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Volumn 190, Issue 16, 2008, Pages 5690-5698

Regulation of autolysis-dependent extracellular DNA release by Enterococcus faecalis extracellular proteases influences biofilm development

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL ENZYME; DEOXYRIBONUCLEASE; GELATINASE; SERINE PROTEINASE;

EID: 49449108621     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00314-08     Document Type: Article
Times cited : (252)

References (59)
  • 1
    • 0034090109 scopus 로고    scopus 로고
    • Quantitative detection of Streptococcus pneumoniae cells harbouring single or multiple copies of the gene encoding the green fluorescent protein
    • Acebo, P., C. Nieto, M. A. Corrales, M. Espinosa, and P. Lopez. 2000. Quantitative detection of Streptococcus pneumoniae cells harbouring single or multiple copies of the gene encoding the green fluorescent protein. Microbiology 146(Pt. 6): 1267-1273.
    • (2000) Microbiology , vol.146 , Issue.PART. 6 , pp. 1267-1273
    • Acebo, P.1    Nieto, C.2    Corrales, M.A.3    Espinosa, M.4    Lopez, P.5
  • 3
    • 36048961413 scopus 로고    scopus 로고
    • Strong biofilm production, antibiotic multi-resistance, and high gelE expression in epidemic clones of Enterococcus faecalis from orthopaedic implant infections
    • Arciola, C. R., L. Baldassarri, D. Campoccia, R. Creti, V. Pirini, J. Huebner, and L. Montanaro. 2008. Strong biofilm production, antibiotic multi-resistance, and high gelE expression in epidemic clones of Enterococcus faecalis from orthopaedic implant infections. Biomaterials 29:580-586.
    • (2008) Biomaterials , vol.29 , pp. 580-586
    • Arciola, C.R.1    Baldassarri, L.2    Campoccia, D.3    Creti, R.4    Pirini, V.5    Huebner, J.6    Montanaro, L.7
  • 4
    • 34548008613 scopus 로고    scopus 로고
    • The biological role of death and lysis in biofilm development
    • Bayles, K. W. 2007. The biological role of death and lysis in biofilm development. Nat. Rev. Microbiol. 5:721-726.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 721-726
    • Bayles, K.W.1
  • 5
    • 3342953960 scopus 로고    scopus 로고
    • Bacterial linguistic communication and social intelligence
    • Ben Jacob, E., I. Becker, Y. Shapira, and H. Levine. 2004. Bacterial linguistic communication and social intelligence. Trends Microbiol. 12:366-372.
    • (2004) Trends Microbiol , vol.12 , pp. 366-372
    • Ben Jacob, E.1    Becker, I.2    Shapira, Y.3    Levine, H.4
  • 6
    • 10044237879 scopus 로고    scopus 로고
    • Signal transduction, quorum-sensing, and extracellular protease activity in Enterococcus faecalis biofilm formation
    • Carniol, K., and M. S. Gilmore. 2004. Signal transduction, quorum-sensing, and extracellular protease activity in Enterococcus faecalis biofilm formation. J. Bacteriol. 186:8161-8163.
    • (2004) J. Bacteriol , vol.186 , pp. 8161-8163
    • Carniol, K.1    Gilmore, M.S.2
  • 8
    • 33847129667 scopus 로고    scopus 로고
    • Cannibalism and fratricide: Mechanisms and raisons d'etre
    • Claverys, J. P., and L. S. Havarstein. 2007. Cannibalism and fratricide: mechanisms and raisons d'etre. Nat. Rev. Microbiol. 5:219-229.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 219-229
    • Claverys, J.P.1    Havarstein, L.S.2
  • 9
    • 0033591467 scopus 로고    scopus 로고
    • Costerton, J. W., P. S. Stewart, and E. P. Greenberg. 1999. Bacterial biofilms: a common cause of persistent infections. Science 284:1318-1322.
    • Costerton, J. W., P. S. Stewart, and E. P. Greenberg. 1999. Bacterial biofilms: a common cause of persistent infections. Science 284:1318-1322.
