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Volumn 186, Issue 17, 2004, Pages 5629-5639

The Enterococcus faecalis fsr two-component system controls biofilm development through production of gelatinase

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE; METALLOPROTEINASE; ZINC;

EID: 4344682069     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.17.5629-5639.2004     Document Type: Article
Times cited : (248)

References (49)
  • 1
    • 0027169704 scopus 로고
    • The accessory gene regulator (agr) controls Staphyloccoccus aureus virulence in a murine arthritis model
    • Abdelnour, A., S. Arvidson, T. Bremell, C. Ryden, and A. Tarkowski. 1993. The accessory gene regulator (agr) controls Staphyloccoccus aureus virulence in a murine arthritis model. Infect. Immun. 61:3879-3885.
    • (1993) Infect. Immun. , vol.61 , pp. 3879-3885
    • Abdelnour, A.1    Arvidson, S.2    Bremell, T.3    Ryden, C.4    Tarkowski, A.5
  • 3
    • 0038304134 scopus 로고    scopus 로고
    • Alpha-toxin is required for biofilm formation by Staphylococcus aureus
    • Caiazza, N. C., and G. A. O'Toole. 2003. Alpha-toxin is required for biofilm formation by Staphylococcus aureus. J. Bacteriol. 185:3214-3217.
    • (2003) J. Bacteriol. , vol.185 , pp. 3214-3217
    • Caiazza, N.C.1    O'Toole, G.A.2
  • 4
    • 0032968219 scopus 로고    scopus 로고
    • Role of hemolysin BL in the pathogenesis of extraintestinal Bacillus cereus infection assessed in an endophthalmitis model
    • Callegan, M. C., B. D. Jett, L. E. Hancock, and M. S. Gilmore. 1999. Role of hemolysin BL in the pathogenesis of extraintestinal Bacillus cereus infection assessed in an endophthalmitis model. Infect. Immun. 67:3357-3366.
    • (1999) Infect. Immun. , vol.67 , pp. 3357-3366
    • Callegan, M.C.1    Jett, B.D.2    Hancock, L.E.3    Gilmore, M.S.4
  • 6
    • 0033923852 scopus 로고    scopus 로고
    • Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein
    • Collin, M., and A. Olsen. 2000. Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein. Mol. Microbiol. 36:1306-1318.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1306-1318
    • Collin, M.1    Olsen, A.2
  • 7
    • 0028929250 scopus 로고
    • Incidence of hemolysin, gelatinase, and aggregation substance among enterococci isolated from patients with endocarditis and other infections and from feces of hospitalized and community-based persons
    • Coque, T. M., J. E. Patterson, J. M. Steckelberg, and B. E. Murray. 1995. Incidence of hemolysin, gelatinase, and aggregation substance among enterococci isolated from patients with endocarditis and other infections and from feces of hospitalized and community-based persons. J. Infect. Dis. 171: 1223-1229.
    • (1995) J. Infect. Dis. , vol.171 , pp. 1223-1229
    • Coque, T.M.1    Patterson, J.E.2    Steckelberg, J.M.3    Murray, B.E.4
  • 8
    • 0025149087 scopus 로고
    • High efficiency introduction of plasmid DNA into glycine treated Enterococcus faecalis by electroporation
    • Cruz-Rodz, A. L., and M. S. Gilmore. 1990. High efficiency introduction of plasmid DNA into glycine treated Enterococcus faecalis by electroporation. Mol. Gen. Genet. 224:152-154.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 152-154
    • Cruz-Rodz, A.L.1    Gilmore, M.S.2
  • 9
    • 0034912050 scopus 로고    scopus 로고
    • Genetic competence and transformation in oral streptococci
    • Cvitkovitch, D. G. 2001. Genetic competence and transformation in oral streptococci. Crit. Rev. Oral Biol. Med. 12:217-243.
    • (2001) Crit. Rev. Oral Biol. Med. , vol.12 , pp. 217-243
    • Cvitkovitch, D.G.1
  • 10
    • 0028022637 scopus 로고
    • Two-component regulators and genetic competence in Bacillus subtilis
    • Dubnau, D., J. Hahn, M. Roggiani, F. Piazza, and Y. Weinrauch. 1994. Two-component regulators and genetic competence in Bacillus subtilis. Res. Microbiol. 145:403-411.
