메뉴 건너뛰기




Volumn 191, Issue 8, 2009, Pages 2601-2612

The orphan response regulator CovR: A globally negative modulator of virulence in Streptococcus suis serotype 2

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COVR PROTEIN; UNCLASSIFIED DRUG; REPRESSOR PROTEIN;

EID: 65249142114     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01309-08     Document Type: Article
Times cited : (63)

References (82)
  • 1
    • 0017360957 scopus 로고
    • Antigenic specificity of opsonophagocytic antibodies in rabbit anti-sera to group B streptococci
    • Baltimore, R. S., D. L. Kasper, C. J. Baker, and D. K. Goroff. 1977. Antigenic specificity of opsonophagocytic antibodies in rabbit anti-sera to group B streptococci. J. Immunol. 118:673-678.
    • (1977) J. Immunol , vol.118 , pp. 673-678
    • Baltimore, R.S.1    Kasper, D.L.2    Baker, C.J.3    Goroff, D.K.4
  • 2
    • 29144518548 scopus 로고    scopus 로고
    • Barabote, R. D., and M. H. Saier, Jr. 2005. Comparative genomic analyses of the bacterial phosphotransferase system. Microbiol. Mol. Biol. Rev. 69:608-634.
    • Barabote, R. D., and M. H. Saier, Jr. 2005. Comparative genomic analyses of the bacterial phosphotransferase system. Microbiol. Mol. Biol. Rev. 69:608-634.
  • 3
    • 16344373478 scopus 로고    scopus 로고
    • Strategic targets of essential host-pathogen interactions
    • Blasi, F., P. Tarsia, and S. Aliberti. 2005. Strategic targets of essential host-pathogen interactions. Respiration 72:9-25.
    • (2005) Respiration , vol.72 , pp. 9-25
    • Blasi, F.1    Tarsia, P.2    Aliberti, S.3
  • 4
    • 0035169610 scopus 로고    scopus 로고
    • Inactivation of the srtA gene in Streptococcus gordonii inhibits cell wall anchoring of surface proteins and decreases in vitro and in vivo adhesion
    • Bolken, T. C., C. A. Franke, K. F. Jones, G. O. Zeller, C. H. Jones, E. K. Dutton, and D. E. Hruby. 2001. Inactivation of the srtA gene in Streptococcus gordonii inhibits cell wall anchoring of surface proteins and decreases in vitro and in vivo adhesion. Infect. Immun. 69:75-80.
    • (2001) Infect. Immun , vol.69 , pp. 75-80
    • Bolken, T.C.1    Franke, C.A.2    Jones, K.F.3    Zeller, G.O.4    Jones, C.H.5    Dutton, E.K.6    Hruby, D.E.7
  • 6
    • 0029935785 scopus 로고    scopus 로고
    • In vitro phagocytosis and survival of Streptococcus suis capsular type 2 inside murine macrophages
    • Brazeau, C., M. Gottschalk, S. Vincelette, and B. Martineau-Doize. 1996. In vitro phagocytosis and survival of Streptococcus suis capsular type 2 inside murine macrophages. Microbiology 142:1231-1237.
    • (1996) Microbiology , vol.142 , pp. 1231-1237
    • Brazeau, C.1    Gottschalk, M.2    Vincelette, S.3    Martineau-Doize, B.4
  • 7
    • 0023946229 scopus 로고
    • Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance
    • Casiano-Colon, A., and R. E. Marquis. 1988. Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance. Appl. Environ. Microbiol. 54:1318-1324.
    • (1988) Appl. Environ. Microbiol , vol.54 , pp. 1318-1324
    • Casiano-Colon, A.1    Marquis, R.E.2
  • 9
    • 0031936119 scopus 로고    scopus 로고
    • Streptococcus suis serotype 2 mutants deficient in capsular expression
    • Charland, N., J. Harel, M. Kobisch, S. Lacasse, and M. Gottschalk. 1998. Streptococcus suis serotype 2 mutants deficient in capsular expression. Microbiology 144:325-332.
    • (1998) Microbiology , vol.144 , pp. 325-332
    • Charland, N.1    Harel, J.2    Kobisch, M.3    Lacasse, S.4    Gottschalk, M.5
  • 10
    • 0033963551 scopus 로고    scopus 로고
    • Streptococcus suis serotype 2 interactions with human brain microvascular endothelial cells
    • Charland, N., V. Nizet, C. E. Rubens, K. S. Kim, S. Lacouture, and M. Gottschalk. 2000. Streptococcus suis serotype 2 interactions with human brain microvascular endothelial cells. Infect. Immun. 68:637-643.
