메뉴 건너뛰기




Volumn 27, Issue 3, 2010, Pages 317-326

Sub-lethal stress effects on virulence gene expression in Enterococcus faecalis

Author keywords

Enterococcus faecalis; Gene expression; Stress response; Virulence

Indexed keywords

BACTERIAL DNA; INORGANIC SALT; VIRULENCE FACTOR;

EID: 77949266533     PISSN: 07400020     EISSN: 10959998     Source Type: Journal    
DOI: 10.1016/j.fm.2009.11.008     Document Type: Article
Times cited : (36)

References (78)
  • 1
    • 0032810422 scopus 로고    scopus 로고
    • Microbial stress response in minimal processing
    • Abee T., and Wouters J.A. Microbial stress response in minimal processing. Int. J. Food Microbiol. 50 (1999) 65-91
    • (1999) Int. J. Food Microbiol. , vol.50 , pp. 65-91
    • Abee, T.1    Wouters, J.A.2
  • 3
    • 20444493331 scopus 로고    scopus 로고
    • The interaction between bacteria and bile
    • Begley M., Gahan C.G., and Hill C. The interaction between bacteria and bile. FEMS Microbiol. Rev. 29 (2005) 625-651
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 625-651
    • Begley, M.1    Gahan, C.G.2    Hill, C.3
  • 4
    • 33646011978 scopus 로고    scopus 로고
    • Comparison of OG1RF and an isogenic fsrB deletion mutant by transcriptional analysis: the Fsr system of Enterococcus faecalis is more than the activator of gelatinase and serine protease
    • Bourgogne A., Hilsenbeck S.G., Dunny G.M., and Murray B.E. Comparison of OG1RF and an isogenic fsrB deletion mutant by transcriptional analysis: the Fsr system of Enterococcus faecalis is more than the activator of gelatinase and serine protease. J. Bacteriol. 188 (2006) 2875-2884
    • (2006) J. Bacteriol. , vol.188 , pp. 2875-2884
    • Bourgogne, A.1    Hilsenbeck, S.G.2    Dunny, G.M.3    Murray, B.E.4
  • 5
    • 13944253375 scopus 로고    scopus 로고
    • Homofermentative lactic acid bacteria of a traditional cheese, Comlek peyniri from Cappadocia region
    • Bulut C., Gunes H., Okuklu B., Harsa S., Kilic S., Coban H.S., and Yenidunya A.F. Homofermentative lactic acid bacteria of a traditional cheese, Comlek peyniri from Cappadocia region. J. Dairy Res. 72 (2005) 19-24
    • (2005) J. Dairy Res. , vol.72 , pp. 19-24
    • Bulut, C.1    Gunes, H.2    Okuklu, B.3    Harsa, S.4    Kilic, S.5    Coban, H.S.6    Yenidunya, A.F.7
  • 7
    • 1142298585 scopus 로고    scopus 로고
    • clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance
    • Chastanet A., Derre I., Nair S., and Msadek T. clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance. J. Bacteriol. 186 (2004) 1165-1174
    • (2004) J. Bacteriol. , vol.186 , pp. 1165-1174
    • Chastanet, A.1    Derre, I.2    Nair, S.3    Msadek, T.4
  • 8
    • 0141725789 scopus 로고    scopus 로고
    • The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells
    • Coburn P.S., and Gilmore M.S. The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells. Cell Microbiol. 5 (2003) 661-669
    • (2003) Cell Microbiol. , vol.5 , pp. 661-669
    • Coburn, P.S.1    Gilmore, M.S.2
  • 9
    • 11144287200 scopus 로고    scopus 로고
    • Enterococcus faecalis senses target cells and in response expresses cytolysin
    • Coburn P.S., Pillar C.M., Jett B.D., Haas W., and Gilmore M.S. Enterococcus faecalis senses target cells and in response expresses cytolysin. Science 306 (2004) 2270-2272
    • (2004) Science , vol.306 , pp. 2270-2272
    • Coburn, P.S.1    Pillar, C.M.2    Jett, B.D.3    Haas, W.4    Gilmore, M.S.5
  • 10
    • 0038216568 scopus 로고    scopus 로고
    • Cytolysin gene expression in Enterococcus faecalis is regulated in response to aerobiosis conditions
    • Day A.M., Cove J.H., and Phillips-Jones M.K. Cytolysin gene expression in Enterococcus faecalis is regulated in response to aerobiosis conditions. Mol. Genet. Genomics 269 (2003) 31-39
