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Volumn 9, Issue 3, 2014, Pages

Streptococcus iniae SF1: Complete genome sequence, proteomic profile, and immunoprotective antigens

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; AGGLUTININ RECEPTOR; ALKALINE AMYLOPULLULANASE; ALPHA HEMOLYSIN; AMIDASE; AUTOLYSIN; BACTERIAL ANTIGEN; BACTERIAL ENZYME; CAMP FACTOR; COLLAGEN BINDING PROTEIN; EXOENZYME; GLYCOSYLTRANSFERASE; IMMUNOGLOBULIN BINDING FACTOR; LMB GENE; LYSOZYME; PEPTIDASE C5; PROTEINASE; SERINE RICH GLYCOPROTEIN ADHESIN; SIM PROTEIN; STREPTOLYSIN S; UNCLASSIFIED DRUG; ZN PROTEASE; BACTERIAL PROTEIN; BACTERIAL VACCINE; RECOMBINANT VACCINE; VIRULENCE FACTOR;

EID: 84897989441     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0091324     Document Type: Article
Times cited : (41)

References (111)
  • 1
    • 34247120555 scopus 로고    scopus 로고
    • Streptococcus iniae: An aquatic pathogen of global veterinary significance and a challenging candidate for reliable vaccination
    • DOI 10.1016/j.vetmic.2007.03.002, PII S0378113507001356
    • Agnew W, Barnes AC (2007) Streptococcus iniae: an aquatic pathogen of global veterinary significance and a challenging candidate for reliable vaccination. Vet Microbiol 122: 1-15. (Pubitemid 46589915)
    • (2007) Veterinary Microbiology , vol.122 , Issue.1-2 , pp. 1-15
    • Agnew, W.1    Barnes, A.C.2
  • 2
    • 84897997458 scopus 로고    scopus 로고
    • Streptococcus diseases of farmed marine fish
    • Du J (2001) Streptococcus diseases of farmed marine fish. Modern Fisheries 5: 28-29.
    • (2001) Modern Fisheries , vol.5 , pp. 28-29
    • Du, J.1
  • 3
    • 33747807588 scopus 로고    scopus 로고
    • Streptococcus iniae: An emerging pathogen in the aquaculture industry
    • Low DE, Liu E FJ, McGeer A (1999) Streptococcus iniae: an emerging pathogen in the aquaculture industry. Emerging infections: 53-66.
    • (1999) Emerging Infections , pp. 53-66
    • Low, D.E.1    Liu, E.F.J.2    McGeer, A.3
  • 4
    • 73949121153 scopus 로고    scopus 로고
    • Towards control of Streptococcus iniae
    • Baiano JC, Barnes AC (2009) Towards control of Streptococcus iniae. Emerg Infect Dis 15: 1891-1896.
    • (2009) Emerg Infect Dis , vol.15 , pp. 1891-1896
    • Baiano, J.C.1    Barnes, A.C.2
  • 5
    • 84861153316 scopus 로고    scopus 로고
    • CpsY influences Streptococcus iniae cell wall adaptations important for neutrophil intracellular survival
    • Allen JP, Neely MN (2012) CpsY influences Streptococcus iniae cell wall adaptations important for neutrophil intracellular survival. Infect Immun 80: 1707-1715.
    • (2012) Infect Immun , vol.80 , pp. 1707-1715
    • Allen, J.P.1    Neely, M.N.2
  • 6
    • 44049087544 scopus 로고    scopus 로고
    • Identification and molecular characterisation of a fibrinogen binding protein from Streptococcus iniae
    • Baiano JC, Tumbol RA, Umapathy A, Barnes AC (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, J.C.1    Tumbol, R.A.2    Umapathy, A.3    Barnes, A.C.4
  • 8
    • 0036785660 scopus 로고    scopus 로고
    • Identification of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease
    • Fuller JD, Camus AC, Duncan CL, Nizet V, Bast DJ, et al. (2002) Identification of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease. Infect Immun 70: 5730-5739.
    • (2002) Infect Immun , vol.70 , pp. 5730-5739
    • Fuller, J.D.1    Camus, A.C.2    Duncan, C.L.3    Nizet, V.4    Bast, D.J.5
  • 9
    • 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 JB, Aziz RK, Vicknair MR, Nizet V, Buchanan JT (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, J.T.5
  • 10
    • 77949623035 scopus 로고    scopus 로고
    • A pivotal role for the Streptococcus iniae extracellular polysaccharide in triggering proinflammatory cytokines transcription and inducing death in rainbow trout
    • Eyngor M, Lublin A, Shapira R, Hurvitz A, Zlotkin A, et al. (2010) A pivotal role for the Streptococcus iniae extracellular polysaccharide in triggering proinflammatory cytokines transcription and inducing death in rainbow trout. FEMS Microbiol Lett 305: 109-120.
