메뉴 건너뛰기




Volumn 193, Issue 13, 2011, Pages 3356-3366

Complete genome sequence and immunoproteomic analyses of the bacterial fish pathogen Streptococcus parauberis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; CHAPERONIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

EID: 79959395541     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00182-11     Document Type: Article
Times cited : (44)

References (102)
  • 1
    • 0026712869 scopus 로고
    • The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication
    • Adams, D. E., E. M. Shekhtman, E. L. Zechiedrich, M. B. Schmid, and N. R. Cozzarelli. 1992. The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication. Cell 71:277-288.
    • (1992) Cell , vol.71 , pp. 277-288
    • Adams, D.E.1    Shekhtman, E.M.2    Zechiedrich, E.L.3    Schmid, M.B.4    Cozzarelli, N.R.5
  • 2
    • 0037195085 scopus 로고    scopus 로고
    • Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen
    • Ajdić, D., et al. 2002. Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc. Natl. Acad. Sci. U. S. A. 99:14434-14439.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14434-14439
    • Ajdić, D.1
  • 3
    • 3242791921 scopus 로고    scopus 로고
    • Polymerase chain reaction mediated identification of Streptococcus uberis and Streptococcus parauberis using species-specific sequences of the genes encoding superoxide dismutase A and chaperonin 60
    • Alber, J., A. El-Sayed, C. Lämmler, A. A. Hassan, and M. Zschöck. 2004. Polymerase chain reaction mediated identification of Streptococcus uberis and Streptococcus parauberis using species-specific sequences of the genes encoding superoxide dismutase A and chaperonin 60 . J. Vet. Med. B Infect. Dis. Vet. Public Health 51:180-184.
    • (2004) J. Vet. Med. B Infect. Dis. Vet. Public Health. , vol.51 , pp. 180-184
    • Alber, J.1    El-Sayed, A.2    Lämmler, C.3    Hassan, A.A.4    Zschöck, M.5
  • 4
    • 0001136897 scopus 로고
    • Drug resistance in a non-hemolytic Streptococcus sp. isolated from cultured yellowtail Seriola quinqueradiata
    • Aoki, T., K. Takami, and T. Kaito. 1990. Drug resistance in a non-hemolytic Streptococcus sp. isolated from cultured yellowtail Seriola quinqueradiata. Dis. Aquat. Organ. 8:171-177.
    • (1990) Dis. Aquat. Organ. , vol.8 , pp. 171-177
    • Aoki, T.1    Takami, K.2    Kaito, T.3
  • 5
    • 0033541674 scopus 로고    scopus 로고
    • Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry
    • Arnold, R. J., and J. P. Reilly. 1999. Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry. Anal. Biochem. 269:105-112.
    • (1999) Anal. Biochem. , vol.269 , pp. 105-112
    • Arnold, R.J.1    Reilly, J.P.2
  • 6
    • 0031656714 scopus 로고    scopus 로고
    • Molecular analysis of the capsule gene region of group A Streptococcus: the hasAB genes are sufficient for capsule expression
    • Ashbaugh, C. D., S. Alberti, and M. R. Wessles. 1998. Molecular analysis of the capsule gene region of group A Streptococcus: the hasAB genes are sufficient for capsule expression. J. Bacteriol. 180:4955-4959.
    • (1998) J. Bacteriol. , vol.180 , pp. 4955-4959
    • Ashbaugh, C.D.1    Alberti, S.2    Wessles, M.R.3
  • 7
    • 0031944979 scopus 로고    scopus 로고
    • Novel assay reveals multiple pathways regulating stress-induced accumulations of inorganic polyphosphate in Escherichia coli
    • Ault-Riché, D., C. D. Fraley, C. M. Tzeng, and A. Kornberg. 1998. Novel assay reveals multiple pathways regulating stress-induced accumulations of inorganic polyphosphate in Escherichia coli. J. Bacteriol. 180:1841-1847.
    • (1998) J. Bacteriol. , vol.180 , pp. 1841-1847
    • Ault-Riché, D.1    Fraley, C.D.2    Tzeng, C.M.3    Kornberg, A.4
  • 9
    • 0032900737 scopus 로고    scopus 로고
    • CRITICA: coding region identification tool invoking comparative analysis
    • Badger, J. H., and G. J. Olsen. 1999. CRITICA: coding region identification tool invoking comparative analysis. Mol. Biol. Evol. 16:512-524.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 512-524
    • Badger, J.H.1    Olsen, G.J.2
  • 10
    • 44049087544 scopus 로고    scopus 로고
    • Identification and molecular characterisation of a fibrinogen binding protein from Streptococcus iniae
    • Baiano, F. C. F., R. A. Tumbol, A. Umapathy, and A. C. Hurvitz. 2008. Identification and molecular characterisation of a fibrinogen binding protein from Streptococcus iniae. BMC Microbiol. 8:67.