    • (2003) Mol. Genet. Genomics , vol.269 , pp. 31-39
    • Day, A.M.1    Cove, J.H.2    Phillips-Jones, M.K.3
  • 11
    • 0035315807 scopus 로고    scopus 로고
    • Molecular screening of Enterococcus virulence determinants and potential for genetic exchange between food and medical isolates
    • Eaton T.J., and Gasson M.J. Molecular screening of Enterococcus virulence determinants and potential for genetic exchange between food and medical isolates. Appl. Environ. Microbiol. 67 (2001) 1628-1635
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1628-1635
    • Eaton, T.J.1    Gasson, M.J.2
  • 12
    • 2542570324 scopus 로고    scopus 로고
    • Contribution of gelatinase, serine protease, and fsr to the pathogenesis of Enterococcus faecalis endophthalmitis
    • Engelbert M., Mylonakis E., Ausubel F.M., Calderwood S.B., and Gilmore M.S. Contribution of gelatinase, serine protease, and fsr to the pathogenesis of Enterococcus faecalis endophthalmitis. Infect. Immun. 72 (2004) 3628-3633
    • (2004) Infect. Immun. , vol.72 , pp. 3628-3633
    • Engelbert, M.1    Mylonakis, E.2    Ausubel, F.M.3    Calderwood, S.B.4    Gilmore, M.S.5
  • 13
    • 0029885478 scopus 로고    scopus 로고
    • Defense against lethal treatments and de novo protein synthesis induced by NaCl in Enterococcus faecalis ATCC 19433
    • Flahaut S., Benachour A., Giard J.C., Boutibonnes P., and Auffray Y. Defense against lethal treatments and de novo protein synthesis induced by NaCl in Enterococcus faecalis ATCC 19433. Arch. Microbiol. 165 (1996) 317-324
    • (1996) Arch. Microbiol. , vol.165 , pp. 317-324
    • Flahaut, S.1    Benachour, A.2    Giard, J.C.3    Boutibonnes, P.4    Auffray, Y.5
  • 14
    • 0030015503 scopus 로고    scopus 로고
    • Comparison of the bile salts and sodium dodecyl sulfate stress responses in Enterococcus faecalis
    • Flahaut S., Frere J., Boutibonnes P., and Auffray Y. Comparison of the bile salts and sodium dodecyl sulfate stress responses in Enterococcus faecalis. Appl. Environ. Microbiol. 62 (1996) 2416-2420
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2416-2420
    • Flahaut, S.1    Frere, J.2    Boutibonnes, P.3    Auffray, Y.4
  • 15
    • 0029978528 scopus 로고    scopus 로고
    • Relationship between stress response toward bile salts, acid and heat treatment in Enterococcus faecalis
    • Flahaut S., Hartke A., Giard J.C., Benachour A., Boutibonnes P., and Auffray Y. Relationship between stress response toward bile salts, acid and heat treatment in Enterococcus faecalis. FEMS Microbiol. Lett. 138 (1996) 49-54
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 49-54
    • Flahaut, S.1    Hartke, A.2    Giard, J.C.3    Benachour, A.4    Boutibonnes, P.5    Auffray, Y.6
  • 17
    • 0038236437 scopus 로고    scopus 로고
    • Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
    • Frees D., Qazi S.N., Hill P.J., and Ingmer H. Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence. Mol. Microbiol. 48 (2003) 1565-1578
    • (2003) Mol. Microbiol. , vol.48 , pp. 1565-1578
    • Frees, D.1    Qazi, S.N.2    Hill, P.J.3    Ingmer, H.4
  • 18
    • 33846942977 scopus 로고    scopus 로고
    • Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria
    • Frees D., Savijoki K., Varmanen P., and Ingmer H. Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria. Mol. Microbiol. 63 (2007) 1285-1295
    • (2007) Mol. Microbiol. , vol.63 , pp. 1285-1295
    • Frees, D.1    Savijoki, K.2    Varmanen, P.3    Ingmer, H.4
  • 19
    • 28444470162 scopus 로고    scopus 로고
    • Global virulence regulation in Staphylococcus aureus: pinpointing the roles of ClpP and ClpX in the sar/agr regulatory network