    • (2000) Infect. Immun , vol.68 , pp. 637-643
    • Charland, N.1    Nizet, V.2    Rubens, C.E.3    Kim, K.S.4    Lacouture, S.5    Gottschalk, M.6
  • 11
    • 55849107401 scopus 로고    scopus 로고
    • Chen, C., J. Tang, W. Dong, C. Wang, Y. Feng, et al. 2007. A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates. PLoS ONE 2:e315.
    • Chen, C., J. Tang, W. Dong, C. Wang, Y. Feng, et al. 2007. A glimpse of streptococcal toxic shock syndrome from comparative genomics of S. suis 2 Chinese isolates. PLoS ONE 2:e315.
  • 12
    • 0031987985 scopus 로고    scopus 로고
    • In vivo and ex vivo regulation of bacterial virulence gene expression
    • Cotter, P. A., and J. F. Miller. 1998. In vivo and ex vivo regulation of bacterial virulence gene expression. Curr. Opin. Microbiol. 1:17-26.
    • (1998) Curr. Opin. Microbiol , vol.1 , pp. 17-26
    • Cotter, P.A.1    Miller, J.F.2
  • 13
    • 0034098912 scopus 로고    scopus 로고
    • Characterization of an isogenic mutant of Streptococcus pyogenes Manfredo lacking the ability to make streptococcal acid glycoprotein
    • Degnan, B. A., M. C. Fontaine, A. H. Doebereiner, J. J. Lee, P. Mastroeni, G. Dougan, J. A. Goodacre, and M. A. Kehoe. 2000. Characterization of an isogenic mutant of Streptococcus pyogenes Manfredo lacking the ability to make streptococcal acid glycoprotein. Infect. Immun. 68:2441-2448.
    • (2000) Infect. Immun , vol.68 , pp. 2441-2448
    • Degnan, B.A.1    Fontaine, M.C.2    Doebereiner, A.H.3    Lee, J.J.4    Mastroeni, P.5    Dougan, G.6    Goodacre, J.A.7    Kehoe, M.A.8
  • 14
    • 0036401075 scopus 로고    scopus 로고
    • Response regulator important in pathogenesis of Streptococcus suis serotype 2
    • de Greeff, A., H. Buys, L. van Alphen, and H. E. Smith. 2002. Response regulator important in pathogenesis of Streptococcus suis serotype 2. Microb. Pathog. 33:185-192.
    • (2002) Microb. Pathog , vol.33 , pp. 185-192
    • de Greeff, A.1    Buys, H.2    van Alphen, L.3    Smith, H.E.4
  • 15
    • 0036180962 scopus 로고    scopus 로고
    • Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2
    • de Greeff, A., H. Buys, R. Verhaar, J. Dijkstra, L. van Alphen, and H. E. Smith. 2002. Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2. Infect. Immun. 70:1319-1325.
    • (2002) Infect. Immun , vol.70 , pp. 1319-1325
    • de Greeff, A.1    Buys, H.2    Verhaar, R.3    Dijkstra, J.4    van Alphen, L.5    Smith, H.E.6
  • 16
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher, J., C. Francke, and P. W. Postma. 2006. How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol. Mol. Biol. Rev. 70:939-1031.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 17
    • 0035313287 scopus 로고    scopus 로고
    • Spontaneous mutations in the CsrRS two-component regulatory system of Streptococcus pyogenes result in enhanced virulence in a murine model of skin and soft tissue infection
    • Engleberg, N. C., A. Heath, A. Miller, C. Rivera, and V. J. DiRita. 2001. Spontaneous mutations in the CsrRS two-component regulatory system of Streptococcus pyogenes result in enhanced virulence in a murine model of skin and soft tissue infection. J. Infect. Dis. 183:1043-1054.
    • (2001) J. Infect. Dis , vol.183 , pp. 1043-1054
    • Engleberg, N.C.1    Heath, A.2    Miller, A.3    Rivera, C.4    DiRita, V.J.5
  • 18
    • 0842327156 scopus 로고    scopus 로고
    • Contribution of CsrR-regulated virulence factors to the progress and outcome of murine skin infections by Streptococcus pyogenes
    • Engleberg, N. C., A. Heath, K. Vardaman, and V. J. DiRita. 2004. Contribution of CsrR-regulated virulence factors to the progress and outcome of murine skin infections by Streptococcus pyogenes. Infect. Immun. 72:623-628.
    • (2004) Infect. Immun , vol.72 , pp. 623-628
    • Engleberg, N.C.1    Heath, A.2    Vardaman, K.3    DiRita, V.J.4
  • 19
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal trans-duction in Bacillus subtilis: How one organism sees its world
    • Fabret, C., V. A. Feher, and J. A. Hoch. 1999. Two-component signal trans-duction in Bacillus subtilis: how one organism sees its world. J. Bacteriol. 181:1975-1983.