    • (1994) Res. Microbiol. , vol.145 , pp. 403-411
    • Dubnau, D.1    Hahn, J.2    Roggiani, M.3    Piazza, F.4    Weinrauch, Y.5
  • 12
    • 0033963304 scopus 로고    scopus 로고
    • Direct quantitative transcript analysis of the agr regulon of Staphylococcus aureus during human infection in comparison to the expression profile in vitro
    • Goerke, C., S. Campana, M. G. Bayer, G. Doring, K. Botzenhart, and C. Wolz. 2000. Direct quantitative transcript analysis of the agr regulon of Staphylococcus aureus during human infection in comparison to the expression profile in vitro. Infect. Immun. 68:1304-1311.
    • (2000) Infect. Immun. , vol.68 , pp. 1304-1311
    • Goerke, C.1    Campana, S.2    Bayer, M.G.3    Doring, G.4    Botzenhart, K.5    Wolz, C.6
  • 13
    • 0034932885 scopus 로고    scopus 로고
    • Impact of the regulatory loci agr, sarA and sae of Staphylococcus aureus on the induction of α-toxin during device-related infection resolved by direct quantitative transcript analysis
    • Goerke, C., U. Fluckiger, A. Steinhuber, W. Zimmerli, and C. Wolz., 2001. Impact of the regulatory loci agr, sarA and sae of Staphylococcus aureus on the induction of α-toxin during device-related infection resolved by direct quantitative transcript analysis. Mol. Microbiol. 40:1439-1447.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1439-1447
    • Goerke, C.1    Fluckiger, U.2    Steinhuber, A.3    Zimmerli, W.4    Wolz, C.5
  • 14
    • 0036837964 scopus 로고    scopus 로고
    • Two-component signal transduction in Enterococcus faecalis
    • Hancock, L., and M. Perego. 2002. Two-component signal transduction in Enterococcus faecalis. J. Bacteriol. 184:5819-5825.
    • (2002) J. Bacteriol. , vol.184 , pp. 5819-5825
    • Hancock, L.1    Perego, M.2
  • 17
    • 0034832026 scopus 로고    scopus 로고
    • Peptide pheromone-dependent regulation of antimicrobial peptide production in Gram-positive bacteria: A case of multicellular behavior
    • Kleerebezem, M., and L. E. Quadri. 2001. Peptide pheromone-dependent regulation of antimicrobial peptide production in Gram-positive bacteria: a case of multicellular behavior. Peptides 22:1579-1596.
    • (2001) Peptides , vol.22 , pp. 1579-1596
    • Kleerebezem, M.1    Quadri, L.E.2
  • 18
    • 0030814729 scopus 로고    scopus 로고
    • Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria
    • Kleerebezem, M., L. E. N. Quadri, O. P. Kuipers, and W. de Vos. 1997. Quorum sensing by peptide pheromones and two-component signal-transduction systems in Gram-positive bacteria. Mol. Microbiol. 24:895-904.
    • (1997) Mol. Microbiol. , vol.24 , pp. 895-904
    • Kleerebezem, M.1    Quadri, L.E.N.2    Kuipers, O.P.3    De Vos, W.4
  • 19
    • 0346435112 scopus 로고    scopus 로고
    • Esp-independent biofilm formation by Enterococcus faecalis
    • Kristich, C. J., Y. H. Li, D. G. Cvitkovitch, and G. M. Dunny. 2004. Esp-independent biofilm formation by Enterococcus faecalis. J. Bacteriol. 186:154-163.
    • (2004) J. Bacteriol. , vol.186 , pp. 154-163
    • Kristich, C.J.1    Li, Y.H.2    Cvitkovitch, D.G.3    Dunny, G.M.4
  • 20
    • 0025826822 scopus 로고
    • Cellular functions of metalloendoproteinases
    • Lennarz, W. J., and W. J. Strittmatter. 1991. Cellular functions of metalloendoproteinases. Biochim. Biophys. Acta 1071:149-158.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 149-158
    • Lennarz, W.J.1    Strittmatter, W.J.2
  • 21
    • 0036233112 scopus 로고    scopus 로고
    • A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation
    • Li, Y.-H., N. Tang, M. B. Aspiras, P. C. Y. Lau, J. H. Lee, R. P. Ellen, and D. G. Cvitkovitch. 2002. A quorum-sensing signaling system essential for genetic competence in Streptococcus mutans is involved in biofilm formation. J. Bacteriol. 184:2699-2708.