    • Frees D., Sorensen K., and Ingmer H. Global virulence regulation in Staphylococcus aureus: pinpointing the roles of ClpP and ClpX in the sar/agr regulatory network. Infect. Immun. 73 (2005) 8100-8108
    • (2005) Infect. Immun. , vol.73 , pp. 8100-8108
    • Frees, D.1    Sorensen, K.2    Ingmer, H.3
  • 20
    • 43049091873 scopus 로고    scopus 로고
    • Modeling the aminogenic potential of Enterococcus faecalis EF37 in dry fermented sausages through chemical and molecular approaches
    • Gardini F., Bover-Cid S., Tofalo R., Belletti N., Gatto V., Suzzi G., and Torriani S. Modeling the aminogenic potential of Enterococcus faecalis EF37 in dry fermented sausages through chemical and molecular approaches. Appl. Environ. Microbiol. 74 (2008) 2740-2750
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 2740-2750
    • Gardini, F.1    Bover-Cid, S.2    Tofalo, R.3    Belletti, N.4    Gatto, V.5    Suzzi, G.6    Torriani, S.7
  • 21
    • 0031039933 scopus 로고    scopus 로고
    • Glucose starvation response in Enterococcus faecalis JH2-2: survival and protein analysis
    • Giard J.C., Hartke A., Flahaut S., Boutibonnes P., and Auffray Y. Glucose starvation response in Enterococcus faecalis JH2-2: survival and protein analysis. Res. Microbiol. 148 (1997) 27-35
    • (1997) Res. Microbiol. , vol.148 , pp. 27-35
    • Giard, J.C.1    Hartke, A.2    Flahaut, S.3    Boutibonnes, P.4    Auffray, Y.5
  • 24
    • 0033905692 scopus 로고    scopus 로고
    • Inactivation of the stress- and starvation-inducible gls24 operon has a pleiotrophic effect on cell morphology, stress sensitivity, and gene expression in Enterococcus faecalis
    • Giard J.C., Rince A., Capiaux H., Auffray Y., and Hartke A. Inactivation of the stress- and starvation-inducible gls24 operon has a pleiotrophic effect on cell morphology, stress sensitivity, and gene expression in Enterococcus faecalis. J. Bacteriol. 182 (2000) 4512-4520
    • (2000) J. Bacteriol. , vol.182 , pp. 4512-4520
    • Giard, J.C.1    Rince, A.2    Capiaux, H.3    Auffray, Y.4    Hartke, A.5
  • 25
    • 0036282252 scopus 로고    scopus 로고
    • Enterococci from foods
    • Giraffa G. Enterococci from foods. FEMS Microbiol. Rev. 26 (2002) 163-171
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 163-171
    • Giraffa, G.1
  • 26
    • 0142227685 scopus 로고    scopus 로고
    • Functionality of enterococci in dairy products
    • Giraffa G. Functionality of enterococci in dairy products. Int. J. Food Microbiol. 88 (2003) 215-222
    • (2003) Int. J. Food Microbiol. , vol.88 , pp. 215-222
    • Giraffa, G.1
  • 27
    • 0037011936 scopus 로고    scopus 로고
    • Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction
    • Haas W., Shepard B.D., and Gilmore M.S. Two-component regulator of Enterococcus faecalis cytolysin responds to quorum-sensing autoinduction. Nature 415 (2002) 84-87
    • (2002) Nature , vol.415 , pp. 84-87
    • Haas, W.1    Shepard, B.D.2    Gilmore, M.S.3
  • 29
    • 0036837964 scopus 로고    scopus 로고
    • Two-component signal transduction in Enterococcus faecalis
    • Hancock L., and Perego M. Two-component signal transduction in Enterococcus faecalis. J. Bacteriol. 184 (2002) 5819-5825
    • (2002) J. Bacteriol. , vol.184 , pp. 5819-5825
    • Hancock, L.1    Perego, M.2
  • 30
    • 0031765020 scopus 로고    scopus 로고
    • Survival of Enterococcus faecalis in an oligotrophic microcosm: changes in morphology, development of general stress resistance, and analysis of protein synthesis
    • Hartke A., Giard J.C., Laplace J.M., and Auffray Y. Survival of Enterococcus faecalis in an oligotrophic microcosm: changes in morphology, development of general stress resistance, and analysis of protein synthesis. Appl. Environ. Microbiol. 64 (1998) 4238-4245