  • 10
    • 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
  • 11
    • 37449023598 scopus 로고    scopus 로고
    • Full activation of Enterococcus faecalis gelatinase by a C-terminal proteolytic cleavage
    • Del Papa, M. F., L. E. Hancock, V. C. Thomas, and M. Perego. 2007. Full activation of Enterococcus faecalis gelatinase by a C-terminal proteolytic cleavage. J. Bacteriol. 189:8835-8843.
    • (2007) J. Bacteriol , vol.189 , pp. 8835-8843
    • Del Papa, M.F.1    Hancock, L.E.2    Thomas, V.C.3    Perego, M.4
  • 12
    • 0036228505 scopus 로고    scopus 로고
    • Biofilms: Survival mechanisms of clinically relevant microorganisms
    • Donlan, R. M., and J. W. Costerton. 2002. Biofilms: survival mechanisms of clinically relevant microorganisms. Clin. Microbiol. Rev. 15:167-193.
    • (2002) Clin. Microbiol. Rev , vol.15 , pp. 167-193
    • Donlan, R.M.1    Costerton, J.W.2
  • 13
    • 32044465724 scopus 로고    scopus 로고
    • A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin
    • Ellermeier, C. D., E. C. Hobbs, J. E. Gonzalez-Pastor, and R. Losick. 2006. A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin. Cell 124:549-559.
    • (2006) Cell , vol.124 , pp. 549-559
    • Ellermeier, C.D.1    Hobbs, E.C.2    Gonzalez-Pastor, J.E.3    Losick, R.4
  • 14
    • 2542570324 scopus 로고    scopus 로고
    • Contribution of gelatinase, serine protease, and fsr to the pathogenesis of Enterococcus faecalis endophthalmitis
    • Engelbert, M., E. Mylonakis, F. M. Ausubel, S. B. Calderwood, and M. S. Gilmore. 2004. Contribution of gelatinase, serine protease, and fsr to the pathogenesis of Enterococcus faecalis endophthalmitis. Infect. Immun. 72: 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
  • 16
    • 20844444784 scopus 로고    scopus 로고
    • The selective advantage of microbial fratricide
    • Gilmore, M. S., and W. Haas. 2005. The selective advantage of microbial fratricide. Proc. Natl. Acad. Sci. USA 102:8401-8402.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8401-8402
    • Gilmore, M.S.1    Haas, W.2
  • 17
  • 18
    • 20844444771 scopus 로고    scopus 로고
    • Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: Genetic requirements
    • Guiral, S., T. J. Mitchell, B. Martin, and J. P. Claverys. 2005. Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirements. Proc. Natl. Acad. Sci. USA 102:8710-8715.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8710-8715
    • Guiral, S.1    Mitchell, T.J.2    Martin, B.3    Claverys, J.P.4
  • 19
    • 1842612577 scopus 로고    scopus 로고
    • Bacterial biofilms: From the natural environment to infectious diseases
    • Hall-Stoodley, L., J. W. Costerton, and P. Stoodley. 2004. Bacterial biofilms: from the natural environment to infectious diseases. Nat. Rev. Microbiol. 2:95-108.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 95-108
    • Hall-Stoodley, L.1    Costerton, J.W.2    Stoodley, P.3
  • 20
    • 4344682069 scopus 로고    scopus 로고
    • The Enterococcus faecalis fsr two-component system controls biofilm development through production of gelatinase
    • Hancock, L. E., and M. Perego. 2004. The Enterococcus faecalis fsr two-component system controls biofilm development through production of gelatinase. J. Bacteriol. 186:5629-5639.
    • (2004) J. Bacteriol , vol.186 , pp. 5629-5639
    • Hancock, L.E.1    Perego, M.2
  • 22
    • 0031861002 scopus 로고    scopus 로고
    • Multiple-drug resistant enterococci: The nature of the problem and an agenda for the future
    • Huycke, M. M., D. F. Sahm, and M. S. Gilmore. 1998. Multiple-drug resistant enterococci: the nature of the problem and an agenda for the future. Emerg. Infect. Dis. 4:239-249.