    • (2002) J. Bacteriol. , vol.184 , pp. 2699-2708
    • Li, Y.-H.1    Tang, N.2    Aspiras, M.B.3    Lau, P.C.Y.4    Lee, J.H.5    Ellen, R.P.6    Cvitkovitch, D.G.7
  • 22
    • 0038623056 scopus 로고    scopus 로고
    • Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease
    • Lyon, W. R., and M. G. Caparon. 2003. Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease. J. Bacteriol. 185:3661-3667.
    • (2003) J. Bacteriol. , vol.185 , pp. 3661-3667
    • Lyon, W.R.1    Caparon, M.G.2
  • 23
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W. R., C. M. Gibson, and M. G. Caparon. 1998. A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J. 17:6263-6275.
    • (1998) EMBO J. , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 24
    • 0024560589 scopus 로고
    • Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10)
    • Makinen, P.-L., D. B. Clewell, F. An, and K. K. Makinen. 1989. Purification and substrate specificity of a strongly hydrophobic extracellular metalloendopeptidase ("gelatinase") from Streptococcus faecalis (strain 0G1-10). J. Biol. Chem. 264:3325-3334.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3325-3334
    • Makinen, P.-L.1    Clewell, D.B.2    An, F.3    Makinen, K.K.4
  • 25
    • 0028211864 scopus 로고
    • The Enterococcus faecalis extracellular metalloendopeptidase (EC 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues
    • Makinen, P., and K. K. Makinen. 1994. The Enterococcus faecalis extracellular metalloendopeptidase (EC 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues. Biochem. Biophys. Res. Commun. 200:981-985.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 981-985
    • Makinen, P.1    Makinen, K.K.2
  • 26
    • 0036076721 scopus 로고    scopus 로고
    • The Enterococcus faecalis fsrB gene, a key component of the fsr quorum-sensing system, is associated with virulence in the rabbit endophthalmitis model
    • Mylonakis, E., M. Engelbert, X. Qin, C. D. Sifri, B. E. Murray, F. M. Ausubel, M. S. Gilmore, and S. B. Calderwood. 2002. The Enterococcus faecalis fsrB gene, a key component of the fsr quorum-sensing system, is associated with virulence in the rabbit endophthalmitis model. Infect. Immun. 70:4678-4681.
    • (2002) Infect. Immun. , vol.70 , pp. 4678-4681
    • Mylonakis, E.1    Engelbert, M.2    Qin, X.3    Sifri, C.D.4    Murray, B.E.5    Ausubel, F.M.6    Gilmore, M.S.7    Calderwood, S.B.8
  • 27
    • 0034946367 scopus 로고    scopus 로고
    • Gelatinase biosynthesis-activating pheromone: A peptide lactone that mediates a quorum sensing in Enterococcus faecalis
    • Nakayama, J., Y. Cao, T. Horii, S. Sakuda, A. D. L. Akkermans, W. de Vos, and H. Nagasawa. 2001. Gelatinase biosynthesis-activating pheromone: a peptide lactone that mediates a quorum sensing in Enterococcus faecalis. Mol. Microbiol. 41:145-154.
    • (2001) Mol. Microbiol. , vol.41 , pp. 145-154
    • Nakayama, J.1    Cao, Y.2    Horii, T.3    Sakuda, S.4    Akkermans, A.D.L.5    De Vos, W.6    Nagasawa, H.7
  • 28
    • 0036263259 scopus 로고    scopus 로고
    • Biofilm bacteria: Formation and comparative susceptibility to antibiotics
    • Olson, M. E., H. Ceri, D. W. Morck, A. G. Buret, and R. R. Read. 2002. Biofilm bacteria: formation and comparative susceptibility to antibiotics. Can. J. Vet. Res. 66:86-92.
    • (2002) Can. J. Vet. Res. , vol.66 , pp. 86-92
    • Olson, M.E.1    Ceri, H.2    Morck, D.W.3    Buret, A.G.4    Read, R.R.5
  • 30
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., B. Spellerberg, M. Woischnik, B. Pohl, and R. Lütticken, 1996. Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177:137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lütticken, R.5
  • 31
    • 0031573015 scopus 로고    scopus 로고
    • A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to β-galactosidase in Gram-positive bacteria
    • Poyart, C., and P. Trieu-Cuot. 1997. A broad-host-range mobilizable shuttle vector for the construction of transcriptional fusions to β-galactosidase in Gram-positive bacteria. FEMS Microbiol. Lett. 156:193-198.