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4238-4245
    • Hartke, A.1    Giard, J.C.2    Laplace, J.M.3    Auffray, Y.4
  • 31
    • 18444392727 scopus 로고    scopus 로고
    • Quantification of enterococci and human adenoviruses in environmental samples by real-time PCR
    • He J.W., and Jiang S. Quantification of enterococci and human adenoviruses in environmental samples by real-time PCR. Appl. Environ. Microbiol. 71 (2005) 2250-2255
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2250-2255
    • He, J.W.1    Jiang, S.2
  • 32
    • 33745589526 scopus 로고    scopus 로고
    • Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection
    • Henderson B., Allan E., and Coates A.R. Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection. Infect. Immun. 74 (2006) 3693-3706
    • (2006) Infect. Immun. , vol.74 , pp. 3693-3706
    • Henderson, B.1    Allan, E.2    Coates, A.R.3
  • 33
    • 34248332179 scopus 로고    scopus 로고
    • Expression of virulence-related genes by Enterococcus faecalis in response to different environments
    • Hew C.M., Korakli M., and Vogel R.F. Expression of virulence-related genes by Enterococcus faecalis in response to different environments. Syst. Appl. Microbiol. 30 (2007) 257-267
    • (2007) Syst. Appl. Microbiol. , vol.30 , pp. 257-267
    • Hew, C.M.1    Korakli, M.2    Vogel, R.F.3
  • 34
    • 0025052712 scopus 로고
    • Non-radioactive labeling of RNA transcripts in vitro with the hapten dioxigenin (DIG); hybridization and ELISA-based detection
    • Holtken H.J., and Kessler C. Non-radioactive labeling of RNA transcripts in vitro with the hapten dioxigenin (DIG); hybridization and ELISA-based detection. Nucleic Acids Res. 18 (1990) 5843-5851
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5843-5851
    • Holtken, H.J.1    Kessler, C.2
  • 35
    • 77949273574 scopus 로고    scopus 로고
    • Hörmann, S., 2007. Hochdruckinduzierte Stressantwort bei Lactobacillus sanfranciscansis DSM 20451_1hnT. In: Fakultat Wissenschaftzentrum Weihenstephan fur Ernahrung, Landnutzung und Umwelt, Lehrstuhl fur Technische Mikrobiologie. Ph.D. Munchen: Technische Universitat Munchen.
    • Hörmann, S., 2007. Hochdruckinduzierte Stressantwort bei Lactobacillus sanfranciscansis DSM 20451_1hnT. In: Fakultat Wissenschaftzentrum Weihenstephan fur Ernahrung, Landnutzung und Umwelt, Lehrstuhl fur Technische Mikrobiologie. Vol. Ph.D. Munchen: Technische Universitat Munchen.
  • 36
    • 33645462173 scopus 로고    scopus 로고
    • Comparative proteome approach to characterize the high-pressure stress response of Lactobacillus sanfranciscensis DSM 20451(T)
    • Hörmann S., Scheyhing C., Behr J., Pavlovic M., Ehrmann M., and Vogel R.F. Comparative proteome approach to characterize the high-pressure stress response of Lactobacillus sanfranciscensis DSM 20451(T). Proteomics 6 (2006) 1878-1885
    • (2006) Proteomics , vol.6 , pp. 1878-1885
    • Hörmann, S.1    Scheyhing, C.2    Behr, J.3    Pavlovic, M.4    Ehrmann, M.5    Vogel, R.F.6
  • 37
    • 33646772886 scopus 로고    scopus 로고
    • Construction of a new reporter system to study the NaCl-dependent dnaK promoter activity of Lactobacillus sanfranciscensis
    • Hörmann S., Vogel R.F., and Ehrmann M. Construction of a new reporter system to study the NaCl-dependent dnaK promoter activity of Lactobacillus sanfranciscensis. Appl. Microbiol. Biotechnol. 70 (2005) 690-697
    • (2005) Appl. Microbiol. Biotechnol. , vol.70 , pp. 690-697
    • Hörmann, S.1    Vogel, R.F.2    Ehrmann, M.3
  • 38
    • 0031861002 scopus 로고    scopus 로고
    • Multiple-drug resistant enterococci: the nature of the problem and an agenda for the future