    • (1998) Emerg. Infect. Dis , vol.4 , pp. 239-249
    • Huycke, M.M.1    Sahm, D.F.2    Gilmore, M.S.3
  • 23
    • 3142574629 scopus 로고    scopus 로고
    • What drives bacteria to produce a biofilm?
    • Jefferson, K. K. 2004. What drives bacteria to produce a biofilm? FEMS Microbiol. Lett. 236:163-173.
    • (2004) FEMS Microbiol. Lett , vol.236 , pp. 163-173
    • Jefferson, K.K.1
  • 24
    • 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., J. Potempa, J. L. Moon, J. Travis, and B. E. Murray. 2005. 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: 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
  • 25
    • 33846993832 scopus 로고    scopus 로고
    • Development of a host-genotype-independent counterselectable marker and a high-frequency conjugative delivery system and their use in genetic analysis of Enterococcus faecalis
    • Kristich, C. J., J. R. Chandler, and G. M. Dunny. 2007. Development of a host-genotype-independent counterselectable marker and a high-frequency conjugative delivery system and their use in genetic analysis of Enterococcus faecalis. Plasmid 57:131-144.
    • (2007) Plasmid , vol.57 , pp. 131-144
    • Kristich, C.J.1    Chandler, J.R.2    Dunny, G.M.3
  • 26
    • 0026801262 scopus 로고
    • New thermosensitive plasmid for gram-positive bacteria
    • Maguin, E., P. Duwat, T. Hege, D. Ehrlich, and A. Grass. 1992. New thermosensitive plasmid for gram-positive bacteria. J. Bacteriol. 174:5633-5638.
    • (1992) J. Bacteriol , vol.174 , pp. 5633-5638
    • Maguin, E.1    Duwat, P.2    Hege, T.3    Ehrlich, D.4    Grass, A.5
  • 27
    • 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
  • 28
    • 0028211864 scopus 로고
    • The Enterococcus faecalis extra-cellular metalloendopeptidase (EC 3.4.24.30; coccolysin) inactivates human endothelin at bonds involving hydrophobic amino acid residues
    • Makinen, P. L., and K. K. Makinen. 1994. The Enterococcus faecalis extra-cellular 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.L.1    Makinen, K.K.2
  • 29
    • 37249055056 scopus 로고    scopus 로고
    • Biofilm formation by enterococci
    • ohamed, J. A., and D. B. Huang. 2007. Biofilm formation by enterococci. J. Med. Microbiol. 56:1581-1588.
    • (2007) J. Med. Microbiol , vol.56 , pp. 1581-1588
    • ohamed, J.A.1    Huang, D.B.2
  • 30
    • 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., W. Huang, S. R. Nallapareddy, F. Teng, and B. E. Murray. 2004. Influence of origin of isolates, especially endocarditis isolates, and various genes on biofilm formation by Enterococcus faecalis. Infect. Immun. 72:3658-3663.
    • (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
  • 31
    • 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. Akkermans, W. M. 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.5    de Vos, W.M.6    Nagasawa, H.7
  • 32
    • 33751560989 scopus 로고    scopus 로고
    • Revised model for Enterococcus faecalis fsr quorum-sensing system: The small open reading frame fsrD encodes the gelatinase biosynthesis-activating pheromone propeptide corresponding to staphylococcal agrD
    • Nakayama, J., S. Chen, N. Oyama, K. Nishiguchi, E. A. Azab, E. Tanaka, R. Kariyama, and K. Sonomoto. 2006. Revised model for Enterococcus faecalis fsr quorum-sensing system: the small open reading frame fsrD encodes the gelatinase biosynthesis-activating pheromone propeptide corresponding to staphylococcal agrD. J. Bacteriol. 188:8321-8326.