    • (2010) FEMS Microbiol Lett , vol.305 , pp. 109-120
    • Eyngor, M.1    Lublin, A.2    Shapira, R.3    Hurvitz, A.4    Zlotkin, A.5
  • 11
    • 76449098700 scopus 로고    scopus 로고
    • The novel polysaccharide deacetylase homologue Pdi contributes to virulence of the aquatic pathogen Streptococcus iniae
    • Milani CJ, Aziz RK, Locke JB, Dahesh S, Nizet V, et al. (2010) The novel polysaccharide deacetylase homologue Pdi contributes to virulence of the aquatic pathogen Streptococcus iniae. Microbiology 156: 543-554.
    • (2010) Microbiology , vol.156 , pp. 543-554
    • Milani, C.J.1    Aziz, R.K.2    Locke, J.B.3    Dahesh, S.4    Nizet, V.5
  • 13
    • 33847741407 scopus 로고    scopus 로고
    • Analysis of the polysaccharide capsule of the systemic pathogen Streptococcus iniae and its implications in virulence
    • DOI 10.1128/IAI.01484-06
    • Lowe BA, Miller JD, Neely MN (2007) Analysis of the polysaccharide capsule of the systemic pathogen Streptococcus iniae and its implications in virulence. Infect Immun 75: 1255-1264. (Pubitemid 46385817)
    • (2007) Infection and Immunity , vol.75 , Issue.3 , pp. 1255-1264
    • Lowe, B.A.1    Miller, J.D.2    Neely, M.N.3
  • 14
    • 12844276013 scopus 로고    scopus 로고
    • Large-scale screen highlights the importance of capsule for virulence in the zoonotic pathogen Streptococcus iniae
    • DOI 10.1128/IAI.73.2.921-934.2005
    • Miller JD, Neely MN (2005) Large-scale screen highlights the importance of capsule for virulence in the zoonotic pathogen Streptococcus iniae. Infect Immun 73: 921-934. (Pubitemid 40165751)
    • (2005) Infection and Immunity , vol.73 , Issue.2 , pp. 921-934
    • Miller, J.D.1    Neely, M.N.2
  • 15
    • 84872178149 scopus 로고    scopus 로고
    • The conserved surface M-protein SiMA of Streptococcus iniae is not effective as a cross-protective vaccine against differing capsular serotypes in farmed fish
    • Aviles F, Zhang MM, Chan J, Delamare-Deboutteville J, Green TJ, et al. (2013) The conserved surface M-protein SiMA of Streptococcus iniae is not effective as a cross-protective vaccine against differing capsular serotypes in farmed fish. Vet Microbiol 162: 151-159.
    • (2013) Vet Microbiol , vol.162 , pp. 151-159
    • Aviles, F.1    Zhang, M.M.2    Chan, J.3    Delamare-Deboutteville, J.4    Green, T.J.5
  • 16
    • 0035434675 scopus 로고    scopus 로고
    • Recovery of Streptococcus iniae from Diseased Fish Previously Vaccinated with a Streptococcus Vaccine
    • DOI 10.1128/AEM.67.8.3756-3758.2001
    • Bachrach G, Zlotkin A, Hurvitz A, Evans DL, Eldar A (2001) Recovery of Streptococcus iniae from diseased fish previously vaccinated with a streptococcus vaccine. Appl Environ Microbiol 67: 3756-3758. (Pubitemid 33641257)
    • (2001) Applied and Environmental Microbiology , vol.67 , Issue.8 , pp. 3756-3758
    • Bachrach, G.1    Zlotkin, A.2    Hurvitz, A.3    Evans, D.L.4    Eldar, A.5
  • 17
    • 0037468277 scopus 로고    scopus 로고
    • Streptococcus iniae: Serological differences, presence of capsule and resistance to immune serum killing
    • Barnes AC, Young FM, Horne MT, Ellis AE (2003) Streptococcus iniae: serological differences, presence of capsule and resistance to immune serum killing. Dis Aquat Organ 53: 241-247. (Pubitemid 36386276)
    • (2003) Diseases of Aquatic Organisms , vol.53 , Issue.3 , pp. 241-247
    • Barnes, A.C.1    Young, F.M.2    Horne, M.T.3    Ellis, A.E.4
  • 18
    • 55949120560 scopus 로고    scopus 로고
    • Emergence of novel Streptococcus iniae exopolysaccharide-producing strains following vaccination with nonproducing strains
