-associated surface proteins ErpP, ErpA, and ErpC bind human plasminogen. Infect Immun 77: 300-306.
    • (2009) Infect Immun , vol.77 , pp. 300-306
    • Brissette, C.A.1    Haupt, K.2    Barthel, D.3    Cooley, A.E.4    Bowman, A.5    Skerka, C.6
  • 6
    • 32944455152 scopus 로고    scopus 로고
    • Borrelia burgdorferi BmpA, BmpB, and BmpD proteins are expressed in human infection and contribute to P39 immunoblot reactivity in patients with Lyme disease
    • Bryksin, A.V., Godfrey, H.P., Carbonaro, C.A., Wormser, G.P., Aguero-Rosenfeld, M.E., and Cabello, F.C. (2005) Borrelia burgdorferi BmpA, BmpB, and BmpD proteins are expressed in human infection and contribute to P39 immunoblot reactivity in patients with Lyme disease. Clin Diagn Lab Immunol 12: 935-940.
    • (2005) Clin Diagn Lab Immunol , vol.12 , pp. 935-940
    • Bryksin, A.V.1    Godfrey, H.P.2    Carbonaro, C.A.3    Wormser, G.P.4    Aguero-Rosenfeld, M.E.5    Cabello, F.C.6
  • 7
    • 79960955642 scopus 로고    scopus 로고
    • The hybrid histidine kinase Hk1 is part of a two-component system that is essential for survival of Borrelia burgdorferi in feeding Ixodes scapularis ticks
    • Caimano, M.J., Kenedy, M.R., Kairu, T., Desrosiers, D.C., Harman, M., Dunham-Ems, S., etal. (2011) The hybrid histidine kinase Hk1 is part of a two-component system that is essential for survival of Borrelia burgdorferi in feeding Ixodes scapularis ticks. Infect Immun 79: 3117-3130.
    • (2011) Infect Immun , vol.79 , pp. 3117-3130
    • Caimano, M.J.1    Kenedy, M.R.2    Kairu, T.3    Desrosiers, D.C.4    Harman, M.5    Dunham-Ems, S.6
  • 8
    • 84869073827 scopus 로고    scopus 로고
    • The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide
    • Cassone, M., Gagne, A.L., Spruce, L.A., Seeholzer, S.H., and Sebert, M.E. (2012) The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide. J Biol Chem 287: 38449-38459.
    • (2012) J Biol Chem , vol.287 , pp. 38449-38459
    • Cassone, M.1    Gagne, A.L.2    Spruce, L.A.3    Seeholzer, S.H.4    Sebert, M.E.5
  • 10
    • 79951967246 scopus 로고    scopus 로고
    • HTRA proteases: regulated proteolysis in protein quality control
    • Clausen, T., Kaiser, M., Huber, R., and Ehrmann, M. (2011) HTRA proteases: regulated proteolysis in protein quality control. Nat Rev Mol Cell Biol 12: 152-162.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 152-162
    • Clausen, T.1    Kaiser, M.2    Huber, R.3    Ehrmann, M.4
  • 11
    • 0141669098 scopus 로고    scopus 로고
    • The urokinase receptor can be induced by Borrelia burgdorferi through receptors of the innate immune system
    • Coleman, J.L., and Benach, J.L. (2003) The urokinase receptor can be induced by Borrelia burgdorferi through receptors of the innate immune system. Infect Immun 71: 5556-5564.
    • (2003) Infect Immun , vol.71 , pp. 5556-5564
    • Coleman, J.L.1    Benach, J.L.2
  • 12
    • 0031587871 scopus 로고    scopus 로고
    • Plasminogen is required for efficient dissemination of B.burgdorferi in ticks and for enhancement of spirochetemia in mice
    • Coleman, J.L., Gebbia, J.A., Piesman, J., Degen, J.L., Bugge, T.H., and Benach, J.L. (1997) Plasminogen is required for efficient dissemination of B.burgdorferi in ticks and for enhancement of spirochetemia in mice. Cell 89: 1111-1119.
