메뉴 건너뛰기




Volumn 81, Issue 6, 2011, Pages 1542-1559

HtrA is a major virulence determinant of Bacillus anthracis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; BACTERIUM ANTIBODY; HIGH TEMPERATURE REQUIREMENT A PROTEIN; NEUTRAL PROTEASE A; NEUTRALIZING ANTIBODY; POLYGLUTAMIC ACID; SERINE PROTEINASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 80052697246     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07790.x     Document Type: Article
Times cited : (50)

References (77)
  • 1
    • 10744222163 scopus 로고    scopus 로고
    • The extracellular proteome of B.subtilis under secretion stress conditions
    • Antelmann, H., Darmon, E., Noone, D., Veening, J., Westers, H., Bron, S., etal. (2003) The extracellular proteome of B.subtilis under secretion stress conditions. Mol Microbiol 49: 143-156.
    • (2003) Mol Microbiol , vol.49 , pp. 143-156
    • Antelmann, H.1    Darmon, E.2    Noone, D.3    Veening, J.4    Westers, H.5    Bron, S.6
  • 2
    • 0036893688 scopus 로고    scopus 로고
    • Search for potential vaccine candidate ORFs in the B.anthracis virulence plasmid pXO1-in silico and in vitro screening
    • Ariel, N., Zvi, A., Grosfeld, H., Gat, O., Inbar, Y., Velan, B., etal. (2002) Search for potential vaccine candidate ORFs in the B.anthracis virulence plasmid pXO1-in silico and in vitro screening. Infect Immun 70: 6817-6827.
    • (2002) Infect Immun , vol.70 , pp. 6817-6827
    • Ariel, N.1    Zvi, A.2    Grosfeld, H.3    Gat, O.4    Inbar, Y.5    Velan, B.6
  • 3
    • 0042265058 scopus 로고    scopus 로고
    • Genome-based bioinformatic selection of chromosomal B.anthracis putative vaccine candidates coupled with proteomic identification of surface-associated antigens
    • Ariel, N., Zvi, A., Makarova, K., Chitlaru, T., Elhanany, E., Velan, B., etal. (2003) Genome-based bioinformatic selection of chromosomal B.anthracis putative vaccine candidates coupled with proteomic identification of surface-associated antigens. Infect Immun 71: 4563-4579.
    • (2003) Infect Immun , vol.71 , pp. 4563-4579
    • Ariel, N.1    Zvi, A.2    Makarova, K.3    Chitlaru, T.4    Elhanany, E.5    Velan, B.6
  • 5
    • 25444479087 scopus 로고    scopus 로고
    • The role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans
    • Biswas, S., and Biswas, I. (2005) The role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans. Infect Immun 73: 6923-6934.
    • (2005) Infect Immun , vol.73 , pp. 6923-6934
    • Biswas, S.1    Biswas, I.2
  • 6
    • 0037406725 scopus 로고    scopus 로고
    • Global effects of virulence gene regulators in Bacillus anthracis strain with both virulence plasmids
    • Bourgogne, A., Drysdale, M., Hilsenbeck, S.H., Peterson, S.N., and Koehler, T.M. (2003) Global effects of virulence gene regulators in Bacillus anthracis strain with both virulence plasmids. Infect Immun 71: 2736-2743.
    • (2003) Infect Immun , vol.71 , pp. 2736-2743
    • Bourgogne, A.1    Drysdale, M.2    Hilsenbeck, S.H.3    Peterson, S.N.4    Koehler, T.M.5
  • 7
    • 0942279513 scopus 로고    scopus 로고
    • Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence
    • Cendrowski, S., MacArthur, W., and Hanna, P. (2004) Bacillus anthracis requires siderophore biosynthesis for growth in macrophages and mouse virulence. Mol Microbiol 51: 407-417.
    • (2004) Mol Microbiol , vol.51 , pp. 407-417
    • Cendrowski, S.1    MacArthur, W.2    Hanna, P.3
  • 8
    • 70449449494 scopus 로고    scopus 로고
    • Proteomic studies of Bacillus anthracis
    • Chitlaru, T., and Shafferman, A. (2009) Proteomic studies of Bacillus anthracis. Future Microbiol 4: 983-998.