    • Eyngor M, Tekoah Y, Shapira R, Hurvitz A, Zlotkin A, et al. (2008) Emergence of novel Streptococcus iniae exopolysaccharide-producing strains following vaccination with nonproducing strains. Appl Environ Microbiol 74: 6892-6897.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6892-6897
    • Eyngor, M.1    Tekoah, Y.2    Shapira, R.3    Hurvitz, A.4    Zlotkin, A.5
  • 19
    • 84870802228 scopus 로고    scopus 로고
    • Evolution of the capsular operon of Streptococcus iniae in response to vaccination
    • Millard CM, Baiano JC, Chan C, Yuen B, Aviles F, et al. (2012) Evolution of the capsular operon of Streptococcus iniae in response to vaccination. Appl Environ Microbiol 78: 8219-8226.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 8219-8226
    • Millard, C.M.1    Baiano, J.C.2    Chan, C.3    Yuen, B.4    Aviles, F.5
  • 20
    • 41049090813 scopus 로고    scopus 로고
    • Genetic variability amongst Streptococcus iniae isolates from Australia
    • DOI 10.1111/j.1365-2761.2007.00880.x
    • Nawawi RA, Baiano J, Barnes AC (2008) Genetic variability amongst Streptococcus iniae isolates from Australia. J Fish Dis 31: 305-309. (Pubitemid 351421766)
    • (2008) Journal of Fish Diseases , vol.31 , Issue.4 , pp. 305-309
    • Nawawi, R.A.1    Baiano, J.2    Barnes, A.C.3
  • 21
    • 77649189039 scopus 로고    scopus 로고
    • Identification and immunoprotective analysis of a Streptococcus iniae subunit vaccine candidate
    • Cheng S, Hu YH, Jiao XD, Sun L (2010) Identification and immunoprotective analysis of a Streptococcus iniae subunit vaccine candidate. Vaccine 28: 2636-2641.
    • (2010) Vaccine , vol.28 , pp. 2636-2641
    • Cheng, S.1    Hu, Y.H.2    Jiao, X.D.3    Sun, L.4
  • 22
    • 34248162825 scopus 로고    scopus 로고
    • Cloning, characterization, and molecular application of a beta-agarase gene from Vibrio sp. strain V134
    • Zhang WW, Sun L (2007) Cloning, characterization, and molecular application of a beta-agarase gene from Vibrio sp. strain V134. Appl Environ Microbiol 73: 2825-2831.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2825-2831
    • Zhang, W.W.1    Sun, L.2
  • 24
    • 34147132825 scopus 로고    scopus 로고
    • Identifying bacterial genes and endosymbiont DNA with Glimmer
    • DOI 10.1093/bioinformatics/btm009
    • Delcher AL, Bratke KA, Powers EC, Salzberg SL (2007) Identifying bacterial genes and endosymbiont DNA with Glimmer. Bioinformatics 23: 673-679. (Pubitemid 46554717)
    • (2007) Bioinformatics , vol.23 , Issue.6 , pp. 673-679
    • Delcher, A.L.1    Bratke, K.A.2    Powers, E.C.3    Salzberg, S.L.4
  • 25
    • 34247218466 scopus 로고    scopus 로고
    • Allergens as eukaryotic proteins lacking bacterial homologues
    • DOI 10.1016/j.molimm.2007.01.019, PII S0161589007000454
    • Emanuelsson C, Spangfort MD (2007) Allergens as eukaryotic proteins lacking bacterial homologues. Mol Immunol 44: 3256-3260. (Pubitemid 46610500)
    • (2007) Molecular Immunology , vol.44 , Issue.12 , pp. 3256-3260
    • Emanuelsson, C.1    Spangfort, M.D.2
  • 26
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: A program for improved detection of transfer RNA genes in genomic sequence
    • DOI 10.1093/nar/25.5.955
    • Lowe TM, Eddy SR (1997) tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res 25: 955-964. (Pubitemid 27298263)
    • (1997) Nucleic Acids Research , vol.25 , Issue.5 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 32
    • 84883422663 scopus 로고    scopus 로고
    • Megalocytivirus-induced proteins of turbot (Scophthalmus maximus): Identification and antiviral potential
    • Zhang J, Hu YH, Xiao ZZ, Sun L (2013) Megalocytivirus-induced proteins of turbot (Scophthalmus maximus): Identification and antiviral potential. J Proteomics 91C: 430-443.