    • Huycke M.M., Sahm D.F., and Gilmore M.S. Multiple-drug resistant enterococci: the nature of the problem and an agenda for the future. Emerg. Infect. Dis. 4 (1998) 239-249
    • (1998) Emerg. Infect. Dis. , vol.4 , pp. 239-249
    • Huycke, M.M.1    Sahm, D.F.2    Gilmore, M.S.3
  • 39
    • 0034916351 scopus 로고    scopus 로고
    • Out of the iron age: new insights into the critical role of manganese homeostasis in bacteria
    • Jakubovics N.S., and Jenkinson H.F. Out of the iron age: new insights into the critical role of manganese homeostasis in bacteria. Microbiology 147 (2001) 1709-1718
    • (2001) Microbiology , vol.147 , pp. 1709-1718
    • Jakubovics, N.S.1    Jenkinson, H.F.2
  • 40
    • 0026753080 scopus 로고
    • Contribution of the pAD1-encoded cytolysin to the severity of experimental Enterococcus faecalis endophthalmitis
    • Jett B.D., Jensen H.G., Nordquist R.E., and Gilmore M.S. Contribution of the pAD1-encoded cytolysin to the severity of experimental Enterococcus faecalis endophthalmitis. Infect. Immun. 60 (1992) 2445-2452
    • (1992) Infect. Immun. , vol.60 , pp. 2445-2452
    • Jett, B.D.1    Jensen, H.G.2    Nordquist, R.E.3    Gilmore, M.S.4
  • 41
    • 11144333056 scopus 로고    scopus 로고
    • Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities
    • Kawalec M., Potempa J., Moon J.L., Travis J., and Murray B.E. Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities. J. Bacteriol. 187 (2005) 266-275
    • (2005) J. Bacteriol. , vol.187 , pp. 266-275
    • Kawalec, M.1    Potempa, J.2    Moon, J.L.3    Travis, J.4    Murray, B.E.5
  • 42
    • 0030895818 scopus 로고    scopus 로고
    • Induction of heat shock proteins DnaK, GroEL, and GroES by salt stress in Lactococcus lactis
    • Kilstrup M., Jacobsen S., Hammer K., and Vogensen F.K. Induction of heat shock proteins DnaK, GroEL, and GroES by salt stress in Lactococcus lactis. Appl. Environ. Microbiol. 63 (1997) 1826-1837
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1826-1837
    • Kilstrup, M.1    Jacobsen, S.2    Hammer, K.3    Vogensen, F.K.4
  • 43
    • 0035865140 scopus 로고    scopus 로고
    • Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor
    • Kruger E., Zuhlke D., Witt E., Ludwig H., and Hecker M. Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor. Embo J. 20 (2001) 852-863
    • (2001) Embo J. , vol.20 , pp. 852-863
    • Kruger, E.1    Zuhlke, D.2    Witt, E.3    Ludwig, H.4    Hecker, M.5
  • 47
    • 0037322048 scopus 로고    scopus 로고
    • Manganese-dependent regulation of the endocarditis-associated virulence factor EfaA of Enterococcus faecalis
    • Low Y.L., Jakubovics N.S., Flatman J.C., Jenkinson H.F., and Smith A.W. Manganese-dependent regulation of the endocarditis-associated virulence factor EfaA of Enterococcus faecalis. J. Med. Microbiol. 52 (2003) 113-119
    • (2003) J. Med. Microbiol. , vol.52 , pp. 113-119
    • Low, Y.L.1    Jakubovics, N.S.2    Flatman, J.C.3    Jenkinson, H.F.4    Smith, A.W.5
  • 48
    • 0028963390 scopus 로고
    • Cloning of an Enterococcus faecalis endocarditis antigen: homology with adhesins from some oral streptococci
    • Lowe A.M., Lambert P.A., and Smith A.W. Cloning of an Enterococcus faecalis endocarditis antigen: homology with adhesins from some oral streptococci. Infect. Immun. 63 (1995) 703-706
    • (1995) Infect. Immun. , vol.63 , pp. 703-706
    • Lowe, A.M.1    Lambert, P.A.2    Smith, A.W.3
  • 49
    • 33745434063 scopus 로고    scopus 로고
    • Involvement of Bacillus subtilis ClpE in CtsR degradation and protein quality control
    • Miethke M., Hecker M., and Gerth U. Involvement of Bacillus subtilis ClpE in CtsR degradation and protein quality control. J. Bacteriol. 188 (2006) 4610-4619
    • (2006) J. Bacteriol. , vol.188 , pp. 4610-4619