    • (1999) J. Bacteriol , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 20
    • 0025507435 scopus 로고
    • Surface proteins of coagulase-negative staphylococci: Their role in adherence to biomaterials and in opsonization
    • Fleer, A., C. P. Timmerman, J. M. Besnier, A. Pascual, and J. Verhoef. 1990. Surface proteins of coagulase-negative staphylococci: their role in adherence to biomaterials and in opsonization. J. Biomater. Appl. 5:154-165.
    • (1990) J. Biomater. Appl , vol.5 , pp. 154-165
    • Fleer, A.1    Timmerman, C.P.2    Besnier, J.M.3    Pascual, A.4    Verhoef, J.5
  • 21
    • 0033813409 scopus 로고    scopus 로고
    • Identification of Actinobacittus pleuropneumoniae virulence genes using signature-tagged mutagenesis in a swine infection model
    • Fuller, T. E., S. Martin, J. F. Teel, G. R. Alaniz, M. J. Kennedy, and D. E. Lowery. 2000. Identification of Actinobacittus pleuropneumoniae virulence genes using signature-tagged mutagenesis in a swine infection model. Microb. Pathog. 29:39-51.
    • (2000) Microb. Pathog , vol.29 , pp. 39-51
    • Fuller, T.E.1    Martin, S.2    Teel, J.F.3    Alaniz, G.R.4    Kennedy, M.J.5    Lowery, D.E.6
  • 23
    • 0000661051 scopus 로고    scopus 로고
    • Organization and function of transcription regulatory elements
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, 2nd ed. ASM Press, Washington, DC
    • Gralla, J. D., and J. Collado-Vides. 1996. Organization and function of transcription regulatory elements, p. 1232-1245. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1232-1245
    • Gralla, J.D.1    Collado-Vides, J.2
  • 24
    • 30744434891 scopus 로고    scopus 로고
    • Structure, regulation, and putative function of the arginine deiminase system of Streptococcus suis
    • Gruening, P., M. Fulde, P. Valentin-Weigand, and R. Goethe. 2006. Structure, regulation, and putative function of the arginine deiminase system of Streptococcus suis. J. Bacteriol. 188:361-369.
    • (2006) J. Bacteriol , vol.188 , pp. 361-369
    • Gruening, P.1    Fulde, M.2    Valentin-Weigand, P.3    Goethe, R.4
  • 25
    • 23944460126 scopus 로고    scopus 로고
    • Systematic targeted mutagenesis of Brucella melitensis 16M reveals a major role for GntR regulators in the control of virulence
    • Haine, V., A. Sinon, F. Van Steen, S. Rousseau, M. Dozot, P. Lestrate, C. Lambert, J. J. Letesson, and X. De Bolle. 2005. Systematic targeted mutagenesis of Brucella melitensis 16M reveals a major role for GntR regulators in the control of virulence. Infect. Immun. 73:5578-5586.
    • (2005) Infect. Immun , vol.73 , pp. 5578-5586
    • Haine, V.1    Sinon, A.2    Van Steen, F.3    Rousseau, S.4    Dozot, M.5    Lestrate, P.6    Lambert, C.7    Letesson, J.J.8    De Bolle, X.9
  • 26
    • 0036047758 scopus 로고    scopus 로고
    • Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors
    • Hava, D. L., and A. Camilli. 2002. Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol. Microbiol. 45:1389-1406.
    • (2002) Mol. Microbiol , vol.45 , pp. 1389-1406
    • Hava, D.L.1    Camilli, A.2
  • 27
    • 0032856769 scopus 로고    scopus 로고
    • A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B
    • Heath, A., V. J. DiRita, N. L. Barg, and N. C. Engleberg. 1999. A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B. Infect. Immun. 67:5298-5305.
    • (1999) Infect. Immun , vol.67 , pp. 5298-5305
    • Heath, A.1    DiRita, V.J.2    Barg, N.L.3    Engleberg, N.C.4
  • 29
    • 0028853680 scopus 로고
    • Methylglyoxal and regulation of its metabolism in microorganisms
    • Inoue, Y., and A. Kimura. 1995. Methylglyoxal and regulation of its metabolism in microorganisms. Adv. Microb. Physiol. 37:177-227.
    • (1995) Adv. Microb. Physiol , vol.37 , pp. 177-227
    • Inoue, Y.1    Kimura, A.2
  • 30
    • 0028231216 scopus 로고
    • Identification, purification, and characterization of a thiol-activated hemolysin (suilysin) of Streptococcus suis
    • Jacobs, A. A., P. L. Loeffen, A. J. van den Berg, and P. K. Storm. 1994. Identification, purification, and characterization of a thiol-activated hemolysin (suilysin) of Streptococcus suis. Infect. Immun. 62:1742-1748.
