메뉴 건너뛰기




Volumn 159, Issue PART 10, 2013, Pages 2153-2161

Cold-shock RNA-binding protein CspR is also exposed to the surface of Enterococcus faecalis

Author keywords

[No Author keywords available]

Indexed keywords

COLD SHOCK PROTEIN; CSPR PROTEIN; IMMUNOGLOBULIN G; POLYPEPTIDE; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84884747785     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.071076-0     Document Type: Article
Times cited : (9)

References (54)
  • 2
    • 77949517375 scopus 로고    scopus 로고
    • A proteomic view of an important human pathogen-towards the quantification of the entire Staphylococcus aureus proteome
    • other authors
    • Becher, D., Hempel, K., Sievers, S., Zühlke, D., Pané-Farré, J., Otto, A., Fuchs, S., Albrecht, D., Bernhardt, J. & other authors (2009). A proteomic view of an important human pathogen-towards the quantification of the entire Staphylococcus aureus proteome. PLoS ONE 4, e8176.
    • (2009) PLoS ONE , vol.4
    • Becher, D.1    Hempel, K.2    Sievers, S.3    Zühlke, D.4    Pané-Farré, J.5    Otto, A.6    Fuchs, S.7    Albrecht, D.8    Bernhardt, J.9
  • 7
    • 34247109118 scopus 로고    scopus 로고
    • Hfq structure, function and ligand binding
    • Brennan, R. G. & Link, T. M. (2007). Hfq structure, function and ligand binding. Curr Opin Microbiol 10, 125-133.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 125-133
    • Brennan, R.G.1    Link, T.M.2
  • 8
    • 75249100904 scopus 로고    scopus 로고
    • The role of Hfq in bacterial pathogens
    • Chao, Y. & Vogel, J. (2010). The role of Hfq in bacterial pathogens. Curr Opin Microbiol 13, 24-33.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 24-33
    • Chao, Y.1    Vogel, J.2
  • 9
    • 2442645227 scopus 로고    scopus 로고
    • The RNA-binding protein Hfq of Listeria monocytogenes: Role in stress tolerance and virulence
    • Christiansen, J. K., Larsen, M. H., Ingmer, H., Søgaard-Andersen, L. & Kallipolitis, B. H. (2004). The RNA-binding protein Hfq of Listeria monocytogenes: role in stress tolerance and virulence. J Bacteriol 186, 3355-3362.
    • (2004) J Bacteriol , vol.186 , pp. 3355-3362
    • Christiansen, J.K.1    Larsen, M.H.2    Ingmer, H.3    Søgaard-Andersen, L.4    Kallipolitis, B.H.5
  • 10
    • 77952660427 scopus 로고    scopus 로고
    • Altered growth, pigmentation, and antimicrobial susceptibility properties of Staphylococcus aureus due to loss of the major cold shock gene cspB
    • Duval, B. D., Mathew, A., Satola, S. W. & Shafer, W. M. (2010). Altered growth, pigmentation, and antimicrobial susceptibility properties of Staphylococcus aureus due to loss of the major cold shock gene cspB. Antimicrob Agents Chemother 54, 2283-2290.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 2283-2290
    • Duval, B.D.1    Mathew, A.2    Satola, S.W.3    Shafer, W.M.4
  • 12
    • 63149194170 scopus 로고    scopus 로고
    • Multiple posttranscriptional regulatory mechanisms partner to control ethanolamine utilization in Enterococcus faecalis
    • Fox, K. A., Ramesh, A., Stearns, J. E., Bourgogne, A., Reyes-Jara, A., Winkler, W. C. & Garsin, D. A. (2009). Multiple posttranscriptional regulatory mechanisms partner to control ethanolamine utilization in Enterococcus faecalis. Proc Natl Acad Sci U S A 106, 4435-4440.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4435-4440
    • Fox, K.A.1    Ramesh, A.2    Stearns, J.E.3    Bourgogne, A.4    Reyes-Jara, A.5    Winkler, W.C.6    Garsin, D.A.7
  • 13
    • 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. & Hartke, A. (2000). 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, 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
  • 16
    • 0029823884 scopus 로고    scopus 로고
    • Some like it cold: Response of microorganisms to cold shock
    • Graumann, P. & Marahiel, M. A. (1996). Some like it cold: response of microorganisms to cold shock. Arch Microbiol 166, 293-300.
    • (1996) Arch Microbiol , vol.166 , pp. 293-300
    • Graumann, P.1    Marahiel, M.A.2
  • 17
    • 0031658803 scopus 로고    scopus 로고
    • A superfamily of proteins that contain the cold-shock domain