    • (2009) Future Microbiol , vol.4 , pp. 983-998
    • Chitlaru, T.1    Shafferman, A.2
  • 9
    • 1542720741 scopus 로고    scopus 로고
    • Identification of chromosomally encoded membranal polypeptides of Bacillus anthracis by a proteomic analysis: prevalence of proteins containing S-layer homology domains
    • Chitlaru, T., Ariel, N., Zvi, A., Lion, M., Velan, B., Shafferman, A., and Elhanany, E. (2004) Identification of chromosomally encoded membranal polypeptides of Bacillus anthracis by a proteomic analysis: prevalence of proteins containing S-layer homology domains. Proteomics 4: 677-691.
    • (2004) Proteomics , vol.4 , pp. 677-691
    • Chitlaru, T.1    Ariel, N.2    Zvi, A.3    Lion, M.4    Velan, B.5    Shafferman, A.6    Elhanany, E.7
  • 11
    • 34249886795 scopus 로고    scopus 로고
    • Identification of in vivo expressed immunogenic proteins by serological proteome analysis of Bacillus anthracis secretome
    • Chitlaru, T., Gat, O., Gozlan, Y., Grosfeld, H., Inbar, I., and Shafferman, A. (2007) Identification of in vivo expressed immunogenic proteins by serological proteome analysis of Bacillus anthracis secretome. Infect Immun 75: 2841-2852.
    • (2007) Infect Immun , vol.75 , pp. 2841-2852
    • Chitlaru, T.1    Gat, O.2    Gozlan, Y.3    Grosfeld, H.4    Inbar, I.5    Shafferman, A.6
  • 13
    • 78650563014 scopus 로고    scopus 로고
    • Progress and novel strategies in vaccine development and treatment of anthrax
    • Chitlaru, T., Altboum, Z., Reuveny, S., and Shafferman, A. (2011) Progress and novel strategies in vaccine development and treatment of anthrax. Immunol Rev 239: 221-236.
    • (2011) Immunol Rev , vol.239 , pp. 221-236
    • Chitlaru, T.1    Altboum, Z.2    Reuveny, S.3    Shafferman, A.4
  • 14
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: implications for Protein composition and cell fate
    • Clausen, T., Southan, C., and Ehrmann, M. (2002) The HtrA family of proteases: implications for Protein composition and cell fate. Mol Cell 10: 443-455.
    • (2002) Mol Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 15
    • 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 12: 152-162.
    • (2011) Nat Rev , vol.12 , pp. 152-162
    • Clausen, T.1    Kaiser, M.2    Huber, R.3    Ehrmann, M.4
  • 16
    • 0033914197 scopus 로고    scopus 로고
    • Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus anthracis spore vaccines protect against anthrax
    • Cohen, S., Mendelson, I., Altboum, Z., Kobiler, D., Elhanany, E., Bino, T., etal. (2000) Attenuated nontoxinogenic and nonencapsulated recombinant Bacillus anthracis spore vaccines protect against anthrax. Infect Immun 68: 4549-4558.
    • (2000) Infect Immun , vol.68 , pp. 4549-4558
    • Cohen, S.1    Mendelson, I.2    Altboum, Z.3    Kobiler, D.4    Elhanany, E.5    Bino, T.6
  • 18
    • 70350708307 scopus 로고    scopus 로고
    • Membrane translocation by anthrax toxin
    • Collier, R.J. (2009) Membrane translocation by anthrax toxin. Mol Aspects Med 30: 413-422.
    • (2009) Mol Aspects Med , vol.30 , pp. 413-422
    • Collier, R.J.1
  • 19
    • 46249116534 scopus 로고    scopus 로고
    • Requirements for surface expression and function of Adhesin P1 from Streptococcus mutans
    • Crowley, P.J., Seifert, T.B., Isoda, R., van Tilburg, M., Oli, M.W., Robinette, R.A., etal. (2008) Requirements for surface expression and function of Adhesin P1 from Streptococcus mutans. Infect Immun 76: 2456-2468.