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 193-198
    • Poyart, C.1    Trieu-Cuot, P.2
  • 32
    • 0034061486 scopus 로고    scopus 로고
    • Effects of Enterococcus faecalis fsr genes on production of gelatinase and a serine protease and virulence
    • Qin, X., K. V. Singh, G. M. Weinstock, and B. E. Murray. 2000. Effects of Enterococcus faecalis fsr genes on production of gelatinase and a serine protease and virulence. Infect. Immun. 68:2579-2586.
    • (2000) Infect. Immun. , vol.68 , pp. 2579-2586
    • Qin, X.1    Singh, K.V.2    Weinstock, G.M.3    Murray, B.E.4
  • 33
    • 0035038936 scopus 로고    scopus 로고
    • Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF
    • Qin, X., K. V. Singh, G. M. Weinstock, and B. E. Murray. 2001. Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF. J. Bacteriol. 183:3372-3382.
    • (2001) J. Bacteriol. , vol.183 , pp. 3372-3382
    • Qin, X.1    Singh, K.V.2    Weinstock, G.M.3    Murray, B.E.4
  • 34
    • 0036271592 scopus 로고    scopus 로고
    • Proteolysis and its regulation at the surface of Streptococcus pyogenes
    • Rasmussen, M., and L. Bjorck. 2002. Proteolysis and its regulation at the surface of Streptococcus pyogenes. Mol. Microbiol. 43:537-544.
    • (2002) Mol. Microbiol. , vol.43 , pp. 537-544
    • Rasmussen, M.1    Bjorck, L.2
  • 35
    • 0142029151 scopus 로고    scopus 로고
    • Loss of hemolysin expression in Staphylococcus aureus agr mutants correlates with selective survival during mixed inflections in murine abscesses and wounds
    • Schwan, W. R., M. H. Langhorne, H. D. Ritchie, and C. K. Stover. 2003. Loss of hemolysin expression in Staphylococcus aureus agr mutants correlates with selective survival during mixed inflections in murine abscesses and wounds. FEMS Immunol. Med. Microbiol. 38:23-28.
    • (2003) FEMS Immunol. Med. Microbiol. , vol.38 , pp. 23-28
    • Schwan, W.R.1    Langhorne, M.H.2    Ritchie, H.D.3    Stover, C.K.4
  • 36
    • 0037071849 scopus 로고    scopus 로고
    • Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis
    • Shankar, N., A. S. Baghdayan, and M. S. Gilmore. 2002. Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis. Nature 417:746-750.
    • (2002) Nature , vol.417 , pp. 746-750
    • Shankar, N.1    Baghdayan, A.S.2    Gilmore, M.S.3
  • 37
    • 0036786499 scopus 로고    scopus 로고
    • Virulence effect of Enterococcus faecalis protease genes and the quorum-sensing locus fsr in Caenorhabditis elegans and mice
    • Sifri, C. D., E. Mylonakis, K. V. Singh, X. Qin, D. A. Garsin, B. E. Murray, F. M. Ausubel and S. B. Calderwood. 2002. Virulence effect of Enterococcus faecalis protease genes and the quorum-sensing locus fsr in Caenorhabditis elegans and mice. Infect. Immun. 70:5647-5650.
    • (2002) Infect. Immun. , vol.70 , pp. 5647-5650
    • Sifri, C.D.1    Mylonakis, E.2    Singh, K.V.3    Qin, X.4    Garsin, D.A.5    Murray, B.E.6    Ausubel, F.M.7    Calderwood, S.B.8
  • 38
    • 0031755702 scopus 로고    scopus 로고
    • Generation and testing of mutants of Enterococcus faecalis in a mouse peritonitis model
    • Singh, K. V., X. Qin, G. M. Weinstock, and B. E. Murray. 1998. Generation and testing of mutants of Enterococcus faecalis in a mouse peritonitis model. J. Infect. Dis. 178:1416-1420.
    • (1998) J. Infect. Dis. , vol.178 , pp. 1416-1420
    • Singh, K.V.1    Qin, X.2    Weinstock, G.M.3    Murray, B.E.4
  • 39
    • 0035990926 scopus 로고    scopus 로고
    • Virulence- and antibiotic resistance-associated two-component signal transduction systems of Gram-positive pathogenic bacteria as targets for antimicrobial therapy
    • Stephenson, K., and J. A. Hoch. 2002. Virulence- and antibiotic resistance-associated two-component signal transduction systems of Gram-positive pathogenic bacteria as targets for antimicrobial therapy. Pharmacol. Ther. 93:293-305.