    • (1994) Infect. Immun , vol.62 , pp. 1742-1748
    • Jacobs, A.A.1    Loeffen, P.L.2    van den Berg, A.J.3    Storm, P.K.4
  • 31
    • 13244268247 scopus 로고    scopus 로고
    • Regulation of virulence by a two-component system in group B streptococcus
    • Jiang, S. M., M. J. Cieslewicz, D. L. Kasper, and M. R. Wessels. 2005. Regulation of virulence by a two-component system in group B streptococcus. J. Bacteriol. 187:1105-1113.
    • (2005) J. Bacteriol , vol.187 , pp. 1105-1113
    • Jiang, S.M.1    Cieslewicz, M.J.2    Kasper, D.L.3    Wessels, M.R.4
  • 32
    • 0033775014 scopus 로고    scopus 로고
    • Identification of Streptococcus agalactiae virulence genes in the neonatal rat sepsis model using signature-tagged mutagenesis
    • Jones, A. L., K M. Knoll, and C. E. Rubens. 2000. Identification of Streptococcus agalactiae virulence genes in the neonatal rat sepsis model using signature-tagged mutagenesis. Mol. Microbiol. 37:1444-1455.
    • (2000) Mol. Microbiol , vol.37 , pp. 1444-1455
    • Jones, A.L.1    Knoll, K.M.2    Rubens, C.E.3
  • 33
    • 0032703938 scopus 로고    scopus 로고
    • Methylglyoxal in living organisms: Chemistry, biochemistry, toxicology and biological implications
    • Kalapos, M. P. 1999. Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol. Lett. 110:145-175.
    • (1999) Toxicol. Lett , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 34
    • 0030253290 scopus 로고    scopus 로고
    • Comparative preparation methods of sialylated capsule antigen from Streptococcus suis type 2 with type specific antigenicity
    • Katsumi, M., T. Saito, Y. Kataoka, T. Itoh, N. Kikuchi, and T. Hiramune. 1996. Comparative preparation methods of sialylated capsule antigen from Streptococcus suis type 2 with type specific antigenicity. J. Vet. Med. Sci. 58:947-952.
    • (1996) J. Vet. Med. Sci , vol.58 , pp. 947-952
    • Katsumi, M.1    Saito, T.2    Kataoka, Y.3    Itoh, T.4    Kikuchi, N.5    Hiramune, T.6
  • 35
    • 0037406692 scopus 로고    scopus 로고
    • Inactivation of the srtA gene affects localization of surface proteins and decreases adhesion of Streptococcus pneumoniae to human pharyngeal cells in vitro
    • Kharat, A. S., and A. Tomasz. 2003. Inactivation of the srtA gene affects localization of surface proteins and decreases adhesion of Streptococcus pneumoniae to human pharyngeal cells in vitro. Infect. Immun. 71:2758-2765.
    • (2003) Infect. Immun , vol.71 , pp. 2758-2765
    • Kharat, A.S.1    Tomasz, A.2
  • 37
    • 0037180568 scopus 로고    scopus 로고
    • The analysis of the intramacrophagic virulome of Brucella suis deciphers the environment encountered by the pathogen inside the macrophage host cell
    • Kohler, S., V. Foulongne, S. Ouahrani-Bettache, G. Bourg, J. Teyssier, M. Ramuz, and J. P. Liautard. 2002. The analysis of the intramacrophagic virulome of Brucella suis deciphers the environment encountered by the pathogen inside the macrophage host cell. Proc. Natl. Acad. Sci. USA 99: 15711-15716.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15711-15716
    • Kohler, S.1    Foulongne, V.2    Ouahrani-Bettache, S.3    Bourg, G.4    Teyssier, J.5    Ramuz, M.6    Liautard, J.P.7
  • 38
    • 35648957713 scopus 로고    scopus 로고
    • Involvement of the detoxifying enzyme lactoylglutathione lyase in Streptococcus mutans aciduricity
    • Korithoski, B., C. M. Levesque, and D. G. Cvitkovitch. 2007. Involvement of the detoxifying enzyme lactoylglutathione lyase in Streptococcus mutans aciduricity. J. Bacteriol. 189:7586-7592.