    • (1997) Cell , vol.89 , pp. 1111-1119
    • Coleman, J.L.1    Gebbia, J.A.2    Piesman, J.3    Degen, J.L.4    Bugge, T.H.5    Benach, J.L.6
  • 13
    • 0032769770 scopus 로고    scopus 로고
    • Plasmin-coated Borrelia burgdorferi degrades soluble and insoluble components of the mammalian extracellular matrix
    • Coleman, J.L., Roemer, E.J., and Benach, J.L. (1999) Plasmin-coated Borrelia burgdorferi degrades soluble and insoluble components of the mammalian extracellular matrix. Infect Immun 67: 3929-3936.
    • (1999) Infect Immun , vol.67 , pp. 3929-3936
    • Coleman, J.L.1    Roemer, E.J.2    Benach, J.L.3
  • 14
    • 0035160526 scopus 로고    scopus 로고
    • Borrelia burgdorferi and other bacterial products induce expression and release of the urokinase receptor (CD87)
    • Coleman, J.L., Gebbia, J.A., and Benach, J.L. (2001) Borrelia burgdorferi and other bacterial products induce expression and release of the urokinase receptor (CD87). J Immunol 166: 473-480.
    • (2001) J Immunol , vol.166 , pp. 473-480
    • Coleman, J.L.1    Gebbia, J.A.2    Benach, J.L.3
  • 15
    • 73549116779 scopus 로고    scopus 로고
    • Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functions
    • and () . : .
    • Coleman, J.L., Katona, L.I., Kuhlow, C., Toledo, A., Okan, N.A., Tokarz, R., and Benach, J.L. (2009) Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functions. PLoS Pathog 5: e1000676.
    • (2009) PLoS Pathog , vol.5
    • Coleman, J.L.1    Katona, L.I.2    Kuhlow, C.3    Toledo, A.4    Okan, N.A.5    Tokarz, R.6    Benach, J.L.7
  • 16
    • 84862577056 scopus 로고    scopus 로고
    • Membrane proteases in the bacterial protein secretion and quality control pathway
    • Dalbey, R.E., Wang, P., and van Dijl, J.M. (2012) Membrane proteases in the bacterial protein secretion and quality control pathway. Microbiol Mol Biol Rev 76: 311-330.
    • (2012) Microbiol Mol Biol Rev , vol.76 , pp. 311-330
    • Dalbey, R.E.1    Wang, P.2    van Dijl, J.M.3
  • 17
    • 0035147441 scopus 로고    scopus 로고
    • Two independent transcriptional units control the complex and simultaneous expression of the bmp paralogous chromosomal gene family in Borrelia burgdorferi
    • Dobrikova, E.Y., Bugrysheva, J., and Cabello, F.C. (2001) Two independent transcriptional units control the complex and simultaneous expression of the bmp paralogous chromosomal gene family in Borrelia burgdorferi. Mol Microbiol 39: 370-378.
    • (2001) Mol Microbiol , vol.39 , pp. 370-378
    • Dobrikova, E.Y.1    Bugrysheva, J.2    Cabello, F.C.3
  • 18
    • 10944243117 scopus 로고    scopus 로고
    • Proteolysis as a regulatory mechanism
    • Ehrmann, M., and Clausen, T. (2004) Proteolysis as a regulatory mechanism. Annu Rev Genet 38: 709-724.
    • (2004) Annu Rev Genet , vol.38 , pp. 709-724
    • Ehrmann, M.1    Clausen, T.2
  • 19
    • 0036126988 scopus 로고    scopus 로고
    • Clonal polymorphism of Borrelia burgdorferi strain B31 MI: implications for mutagenesis in an infectious strain background
    • Elias, A.F., Stewart, P.E., Grimm, D., Caimano, M.J., Eggers, C.H., Tilly, K., etal. (2002) Clonal polymorphism of Borrelia burgdorferi strain B31 MI: implications for mutagenesis in an infectious strain background. Infect Immun 70: 2139-2150.
    • (2002) Infect Immun , vol.70 , pp. 2139-2150
    • Elias, A.F.1    Stewart, P.E.2    Grimm, D.3    Caimano, M.J.4    Eggers, C.H.5    Tilly, K.6
  • 20
    • 0029908161 scopus 로고    scopus 로고
    • The HtrA stress response protease contributes to resistance of Brucella abortus to killing by murine phagocytes
    • Elzer, P.H., Phillips, R.W., Robertson, G.T., Roop, R.M., 2nd (1996) The HtrA stress response protease contributes to resistance of Brucella abortus to killing by murine phagocytes. Infect Immun 64: 4838-4841.