    • (2008) Infect Immun , vol.76 , pp. 2456-2468
    • Crowley, P.J.1    Seifert, T.B.2    Isoda, R.3    van Tilburg, M.4    Oli, M.W.5    Robinette, R.A.6
  • 20
    • 58449131069 scopus 로고    scopus 로고
    • Four superoxide dismutases contribute to Bacillus anthracis virulence and provide spores with redundant protection from oxidative stress
    • Cybulski, R.J., Sanz, P., Alem, F., Stibitz, S., Bull, R.L., and O'brian, A.D. (2009) Four superoxide dismutases contribute to Bacillus anthracis virulence and provide spores with redundant protection from oxidative stress. Infect Immun 77: 274-285.
    • (2009) Infect Immun , vol.77 , pp. 274-285
    • Cybulski, R.J.1    Sanz, P.2    Alem, F.3    Stibitz, S.4    Bull, R.L.5    O'brian, A.D.6
  • 21
    • 0030998321 scopus 로고    scopus 로고
    • E and the Cpx signal transduction system control the synthesis of periplasmic protein-folding enzymes in E.coli
    • E and the Cpx signal transduction system control the synthesis of periplasmic protein-folding enzymes in E.coli. Genes Dev 11: 1183-1193.
    • (1997) Genes Dev , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 22
    • 0036786262 scopus 로고    scopus 로고
    • Anovel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of B.subtillis
    • Darmon, E., Noone, D., Masson, A., Bron, S., Kuipers, O.P., Devine, K.M., and van Dijl, J.M. (2002) Anovel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of B.subtillis. J Bacteriol 184: 5661-5671.
    • (2002) J Bacteriol , vol.184 , pp. 5661-5671
    • Darmon, E.1    Noone, D.2    Masson, A.3    Bron, S.4    Kuipers, O.P.5    Devine, K.M.6    van Dijl, J.M.7
  • 23
    • 62649122954 scopus 로고    scopus 로고
    • Bacteriocin activity of Streptococcus pneumoniae is controlled by the serine protease HtrA via posttranscriptional regulation
    • Dawid, S., Sebert, M.E., and Weiser, J.N. (2009) Bacteriocin activity of Streptococcus pneumoniae is controlled by the serine protease HtrA via posttranscriptional regulation. J Bacteriol 191: 1509-1518.
    • (2009) J Bacteriol , vol.191 , pp. 1509-1518
    • Dawid, S.1    Sebert, M.E.2    Weiser, J.N.3
  • 24
    • 56749173808 scopus 로고    scopus 로고
    • A matter of life and death: cell wall homeostasis and the WalKR(YyCF) essential signal transduction pathway
    • Dubrac, S., Bisicchia, P., Devine, K.M., and Msadek, T. (2008) A matter of life and death: cell wall homeostasis and the WalKR(YyCF) essential signal transduction pathway. Mol Microbiol 70: 1307-1322.
    • (2008) Mol Microbiol , vol.70 , pp. 1307-1322
    • Dubrac, S.1    Bisicchia, P.2    Devine, K.M.3    Msadek, T.4
  • 25
    • 70350705851 scopus 로고    scopus 로고
    • The surface of Bacillus anthracis
    • Fouet, A. (2009) The surface of Bacillus anthracis. Mol Aspects Med 30: 374-385.
    • (2009) Mol Aspects Med , vol.30 , pp. 374-385
    • Fouet, A.1
  • 26
    • 0036022857 scopus 로고    scopus 로고
    • Bacillus anthracis cell envelope components
    • Fouet, A., and Mesnage, S. (2002) Bacillus anthracis cell envelope components. Curr Top Microbiol Immunol 271: 87-113.
    • (2002) Curr Top Microbiol Immunol , vol.271 , pp. 87-113
    • Fouet, A.1    Mesnage, S.2
  • 28
    • 70350719196 scopus 로고    scopus 로고
    • Preparedness for an anthrax attack
    • Franz, D.R. (2009) Preparedness for an anthrax attack. Mol Aspects Med 30: 503-510.