    • (2008) BMC Microbiol , vol.8 , pp. 67
    • Baiano, F.C.F.1    Tumbol, R.A.2    Umapathy, A.3    Hurvitz, A.C.4
  • 11
    • 0022457545 scopus 로고
    • Acid tolerance, proton permeabilities, and membrane ATPases of oral streptococci
    • Bender, G. R., S. V. Sutton, and R. E. Marquis. 1986. Acid tolerance, proton permeabilities, and membrane ATPases of oral streptococci. Infect. Immun. 53:331-338.
    • (1986) Infect. Immun. , vol.53 , pp. 331-338
    • Bender, G.R.1    Sutton, S.V.2    Marquis, R.E.3
  • 12
    • 0025998182 scopus 로고
    • Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences
    • Bentley, R. W., J. A. Leigh, and M. D. Collins. 1991. Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences. Int. J. Syst. Bacteriol. 41:487-494.
    • (1991) Int. J. Syst. Bacteriol. , vol.41 , pp. 487-494
    • Bentley, R.W.1    Leigh, J.A.2    Collins, M.D.3
  • 13
    • 0032784646 scopus 로고    scopus 로고
    • Proteomics: quantitative and physical mapping of cellular proteins
    • Blackstock, W. P., and M. P. Weir. 1999. Proteomics: quantitative and physical mapping of cellular proteins. Trends Biotechnol. 17:121-127.
    • (1999) Trends Biotechnol , vol.17 , pp. 121-127
    • Blackstock, W.P.1    Weir, M.P.2
  • 14
    • 19944414611 scopus 로고    scopus 로고
    • Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus
    • Bolotin, A., et al. 2004. Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus. Nat. Biotechnol. 22:1554-1558.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1554-1558
    • Bolotin, A.1
  • 15
    • 0031042682 scopus 로고    scopus 로고
    • Plasminogen activation by invasive human pathogens
    • Boyle, M. D., and R. Lottenberg. 1997. Plasminogen activation by invasive human pathogens. Thromb. Haemost. 77:1-10.
    • (1997) Thromb. Haemost. , vol.77 , pp. 1-10
    • Boyle, M.D.1    Lottenberg, R.2
  • 16
    • 0034101261 scopus 로고    scopus 로고
    • Proteomics in medical microbiology
    • Cash, P. 2000. Proteomics in medical microbiology. Electrophoresis 21: 1187-1201.
    • (2000) Electrophoresis , vol.21 , pp. 1187-1201
    • Cash, P.1
  • 18
    • 0032957449 scopus 로고    scopus 로고
    • DnaA boxes are important elements in setting the initiation mass of Escherichia coli
    • Christensen, B. B., T. Atlung, and F. G. Hansen. 1999. DnaA boxes are important elements in setting the initiation mass of Escherichia coli. J. Bacteriol. 181:2683-2688.
    • (1999) J. Bacteriol. , vol.181 , pp. 2683-2688
    • Christensen, B.B.1    Atlung, T.2    Hansen, F.G.3
  • 19
    • 17644397901 scopus 로고    scopus 로고
    • Surface analyses and immune reactivities of major cell wall-associated proteins of group A streptococcus
    • Cole, J. N., et al. 2005. Surface analyses and immune reactivities of major cell wall-associated proteins of group A streptococcus. Infect. Immun. 73: 3137-3146.
    • (2005) Infect. Immun. , vol.73 , pp. 3137-3146
    • Cole, J.N.1
  • 20
    • 0035321652 scopus 로고    scopus 로고
    • Comparative proteomics of bacterial pathogens
    • Cordwell, S. J., A. S. Nouwens, and B. J. Walsh. 2001. Comparative proteomics of bacterial pathogens. Proteomics 1:461-472.
    • (2001) Proteomics , vol.1 , pp. 461-472
    • Cordwell, S.J.1    Nouwens, A.S.2    Walsh, B.J.3
  • 21
    • 0028106317 scopus 로고
    • Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci
    • Courtney, H. S., Y. Li, J. B. Dale, and D. L. Hasty. 1994. Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci. Infect. Immun. 62:3937-3946.