    • (1996) Infect Immun , vol.64 , pp. 4838-4841
    • Elzer, P.H.1    Phillips, R.W.2    Robertson, G.T.3    Roop, R.M.4    2nd5
  • 21
    • 0031470826 scopus 로고    scopus 로고
    • Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi
    • Fraser, C.M., Casjens, S., Huang, W.M., Sutton, G.G., Clayton, R., Lathigra, R., etal. (1997) Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi. Nature 390: 580-586.
    • (1997) Nature , vol.390 , pp. 580-586
    • Fraser, C.M.1    Casjens, S.2    Huang, W.M.3    Sutton, G.G.4    Clayton, R.5    Lathigra, R.6
  • 22
    • 0032920997 scopus 로고    scopus 로고
    • The plasminogen activation system enhances brain and heart invasion in murine relapsing fever borreliosis
    • Gebbia, J.A., Monco, J.C., Degen, J.L., Bugge, T.H., and Benach, J.L. (1999) The plasminogen activation system enhances brain and heart invasion in murine relapsing fever borreliosis. J Clin Invest 103: 81-87.
    • (1999) J Clin Invest , vol.103 , pp. 81-87
    • Gebbia, J.A.1    Monco, J.C.2    Degen, J.L.3    Bugge, T.H.4    Benach, J.L.5
  • 23
    • 33645822747 scopus 로고    scopus 로고
    • Relapsing fever spirochaetes produce a serine protease that provides resistance to oxidative stress and killing by neutrophils
    • Guyard, C., Battisti, J.M., Raffel, S.J., Schrumpf, M.E., Whitney, A.R., Krum, J.G., etal. (2006) Relapsing fever spirochaetes produce a serine protease that provides resistance to oxidative stress and killing by neutrophils. Mol Microbiol 60: 710-722.
    • (2006) Mol Microbiol , vol.60 , pp. 710-722
    • Guyard, C.1    Battisti, J.M.2    Raffel, S.J.3    Schrumpf, M.E.4    Whitney, A.R.5    Krum, J.G.6
  • 24
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 4121-4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 25
    • 33745763276 scopus 로고    scopus 로고
    • Reciprocal upregulation of urokinase plasminogen activator and its inhibitor, PAI-2, by Borrelia burgdorferi affects bacterial penetration and host-inflammatory response
    • Haile, W.B., Coleman, J.L., and Benach, J.L. (2006) Reciprocal upregulation of urokinase plasminogen activator and its inhibitor, PAI-2, by Borrelia burgdorferi affects bacterial penetration and host-inflammatory response. Cell Microbiol 8: 1349-1360.
    • (2006) Cell Microbiol , vol.8 , pp. 1349-1360
    • Haile, W.B.1    Coleman, J.L.2    Benach, J.L.3
  • 27
    • 77957232471 scopus 로고    scopus 로고
    • Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion
    • Hoy, B., Lower, M., Weydig, C., Carra, G., Tegtmeyer, N., Geppert, T., etal. (2010) Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion. EMBO Rep 11: 798-804.
    • (2010) EMBO Rep , vol.11 , pp. 798-804
    • Hoy, B.1    Lower, M.2    Weydig, C.3    Carra, G.4    Tegtmeyer, N.5    Geppert, T.6
  • 28
    • 84858959572 scopus 로고    scopus 로고
    • Distinct roles of secreted HtrA proteases from gram-negative pathogens in cleaving the junctional protein and tumor suppressor E-cadherin
    • Hoy, B., Geppert, T., Boehm, M., Reisen, F., Plattner, P., Gadermaier, G., etal. (2012) Distinct roles of secreted HtrA proteases from gram-negative pathogens in cleaving the junctional protein and tumor suppressor E-cadherin. J Biol Chem 287: 10115-10120.