    • (2009) Mol Aspects Med , vol.30 , pp. 503-510
    • Franz, D.R.1
  • 29
    • 0037306598 scopus 로고    scopus 로고
    • Use of a promoter trap system in Bacillus anthracis and Bacillus subtilis for the development of recombinant protective antigen-based vaccines
    • Gat, O., Inbar, I., Aloni-Grinstein, R., Zahavy, E., Kronman, C., Mendelson, I., etal. (2003) Use of a promoter trap system in Bacillus anthracis and Bacillus subtilis for the development of recombinant protective antigen-based vaccines. Infect Immun 71: 801-813.
    • (2003) Infect Immun , vol.71 , pp. 801-813
    • Gat, O.1    Inbar, I.2    Aloni-Grinstein, R.3    Zahavy, E.4    Kronman, C.5    Mendelson, I.6
  • 30
    • 26944486892 scopus 로고    scopus 로고
    • The solute-binding component of a putative Mn(II) ABC transporter (MntA) is a novel Bacillus anthracis virulence determinant
    • Gat, O., Mendelson, I., Chitlaru, T., Ariel, N., Altboum, Z., Levy, H., etal. (2005) The solute-binding component of a putative Mn(II) ABC transporter (MntA) is a novel Bacillus anthracis virulence determinant. Mol Microbiol 58: 533-551.
    • (2005) Mol Microbiol , vol.58 , pp. 533-551
    • Gat, O.1    Mendelson, I.2    Chitlaru, T.3    Ariel, N.4    Altboum, Z.5    Levy, H.6
  • 31
    • 33745617720 scopus 로고    scopus 로고
    • Search for Bacillus anthracis potential vaccine candidates by a functional genomic-serologic screen
    • Gat, O., Grosfeld, H., Ariel, N., Inbar, I., Zaide, G., Broder, I., etal. (2006) Search for Bacillus anthracis potential vaccine candidates by a functional genomic-serologic screen. Infect Immun 74: 3987-4001.
    • (2006) Infect Immun , vol.74 , pp. 3987-4001
    • Gat, O.1    Grosfeld, H.2    Ariel, N.3    Inbar, I.4    Zaide, G.5    Broder, I.6
  • 32
    • 34249908056 scopus 로고    scopus 로고
    • In vitro screen of bioinformatically selected Bacillus anthracis vaccine candidates by coupled transcription, translation and immunoprecipitation analysis
    • Grandi, G. (ed.). Totowa, NJ: Humana Press
    • Gat, O., Grosfeld, H., and Shafferman, A. (2007) In vitro screen of bioinformatically selected Bacillus anthracis vaccine candidates by coupled transcription, translation and immunoprecipitation analysis. In Methods in Molecular Biology, Vol. 375. In Vitro Transcription and Translation Proteocols. Grandi, G. (ed.). Totowa, NJ: Humana Press, pp. 211-233.
    • (2007) Methods in Molecular Biology, Vol. 375. In Vitro Transcription and Translation Proteocols , pp. 211-233
    • Gat, O.1    Grosfeld, H.2    Shafferman, A.3
  • 33
    • 54249105484 scopus 로고    scopus 로고
    • Characterization of Bacillus anthracis iron-regulated surface determinant (Isd) proteins containing NEAT domains
    • Gat, O., Zaide, G., Inbar, I., Grosfeld, H., Chitlaru, T., Levy, H., and Shafferman, A. (2008) Characterization of Bacillus anthracis iron-regulated surface determinant (Isd) proteins containing NEAT domains. Mol Microbiol 70: 983-999.
    • (2008) Mol Microbiol , vol.70 , pp. 983-999
    • Gat, O.1    Zaide, G.2    Inbar, I.3    Grosfeld, H.4    Chitlaru, T.5    Levy, H.6    Shafferman, A.7
  • 34
    • 0031055751 scopus 로고    scopus 로고
    • AtxA activates the transcription of genes harbored by both Bacillus anthracis virulence plasmids
    • Guignot, J., Mock, M., and Fouet, A. (1997) AtxA activates the transcription of genes harbored by both Bacillus anthracis virulence plasmids. FEMS Microbiol Lett 15: 203-207.