    • (1994) Infect. Immun. , vol.62 , pp. 3937-3946
    • Courtney, H.S.1    Li, Y.2    Dale, J.B.3    Hasty, D.L.4
  • 22
    • 0029099312 scopus 로고
    • Hyaluronic acid synthesis operon (has) expression in group A streptococci
    • Crater, D. L., and I. van de Rijn. 1995. Hyaluronic acid synthesis operon (has) expression in group A streptococci. J. Biol. Chem. 270:18452-18458.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18452-18458
    • Crater, D.L.1    van de Rijn, I.2
  • 23
    • 0028824134 scopus 로고
    • Molecular characterization of hasC from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose pyrophosphorylase activity
    • Crater, D. L., B. A. Dougherty, and I. van de Rijn. 1995. Molecular characterization of hasC from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose pyrophosphorylase activity. J. Biol. Chem. 270:28676-28680.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28676-28680
    • Crater, D.L.1    Dougherty, B.A.2    van de Rijn, I.3
  • 24
    • 0028221239 scopus 로고
    • Genetically altered levels of inorganic polyphosphate in Escherichia coli
    • Crooke, E., M. Akiyama, N. N. Rao, and A. Kornberg. 1994. Genetically altered levels of inorganic polyphosphate in Escherichia coli. J. Biol. Chem. 269:6290-6295.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6290-6295
    • Crooke, E.1    Akiyama, M.2    Rao, N.N.3    Kornberg, A.4
  • 25
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M. W. 2000. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13:470-511.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 26
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L., E. Dassa, C. Orelle, and J. Chen. 2008. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72:317-364.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 28
    • 0002324683 scopus 로고    scopus 로고
    • Streptococcosis in cultured turbot (Schophtalmus maximus) associated with Streptococcus parauberis
    • Doménech, A., et al. 1996. Streptococcosis in cultured turbot (Schophtalmus maximus) associated with Streptococcus parauberis. J. Fish Dis. 19:33-38.
    • (1996) J. Fish Dis. , vol.19 , pp. 33-38
    • Doménech, A.1
  • 29
    • 0026551702 scopus 로고
    • Molecular characterization of a locus required for hyaluronic acid capsule production in group A streptococci
    • Dougherty, B. A., and I. van de Rijn. 1992. Molecular characterization of a locus required for hyaluronic acid capsule production in group A streptococci. J. Exp. Med. 175:1291-1299.
    • (1992) J. Exp. Med. , vol.175 , pp. 1291-1299
    • Dougherty, B.A.1    van de Rijn, I.2
  • 30
    • 0027478026 scopus 로고
    • Molecular characterization of hasB from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose dehydrogenase activity
    • Dougherty, B. A., and I. van de Rijn. 1993. Molecular characterization of hasB from an operon required for hyaluronic acid synthesis in group A streptococci. Demonstration of UDP-glucose dehydrogenase activity. J. Biol. Chem. 268:7118-7124.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7118-7124
    • Dougherty, B.A.1    van de Rijn, I.2
  • 31
    • 0028032079 scopus 로고
    • Molecular characterization of hasA from an operon required for hyaluronic acid synthesis in group A streptococci
    • Dougherty, B. A., and I. van de Rijn. 1994. Molecular characterization of hasA from an operon required for hyaluronic acid synthesis in group A streptococci. J. Biol. Chem. 269:169-175.
    • (1994) J. Biol. Chem. , vol.269 , pp. 169-175
    • Dougherty, B.A.1    van de Rijn, I.2
  • 32
    • 0025313681 scopus 로고
    • Penicillin-resistant viridans streptococci have obtained altered penicillin-binding protein genes from penicillin-resistant strains of Streptococcus pneumoniae
    • Dowson, C. G., et al. 1990. Penicillin-resistant viridans streptococci have obtained altered penicillin-binding protein genes from penicillin-resistant strains of Streptococcus pneumoniae. Proc. Natl. Acad. Sci. U. S. A. 87: 5858-5862.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 5858-5862
    • Dowson, C.G.1
  • 33
    • 0027165733 scopus 로고
    • Evolution of penicillin resistance in Streptococcus pneumoniae; the role of Streptococcus mitis in the formation of a low affinity PBP2B in S. pneumoniae
    • Dowson, C. G., T. J. Coffey, C. Kell, and R. A. Whiley. 1993. Evolution of penicillin resistance in Streptococcus pneumoniae; the role of Streptococcus mitis in the formation of a low affinity PBP2B in S. pneumoniae. Mol. Microbiol. 9:635-643.
    • (1993) Mol. Microbiol. , vol.9 , pp. 635-643
    • Dowson, C.G.1    Coffey, T.J.2    Kell, C.3    Whiley, R.A.4
  • 34
    • 0028882127 scopus 로고
    • Streptococcus shiloi, the name for an agent causing septicemic infection in fish, is a junior synonym of Streptococcus iniae
    • Eldar, A., et al. 1995. Streptococcus shiloi, the name for an agent causing septicemic infection in fish, is a junior synonym of Streptococcus iniae. Int. J. Syst. Bacteriol. 45:840-842.