    • (2012) J Biol Chem , vol.287 , pp. 10115-10120
    • Hoy, B.1    Geppert, T.2    Boehm, M.3    Reisen, F.4    Plattner, P.5    Gadermaier, G.6
  • 29
    • 71749086886 scopus 로고    scopus 로고
    • Proteases in bacterial pathogenesis
    • Ingmer, H., and Brondsted, L. (2009) Proteases in bacterial pathogenesis. Res Microbiol 160: 704-710.
    • (2009) Res Microbiol , vol.160 , pp. 704-710
    • Ingmer, H.1    Brondsted, L.2
  • 31
    • 0034868619 scopus 로고    scopus 로고
    • Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes
    • Jones, C.H., Bolken, T.C., Jones, K.F., Zeller, G.O., and Hruby, D.E. (2001) Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes. Infect Immun 69: 5538-5545.
    • (2001) Infect Immun , vol.69 , pp. 5538-5545
    • Jones, C.H.1    Bolken, T.C.2    Jones, K.F.3    Zeller, G.O.4    Hruby, D.E.5
  • 32
    • 0034141729 scopus 로고    scopus 로고
    • A bactericidal monoclonal antibody elicits a change in its antigen, OspB of Borrelia burgdorferi, that can be detected by limited proteolysis
    • Katona, L.I., Ayalew, S., Coleman, J.L., and Benach, J.L. (2000) A bactericidal monoclonal antibody elicits a change in its antigen, OspB of Borrelia burgdorferi, that can be detected by limited proteolysis. J Immunol 164: 1425-1431.
    • (2000) J Immunol , vol.164 , pp. 1425-1431
    • Katona, L.I.1    Ayalew, S.2    Coleman, J.L.3    Benach, J.L.4
  • 34
    • 84860816318 scopus 로고    scopus 로고
    • Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival
    • Kim, S., and Sauer, R.T. (2012) Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival. Proc Natl Acad Sci USA 109: 7263-7268.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 7263-7268
    • Kim, S.1    Sauer, R.T.2
  • 35
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M., and Clausen, T. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416: 455-459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 36
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer, T., Sawa, J., Schafer, E., Saibil, H.R., Ehrmann, M., and Clausen, T. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453: 885-890.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 37
    • 80053599548 scopus 로고    scopus 로고
    • Specificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing
    • Kumru, O.S., Bunikis, I., Sorokina, I., Bergstrom, S., and Zuckert, W.R. (2011) Specificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing. J Bacteriol 193: 5759-5765.
    • (2011) J Bacteriol , vol.193 , pp. 5759-5765
    • Kumru, O.S.1    Bunikis, I.2    Sorokina, I.3    Bergstrom, S.4    Zuckert, W.R.5
  • 38
    • 67649811039 scopus 로고    scopus 로고
    • The bactericidal effect of a complement-independent antibody is osmolytic and specific to Borrelia
    • LaRocca, T.J., Holthausen, D.J., Hsieh, C., Renken, C., Mannella, C.A., and Benach, J.L. (2009) The bactericidal effect of a complement-independent antibody is osmolytic and specific to Borrelia. Proc Natl Acad Sci USA 106: 10752-10757.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10752-10757
    • LaRocca, T.J.1    Holthausen, D.J.2    Hsieh, C.3    Renken, C.4    Mannella, C.A.5    Benach, J.L.6
  • 39
    • 77958089989 scopus 로고    scopus 로고
    • Cholesterol lipids of Borrelia burgdorferi form lipid rafts and are required for the bactericidal activity of a complement-independent antibody
    • LaRocca, T.J., Crowley, J.T., Cusack, B.J., Pathak, P., Benach, J., London, E., etal. (2010) Cholesterol lipids of Borrelia burgdorferi form lipid rafts and are required for the bactericidal activity of a complement-independent antibody. Cell Host Microbe 8: 331-342.
    • (2010) Cell Host Microbe , vol.8 , pp. 331-342
    • LaRocca, T.J.1    Crowley, J.T.2    Cusack, B.J.3    Pathak, P.4    Benach, J.5    London, E.6
  • 40
    • 0029947971 scopus 로고    scopus 로고
    • Construction and characterization of a Yersinia enterocolitica O:8 high-temperature requirement (htrA) isogenic mutant
    • Li, S.R., Dorrell, N., Everest, P.H., Dougan, G., and Wren, B.W. (1996) Construction and characterization of a Yersinia enterocolitica O:8 high-temperature requirement (htrA) isogenic mutant. Infect Immun 64: 2088-2094.