    • Graumann, P. L. & Marahiel, M. A. (1998). A superfamily of proteins that contain the cold-shock domain. Trends Biochem Sci 23, 286-290.
    • (1998) Trends Biochem Sci , vol.23 , pp. 286-290
    • Graumann, P.L.1    Marahiel, M.A.2
  • 18
    • 0033002716 scopus 로고    scopus 로고
    • Cold shock proteins CspB and CspC are major stationary-phase-induced proteins in Bacillus subtilis
    • Graumann, P. L. & Marahiel, M. A. (1999). Cold shock proteins CspB and CspC are major stationary-phase-induced proteins in Bacillus subtilis. Arch Microbiol 171, 135-138.
    • (1999) Arch Microbiol , vol.171 , pp. 135-138
    • Graumann, P.L.1    Marahiel, M.A.2
  • 19
    • 0030826392 scopus 로고    scopus 로고
    • A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures
    • Graumann, P., Wendrich, T. M., Weber, M. H., Schröder, K. & Marahiel, M. A. (1997). A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures. Mol Microbiol 25, 741-756.
    • (1997) Mol Microbiol , vol.25 , pp. 741-756
    • Graumann, P.1    Wendrich, T.M.2    Weber, M.H.3    Schröder, K.4    Marahiel, M.A.5
  • 20
    • 0043166304 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional control of cold-shock genes
    • Gualerzi, C. O., Giuliodori, A. M. & Pon, C. L. (2003). Transcriptional and post-transcriptional control of cold-shock genes. J Mol Biol 331, 527-539.
    • (2003) J Mol Biol , vol.331 , pp. 527-539
    • Gualerzi, C.O.1    Giuliodori, A.M.2    Pon, C.L.3
  • 21
    • 0037022294 scopus 로고    scopus 로고
    • The capsular polysaccharide of Enterococcus faecalis and its relationship to other polysaccharides in the cell wall
    • Hancock, L. E. & Gilmore, M. S. (2002). The capsular polysaccharide of Enterococcus faecalis and its relationship to other polysaccharides in the cell wall. Proc Natl Acad Sci U S A 99, 1574-1579.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1574-1579
    • Hancock, L.E.1    Gilmore, M.S.2
  • 22
    • 79953718512 scopus 로고    scopus 로고
    • Quantitative proteomic view on secreted, cell surfaceassociated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions
    • Hempel, K., Herbst, F.-A., Moche, M., Hecker, M. & Becher, D. (2011). Quantitative proteomic view on secreted, cell surfaceassociated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions. J Proteome Res 10, 1657-1666.
    • (2011) J Proteome Res , vol.10 , pp. 1657-1666
    • Hempel, K.1    Herbst, F.-A.2    Moche, M.3    Hecker, M.4    Becher, D.5
  • 23
    • 34250720036 scopus 로고    scopus 로고
    • Structure and function of bacterial cold shock proteins
    • Horn, G., Hofweber, R., Kremer, W. & Kalbitzer, H. R. (2007). Structure and function of bacterial cold shock proteins. Cell Mol Life Sci 64, 1457-1470.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1457-1470
    • Horn, G.1    Hofweber, R.2    Kremer, W.3    Kalbitzer, H.R.4
  • 24
    • 0033914435 scopus 로고    scopus 로고
    • Prophylactic and therapeutic efficacy of antibodies to a capsular polysaccharide shared among vancomycin-sensitive and-resistant enterococci
    • Huebner, J., Quaas, A., Krueger, W. A., Goldmann, D. A. & Pier, G. B. (2000). Prophylactic and therapeutic efficacy of antibodies to a capsular polysaccharide shared among vancomycin-sensitive and-resistant enterococci. Infect Immun 68, 4631-4636.
    • (2000) Infect Immun , vol.68 , pp. 4631-4636
    • Huebner, J.1    Quaas, A.2    Krueger, W.A.3    Goldmann, D.A.4    Pier, G.B.5
  • 25
    • 78049496542 scopus 로고    scopus 로고
    • Molecular pathogenesis of Listeria monocytogenes in the alternative model host Galleria mellonella
    • Joyce, S. A. & Gahan, C. G. M. (2010). Molecular pathogenesis of Listeria monocytogenes in the alternative model host Galleria mellonella. Microbiology 156, 3456-3468.
    • (2010) Microbiology , vol.156 , pp. 3456-3468
    • Joyce, S.A.1    Gahan, C.G.M.2
  • 26
    • 84870523148 scopus 로고    scopus 로고
    • Galleria mellonella as a model host for human pathogens: Recent studies and new perspectives
    • Junqueira, J. C. (2012). Galleria mellonella as a model host for human pathogens: recent studies and new perspectives. Virulence 3, 474-476.