    • (2007) J. Bacteriol , vol.189 , pp. 7586-7592
    • Korithoski, B.1    Levesque, C.M.2    Cvitkovitch, D.G.3
  • 39
    • 0000186326 scopus 로고
    • Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system
    • Kundig, W., S. Ghosh, and S. Roseman. 1964. Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system. Proc. Natl. Acad. Sci. USA 52:1067-1074.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.52 , pp. 1067-1074
    • Kundig, W.1    Ghosh, S.2    Roseman, S.3
  • 40
    • 21144462780 scopus 로고    scopus 로고
    • The SrtA sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine
    • Lalioui, L., E. Pellegrini, S. Dramsi, M. Baptista, N. Bourgeois, F. Doucet-Populaire, C. Rusniok, M. Zouine, P. Glaser, F. Kunst, C. Poyart, and P. Trieu-Cuot. 2005. The SrtA sortase of Streptococcus agalactiae is required for cell wall anchoring of proteins containing the LPXTG motif, for adhesion to epithelial cells, and for colonization of the mouse intestine. Infect. Immun. 73:3342-3350.
    • (2005) Infect. Immun , vol.73 , pp. 3342-3350
    • Lalioui, L.1    Pellegrini, E.2    Dramsi, S.3    Baptista, M.4    Bourgeois, N.5    Doucet-Populaire, F.6    Rusniok, C.7    Zouine, M.8    Glaser, P.9    Kunst, F.10    Poyart, C.11    Trieu-Cuot, P.12
  • 41
    • 0033870279 scopus 로고    scopus 로고
    • Interactions between Streptococcus suis serotype 2 and different epithelial cell lines
    • Lalonde, M., M. Segura, S. Lacouture, and M. Gottschalk. 2000. Interactions between Streptococcus suis serotype 2 and different epithelial cell lines. Microbiology 146:1913-1921.
    • (2000) Microbiology , vol.146 , pp. 1913-1921
    • Lalonde, M.1    Segura, M.2    Lacouture, S.3    Gottschalk, M.4
  • 44
    • 0344420127 scopus 로고    scopus 로고
    • Attenuated signature-tagged mutagenesis mutants of Brucella melitensis identified during the acute phase of infection in mice
    • Lestrate, P., A. Dricot, R. M. Delrue, C. Lambert, V. Martinelli, X. De Bolle, J. J. Letesson, and A. Tibor. 2003. Attenuated signature-tagged mutagenesis mutants of Brucella melitensis identified during the acute phase of infection in mice. Infect. Immun. 71:7053-7060.
    • (2003) Infect. Immun , vol.71 , pp. 7053-7060
    • Lestrate, P.1    Dricot, A.2    Delrue, R.M.3    Lambert, C.4    Martinelli, V.5    De Bolle, X.6    Letesson, J.J.7    Tibor, A.8
  • 45
    • 0031669931 scopus 로고    scopus 로고
    • Identification of csrR/csrS, a genetic locus that regulates hyaluronic acid capsule synthesis in group A Streptococcus
    • Levin, J. C., and M. R. Wessels. 1998. Identification of csrR/csrS, a genetic locus that regulates hyaluronic acid capsule synthesis in group A Streptococcus. Mol. Microbiol. 30:209-219.
    • (1998) Mol. Microbiol , vol.30 , pp. 209-219
    • Levin, J.C.1    Wessels, M.R.2
  • 46
    • 47749113315 scopus 로고    scopus 로고
    • Li, M., C. Wang, Y. Feng, X. Pan, G. Cheng, J. Wang, J. Ge, F. Zheng, M. Cao, Y. Dong, D. Liu, J. Wang, Y. Lin, H. Du, G. F. Gao, X. Wang, F. Hu, and J. Tang. 2008. SalK/SalR, a two-component signal transduction system, is essential for full virulence of highly invasive Streptococcus suis serotype 2. PLoS ONE 3:e2080.
    • Li, M., C. Wang, Y. Feng, X. Pan, G. Cheng, J. Wang, J. Ge, F. Zheng, M. Cao, Y. Dong, D. Liu, J. Wang, Y. Lin, H. Du, G. F. Gao, X. Wang, F. Hu, and J. Tang. 2008. SalK/SalR, a two-component signal transduction system, is essential for full virulence of highly invasive Streptococcus suis serotype 2. PLoS ONE 3:e2080.
  • 48
    • 1142309598 scopus 로고    scopus 로고
    • Lun, S., and P. J. Willson. 2004. Expression of green fluorescent protein and its application in pathogenesis studies of serotype 2 Streptococcus suis.J. Microbiol. Methods 56:401-412.
    • Lun, S., and P. J. Willson. 2004. Expression of green fluorescent protein and its application in pathogenesis studies of serotype 2 Streptococcus suis.J. Microbiol. Methods 56:401-412.
  • 50
    • 0031882801 scopus 로고    scopus 로고
    • The role of sialic acid in opsonin-dependent and opsonin-independent adhesion of Listeria monocytogenes to murine peritoneal macrophages
    • Maganti, S., M. M. Pierce, A. Hoffmaster, and F. G. Rodgers. 1998. The role of sialic acid in opsonin-dependent and opsonin-independent adhesion of Listeria monocytogenes to murine peritoneal macrophages. Infect. Immun. 66:620-626.