    • (1996) Infect Immun , vol.64 , pp. 2088-2094
    • Li, S.R.1    Dorrell, N.2    Everest, P.H.3    Dougan, G.4    Wren, B.W.5
  • 41
    • 33846217722 scopus 로고    scopus 로고
    • The Lyme disease agent Borrelia burgdorferi requires BB0690, a Dps homologue, to persist within ticks
    • Li, X., Pal, U., Ramamoorthi, N., Liu, X., Desrosiers, D.C., Eggers, C.H., etal. (2007) The Lyme disease agent Borrelia burgdorferi requires BB0690, a Dps homologue, to persist within ticks. Mol Microbiol 63: 694-710.
    • (2007) Mol Microbiol , vol.63 , pp. 694-710
    • Li, X.1    Pal, U.2    Ramamoorthi, N.3    Liu, X.4    Desrosiers, D.C.5    Eggers, C.H.6
  • 42
    • 0024519269 scopus 로고
    • Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • Lipinska, B., Fayet, O., Baird, L., and Georgopoulos, C. (1989) Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J Bacteriol 171: 1574-1584.
    • (1989) J Bacteriol , vol.171 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 43
    • 0025317783 scopus 로고
    • The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase
    • Lipinska, B., Zylicz, M., and Georgopoulos, C. (1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J Bacteriol 172: 1791-1797.
    • (1990) J Bacteriol , vol.172 , pp. 1791-1797
    • Lipinska, B.1    Zylicz, M.2    Georgopoulos, C.3
  • 44
    • 33646243208 scopus 로고    scopus 로고
    • Changing cellular location of CheZ predicted by molecular simulations
    • Lipkow, K. (2006) Changing cellular location of CheZ predicted by molecular simulations. PLoS Comput Biol 2: e39.
    • (2006) PLoS Comput Biol , vol.2
    • Lipkow, K.1
  • 46
    • 55649113505 scopus 로고    scopus 로고
    • Prediction of extracellular proteases of the human pathogen Helicobacter pylori reveals proteolytic activity of the Hp1018/19 protein HtrA
    • and () . : .
    • Lower, M., Weydig, C., Metzler, D., Reuter, A., Starzinski-Powitz, A., Wessler, S., and Schneider, G. (2008) Prediction of extracellular proteases of the human pathogen Helicobacter pylori reveals proteolytic activity of the Hp1018/19 protein HtrA. PLoS ONE 3: e3510.
    • (2008) PLoS ONE , vol.3
    • Lower, M.1    Weydig, C.2    Metzler, D.3    Reuter, A.4    Starzinski-Powitz, A.5    Wessler, S.6    Schneider, G.7
  • 47
    • 33846037385 scopus 로고    scopus 로고
    • Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response
    • McBroom, A.J., and Kuehn, M.J. (2007) Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response. Mol Microbiol 63: 545-558.
    • (2007) Mol Microbiol , vol.63 , pp. 545-558
    • McBroom, A.J.1    Kuehn, M.J.2
  • 48
    • 41249087703 scopus 로고    scopus 로고
    • Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control
    • Meltzer, M., Hasenbein, S., Hauske, P., Kucz, N., Merdanovic, M., Grau, S., etal. (2008) Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control. Angew Chem Int Ed Engl 47: 1332-1334.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 1332-1334
    • Meltzer, M.1    Hasenbein, S.2    Hauske, P.3    Kucz, N.4    Merdanovic, M.5    Grau, S.6
  • 49
    • 72049089291 scopus 로고    scopus 로고
    • Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli
    • Meltzer, M., Hasenbein, S., Mamant, N., Merdanovic, M., Poepsel, S., Hauske, P., etal. (2009) Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli. Res Microbiol 160: 660-666.