    • (2006) J. Bacteriol , vol.188 , pp. 8321-8326
    • Nakayama, J.1    Chen, S.2    Oyama, N.3    Nishiguchi, K.4    Azab, E.A.5    Tanaka, E.6    Kariyama, R.7    Sonomoto, K.8
  • 33
    • 0036275617 scopus 로고    scopus 로고
    • Description of a 23.9-kilobase chromosomal deletion containing a region encoding/sr genes which mainly determines the gelatinase-negative phenotype of clinical isolates of Enterococcus faecalis in urine
    • Nakayama, J., R. Kariyama, and H. Kumon. 2002. Description of a 23.9-kilobase chromosomal deletion containing a region encoding/sr genes which mainly determines the gelatinase-negative phenotype of clinical isolates of Enterococcus faecalis in urine. Appl. Environ. Microbiol. 68:3152-3155.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 3152-3155
    • Nakayama, J.1    Kariyama, R.2    Kumon, H.3
  • 35
    • 0037725380 scopus 로고    scopus 로고
    • Construction of the mobilizable plasmid pMV158GFP, a derivative of pMV158 that carries the gene encoding the green fluorescent protein
    • Nieto, C., and M. Espinosa. 2003. Construction of the mobilizable plasmid pMV158GFP, a derivative of pMV158 that carries the gene encoding the green fluorescent protein. Plasmid 49:281-285.
    • (2003) Plasmid , vol.49 , pp. 281-285
    • Nieto, C.1    Espinosa, M.2
  • 36
    • 34147124896 scopus 로고    scopus 로고
    • Extracellular gelatinase of Enterococcus faecalis destroys a defense system in insect hemolymph and human serum
    • Park, S. Y., K. M. Kim, J. H. Lee, S. J. Seo, and I. H. Lee. 2007. Extracellular gelatinase of Enterococcus faecalis destroys a defense system in insect hemolymph and human serum. Infect. Immun. 75:1861-1869.
    • (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
  • 38
    • 0029320145 scopus 로고
    • A versatile quick-prep of genomic DNA from gram-positive bacteria
    • Pospiech, A., and B. Neumann. 1995. A versatile quick-prep of genomic DNA from gram-positive bacteria. Trends Genet. 11:217-218.
    • (1995) Trends Genet , vol.11 , pp. 217-218
    • Pospiech, A.1    Neumann, B.2
  • 39
    • 0035038936 scopus 로고    scopus 로고
    • Characterization of fsr, a regulator controlling expression of gelatinase and serine protease in Enterococcus faecalis OGlRF
    • 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 OGlRF. 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
  • 40
    • 0034061486 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 41
    • 34447517612 scopus 로고    scopus 로고
    • Role of autolysin-mediated DNA release in biofilm formation of Staphylococcus epidermidis
    • Qin, Z., Y. Ou, L. Yang, Y. Zhu, T. Tolker-Nielsen, S. Molin, and D. Qu. 2007. Role of autolysin-mediated DNA release in biofilm formation of Staphylococcus epidermidis. Microbiology 153:2083-2092.
    • (2007) Microbiology , vol.153 , pp. 2083-2092
    • Qin, Z.1    Ou, Y.2    Yang, L.3    Zhu, Y.4    Tolker-Nielsen, T.5    Molin, S.6    Qu, D.7
  • 42
    • 0035167096 scopus 로고    scopus 로고
    • Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease
    • Rice, K., R. Peralta, D. Bast, J. de Azavedo, and M. J. McGavin. 2001. Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease. Infect. Immun. 69:159-169.
    • (2001) Infect. Immun , vol.69 , pp. 159-169
    • Rice, K.1    Peralta, R.2    Bast, D.3    de Azavedo, J.4    McGavin, M.J.5
  • 43
  • 44
    • 0019503042 scopus 로고
    • Adherence of Acinetobacter calcoaceticus RAG-1 to human epithelial cells and to hexadecane
    • Rosenberg, M., A. Perry, E. A. Bayer, D. L. Gutnick, E. Rosenberg, and I. Ofek. 1981. Adherence of Acinetobacter calcoaceticus RAG-1 to human epithelial cells and to hexadecane. Infect. Immun. 33:29-33.
    • (1981) Infect. Immun , vol.33 , pp. 29-33
    • Rosenberg, M.1    Perry, A.2    Bayer, E.A.3    Gutnick, D.L.4    Rosenberg, E.5    Ofek, I.6
  • 45
    • 33645129089 scopus 로고    scopus 로고
    • Sandoe, J. A., J. Wysome, A. P. West, J. Heritage, and M. H. Wilcox. 20C 6. Measurement of ampicillin, vancomycin, linezolid, and gentamicin activity against enterococcal biofilms. J. Antimicrob. Chemother. 57:767-770.