    • (1998) Infect. Immun , vol.66 , pp. 620-626
    • Maganti, S.1    Pierce, M.M.2    Hoffmaster, A.3    Rodgers, F.G.4
  • 51
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary, W. R., and J. B. Stock. 1994. Acetyl phosphate and the activation of two-component response regulators. J. Biol. Chem. 269:31567-31572.
    • (1994) J. Biol. Chem , vol.269 , pp. 31567-31572
    • McCleary, W.R.1    Stock, J.B.2
  • 52
    • 0024437993 scopus 로고
    • Purification and characterization of the deoR repressor of Escherichia coli
    • Mortensen, L., G. Dandanell, and K. Hammer. 1989. Purification and characterization of the deoR repressor of Escherichia coli. EMBO J. 8:325-331.
    • (1989) EMBO J , vol.8 , pp. 325-331
    • Mortensen, L.1    Dandanell, G.2    Hammer, K.3
  • 53
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V., and V. A. Fischetti. 1992. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 176:415-426.
    • (1992) J. Exp. Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 54
    • 0027291428 scopus 로고
    • Phosphoenolpyru-vate:carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1993. Phosphoenolpyru-vate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:543-594.
    • (1993) Microbiol. Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 55
    • 0028073849 scopus 로고
    • Identification of a fatty acyl responsive regulator (FarR) in Escherichia coli
    • Quail, M. A., C. E. Dempsey, and J. R. Guest. 1994. Identification of a fatty acyl responsive regulator (FarR) in Escherichia coli. FEBS Lett. 356:183-187.
    • (1994) FEBS Lett , vol.356 , pp. 183-187
    • Quail, M.A.1    Dempsey, C.E.2    Guest, J.R.3
  • 56
    • 0033975250 scopus 로고    scopus 로고
    • The Brucella abortus Lon functions as a generalized stress response protease and is required for wild-type virulence in BALB/c mice
    • Robertson, G. T., M. E. Kovach, C. A. Allen, T. A. Ficht, and R. M. Roop II. 2000. The Brucella abortus Lon functions as a generalized stress response protease and is required for wild-type virulence in BALB/c mice. Mol. Microbiol. 35:577-588.
    • (2000) Mol. Microbiol , vol.35 , pp. 577-588
    • Robertson, G.T.1    Kovach, M.E.2    Allen, C.A.3    Ficht, T.A.4    Roop II, R.M.5
  • 57
    • 0142011077 scopus 로고    scopus 로고
    • The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells
    • Roche, F. M., M. Meehan, and T. J. Foster. 2003. The Staphylococcus aureus surface protein SasG and its homologues promote bacterial adherence to human desquamated nasal epithelial cells. Microbiology 149:2759-2767.
    • (2003) Microbiology , vol.149 , pp. 2759-2767
    • Roche, F.M.1    Meehan, M.2    Foster, T.J.3
  • 58
    • 0029039486 scopus 로고
    • Protein phosphorylation and regulation of carbon metabolism in gram-negative versus gram-positive bacteria
    • Saier, M. H., Jr., S. Chauvaux, J. Deutscher, J. Reizer, and J. J. Ye. 1995. Protein phosphorylation and regulation of carbon metabolism in gram-negative versus gram-positive bacteria. Trends Biochem. Sci. 20:267-271.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 267-271
    • Saier Jr., M.H.1    Chauvaux, S.2    Deutscher, J.3    Reizer, J.4    Ye, J.J.5
  • 59
    • 0029060960 scopus 로고
    • Properties of a Streptococcus suis isolate of serotype 2 and two capsular mutants
    • Salasia, S. I., C. Lammler, and G. Herrmann. 1995. Properties of a Streptococcus suis isolate of serotype 2 and two capsular mutants. Vet. Microbiol. 45:151-156.
    • (1995) Vet. Microbiol , vol.45 , pp. 151-156
    • Salasia, S.I.1    Lammler, C.2    Herrmann, G.3
  • 60
    • 0034694128 scopus 로고    scopus 로고
    • Effect of experimental treatment on housekeeping gene expression: Validation by real-time, quantitative RT-PCR
    • Schmittgen, T. D., and B. A. Zakrajsek. 2000. Effect of experimental treatment on housekeeping gene expression: validation by real-time, quantitative RT-PCR. J. Biochem. Biophys. Methods 46:69-81.