    • (1997) FEMS Microbiol Lett , vol.15 , pp. 203-207
    • Guignot, J.1    Mock, M.2    Fouet, A.3
  • 35
    • 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
    • Hal Jones, C., Bolken, T.C., Jones, K.F.G., Zeller, 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
    • Hal Jones, C.1    Bolken, T.C.2    Jones, K.F.G.3    Zeller, O.4    Hruby, D.E.5
  • 36
    • 35848954992 scopus 로고    scopus 로고
    • SigB-Dependent general stress response in B.subtilis and related gram-positive bacteria
    • Hecker, M., Pane-Farre, J., and Volker, U. (2007) SigB-Dependent general stress response in B.subtilis and related gram-positive bacteria. Annu Rev Microbiol 61: 215-236.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 215-236
    • Hecker, M.1    Pane-Farre, J.2    Volker, U.3
  • 38
    • 77957232471 scopus 로고    scopus 로고
    • Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion
    • Hoy, B., Löwer, 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    Löwer, M.2    Weydig, C.3    Carra, G.4    Tegtmeyer, N.5    Geppert, T.6
  • 39
    • 0035788801 scopus 로고    scopus 로고
    • A novel two-component regulatory system in Bacillus subtillis for the survival of severe secretion stress
    • Hyyrylainen, H.L., Bolhuis, A., Darmon, E., Muukonen, L., Koski, P., Vitikainen, M., etal. (2001) A novel two-component regulatory system in Bacillus subtillis for the survival of severe secretion stress. Mol Microbiol 41: 1159-1172.
    • (2001) Mol Microbiol , vol.41 , pp. 1159-1172
    • Hyyrylainen, H.L.1    Bolhuis, A.2    Darmon, E.3    Muukonen, L.4    Koski, P.5    Vitikainen, M.6
  • 40
    • 2542617706 scopus 로고    scopus 로고
    • Role of HtrA in the virulence and competence of Streptococcus pneumoniae
    • Ibrahim, Y.M., Kerr, A.R., McCluskey, J., and Mitchell, T.J. (2004) Role of HtrA in the virulence and competence of Streptococcus pneumoniae. Infect Immun 72: 3584-3591.
    • (2004) Infect Immun , vol.72 , pp. 3584-3591
    • Ibrahim, Y.M.1    Kerr, A.R.2    McCluskey, J.3    Mitchell, T.J.4
  • 41
    • 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
  • 42
    • 78650893958 scopus 로고    scopus 로고
    • Examining the role of purine biosynthesis in Bacillus anthracis pathogenesis and virulence
    • Jenkins, A., Cote, C., Twenhafel, N., Merkel, T., Bozue, J., and Welkos, S. (2011) Examining the role of purine biosynthesis in Bacillus anthracis pathogenesis and virulence. Infect Immun 79: 153-166.
    • (2011) Infect Immun , vol.79 , pp. 153-166
    • Jenkins, A.1    Cote, C.2    Twenhafel, N.3    Merkel, T.4    Bozue, J.5    Welkos, S.6
  • 43
    • 74349118819 scopus 로고    scopus 로고
    • BslA, the S-layer adhesin of B.anthracis, is a virulence factor for anthrax pathogenesis
    • Kern, J., and Schneewind, O. (2010) BslA, the S-layer adhesin of B.anthracis, is a virulence factor for anthrax pathogenesis. Mol Microbiol 75: 324-332.
    • (2010) Mol Microbiol , vol.75 , pp. 324-332
    • Kern, J.1    Schneewind, O.2
  • 44
    • 77955551189 scopus 로고    scopus 로고
    • Bacillus anthracis surface-layer proteins assemble by binding to the secondary cell wall polysaccharide in a manner that requires csaB and tagO
    • Kern, J., Ryan, C., Faull, K., and Schneewind, O. (2010) Bacillus anthracis surface-layer proteins assemble by binding to the secondary cell wall polysaccharide in a manner that requires csaB and tagO. J Mol Biol 401: 757-775.
    • (2010) J Mol Biol , vol.401 , pp. 757-775
    • Kern, J.1    Ryan, C.2    Faull, K.3    Schneewind, O.4
  • 45
    • 0028088404 scopus 로고
    • Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity
    • Klimpel, K.R., Arora, N., and Leppla, S.H. (1994) Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol Microbiol 13: 1093-1100.