    • (2012) Virulence , vol.3 , pp. 474-476
    • Junqueira, J.C.1
  • 30
    • 35548978615 scopus 로고    scopus 로고
    • Escheriosome-mediated delivery of recombinant ribosomal L7/L12 protein confers protection against murine brucellosis
    • Mallick, A. I., Singha, H., Khan, S., Anwar, T., Ansari, M. A., Khalid, R., Chaudhuri, P. & Owais, M. (2007). Escheriosome-mediated delivery of recombinant ribosomal L7/L12 protein confers protection against murine brucellosis. Vaccine 25, 7873-7884.
    • (2007) Vaccine , vol.25 , pp. 7873-7884
    • Mallick, A.I.1    Singha, H.2    Khan, S.3    Anwar, T.4    Ansari, M.A.5    Khalid, R.6    Chaudhuri, P.7    Owais, M.8
  • 33
    • 0025100795 scopus 로고
    • The life and times of the Enterococcus
    • Murray, B. E. (1990). The life and times of the Enterococcus. Clin Microbiol Rev 3, 46-65.
    • (1990) Clin Microbiol Rev , vol.3 , pp. 46-65
    • Murray, B.E.1
  • 34
    • 50349083332 scopus 로고    scopus 로고
    • Safety assessment of dairy microorganisms: The Enterococcus genus
    • Ogier, J.-C. & Serror, P. (2008). Safety assessment of dairy microorganisms: the Enterococcus genus. Int J Food Microbiol 126, 291-301.
    • (2008) Int J Food Microbiol , vol.126 , pp. 291-301
    • Ogier, J.-C.1    Serror, P.2
  • 35
    • 0032858516 scopus 로고    scopus 로고
    • Sequence-selective interactions with RNA by CspB, CspC and CspE, members of the CspA family of Escherichia coli
    • Phadtare, S. & Inouye, M. (1999). Sequence-selective interactions with RNA by CspB, CspC and CspE, members of the CspA family of Escherichia coli. Mol Microbiol 33, 1004-1014.
    • (1999) Mol Microbiol , vol.33 , pp. 1004-1014
    • Phadtare, S.1    Inouye, M.2
  • 36
    • 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. & Murray, B. E. (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
  • 41
    • 0029078286 scopus 로고
    • Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif
    • Schröder, K., Graumann, P., Schnuchel, A., Holak, T. A. & Marahiel, M. A. (1995). Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif. Mol Microbiol 16, 699-708.
    • (1995) Mol Microbiol , vol.16 , pp. 699-708
    • Schröder, K.1    Graumann, P.2    Schnuchel, A.3    Holak, T.A.4    Marahiel, M.A.5
  • 42
    • 0034973596 scopus 로고    scopus 로고
    • Role of Enterococcus faecalis surface protein Esp in the pathogenesis of ascending urinary tract infection
    • Shankar, N., Lockatell, C. V., Baghdayan, A. S., Drachenberg, C., Gilmore, M. S. & Johnson, D. E. (2001). Role of Enterococcus faecalis surface protein Esp in the pathogenesis of ascending urinary tract infection. Infect Immun 69, 4366-4372.
    • (2001) Infect Immun , vol.69 , pp. 4366-4372
    • Shankar, N.1    Lockatell, C.V.2    Baghdayan, A.S.3    Drachenberg, C.4    Gilmore, M.S.5    Johnson, D.E.6
  • 43
    • 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. & Gilmore, M. S. (2002). Differential expression of virulence-related genes in Enterococcus faecalis in response to biological cues in serum and urine. Infect Immun 70, 4344-4352.
    • (2002) Infect Immun , vol.70 , pp. 4344-4352
    • Shepard, B.D.1    Gilmore, M.S.2
  • 44
    • 84861162318 scopus 로고    scopus 로고
    • Efficacy of ceftobiprole Medocaril against Enterococcus faecalis in a murine urinary tract infection model
    • Singh, K. V. & Murray, B. E. (2012). Efficacy of ceftobiprole Medocaril against Enterococcus faecalis in a murine urinary tract infection model. Antimicrob Agents Chemother 56, 3457-3460.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 3457-3460
    • Singh, K.V.1    Murray, B.E.2
  • 45
    • 34249079398 scopus 로고    scopus 로고
    • Importance of the ebp (endocarditis-and biofilm-associated pilus) locus in the pathogenesis of Enterococcus faecalis ascending urinary tract infection
    • Singh, K. V., Nallapareddy, S. R. & Murray, B. E. (2007). Importance of the ebp (endocarditis-and biofilm-associated pilus) locus in the pathogenesis of Enterococcus faecalis ascending urinary tract infection. J Infect Dis 195, 1671-1677.