    • (2009) Res Microbiol , vol.160 , pp. 660-666
    • Meltzer, M.1    Hasenbein, S.2    Mamant, N.3    Merdanovic, M.4    Poepsel, S.5    Hauske, P.6
  • 51
    • 28044460791 scopus 로고    scopus 로고
    • CheX is a phosphorylated CheY phosphatase essential for Borrelia burgdorferi chemotaxis
    • Motaleb, M.A., Miller, M.R., Li, C., Bakker, R.G., Goldstein, S.F., Silversmith, R.E., etal. (2005) CheX is a phosphorylated CheY phosphatase essential for Borrelia burgdorferi chemotaxis. J Bacteriol 187: 7963-7969.
    • (2005) J Bacteriol , vol.187 , pp. 7963-7969
    • Motaleb, M.A.1    Miller, M.R.2    Li, C.3    Bakker, R.G.4    Goldstein, S.F.5    Silversmith, R.E.6
  • 52
    • 79959326874 scopus 로고    scopus 로고
    • CheY3 of Borrelia burgdorferi is the key response regulator essential for chemotaxis and forms a long-lived phosphorylated intermediate
    • Motaleb, M.A., Sultan, S.Z., Miller, M.R., Li, C., and Charon, N.W. (2011a) CheY3 of Borrelia burgdorferi is the key response regulator essential for chemotaxis and forms a long-lived phosphorylated intermediate. J Bacteriol 193: 3332-3341.
    • (2011) J Bacteriol , vol.193 , pp. 3332-3341
    • Motaleb, M.A.1    Sultan, S.Z.2    Miller, M.R.3    Li, C.4    Charon, N.W.5
  • 53
    • 79959326635 scopus 로고    scopus 로고
    • A novel gene inactivation system reveals altered periplasmic flagellar orientation in a Borrelia burgdorferi fliL mutant
    • Motaleb, M.A., Pitzer, J.E., Sultan, S.Z., and Liu, J. (2011b) A novel gene inactivation system reveals altered periplasmic flagellar orientation in a Borrelia burgdorferi fliL mutant. J Bacteriol 193: 3324-3331.
    • (2011) J Bacteriol , vol.193 , pp. 3324-3331
    • Motaleb, M.A.1    Pitzer, J.E.2    Sultan, S.Z.3    Liu, J.4
  • 54
    • 34948834697 scopus 로고    scopus 로고
    • CheX in the three-phosphatase system of bacterial chemotaxis
    • Muff, T.J., Foster, R.M., Liu, P.J., and Ordal, G.W. (2007) CheX in the three-phosphatase system of bacterial chemotaxis. J Bacteriol 189: 7007-7013.
    • (2007) J Bacteriol , vol.189 , pp. 7007-7013
    • Muff, T.J.1    Foster, R.M.2    Liu, P.J.3    Ordal, G.W.4
  • 55
    • 0034877748 scopus 로고    scopus 로고
    • Delayed invasion of the kidney and brain by Borrelia crocidurae in plasminogen-deficient mice
    • Nordstrand, A., Shamaei-Tousi, A., Ny, A., and Bergstrom, S. (2001) Delayed invasion of the kidney and brain by Borrelia crocidurae in plasminogen-deficient mice. Infect Immun 69: 5832-5839.
    • (2001) Infect Immun , vol.69 , pp. 5832-5839
    • Nordstrand, A.1    Shamaei-Tousi, A.2    Ny, A.3    Bergstrom, S.4
  • 56
    • 39349089426 scopus 로고    scopus 로고
    • A differential role for BB0365 in the persistence of Borrelia burgdorferi in mice and ticks
    • Pal, U., Dai, J., Li, X., Neelakanta, G., Luo, P., Kumar, M., etal. (2008) A differential role for BB0365 in the persistence of Borrelia burgdorferi in mice and ticks. J Infect Dis 197: 148-155.
    • (2008) J Infect Dis , vol.197 , pp. 148-155
    • Pal, U.1    Dai, J.2    Li, X.3    Neelakanta, G.4    Luo, P.5    Kumar, M.6
  • 57
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M.J., and Wren, B.W. (1997) The HtrA family of serine proteases. Mol Microbiol 26: 209-221.