    • (2000) J. Biochem. Biophys. Methods , vol.46 , pp. 69-81
    • Schmittgen, T.D.1    Zakrajsek, B.A.2
  • 61
    • 0036129770 scopus 로고    scopus 로고
    • CD14-dependent and -independent cytokine and chemokine production by human THP-1 monocytes stimulated by Streptococcus suis capsular type 2
    • Segura, M., N. Vadeboncoeur, and M. Gottschalk. 2002. CD14-dependent and -independent cytokine and chemokine production by human THP-1 monocytes stimulated by Streptococcus suis capsular type 2. Clin. Exp. Immunol. 127:243-254.
    • (2002) Clin. Exp. Immunol , vol.127 , pp. 243-254
    • Segura, M.1    Vadeboncoeur, N.2    Gottschalk, M.3
  • 62
    • 0344588809 scopus 로고    scopus 로고
    • Streptococcus suis and group B Streptococcus differ in their interactions with murine macrophages
    • Segura, M. A., P. Cleroux, and M. Gottschalk. 1998. Streptococcus suis and group B Streptococcus differ in their interactions with murine macrophages. FEMS Immunol. Med. Microbiol. 21:189-195.
    • (1998) FEMS Immunol. Med. Microbiol , vol.21 , pp. 189-195
    • Segura, M.A.1    Cleroux, P.2    Gottschalk, M.3
  • 63
    • 0033040620 scopus 로고    scopus 로고
    • Identification and characterization of the cps locus of Streptococcus suis serotype 2: The capsule protects against phagocytosis and is an important virulence factor
    • Smith, H. E., M. Damman, J. van der Velde, F. Wagenaar, H. J. Wisselink, N. Stockhofe-Zurwieden, and M. A. Smits. 1999. Identification and characterization of the cps locus of Streptococcus suis serotype 2: the capsule protects against phagocytosis and is an important virulence factor. Infect. Immun. 67:1750-1756.
    • (1999) Infect. Immun , vol.67 , pp. 1750-1756
    • Smith, H.E.1    Damman, M.2    van der Velde, J.3    Wagenaar, F.4    Wisselink, H.J.5    Stockhofe-Zurwieden, N.6    Smits, M.A.7
  • 64
    • 0028861689 scopus 로고
    • High-efficiency transformation and gene inactivation in Streptococcus suis type 2
    • Smith, H. E., H. J. Wisselink, U. Vecht, A. L. Gielkens, and M. A. Smits. 1995. High-efficiency transformation and gene inactivation in Streptococcus suis type 2. Microbiology 141:181-188.
    • (1995) Microbiology , vol.141 , pp. 181-188
    • Smith, H.E.1    Wisselink, H.J.2    Vecht, U.3    Gielkens, A.L.4    Smits, M.A.5
  • 65
  • 67
    • 40749113609 scopus 로고    scopus 로고
    • A chemokine-degrading extracellular protease made by group A Streptococcus alters pathogenesis by enhancing evasion of the innate immune response
    • Sumby, P., S. Zhang, A. R. Whitney, F. Falugi, G. Grandi, E. A. Graviss, F. R. Deleo, and J. M. Musser. 2008. A chemokine-degrading extracellular protease made by group A Streptococcus alters pathogenesis by enhancing evasion of the innate immune response. Infect. Immun. 76:978-985.
    • (2008) Infect. Immun , vol.76 , pp. 978-985
    • Sumby, P.1    Zhang, S.2    Whitney, A.R.3    Falugi, F.4    Grandi, G.5    Graviss, E.A.6    Deleo, F.R.7    Musser, J.M.8
  • 68
    • 0035099359 scopus 로고    scopus 로고
    • Construction and characterization of Streptococcus suis-Escherichia coli shuttle cloning vectors
    • Takamatsu, D., M. Osaki, and T. Sekizaki. 2001. Construction and characterization of Streptococcus suis-Escherichia coli shuttle cloning vectors. Plasmid 45:101-113.
    • (2001) Plasmid , vol.45 , pp. 101-113
    • Takamatsu, D.1    Osaki, M.2    Sekizaki, T.3
  • 70
    • 0036156251 scopus 로고    scopus 로고
    • Novel laminin-binding protein of Streptococcus pyogenes, Lbp, is involved in adhesion to epithelial cells
    • Terao, Y., S. Kawabata, E. Kunitomo, I. Nakagawa, and S. Hamada. 2002. Novel laminin-binding protein of Streptococcus pyogenes, Lbp, is involved in adhesion to epithelial cells. Infect. Immun. 70:993-997.
    • (2002) Infect. Immun , vol.70 , pp. 993-997
    • Terao, Y.1    Kawabata, S.2    Kunitomo, E.3    Nakagawa, I.4    Hamada, S.5
  • 71
    • 0036693775 scopus 로고    scopus 로고
    • Global control of sugar metabolism: A gram-positive solution
    • Titgemeyer, F., and W. Hillen. 2002. Global control of sugar metabolism: a gram-positive solution. Antonie van Leeuwenhoek 82:59-71.