    • Sandoe, J. A., J. Wysome, A. P. West, J. Heritage, and M. H. Wilcox. 20C 6. Measurement of ampicillin, vancomycin, linezolid, and gentamicin activity against enterococcal biofilms. J. Antimicrob. Chemother. 57:767-770.
  • 46
    • 0036030617 scopus 로고    scopus 로고
    • Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37
    • Schmidtchen, A., I. M. Frick, E. Andersson, H. Tapper, and L. Bjorck. 2002. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol. Microbiol. 46:157-168.
    • (2002) Mol. Microbiol , vol.46 , pp. 157-168
    • Schmidtchen, A.1    Frick, I.M.2    Andersson, E.3    Tapper, H.4    Bjorck, L.5
  • 47
    • 0035131955 scopus 로고    scopus 로고
    • Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin
    • Schmidtchen, A., I. M. Frick, and L. Bjorck. 2001. Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin. Mol. Microbiol. 39:708-713.
    • (2001) Mol. Microbiol , vol.39 , pp. 708-713
    • Schmidtchen, A.1    Frick, I.M.2    Bjorck, L.3
  • 48
    • 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
  • 49
    • 0014532013 scopus 로고
    • Autolytic enzyme system of Streptococcus faecalis. V. Nature of the autolysin-cell wall complex and its relationship to properties of the autolytic enzyme of Streptococcus faecalis
    • Shockman, G. D., and M. C. Cheney. 1969. Autolytic enzyme system of Streptococcus faecalis. V. Nature of the autolysin-cell wall complex and its relationship to properties of the autolytic enzyme of Streptococcus faecalis. J. Bacteriol. 98:1199-1207.
    • (1969) J. Bacteriol , vol.98 , pp. 1199-1207
    • Shockman, G.D.1    Cheney, M.C.2
  • 50
    • 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
  • 51
    • 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
  • 52
    • 4644372071 scopus 로고    scopus 로고
    • Enterococcal surface protein, Esp, enhances biofilm formation by Enterococcus faecalis
    • Tendolkar, P. M., A. S. Baghdayan, M. S. Gilmore, and N. Shankar. 2004. Enterococcal surface protein, Esp, enhances biofilm formation by Enterococcus faecalis. Infect. Immun. 72:6032-6039.
    • (2004) Infect. Immun , vol.72 , pp. 6032-6039
    • Tendolkar, P.M.1    Baghdayan, A.S.2    Gilmore, M.S.3    Shankar, N.4
  • 53
    • 33644865217 scopus 로고    scopus 로고
    • Putative surface proteins encoded within a novel transferable locus confer a high-biofilm phenotype to Enterococcus faecalis
    • Tendolkar, P. M., A. S. Baghdayan, and N. Shankar. 2006. Putative surface proteins encoded within a novel transferable locus confer a high-biofilm phenotype to Enterococcus faecalis. J. Bacteriol. 18:2063-2072.
    • (2006) J. Bacteriol , vol.18 , pp. 2063-2072
    • Tendolkar, P.M.1    Baghdayan, A.S.2    Shankar, N.3
  • 55
    • 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
  • 56
    • 0037946947 scopus 로고    scopus 로고
    • Role of the Enterococcus faecalis GeIE protease in determination of cellular chain length, supernatant pheromone levels, and degradation of fibrin and mis-folded surface proteins
    • Waters, C. M., M. H. Antiporta, B. E. Murray, and G. M. Dunny. 2003. Role of the Enterococcus faecalis GeIE protease in determination of cellular chain length, supernatant pheromone levels, and degradation of fibrin and mis-folded 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
  • 57
    • 27944442272 scopus 로고    scopus 로고
    • Quorum sensing: Cell-to-cell communication in bacteria
    • Waters, C. M., and B. L. Bassler. 2005. Quorum sensing: cell-to-cell communication in bacteria. Annu. Rev. Cell Dev. Biol. 21:319-346.
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 319-346
    • Waters, C.M.1    Bassler, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.