    • (1997) Mol Microbiol , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 58
    • 76649097688 scopus 로고    scopus 로고
    • Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate
    • Pazy, Y., Motaleb, M.A., Guarnieri, M.T., Charon, N.W., Zhao, R., and Silversmith, R.E. (2010) Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate. Proc Natl Acad Sci USA 107: 1924-1929.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1924-1929
    • Pazy, Y.1    Motaleb, M.A.2    Guarnieri, M.T.3    Charon, N.W.4    Zhao, R.5    Silversmith, R.E.6
  • 59
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen, T.N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 60
    • 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
  • 61
    • 0032438542 scopus 로고    scopus 로고
    • Differential expression of Borrelia burgdorferi proteins during growth in vitro
    • Ramamoorthy, R., and Philipp, M.T. (1998) Differential expression of Borrelia burgdorferi proteins during growth in vitro. Infect Immun 66: 5119-5124.
    • (1998) Infect Immun , vol.66 , pp. 5119-5124
    • Ramamoorthy, R.1    Philipp, M.T.2
  • 62
    • 0030002056 scopus 로고    scopus 로고
    • Molecular characterization, genomic arrangement, and expression of bmpD, a new member of the bmp class of genes encoding membrane proteins of Borrelia burgdorferi
    • Ramamoorthy, R., Povinelli, L., and Philipp, M.T. (1996) Molecular characterization, genomic arrangement, and expression of bmpD, a new member of the bmp class of genes encoding membrane proteins of Borrelia burgdorferi. Infect Immun 64: 1259-1264.
    • (1996) Infect Immun , vol.64 , pp. 1259-1264
    • Ramamoorthy, R.1    Povinelli, L.2    Philipp, M.T.3
  • 63
    • 77951298112 scopus 로고    scopus 로고
    • Molecular transformers in the cell: lessons learned from the DegP protease-chaperone
    • Sawa, J., Heuck, A., Ehrmann, M., and Clausen, T. (2010) Molecular transformers in the cell: lessons learned from the DegP protease-chaperone. Curr Opin Struct Biol 20: 253-258.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 253-258
    • Sawa, J.1    Heuck, A.2    Ehrmann, M.3    Clausen, T.4
  • 65
    • 0025726617 scopus 로고
    • Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product
    • Seol, J.H., Woo, S.K., Jung, E.M., Yoo, S.J., Lee, C.S., Kim, K.J., etal. (1991) Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product. Biochem Biophys Res Commun 176: 730-736.
    • (1991) Biochem Biophys Res Commun , vol.176 , pp. 730-736
    • Seol, J.H.1    Woo, S.K.2    Jung, E.M.3    Yoo, S.J.4    Lee, C.S.5    Kim, K.J.6
  • 66
    • 81755174173 scopus 로고    scopus 로고
    • The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases
    • Singh, N., Kuppili, R.R., and Bose, K. (2011) The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases. Arch Biochem Biophys 516: 85-96.
    • (2011) Arch Biochem Biophys , vol.516 , pp. 85-96
    • Singh, N.1    Kuppili, R.R.2    Bose, K.3
  • 67
    • 1242341364 scopus 로고    scopus 로고
    • The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure
    • Skorko-Glonek, J., Zurawa, D., Tanfani, F., Scire, A., Wawrzynow, A., Narkiewicz, J., etal. (2003) The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure. Biochim Biophys Acta 1649: 171-182.
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 171-182
    • Skorko-Glonek, J.1    Zurawa, D.2    Tanfani, F.3    Scire, A.4    Wawrzynow, A.5    Narkiewicz, J.6
  • 68
    • 58949083095 scopus 로고    scopus 로고
    • The proteolytic activity of the HtrA (DegP) protein from Escherichia coli at low temperatures
    • Skorko-Glonek, J., Sobiecka-Szkatula, A., Narkiewicz, J., and Lipinska, B. (2008) The proteolytic activity of the HtrA (DegP) protein from Escherichia coli at low temperatures. Microbiology 154: 3649-3658.
    • (2008) Microbiology , vol.154 , pp. 3649-3658
    • Skorko-Glonek, J.1    Sobiecka-Szkatula, A.2    Narkiewicz, J.3    Lipinska, B.4
  • 69
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions
    • Sourjik, V., and Berg, H.C. (2000) Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol Microbiol 37: 740-751.