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 840-842
    • Eldar, A.1
  • 35
    • 0031955518 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. I. Accuracy assessment
    • Ewing, B., L. Hillier, M. C. Wendl, and P. Green. 1998. Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res. 8:175-185.
    • (1998) Genome Res , vol.8 , pp. 175-185
    • Ewing, B.1    Hillier, L.2    Wendl, M.C.3    Green, P.4
  • 36
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing, B., and P. Green. 1998. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res. 8:186-194.
    • (1998) Genome Res , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 37
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: how one organism sees its world
    • Fabret, C., V. A. Feher, and J. A. Hoch. 1999. Two-component signal transduction in Bacillus subtilis: how one organism sees its world. J. Bacteriol. 181:1975-1983.
    • (1999) J. Bacteriol. , vol.181 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 38
    • 0036779816 scopus 로고    scopus 로고
    • What happened to the streptococci: overview of taxonomic and nomenclature changes
    • Facklam, R. 2002. What happened to the streptococci: overview of taxonomic and nomenclature changes. Clin. Microbiol. Rev. 15:613-630.
    • (2002) Clin. Microbiol. Rev. , vol.15 , pp. 613-630
    • Facklam, R.1
  • 39
    • 0035836659 scopus 로고    scopus 로고
    • Complete genome sequence of an M1 strain of Streptococcus pyogenes
    • Ferretti, J. J., et al. 2001. Complete genome sequence of an M1 strain of Streptococcus pyogenes. Proc. Natl. Acad. Sci. U. S. A. 98:4658-4663.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4658-4663
    • Ferretti, J.J.1
  • 40
    • 0025761098 scopus 로고
    • Streptococcal M protein
    • Fischetti, V. A. 1991. Streptococcal M protein. Sci. Am. 264:58-65.
    • (1991) Sci. Am. , vol.264 , pp. 58-65
    • Fischetti, V.A.1
  • 41
    • 58149191274 scopus 로고    scopus 로고
    • Rfam: updates to the RNA families database
    • Gardner, P. P., et al. 2009. Rfam: updates to the RNA families database. Nucleic Acids Res. 37:D136-D140.
    • (2009) Nucleic Acids Res , vol.37
    • Gardner, P.P.1
  • 42
    • 77955611529 scopus 로고    scopus 로고
    • Pooled protein immunization for identification of cell surface antigens in Streptococcus sanguinis
    • Ge, X., T. Kitten, C. L. Munro, D. H. Conrad, and P. Xu. 2010. Pooled protein immunization for identification of cell surface antigens in Streptococcus sanguinis. PLoS One. 5:e11666.
    • (2010) PLoS One , vol.5
    • Ge, X.1    Kitten, T.2    Munro, C.L.3    Conrad, D.H.4    Xu, P.5
  • 43
    • 0004901078 scopus 로고
    • Report of streptococcosis in rainbow trout (Oncorhynchus mykiss) in Italy: preliminary note
    • Ghittino, C., and M. Prearo. 1992. Report of streptococcosis in rainbow trout (Oncorhynchus mykiss) in Italy: preliminary note. Boll. Soc. Ital. Patol. Ittica 8:4-11.
    • (1992) Boll. Soc. Ital. Patol. Ittica. , vol.8 , pp. 4-11
    • Ghittino, C.1    Prearo, M.2
  • 44
    • 18644378733 scopus 로고    scopus 로고
    • Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease
    • Glaser, P., et al. 2002. Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease. Mol. Microbiol. 45:1499-1513.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1499-1513
    • Glaser, P.1
  • 45
    • 0031955116 scopus 로고    scopus 로고
    • Consed: a graphical tool for sequence finishing
    • Gordon, D., C. Abajian, and P. Green. 1998. Consed: a graphical tool for sequence finishing. Genome Res. 8:195-202.
    • (1998) Genome Res , vol.8 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 46
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Görg, A., W. Weiss, and M. J. Dunn. 2004. Current two-dimensional electrophoresis technology for proteomics. Proteomics 4:3665-3685.
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Görg, A.1    Weiss, W.2    Dunn, M.J.3
  • 47
    • 0031300081 scopus 로고    scopus 로고
    • Classification and overview of the genera Streptococcus and Enterococcus
    • Hardie, J. M., and R. A. Whiley. 1997. Classification and overview of the genera Streptococcus and Enterococcus. Soc. Appl. Bacteriol. Symp. Ser. 26:1S-11S.
    • (1997) Soc. Appl. Bacteriol. Symp. Ser. , vol.26
    • Hardie, J.M.1    Whiley, R.A.2
  • 48
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch, J. A. 2000. Two-component and phosphorelay signal transduction. Curr. Opin. Microbiol. 3:165-170.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 49
    • 67650658074 scopus 로고    scopus 로고
    • Rapid evolution of virulence and drug resistance in the emerging zoonotic pathogen Streptococcus suis
    • Holden, M. T., et al. 2009. Rapid evolution of virulence and drug resistance in the emerging zoonotic pathogen Streptococcus suis. PLoS One 4:e6072.