    • (1994) Mol Microbiol , vol.13 , pp. 1093-1100
    • Klimpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 47
    • 70350726230 scopus 로고    scopus 로고
    • Bacillus anthracis physiology and genetics
    • Koehler, T.M. (2009) Bacillus anthracis physiology and genetics. Mol Aspects Med 30: 386-396.
    • (2009) Mol Aspects Med , vol.30 , pp. 386-396
    • Koehler, T.M.1
  • 48
  • 49
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla, S. (1982) Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc Natl Acad Sci USA 79: 3162-3166.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3162-3166
    • Leppla, S.1
  • 50
    • 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
  • 52
    • 1342323730 scopus 로고    scopus 로고
    • Role of the serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the Hemolysin Streptolysin S
    • Lyon, W.R., and Caparon, M.G. (2004) Role of the serine protease HtrA (DegP) of Streptococcus pyogenes in the biogenesis of virulence factors SpeB and the Hemolysin Streptolysin S. Infect Immun 72: 1618-1625.
    • (2004) Infect Immun , vol.72 , pp. 1618-1625
    • Lyon, W.R.1    Caparon, M.G.2
  • 53
    • 77953395311 scopus 로고    scopus 로고
    • ClpX contributes to innate defense peptide resistance and virulence phenotypes of Bacillus anthracis
    • McGillivray, S.M., Ebrahimi, C.M., Fisher, N., Sabet, M., Zhang, D.X., Chen, Y., etal. (2009) ClpX contributes to innate defense peptide resistance and virulence phenotypes of Bacillus anthracis. J Innate Immun 1: 494-506.
    • (2009) J Innate Immun , vol.1 , pp. 494-506
    • McGillivray, S.M.1    Ebrahimi, C.M.2    Fisher, N.3    Sabet, M.4    Zhang, D.X.5    Chen, Y.6
  • 54
    • 26944450746 scopus 로고    scopus 로고
    • Efficacious, nontoxigenic Bacillus anthracis spore vaccines based on strains expressing mutant variants of lethal toxin components
    • Mendelson, I., Gat, O., Aloni-Grinstein, R., Altboum, Z., Inbar, I., Kronman, C., etal. (2005) Efficacious, nontoxigenic Bacillus anthracis spore vaccines based on strains expressing mutant variants of lethal toxin components. Vaccine 23: 5688-5697.
    • (2005) Vaccine , vol.23 , pp. 5688-5697
    • Mendelson, I.1    Gat, O.2    Aloni-Grinstein, R.3    Altboum, Z.4    Inbar, I.5    Kronman, C.6
  • 55
    • 0030978176 scopus 로고    scopus 로고
    • Molecular characterization of the Bacillus anthracis main S-layer component: evidence that it is the major cell-associated antigen
    • Mesnage, S., Tosi-Couture, E., Mock, M., Gounon, P., and Fouet, A. (1997) Molecular characterization of the Bacillus anthracis main S-layer component: evidence that it is the major cell-associated antigen. Mol Microbiol 23: 1147-1155.
    • (1997) Mol Microbiol , vol.23 , pp. 1147-1155
    • Mesnage, S.1    Tosi-Couture, E.2    Mock, M.3    Gounon, P.4    Fouet, A.5
  • 56
    • 0034283014 scopus 로고    scopus 로고
    • Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation
    • Mesnage, S., Fontaine, T., Mignot, T., Delepierre, M., Mock, M., and Fouet, A. (2000) Bacterial SLH domain proteins are non-covalently anchored to the cell surface via a conserved mechanism involving wall polysaccharide pyruvylation. EMBO J 19: 4473-4484.
    • (2000) EMBO J , vol.19 , pp. 4473-4484
    • Mesnage, S.1    Fontaine, T.2    Mignot, T.3    Delepierre, M.4    Mock, M.5    Fouet, A.6
  • 57
    • 0037326444 scopus 로고    scopus 로고
    • A plasmid-encoded regulator couples the synthesis of toxins and surface structures in Bacillus anthracis
    • Mignot, T., Mock, M., and Fouet, A. (2003) A plasmid-encoded regulator couples the synthesis of toxins and surface structures in Bacillus anthracis. Mol Microbiol 47: 917-927.