    • (2002) Pharmacol. Ther. , vol.93 , pp. 293-305
    • Stephenson, K.1    Hoch, J.A.2
  • 42
    • 0036127014 scopus 로고    scopus 로고
    • Involvement of PhoP-PhoS homologs in Enterococcus faecalis virulence
    • Teng, F., L. Wang, K. V. Singh, B. E. Murray, and G. M. Weinstock. 2002. Involvement of PhoP-PhoS homologs in Enterococcus faecalis virulence. Infect. Immun. 70:1991-1996.
    • (2002) Infect. Immun. , vol.70 , pp. 1991-1996
    • Teng, F.1    Wang, L.2    Singh, K.V.3    Murray, B.E.4    Weinstock, G.M.5
  • 44
    • 0025334517 scopus 로고
    • A pair of mobilizable shuttle vectors conferring resistance to spectinomycin for molecular cloning in Escherichia coli and in Gram-positive bacteria
    • Trieu-Cuot, P., C. Carlier, C. Poyart-Salmeron, and P. Courvalin. 1990. A pair of mobilizable shuttle vectors conferring resistance to spectinomycin for molecular cloning in Escherichia coli and in Gram-positive bacteria. Nucleic Acids Res. 18:4296.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4296
    • Trieu-Cuot, P.1    Carlier, C.2    Poyart-Salmeron, C.3    Courvalin, P.4
  • 45
    • 0020604683 scopus 로고
    • Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5″-aminoglycoside phosphotransferase type III
    • Trieu-Cuot, P., and P. Courvalin. 1983. Nucleotide sequence of the Streptococcus faecalis plasmid gene encoding the 3′5″-aminoglycoside phosphotransferase type III. Gene 23:331-341.
    • (1983) Gene , vol.23 , pp. 331-341
    • Trieu-Cuot, P.1    Courvalin, P.2
  • 46
    • 0141501142 scopus 로고    scopus 로고
    • Quorum-sensing control of biofilm factors in Staphylococcus epidermidis
    • Vuong, C., C. Gerke, G. A. Somerville, E. R. Fischer, and M. Otto. 2003. Quorum-sensing control of biofilm factors in Staphylococcus epidermidis. J. Infect. Dis. 188:706-718.
    • (2003) J. Infect. Dis. , vol.188 , pp. 706-718
    • Vuong, C.1    Gerke, C.2    Somerville, G.A.3    Fischer, E.R.4    Otto, M.5
  • 47
    • 0033697445 scopus 로고    scopus 로고
    • Impact of the agr quorum-sensing system on adherence to polystyrene in Staphylococcus aureus
    • Vuong, C., H. L. Saenz, F. Gotz, and M. Otto. 2000. Impact of the agr quorum-sensing system on adherence to polystyrene in Staphylococcus aureus. J. Infect. Dis. 182:1688-1693.
    • (2000) J. Infect. Dis. , vol.182 , pp. 1688-1693
    • Vuong, C.1    Saenz, H.L.2    Gotz, F.3    Otto, M.4
  • 48
    • 0037946947 scopus 로고    scopus 로고
    • Role of the Enterococcus faecalis GelE protease in determination of cellular chain length, supernatant pheromone levels, and degradation of fibrin and misfolded surface proteins
    • Waters, C. M., M. H. Antiporta, B. E. Murray, and G. M. Dunny. 2003. Role of the Enterococcus faecalis GelE protease in determination of cellular chain length, supernatant pheromone levels, and degradation of fibrin and misfolded surface proteins. J. Bacteriol. 185:3613-3623.
    • (2003) J. Bacteriol. , vol.185 , pp. 3613-3623
    • Waters, C.M.1    Antiporta, M.H.2    Murray, B.E.3    Dunny, G.M.4
  • 49
    • 0036154488 scopus 로고    scopus 로고
    • Repression of the Staphylococcus aureus accessory gene regulator in serum and in vivo
    • Yarwood, J. M., J. K. McCormick, M. L. Paustian, V. Kapur, and P. M. Schlievert. 2002. Repression of the Staphylococcus aureus accessory gene regulator in serum and in vivo. J. Bacteriol. 194:1095-1101.
    • (2002) J. Bacteriol. , vol.194 , pp. 1095-1101
    • Yarwood, J.M.1    McCormick, J.K.2    Paustian, M.L.3    Kapur, V.4    Schlievert, P.M.5


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