    • (2007) J Infect Dis , vol.195 , pp. 1671-1677
    • Singh, K.V.1    Nallapareddy, S.R.2    Murray, B.E.3
  • 46
    • 84884763787 scopus 로고    scopus 로고
    • Progressive lowering of temperature for immunolabeling and in situ hybridization
    • In, Edited by A. Cavalier, D. Spehner & B. Humbel. Boca Raton, FL: CRC Press
    • Spehner, D. & Cavalier, A. (2008). Progressive lowering of temperature for immunolabeling and in situ hybridization. In Handbook of Cryo-Preparation Methods for Electron Microscopy, pp. 433-465. Edited by A. Cavalier, D. Spehner & B. Humbel. Boca Raton, FL: CRC Press.
    • (2008) Handbook of Cryo-Preparation Methods for Electron Microscopy , pp. 433-465
    • Spehner, D.1    Cavalier, A.2
  • 47
    • 84870040929 scopus 로고    scopus 로고
    • The prevalence and the characterization of the enterococcus species from various clinical samples in a tertiary care hospital
    • Sreeja, S., Babu P R, S. & Prathab, A. G. (2012). The prevalence and the characterization of the enterococcus species from various clinical samples in a tertiary care hospital. J Clin Diagn Res 6, 1486-1488.
    • (2012) J Clin Diagn Res , vol.6 , pp. 1486-1488
    • Sreeja, S.1    Babu, P.R.S.2    Prathab, A.G.3
  • 48
    • 0036714801 scopus 로고    scopus 로고
    • Predicted structure and phyletic distribution of the RNA-binding protein Hfq
    • Sun, X., Zhulin, I. & Wartell, R. M. (2002). Predicted structure and phyletic distribution of the RNA-binding protein Hfq. Nucleic Acids Res 30, 3662-3671.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3662-3671
    • Sun, X.1    Zhulin, I.2    Wartell, R.M.3
  • 49
    • 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. & Murray, B. E. (2005). 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, 472-480.
    • (2005) J Infect Dis , vol.191 , pp. 472-480
    • Teng, F.1    Nannini, E.C.2    Murray, B.E.3
  • 50
    • 42049098165 scopus 로고    scopus 로고
    • Shedding & shaving: Disclosure of proteomic expressions on a bacterial face
    • Tjalsma, H., Lambooy, L., Hermans, P. W. & Swinkels, D. W. (2008). Shedding & shaving: disclosure of proteomic expressions on a bacterial face. Proteomics 8, 1415-1428.
    • (2008) Proteomics , vol.8 , pp. 1415-1428
    • Tjalsma, H.1    Lambooy, L.2    Hermans, P.W.3    Swinkels, D.W.4
  • 51
    • 79960433506 scopus 로고    scopus 로고
    • Hfq and its constellation of RNA
    • Vogel, J. & Luisi, B. F. (2011). Hfq and its constellation of RNA. Nat Rev Microbiol 9, 578-589.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 578-589
    • Vogel, J.1    Luisi, B.F.2
  • 52
    • 0036185045 scopus 로고    scopus 로고
    • Specific identification of three low molecular weight membraneassociated antigens of Helicobacter pylori
    • Voland, P., Weeks, D. L., Vaira, D., Prinz, C. & Sachs, G. (2002). Specific identification of three low molecular weight membraneassociated antigens of Helicobacter pylori. Aliment Pharmacol Ther 16, 533-544.
    • (2002) Aliment Pharmacol Ther , vol.16 , pp. 533-544
    • Voland, P.1    Weeks, D.L.2    Vaira, D.3    Prinz, C.4    Sachs, G.5
  • 53
    • 46449139222 scopus 로고    scopus 로고
    • Preparation of cells and tissues for immuno EM
    • Webster, P., Schwarz, H. & Griffiths, G. (2008). Preparation of cells and tissues for immuno EM. Methods Cell Biol 88, 45-58.
    • (2008) Methods Cell Biol , vol.88 , pp. 45-58
    • Webster, P.1    Schwarz, H.2    Griffiths, G.3
  • 54
    • 3943093972 scopus 로고    scopus 로고
    • Nosocomial bloodstream infections in US hospitals: Analysis of 24,179 cases from a prospective nationwide surveillance study
    • Wisplinghoff, H., Bischoff, T., Tallent, S. M., Seifert, H., Wenzel, R. P. & Edmond, M. B. (2004). Nosocomial bloodstream infections in US hospitals: analysis of 24,179 cases from a prospective nationwide surveillance study. Clin Infect Dis 39, 309-317.
    • (2004) Clin Infect Dis , vol.39 , pp. 309-317
    • Wisplinghoff, H.1    Bischoff, T.2    Tallent, S.M.3    Seifert, H.4    Wenzel, R.P.5    Edmond, M.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.