    • (2003) Mol Microbiol , vol.47 , pp. 917-927
    • Mignot, T.1    Mock, M.2    Fouet, A.3
  • 58
    • 4444242794 scopus 로고    scopus 로고
    • Attenuated Salmonella typhimurium htrA mutants cause fatal infections in mice deficient in NADPH oxidase and destroy NADPH oxidase-deficient macrophage monolayers
    • Mutunga, M., Graham, S., de Hormaeche, R.D., Musson, J.A., Robinson, J.H., etal. (2004) Attenuated Salmonella typhimurium htrA mutants cause fatal infections in mice deficient in NADPH oxidase and destroy NADPH oxidase-deficient macrophage monolayers. Vaccine 22: 4124-4131.
    • (2004) Vaccine , vol.22 , pp. 4124-4131
    • Mutunga, M.1    Graham, S.2    de Hormaeche, R.D.3    Musson, J.A.4    Robinson, J.H.5
  • 59
    • 0035156736 scopus 로고    scopus 로고
    • YkdA and YvtA, HtrA-like serine proteases in Bacillus subtillis engage in negative autoregulation and reciprocal cross-regulation of ykdA and yvtA gene expression
    • Noone, D., Howell, A., Collery, R., and Devine, K.M. (2001) YkdA and YvtA, HtrA-like serine proteases in Bacillus subtillis engage in negative autoregulation and reciprocal cross-regulation of ykdA and yvtA gene expression. J Bacteriol 183: 654-663.
    • (2001) J Bacteriol , vol.183 , pp. 654-663
    • Noone, D.1    Howell, A.2    Collery, R.3    Devine, K.M.4
  • 60
    • 0030812638 scopus 로고    scopus 로고
    • Th HtrA family of serine proteases
    • Pallen, M.J., and Wren, B.W. (1997) Th 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
  • 61
    • 42749095777 scopus 로고    scopus 로고
    • Commingling regulatory systems following acquisition of virulence plasmids by Bacillus anthracis
    • Perego, M., and Hoch, J.A. (2008) Commingling regulatory systems following acquisition of virulence plasmids by Bacillus anthracis. Trends Microbiol 16: 215-221.
    • (2008) Trends Microbiol , vol.16 , pp. 215-221
    • Perego, M.1    Hoch, J.A.2
  • 62
    • 0028935459 scopus 로고
    • Protective immunity induced by Bacillus anthracis toxin-deficient strains
    • Pezard, C., Weber, M., Sirard, J.-C., Berche, P., and Mock, M. (1995) Protective immunity induced by Bacillus anthracis toxin-deficient strains. Infect Immun 63: 1369-1372.
    • (1995) Infect Immun , vol.63 , pp. 1369-1372
    • Pezard, C.1    Weber, M.2    Sirard, J.-C.3    Berche, P.4    Mock, M.5
  • 63
    • 0034108191 scopus 로고    scopus 로고
    • Htr A is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing
    • Poquet, I., Saint, V., Seznec, E., Simoes, N., Bolotin, A., and Gruss, A. (2000) Htr A is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing. Mol Microbiol 35: 1042-1051.
    • (2000) Mol Microbiol , vol.35 , pp. 1042-1051
    • Poquet, I.1    Saint, V.2    Seznec, E.3    Simoes, N.4    Bolotin, A.5    Gruss, A.6
  • 64
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed, L.J., and Muench, H. (1938) A simple method of estimating fifty percent endpoints. Am J Hyg 27: 493-497.
    • (1938) Am J Hyg , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 65
    • 0035055295 scopus 로고    scopus 로고
    • Search for correlates of protective immunity conferred by anthrax vaccine
    • Reuveny, S., White, M.D., Adar, Y.Y., Kafri, Y., Altboum, Z., Gozes, Y., etal. (2001) Search for correlates of protective immunity conferred by anthrax vaccine. Infect Immun 69: 2888-2893.