    • (2009) PLoS One , vol.4
    • Holden, M.T.1
  • 50
    • 63449097053 scopus 로고    scopus 로고
    • Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens
    • Holden, M. T., et al. 2009. Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens. PLoS. Pathog. 5:e1000346.
    • (2009) PLoS. Pathog. , vol.5
    • Holden, M.T.1
  • 51
    • 0034786512 scopus 로고    scopus 로고
    • The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence
    • Holmes, A. R., et al. 2001. The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol. Microbiol. 41:1395-1408.
    • (2001) Mol. Microbiol. , vol.41 , pp. 1395-1408
    • Holmes, A.R.1
  • 52
    • 0034806849 scopus 로고    scopus 로고
    • Genome of the bacterium Streptococcus pneumoniae strain R6
    • Hoskins, J., et al. 2001. Genome of the bacterium Streptococcus pneumoniae strain R6. J. Bacteriol. 183:5709-5717.
    • (2001) J. Bacteriol. , vol.183 , pp. 5709-5717
    • Hoskins, J.1
  • 53
    • 33750970871 scopus 로고    scopus 로고
    • Polyphosphate stores enhance the ability of Vibrio cholerae to overcome environmental stresses in a low-phosphate environment
    • Jahid, I. K., A. J. Silva, and J. A. Benitez. 2006. Polyphosphate stores enhance the ability of Vibrio cholerae to overcome environmental stresses in a low-phosphate environment. Appl. Environ. Microbiol. 72:7043-7049.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 7043-7049
    • Jahid, I.K.1    Silva, A.J.2    Benitez, J.A.3
  • 54
    • 0037093379 scopus 로고    scopus 로고
    • Regulation of sigma factor competition by the alarmone ppGpp
    • Jishage, M., K. Kvint, V. Shingler, and T. Nyström. 2002. Regulation of sigma factor competition by the alarmone ppGpp. Genes Dev. 16:1260-1270.
    • (2002) Genes Dev , vol.16 , pp. 1260-1270
    • Jishage, M.1    Kvint, K.2    Shingler, V.3    Nyström, T.4
  • 55
    • 65649096418 scopus 로고    scopus 로고
    • Serological differentiation of Streptococcus parauberis strains isolated from cultured Japanese flounder in Japan
    • Kanai, K., et al. 2009. Serological differentiation of Streptococcus parauberis strains isolated from cultured Japanese flounder in Japan. Fish Pathol. 44:33-39.
    • (2009) Fish Pathol , vol.44 , pp. 33-39
    • Kanai, K.1
  • 56
    • 25844504233 scopus 로고    scopus 로고
    • Efficacy of protein A-HRP in an immunological study of black rockfish (Sebastes schlegeli Higendorf) humoral immune responses
    • Kang, S. H., et al. 2006. Efficacy of protein A-HRP in an immunological study of black rockfish (Sebastes schlegeli Higendorf) humoral immune responses. Fish Shellfish Immunol. 20:295-304.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 295-304
    • Kang, S.H.1
  • 58
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst, F., et al. 1997. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390:249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1
  • 59
    • 0032816642 scopus 로고    scopus 로고
    • Identification of a new regulator in Streptococcus pneumoniae linking quorum sensing to competence for genetic transformation
    • Lee, M. S., and D. A. Morrison. 1999. Identification of a new regulator in Streptococcus pneumoniae linking quorum sensing to competence for genetic transformation. J. Bacteriol. 181:5004-5016.
    • (1999) J. Bacteriol. , vol.181 , pp. 5004-5016
    • Lee, M.S.1    Morrison, D.A.2
  • 60
    • 0345873477 scopus 로고    scopus 로고
    • An optimized method for the isolation and identification of membrane proteins
    • Lehner, I., M. Niehof, and J. Borlak. 2003. An optimized method for the isolation and identification of membrane proteins. Electrophoresis 24: 1795-1808.
    • (2003) Electrophoresis , vol.24 , pp. 1795-1808
    • Lehner, I.1    Niehof, M.2    Borlak, J.3
  • 61
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    • Lei, B., S. Mackie, S. Lukomski, and J. M. Musser. 2000. Identification and immunogenicity of group A Streptococcus culture supernatant proteins. Infect. Immun. 68:6807-6818.