    • Miethke, M.1    Hecker, M.2    Gerth, U.3
  • 50
    • 2542610000 scopus 로고    scopus 로고
    • Influence of origin of isolates, especially endocarditis isolates, and various genes on biofilm formation by Enterococcus faecalis
    • Mohamed J.A., Huang W., Nallapareddy S.R., Teng F., and Murray B.E. Influence of origin of isolates, especially endocarditis isolates, and various genes on biofilm formation by Enterococcus faecalis. Infect. Immun. 72 (2004) 3658-3663
    • (2004) Infect. Immun. , vol.72 , pp. 3658-3663
    • Mohamed, J.A.1    Huang, W.2    Nallapareddy, S.R.3    Teng, F.4    Murray, B.E.5
  • 51
    • 0025100795 scopus 로고
    • The life and times of the Enterococcus
    • Murray B.E. The life and times of the Enterococcus. Clin. Microbiol. Rev. 3 (1990) 46-65
    • (1990) Clin. Microbiol. Rev. , vol.3 , pp. 46-65
    • Murray, B.E.1
  • 52
    • 0027328958 scopus 로고
    • Generation of restriction map of Enterococcus faecalis OG1 and investigation of growth requirements and regions encoding biosynthetic function
    • Murray B.E., Singh K.V., Ross R.P., Heath J.D., Dunny G.M., and Weinstock G.M. Generation of restriction map of Enterococcus faecalis OG1 and investigation of growth requirements and regions encoding biosynthetic function. J. Bacteriol. 175 (1993) 5216-5223
    • (1993) J. Bacteriol. , vol.175 , pp. 5216-5223
    • Murray, B.E.1    Singh, K.V.2    Ross, R.P.3    Heath, J.D.4    Dunny, G.M.5    Weinstock, G.M.6
  • 54
    • 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., Engelbert M., Qin X., Sifri C.D., Murray B.E., Ausubel F.M., Gilmore M.S., and Calderwood S.B. 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 (2002) 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
  • 55
    • 0034946367 scopus 로고    scopus 로고
    • Gelatinase biosynthesis-activating pheromone: a peptide lactone that mediates a quorum sensing in Enterococcus faecalis
    • Nakayama J., Cao Y., Horii T., Sakuda S., Akkermans A.D., de Vos W.M., and Nagasawa H. Gelatinase biosynthesis-activating pheromone: a peptide lactone that mediates a quorum sensing in Enterococcus faecalis. Mol. Microbiol. 41 (2001) 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.5    de Vos, W.M.6    Nagasawa, H.7
  • 56
    • 33748090607 scopus 로고    scopus 로고
    • Ligand-signaled upregulation of Enterococcus faecalis ace transcription, a mechanism for modulating host-E. faecalis interaction
    • Nallapareddy S.R., and Murray B.E. Ligand-signaled upregulation of Enterococcus faecalis ace transcription, a mechanism for modulating host-E. faecalis interaction. Infect. Immun. 74 (2006) 4982-4989
    • (2006) Infect. Immun. , vol.74 , pp. 4982-4989
    • Nallapareddy, S.R.1    Murray, B.E.2
  • 57
    • 0033862771 scopus 로고    scopus 로고
    • Diversity of ace, a gene encoding a microbial surface component recognizing adhesive matrix molecules, from different strains of Enterococcus faecalis and evidence for production of ace during human infections
    • Nallapareddy S.R., Singh K.V., Duh R.W., Weinstock G.M., and Murray B.E. Diversity of ace, a gene encoding a microbial surface component recognizing adhesive matrix molecules, from different strains of Enterococcus faecalis and evidence for production of ace during human infections. Infect. Immun. 68 (2000) 5210-5217
    • (2000) Infect. Immun. , vol.68 , pp. 5210-5217
    • Nallapareddy, S.R.1    Singh, K.V.2    Duh, R.W.3    Weinstock, G.M.4    Murray, B.E.5
  • 58
    • 27744505626 scopus 로고    scopus 로고
    • Decreased virulence of a gls24 mutant of Enterococcus faecalis OG1RF in an experimental endocarditis model
    • Nannini E.C., Teng F., Singh K.V., and Murray B.E. Decreased virulence of a gls24 mutant of Enterococcus faecalis OG1RF in an experimental endocarditis model. Infect. Immun. 73 (2005) 7772-7774