    • (2000) Mol Microbiol , vol.37 , pp. 740-751
    • Sourjik, V.1    Berg, H.C.2
  • 70
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A., and Ehrmann, M. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97: 339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 71
    • 77953988576 scopus 로고    scopus 로고
    • Analysis of a Borrelia burgdorferi phosphodiesterase demonstrates a role for cyclic-di-guanosine monophosphate in motility and virulence
    • Sultan, S.Z., Pitzer, J.E., Miller, M.R., and Motaleb, M.A. (2010) Analysis of a Borrelia burgdorferi phosphodiesterase demonstrates a role for cyclic-di-guanosine monophosphate in motility and virulence. Mol Microbiol 77: 128-142.
    • (2010) Mol Microbiol , vol.77 , pp. 128-142
    • Sultan, S.Z.1    Pitzer, J.E.2    Miller, M.R.3    Motaleb, M.A.4
  • 72
    • 79961113805 scopus 로고    scopus 로고
    • Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals a role in motility and the enzootic life cycle of Borrelia burgdorferi
    • Sultan, S.Z., Pitzer, J.E., Boquoi, T., Hobbs, G., Miller, M.R., and Motaleb, M.A. (2011) Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals a role in motility and the enzootic life cycle of Borrelia burgdorferi. Infect Immun 79: 3273-3283.
    • (2011) Infect Immun , vol.79 , pp. 3273-3283
    • Sultan, S.Z.1    Pitzer, J.E.2    Boquoi, T.3    Hobbs, G.4    Miller, M.R.5    Motaleb, M.A.6
  • 73
    • 0021104535 scopus 로고
    • Isolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits
    • Swamy, K.H., Chung, C.H., and Goldberg, A.L. (1983) Isolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits. Arch Biochem Biophys 224: 543-554.
    • (1983) Arch Biochem Biophys , vol.224 , pp. 543-554
    • Swamy, K.H.1    Chung, C.H.2    Goldberg, A.L.3
  • 74
    • 84857066761 scopus 로고    scopus 로고
    • The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles
    • Toledo, A., Coleman, J.L., Kuhlow, C.J., Crowley, J.T., and Benach, J.L. (2012) The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles. Infect Immun 80: 359-368.
    • (2012) Infect Immun , vol.80 , pp. 359-368
    • Toledo, A.1    Coleman, J.L.2    Kuhlow, C.J.3    Crowley, J.T.4    Benach, J.L.5
  • 76
    • 0021738226 scopus 로고
    • Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
    • Twining, S.S. (1984) Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal Biochem 143: 30-34.
    • (1984) Anal Biochem , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 77
    • 70350450260 scopus 로고    scopus 로고
    • Borrelia burgdorferi BmpA is a laminin-binding protein
    • Verma, A., Brissette, C.A., Bowman, A., and Stevenson, B. (2009) Borrelia burgdorferi BmpA is a laminin-binding protein. Infect Immun 77: 4940-4946.
    • (2009) Infect Immun , vol.77 , pp. 4940-4946
    • Verma, A.1    Brissette, C.A.2    Bowman, A.3    Stevenson, B.4
  • 78
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
    • Waller, P.R., and Sauer, R.T. (1996) Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J Bacteriol 178: 1146-1153.
    • (1996) J Bacteriol , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 79
    • 79952927866 scopus 로고    scopus 로고
    • The HtrA-like serine protease PepD interacts with and modulates the Mycobacterium tuberculosis 35-kDa antigen outer envelope protein
    • and () . : .
    • White, M.J., Savaryn, J.P., Bretl, D.J., He, H., Penoske, R.M., Terhune, S.S., and Zahrt, T.C. (2011) The HtrA-like serine protease PepD interacts with and modulates the Mycobacterium tuberculosis 35-kDa antigen outer envelope protein. PLoS ONE 6: e18175.
    • (2011) PLoS ONE , vol.6
    • White, M.J.1    Savaryn, J.P.2    Bretl, D.J.3    He, H.4    Penoske, R.M.5    Terhune, S.S.6    Zahrt, T.C.7


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