    • (2000) Infect. Immun. , vol.68 , pp. 6807-6818
    • Lei, B.1    Mackie, S.2    Lukomski, S.3    Musser, J.M.4
  • 62
    • 85016229161 scopus 로고    scopus 로고
    • Large-scale protein identification using mass spectrometry
    • Lin, D., D. L. Tabb, and J. R. Yates III. 2003. Large-scale protein identification using mass spectrometry. Biochim. Biophys. Acta 1646:1-10.
    • (2003) Biochim. Biophys. Acta. , vol.1646 , pp. 1-10
    • Lin, D.1    Tabb, D.L.2    Yates III., J.R.3
  • 63
    • 8144221393 scopus 로고    scopus 로고
    • Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse
    • Ling, E., et al. 2004. Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse. Clin. Exp. Immunol. 138:290-298.
    • (2004) Clin. Exp. Immunol. , vol.138 , pp. 290-298
    • Ling, E.1
  • 64
    • 0342276245 scopus 로고
    • Reversible synthesis of polyribonucleotides with an enzyme from Escherichia coli
    • Littauer, U. Z., and A. Kornberg. 1957. Reversible synthesis of polyribonucleotides with an enzyme from Escherichia coli. J. Biol. Chem. 226:1077-1092.
    • (1957) J. Biol. Chem. , vol.226 , pp. 1077-1092
    • Littauer, U.Z.1    Kornberg, A.2
  • 65
    • 50049085891 scopus 로고    scopus 로고
    • Environmental and growth phase regulation of the Streptococcus gordonii arginine deiminase genes
    • Liu, Y., Y. Dong, Y. Y. Chen, and R. A. Burne. 2008. Environmental and growth phase regulation of the Streptococcus gordonii arginine deiminase genes. Appl. Environ. Microbiol. 74:5023-5030.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 5023-5030
    • Liu, Y.1    Dong, Y.2    Chen, Y.Y.3    Burne, R.A.4
  • 66
    • 0029985398 scopus 로고    scopus 로고
    • Asymmetric substitution patterns in the two DNA strands of bacteria
    • Lobry, J. R. 1996. Asymmetric substitution patterns in the two DNA strands of bacteria. Mol. Biol. Evol. 13:660-665.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 660-665
    • Lobry, J.R.1
  • 67
    • 50949089389 scopus 로고    scopus 로고
    • Streptococcus iniae M-like protein contributes to virulence in fish and is a target for live attenuated vaccine development
    • Locke, J. B., R. K. Aziz, M. R. Vicknair, V. Nizet, and A. C. Buchanan. 2008. Streptococcus iniae M-like protein contributes to virulence in fish and is a target for live attenuated vaccine development. PLoS One 3:e2824.
    • (2008) PLoS One , vol.3
    • Locke, J.B.1    Aziz, R.K.2    Vicknair, M.R.3    Nizet, V.4    Buchanan, A.C.5
  • 68
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence
    • Lowe, T. M., and S. R. Eddy. 1997. tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res. 25:955-964.
    • (1997) Nucleic Acids Res , vol.25 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 70
    • 33750341148 scopus 로고    scopus 로고
    • Comparative genomics of the lactic acid bacteria
    • Makarova, K., et al. 2006. Comparative genomics of the lactic acid bacteria. Proc. Natl. Acad. Sci. U. S. A. 103:15611-15616.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15611-15616
    • Makarova, K.1
  • 71
    • 24044455869 scopus 로고    scopus 로고
    • Genome sequencing in microfabricated highdensity picolitre reactors
    • Margulies, M., et al. 2005. Genome sequencing in microfabricated highdensity picolitre reactors. Nature 437:376-380.
    • (2005) Nature , vol.437 , pp. 376-380
    • Margulies, M.1
  • 72
    • 2442688265 scopus 로고    scopus 로고
    • Multiplex PCR assay for detection of bacterial pathogens associated with warm-Water streptococcosis in fish
    • Mata, A. I., et al. 2004. Multiplex PCR assay for detection of bacterial pathogens associated with warm-Water streptococcosis in fish. Appl. Environ. Microbiol. 70:3183-3187.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3183-3187
    • Mata, A.I.1
  • 73
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto, R. I., M. P. Kline, D. N. Bimston, and J. J. Cotto. 1997. The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem. 32:17-29.
    • (1997) Essays Biochem , vol.32 , pp. 17-29
    • Morimoto, R.I.1    Kline, M.P.2    Bimston, D.N.3    Cotto, J.J.4
  • 74
    • 61449127305 scopus 로고    scopus 로고
    • Phenotypic characteristics of Streptococcus iniae and Streptococcus parauberis isolated from olive flounder (Paralichthys olivaceus)
    • Nho, S. W., et al. 2009. Phenotypic characteristics of Streptococcus iniae and Streptococcus parauberis isolated from olive flounder (Paralichthys olivaceus). FEMS Microbiol. Lett. 293:20-27.