    • (2005) Infect. Immun. , vol.73 , pp. 7772-7774
    • Nannini, E.C.1    Teng, F.2    Singh, K.V.3    Murray, B.E.4
  • 59
    • 34147124896 scopus 로고    scopus 로고
    • Extracellular gelatinase of Enterococcus faecalis destroys a defense system in insect hemolymph and human serum
    • Park S.Y., Kim K.M., Lee J.H., Seo S.J., and Lee I.H. Extracellular gelatinase of Enterococcus faecalis destroys a defense system in insect hemolymph and human serum. Infect. Immun. 75 (2007) 1861-1869
    • (2007) Infect. Immun. , vol.75 , pp. 1861-1869
    • Park, S.Y.1    Kim, K.M.2    Lee, J.H.3    Seo, S.J.4    Lee, I.H.5
  • 60
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29 (2001) e45
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 61
    • 0034061486 scopus 로고    scopus 로고
    • Effects of Enterococcus faecalis fsr genes on production of gelatinase and a serine protease and virulence
    • Qin X., Singh K.V., Weinstock G.M., and Murray B.E. Effects of Enterococcus faecalis fsr genes on production of gelatinase and a serine protease and virulence. Infect. Immun. 68 (2000) 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
  • 62
    • 0035038936 scopus 로고    scopus 로고
    • Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF
    • Qin X., Singh K.V., Weinstock G.M., and Murray B.E. Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OG1RF. J. Bacteriol. 183 (2001) 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
  • 64
    • 0034630096 scopus 로고    scopus 로고
    • Identification of general stress genes in Enterococcus faecalis
    • Rince A., Flahaut S., and Auffray Y. Identification of general stress genes in Enterococcus faecalis. Int. J. Food Microbiol. 55 (2000) 87-91
    • (2000) Int. J. Food Microbiol. , vol.55 , pp. 87-91
    • Rince, A.1    Flahaut, S.2    Auffray, Y.3
  • 65
    • 33646851752 scopus 로고    scopus 로고
    • Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens
    • Rowley G., Spector M., Kormanec J., and Roberts M. Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens. Nat. Rev. Microbiol. 4 (2006) 383-394
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 383-394
    • Rowley, G.1    Spector, M.2    Kormanec, J.3    Roberts, M.4
  • 67
    • 4444382849 scopus 로고    scopus 로고
    • Barotolerance is inducible by preincubation under hydrostatic pressure, cold-, osmotic- and acid-stress conditions in Lactobacillus sanfranciscensis DSM 20451T
    • Scheyhing C.H., Hörmann S., Ehrmann M.A., and Vogel R.F. Barotolerance is inducible by preincubation under hydrostatic pressure, cold-, osmotic- and acid-stress conditions in Lactobacillus sanfranciscensis DSM 20451T. Lett. Appl. Microbiol. 39 (2004) 284-289
    • (2004) Lett. Appl. Microbiol. , vol.39 , pp. 284-289
    • Scheyhing, C.H.1    Hörmann, S.2    Ehrmann, M.A.3    Vogel, R.F.4
  • 68
    • 34447511572 scopus 로고    scopus 로고
    • Enterococcus populations in Pecorino Abruzzese cheese: biodiversity and safety aspects
    • Serio A., Paparella A., Chaves-Lopez C., Corsetti A., and Suzzi G. Enterococcus populations in Pecorino Abruzzese cheese: biodiversity and safety aspects. J. Food Prot. 70 (2007) 1561-1568
    • (2007) J. Food Prot. , vol.70 , pp. 1561-1568
    • Serio, A.1    Paparella, A.2    Chaves-Lopez, C.3    Corsetti, A.4    Suzzi, G.5
  • 69
    • 0036073828 scopus 로고    scopus 로고
    • Differential expression of virulence-related genes in Enterococcus faecalis in response to biological cues in serum and urine
    • Shepard B.D., and Gilmore M.S. Differential expression of virulence-related genes in Enterococcus faecalis in response to biological cues in serum and urine. Infect. Immun. 70 (2002) 4344-4352