    • (2001) Infect Immun , vol.69 , pp. 2888-2893
    • Reuveny, S.1    White, M.D.2    Adar, Y.Y.3    Kafri, Y.4    Altboum, Z.5    Gozes, Y.6
  • 66
    • 11144278533 scopus 로고    scopus 로고
    • Comparative analysis of the roles of HtrA-like surface proteases in two virulent Staphylococcus aureus strains
    • Rigoulay, C., Entenza, J.M., Halpern, D., Widmer, E., Moreillon, P., Poquet, I., and Gruss, A. (2005) Comparative analysis of the roles of HtrA-like surface proteases in two virulent Staphylococcus aureus strains. Infect Immun 73: 563-572.
    • (2005) Infect Immun , vol.73 , pp. 563-572
    • Rigoulay, C.1    Entenza, J.M.2    Halpern, D.3    Widmer, E.4    Moreillon, P.5    Poquet, I.6    Gruss, A.7
  • 67
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch, J.W., and Caparon, M.G. (2005) The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol Microbiol 58: 959-968.
    • (2005) Mol Microbiol , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 71
    • 0033617146 scopus 로고    scopus 로고
    • A temperature dependent qwitch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A., and Ehrmann, M. (1999) A temperature dependent qwitch 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
  • 73
    • 0030934904 scopus 로고    scopus 로고
    • Cross-talk to the genes for Bacillus anthracis capsule synthesis by atxA, the gene encoding the trans-activator of anthrax toxin synthesis
    • Uchida, I., Makino, S., Sekizaki, T., and Terakado, N. (1997) Cross-talk to the genes for Bacillus anthracis capsule synthesis by atxA, the gene encoding the trans-activator of anthrax toxin synthesis. Mol Microbiol 23: 1229-1240.
    • (1997) Mol Microbiol , vol.23 , pp. 1229-1240
    • Uchida, I.1    Makino, S.2    Sekizaki, T.3    Terakado, N.4
  • 74
    • 23044435305 scopus 로고    scopus 로고
    • Secretion of heterologous proteins in Bacillus Subtillis can be improved by engineering cell components affecting post-translocational protein folding and degradation
    • Vitikainen, M., Hyyrylainen, H.-L., Kivimaki, A., and Sarvas, M. (2005) Secretion of heterologous proteins in Bacillus Subtillis can be improved by engineering cell components affecting post-translocational protein folding and degradation. J Appl Microbiol 99: 363-375.
    • (2005) J Appl Microbiol , vol.99 , pp. 363-375
    • Vitikainen, M.1    Hyyrylainen, H.-L.2    Kivimaki, A.3    Sarvas, M.4
  • 75
    • 59749092501 scopus 로고    scopus 로고
    • Involvement of TLR2 innate response to Bacillus anthracis infection
    • Weiss, S., Levy, H., Fisher, M., Kobiler, D., and Altboum, Z. (2009) Involvement of TLR2 innate response to Bacillus anthracis infection. Innate Immun 15: 43-51.
    • (2009) Innate Immun , vol.15 , pp. 43-51
    • Weiss, S.1    Levy, H.2    Fisher, M.3    Kobiler, D.4    Altboum, Z.5
  • 76
    • 84888656864 scopus 로고    scopus 로고
    • The interaction between Bacillus anthracis and macrophages
    • Bergman, N.H. (ed.). Hoboken, NJ: John Wiley & Sons
    • Welkos, S.L., Bozue, J.A., and Cote, C.K. (2011) The interaction between Bacillus anthracis and macrophages. In Bacillus Anthracis and Anthrax. Bergman, N.H. (ed.). Hoboken, NJ: John Wiley & Sons, pp. 179-208.
    • (2011) Bacillus Anthracis and Anthrax , pp. 179-208
    • Welkos, S.L.1    Bozue, J.A.2    Cote, C.K.3
  • 77
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease
    • Wilken, C., Kitzing, K., Kurzbauer, R., Ehrmann, M., and Clausen, T. (2004) Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease. Cell 117: 483-494.
    • (2004) Cell , vol.117 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.