    • (2009) FEMS Microbiol. Lett. , vol.293 , pp. 20-27
    • Nho, S.W.1
  • 76
    • 62949249136 scopus 로고    scopus 로고
    • Antibiotic susceptibility and resistance of Streptococcus iniae and Streptococcus parauberis isolated from olive flounder (Paralichthys olivaceus)
    • Park, Y. K., et al. 2009. Antibiotic susceptibility and resistance of Streptococcus iniae and Streptococcus parauberis isolated from olive flounder (Paralichthys olivaceus). Vet. Microbiol. 136:76-81.
    • (2009) Vet. Microbiol. , vol.136 , pp. 76-81
    • Park, Y.K.1
  • 77
    • 34247122207 scopus 로고    scopus 로고
    • Invasive pneumococcal disease and the potential for prevention by vaccination in the United Kingdom
    • Parsons, H. K., S. C. Metcalf, K. Tomlin, R. C. Read, and D. H. Dockrell. 2007. Invasive pneumococcal disease and the potential for prevention by vaccination in the United Kingdom. J. Infect. 54:435-438.
    • (2007) J. Infect. , vol.54 , pp. 435-438
    • Parsons, H.K.1    Metcalf, S.C.2    Tomlin, K.3    Read, R.C.4    Dockrell, D.H.5
  • 78
    • 0033396514 scopus 로고    scopus 로고
    • Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells
    • Peacock, S. J., T. J. Foster, B. J. Cameron, and A. R. Berendt. 1999. Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells. Microbiology 145:3477-3486.
    • (1999) Microbiology , vol.145 , pp. 3477-3486
    • Peacock, S.J.1    Foster, T.J.2    Cameron, B.J.3    Berendt, A.R.4
  • 79
    • 0028252614 scopus 로고
    • Streptococcus iniae associated with mortality of Tilapia nilotica × T. aurea hybrids
    • Perera, R. P., S. K. Johnson, M. D. Collins, and D. H. Lewis. 1994. Streptococcus iniae associated with mortality of Tilapia nilotica × T. aurea hybrids. J. Aquat. Anim. Health 6:335-340.
    • (1994) J. Aquat. Anim. Health. , vol.6 , pp. 335-340
    • Perera, R.P.1    Johnson, S.K.2    Collins, M.D.3    Lewis, D.H.4
  • 80
    • 0030956641 scopus 로고    scopus 로고
    • Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria
    • Piard, J. C., et al. 1997. Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria. J. Bacteriol. 179:3068-6072.
    • (1997) J. Bacteriol. , vol.179 , pp. 3068-6072
    • Piard, J.C.1
  • 83
    • 0029911577 scopus 로고    scopus 로고
    • Inorganic polyphosphate supports resistance and survival of stationary-phase Escherichia coli
    • Rao, N. N., and A. Kornberg. 1996. Inorganic polyphosphate supports resistance and survival of stationary-phase Escherichia coli. J. Bacteriol. 178:1394-1400.
    • (1996) J. Bacteriol. , vol.178 , pp. 1394-1400
    • Rao, N.N.1    Kornberg, A.2
  • 84
    • 0026649193 scopus 로고
    • Group A streptococcalMproteins: virulence factors and protective antigens
    • Robinson, J. H., and M. A. Kehoe. 1992. Group A streptococcalMproteins: virulence factors and protective antigens. Immunol. Today 13:362-367.
    • (1992) Immunol. Today , vol.13 , pp. 362-367
    • Robinson, J.H.1    Kehoe, M.A.2
  • 85
    • 33748657845 scopus 로고    scopus 로고
    • Production of monoclonal antibodies against serum immunoglobulins of black rockfish (Sebastes schlegeli Higendorf)
    • Shin, G. W., et al. 2006. Production of monoclonal antibodies against serum immunoglobulins of black rockfish (Sebastes schlegeli Higendorf). J. Vet. Sci. 7:293-295.
    • (2006) J. Vet. Sci. , vol.7 , pp. 293-295
    • Shin, G.W.1
  • 86
    • 33744819189 scopus 로고    scopus 로고
    • Discrimination of streptococcosis agents in olive flounder (Paralichthys olivaceus)
    • Shin, G. W., et al. 2006. Discrimination of streptococcosis agents in olive flounder (Paralichthys olivaceus). Bull. Eur. Assoc. Fish Pathol. 26:68-79.
    • (2006) Bull. Eur. Assoc. Fish Pathol. , vol.26 , pp. 68-79
    • Shin, G.W.1
  • 87
    • 33746032621 scopus 로고    scopus 로고
    • Partial two-dimensional gel electrophoresis (2-DE) maps of Streptococcus iniae ATCC29178 and Lactococcus garvieae KG9408
    • Shin, G. W., et al. 2006. Partial two-dimensional gel electrophoresis (2-DE) maps of Streptococcus iniae ATCC29178 and Lactococcus garvieae KG9408. Dis. Aquat. Organ. 70:71-79.