    • (2002) Infect. Immun. , vol.70 , pp. 4344-4352
    • Shepard, B.D.1    Gilmore, M.S.2
  • 70
    • 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., Mylonakis E., Singh K.V., Qin X., Garsin D.A., Murray B.E., Ausubel F.M., and Calderwood S.B. Virulence effect of Enterococcus faecalis protease genes and the quorum-sensing locus fsr in Caenorhabditis elegans and mice. Infect. Immun. 70 (2002) 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
  • 71
    • 0031697165 scopus 로고    scopus 로고
    • In vivo testing of an Enterococcus faecalis efaA mutant and use of efaA homologs for species identification
    • Singh K.V., Coque T.M., Weinstock G.M., and Murray B.E. In vivo testing of an Enterococcus faecalis efaA mutant and use of efaA homologs for species identification. FEMS Immunol. Med. Microbiol. 21 (1998) 323-331
    • (1998) FEMS Immunol. Med. Microbiol. , vol.21 , pp. 323-331
    • Singh, K.V.1    Coque, T.M.2    Weinstock, G.M.3    Murray, B.E.4
  • 72
    • 34648816579 scopus 로고    scopus 로고
    • Transcriptional responses of Enterococcus faecalis V583 to bovine bile and sodium dodecyl sulfate
    • Solheim M., Aakra A., Vebo H., Snipen L., and Nes I.F. Transcriptional responses of Enterococcus faecalis V583 to bovine bile and sodium dodecyl sulfate. Appl. Environ. Microbiol. 73 (2007) 5767-5774
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5767-5774
    • Solheim, M.1    Aakra, A.2    Vebo, H.3    Snipen, L.4    Nes, I.F.5
  • 74
    • 12344323538 scopus 로고    scopus 로고
    • Importance of gls24 in virulence and stress response of Enterococcus faecalis and use of the Gls24 protein as a possible immunotherapy target
    • Teng F., Nannini E.C., and Murray B.E. Importance of gls24 in virulence and stress response of Enterococcus faecalis and use of the Gls24 protein as a possible immunotherapy target. J. Infect. Dis. 191 (2005) 472-480
    • (2005) J. Infect. Dis. , vol.191 , pp. 472-480
    • Teng, F.1    Nannini, E.C.2    Murray, B.E.3
  • 75
    • 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., Antiporta M.H., Murray B.E., and Dunny G.M. 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 (2003) 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
  • 76
    • 0344193588 scopus 로고    scopus 로고
    • Conditional adherence of Enterococcus faecalis to extracellular matrix proteins
    • Xiao J., Hook M., Weinstock G.M., and Murray B.E. Conditional adherence of Enterococcus faecalis to extracellular matrix proteins. FEMS Immunol. Med. Microbiol. 21 (1998) 287-295
    • (1998) FEMS Immunol. Med. Microbiol. , vol.21 , pp. 287-295
    • Xiao, J.1    Hook, M.2    Weinstock, G.M.3    Murray, B.E.4
  • 77
    • 2942529092 scopus 로고    scopus 로고
    • Virulence potential of the staphylococcal adhesin CNA in experimental arthritis is determined by its affinity for collagen
    • Xu Y., Rivas J.M., Brown E.L., Liang X., and Hook M. Virulence potential of the staphylococcal adhesin CNA in experimental arthritis is determined by its affinity for collagen. J. Infect. Dis. 189 (2004) 2323-2333
    • (2004) J. Infect. Dis. , vol.189 , pp. 2323-2333
    • Xu, Y.1    Rivas, J.M.2    Brown, E.L.3    Liang, X.4    Hook, M.5
  • 78
    • 15544385757 scopus 로고    scopus 로고
    • Gelatinase is important for translocation of Enterococcus faecalis across polarized human enterocyte-like T84 cells
    • Zeng J., Teng F., and Murray B.E. Gelatinase is important for translocation of Enterococcus faecalis across polarized human enterocyte-like T84 cells. Infect. Immun. 73 (2005) 1606-1612
    • (2005) Infect. Immun. , vol.73 , pp. 1606-1612
    • Zeng, J.1    Teng, F.2    Murray, B.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.