    • (2002) Antonie van Leeuwenhoek , vol.82 , pp. 59-71
    • Titgemeyer, F.1    Hillen, W.2
  • 72
    • 0033607265 scopus 로고    scopus 로고
    • Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
    • Ton-That, H., G. Liu, S. K. Mazmanian, K. F. Faull, and O. Schneewind. 1999. Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc. Natl. Acad. Sci. USA 96:12424-12429.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12424-12429
    • Ton-That, H.1    Liu, G.2    Mazmanian, S.K.3    Faull, K.F.4    Schneewind, O.5
  • 73
    • 0031900977 scopus 로고    scopus 로고
    • Identification of Salmonella typhimurium genes required for colonization of the chicken alimentary tract and for virulence in newly hatched chicks
    • Turner, A. K., M. A. Lovell, S. D. Hulme, L. Zhang-Barber, and P. A. Barrow. 1998. Identification of Salmonella typhimurium genes required for colonization of the chicken alimentary tract and for virulence in newly hatched chicks. Infect. Immun. 66:2099-2106.
    • (1998) Infect. Immun , vol.66 , pp. 2099-2106
    • Turner, A.K.1    Lovell, M.A.2    Hulme, S.D.3    Zhang-Barber, L.4    Barrow, P.A.5
  • 74
    • 1342323773 scopus 로고    scopus 로고
    • Invasion of porcine brain microvascular endothelial cells by Streptococcus suis serotype 2
    • Vanier, G., M. Segura, P. Friedl, S. Lacouture, and M. Gottschalk. 2004. Invasion of porcine brain microvascular endothelial cells by Streptococcus suis serotype 2. Infect. Immun. 72:1441-1449.
    • (2004) Infect. Immun , vol.72 , pp. 1441-1449
    • Vanier, G.1    Segura, M.2    Friedl, P.3    Lacouture, S.4    Gottschalk, M.5
  • 75
    • 34248365735 scopus 로고    scopus 로고
    • Characterization of the invasion of porcine endothelial cells by Streptococcus suis serotype 2
    • Vanier, G., M. Segura, and M. Gottschalk. 2007. Characterization of the invasion of porcine endothelial cells by Streptococcus suis serotype 2. Can. J. Vet. Res. 71:81-89.
    • (2007) Can. J. Vet. Res , vol.71 , pp. 81-89
    • Vanier, G.1    Segura, M.2    Gottschalk, M.3
  • 76
    • 38649106736 scopus 로고    scopus 로고
    • Disruption of srtA gene in Streptococcus suis results in decreased interactions with endothelial cells and extracellular matrix proteins
    • Vanier, G., T. Sekizaki, M. C. Dominguez-Punaro, M. Esgleas, M. Osaki, D. Takamatsu, M. Segura, and M. Gottschalk. 2008. Disruption of srtA gene in Streptococcus suis results in decreased interactions with endothelial cells and extracellular matrix proteins. Vet. Microbiol. 127:417-424.
    • (2008) Vet. Microbiol , vol.127 , pp. 417-424
    • Vanier, G.1    Sekizaki, T.2    Dominguez-Punaro, M.C.3    Esgleas, M.4    Osaki, M.5    Takamatsu, D.6    Segura, M.7    Gottschalk, M.8
  • 78
    • 0024316972 scopus 로고
    • Definition of a bacterial virulence factor: Sialylation of the group B streptococcal capsule
    • Wessels, M. R., C. E. Rubens, V. J. Benedi, and D. L. Kasper. 1989. Definition of a bacterial virulence factor: sialylation of the group B streptococcal capsule. Proc. Natl. Acad. Sci. USA 86:8983-8987.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8983-8987
    • Wessels, M.R.1    Rubens, C.E.2    Benedi, V.J.3    Kasper, D.L.4
  • 79
    • 0028525681 scopus 로고
    • Relation between encapsulation and various properties of Streptococcus suis
    • Wibawan, I. W., and C. Lammler. 1994. Relation between encapsulation and various properties of Streptococcus suis. Zentralbl. Veterinarmed. B 41:453-459.
    • (1994) Zentralbl. Veterinarmed. B , vol.41 , pp. 453-459
    • Wibawan, I.W.1    Lammler, C.2
  • 80
    • 0025346095 scopus 로고
    • Pathogenesis of meningitis caused by Streptococcus suis type 2
    • Williams, A. E., and W. F. Blakemore. 1990. Pathogenesis of meningitis caused by Streptococcus suis type 2. J. Infect. Dis. 162:474-481.
    • (1990) J. Infect. Dis , vol.162 , pp. 474-481
    • Williams, A.E.1    Blakemore, W.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.