    • (2006) Dis. Aquat. Organ. , vol.70 , pp. 71-79
    • Shin, G.W.1
  • 89
    • 0014689848 scopus 로고
    • The biosynthesis of hyaluronic acid by Streptococcus
    • Stoolmiller, A. C., and A. Dorfman. 1969. The biosynthesis of hyaluronic acid by Streptococcus. J. Biol. Chem. 244:236-246.
    • (1969) J. Biol. Chem. , vol.244 , pp. 236-246
    • Stoolmiller, A.C.1    Dorfman, A.2
  • 90
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura, K., J. Dudley, M. Nei, and S. Kumar. 2007. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24:1596-1599.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 91
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov, R. L., E. V. Koonin, and D. J. Lipman. 1997. A genomic perspective on protein families. Science 278:631-637.
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 92
    • 0035919670 scopus 로고    scopus 로고
    • Complete genome sequence of a virulent isolate of Streptococcus pneumoniae
    • Tettelin, H., et al. 2001. Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293:498-506.
    • (2001) Science , vol.293 , pp. 498-506
    • Tettelin, H.1
  • 93
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 94
    • 0037053383 scopus 로고    scopus 로고
    • Fluoride exposure attenuates expression of Streptococcus pyogenes virulence factors
    • Thongboonkerd, V., et al. 2002. Fluoride exposure attenuates expression of Streptococcus pyogenes virulence factors. J. Biol. Chem. 277:16599-16605.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16599-16605
    • Thongboonkerd, V.1
  • 95
    • 0031822062 scopus 로고    scopus 로고
    • Polyphosphate kinase is highly conserved in many bacterial pathogens
    • Tzeng, C. M., and A. Kornberg. 1998. Polyphosphate kinase is highly conserved in many bacterial pathogens. Mol. Microbiol. 29:381-382.
    • (1998) Mol. Microbiol. , vol.29 , pp. 381-382
    • Tzeng, C.M.1    Kornberg, A.2
  • 96
    • 35648977598 scopus 로고    scopus 로고
    • Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide
    • Vickerman, M. M., S. Iobst, A. M. Jesionowski, and S. R. Gill. 2007. Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide. J. Bacteriol. 189:7799-7807.
    • (2007) J. Bacteriol. , vol.189 , pp. 7799-7807
    • Vickerman, M.M.1    Iobst, S.2    Jesionowski, A.M.3    Gill, S.R.4
  • 97
    • 62749122218 scopus 로고    scopus 로고
    • Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis
    • Ward, P. N., et al. 2009. Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis. BMC Genomics 10:54.
    • (2009) BMC Genomics , vol.10 , pp. 54
    • Ward, P.N.1
  • 98
    • 0025033349 scopus 로고
    • Molecular taxonomic studies on Streptococcus uberis types I and II. Description of Streptococcus parauberis sp. nov
    • Williams, A. M., and M. D. Collins. 1990. Molecular taxonomic studies on Streptococcus uberis types I and II. Description of Streptococcus parauberis sp. nov. J. Appl. Bacteriol. 68:485-490.
    • (1990) J. Appl. Bacteriol. , vol.68 , pp. 485-490
    • Williams, A.M.1    Collins, M.D.2
  • 99
    • 43349103204 scopus 로고    scopus 로고
    • Immunoproteomic assay of surface proteins of Streptococcus suis serotype 9
    • Wu, Z., W. Zhang, and C. Lu. 2008. Immunoproteomic assay of surface proteins of Streptococcus suis serotype 9. FEMS Immunol. Med. Microbiol. 53:52-59.
    • (2008) FEMS Immunol. Med. Microbiol. , vol.53 , pp. 52-59
    • Wu, Z.1    Zhang, W.2    Lu, C.3
  • 101
    • 34247853374 scopus 로고    scopus 로고
    • Genome of the opportunistic pathogen Streptococcus sanguinis
    • Xu, P., et al. 2007. Genome of the opportunistic pathogen Streptococcus sanguinis. J. Bacteriol. 189:3166-3175.
    • (2007) J. Bacteriol. , vol.189 , pp. 3166-3175
    • Xu, P.1
  • 102
    • 17144388984 scopus 로고    scopus 로고
    • Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence
    • Yamamoto, Y., et al. 2005. Respiration metabolism of Group B Streptococcus is activated by environmental haem and quinone and contributes to virulence. Mol. Microbiol. 56:525-534.
    • (2005) Mol. Microbiol. , vol.56 , pp. 525-534
    • Yamamoto, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.