    • (2013) J Proteomics , vol.91 C , pp. 430-443
    • Zhang, J.1    Hu, Y.H.2    Xiao, Z.Z.3    Sun, L.4
  • 33
    • 77951101672 scopus 로고    scopus 로고
    • Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)
    • Zheng WJ, Hu YH, Xiao ZZ, Sun L (2010) Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus) . Fish Shellfish Immunol 28: 829-836.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 829-836
    • Zheng, W.J.1    Hu, Y.H.2    Xiao, Z.Z.3    Sun, L.4
  • 34
    • 84884989819 scopus 로고    scopus 로고
    • SmCCL19, a CC chemokine of turbot (Scophthalmus maximus), induces leukocyte trafficking and promotes antiviral and anti-bacterial defense
    • Chen C, Hu YH, Xiao ZZ, Sun L (2013) SmCCL19, a CC chemokine of turbot (Scophthalmus maximus), induces leukocyte trafficking and promotes antiviral and anti-bacterial defense. Fish Shellfish Immunol 35: 1677-1682.
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 1677-1682
    • Chen, C.1    Hu, Y.H.2    Xiao, Z.Z.3    Sun, L.4
  • 35
    • 75249100656 scopus 로고    scopus 로고
    • Comparative study of the effects of aluminum adjuvants and Freund's incomplete adjuvant on the immune response to an Edwardsiella tarda major antigen
    • Jiao XD, Cheng S, Hu YH, Sun L (2010) Comparative study of the effects of aluminum adjuvants and Freund's incomplete adjuvant on the immune response to an Edwardsiella tarda major antigen. Vaccine 28: 1832-1837.
    • (2010) Vaccine , vol.28 , pp. 1832-1837
    • Jiao, X.D.1    Cheng, S.2    Hu, Y.H.3    Sun, L.4
  • 36
    • 77952422865 scopus 로고    scopus 로고
    • Construction and analysis of an experimental Streptococcus iniae DNA vaccine
    • Sun Y, Hu YH, Liu CS, Sun L (2010) Construction and analysis of an experimental Streptococcus iniae DNA vaccine. Vaccine 28: 3905-3912.
    • (2010) Vaccine , vol.28 , pp. 3905-3912
    • Sun, Y.1    Hu, Y.H.2    Liu, C.S.3    Sun, L.4
  • 37
    • 84898016281 scopus 로고    scopus 로고
    • Whole-genome sequence of the fish virulent strain Streptococcus iniae IUSA-1, isolated from gilthead sea bream (Sparus aurata) and red porgy (Pagrus pagrus)
    • El Aamri F, Acosta F, Real F, Padilla D (2013) Whole-genome sequence of the fish virulent strain Streptococcus iniae IUSA-1, isolated from gilthead sea bream (Sparus aurata) and red porgy (Pagrus pagrus). Genome Announc 1: e0002513.
    • (2013) Genome Announc , vol.1
    • El Aamri, F.1    Acosta, F.2    Real, F.3    Padilla, D.4
  • 41
    • 0032417093 scopus 로고    scopus 로고
    • Base composition skews, replication orientation, and gene orientation in 12 prokaryote genomes
    • DOI 10.1007/PL00006428
    • McLean MJ, Wolfe KH, Devine KM (1998) Base composition skews, replication orientation, and gene orientation in 12 prokaryote genomes. J Mol Evol 47: 691-696. (Pubitemid 29008772)
    • (1998) Journal of Molecular Evolution , vol.47 , Issue.6 , pp. 691-696
    • McLean, M.J.1    Wolfe, K.H.2    Devine, K.M.3
  • 43
    • 35348860808 scopus 로고    scopus 로고
    • A new method for assessing the effect of replication on DNA base composition asymmetry
    • DOI 10.1093/molbev/msm148
    • Necsulea A, Lobry JR (2007) A new method for assessing the effect of replication on DNA base composition asymmetry. Mol Biol Evol 24: 2169-2179. (Pubitemid 47574719)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.10 , pp. 2169-2179
    • Necsulea, A.1    Lobry, J.R.2
  • 44
    • 34250662138 scopus 로고    scopus 로고
    • The CRISPRdb database and tools to display CRISPRs and to generate dictionaries of spacers and repeats
    • Grissa I, Vergnaud G, Pourcel C (2007) The CRISPRdb database and tools to display CRISPRs and to generate dictionaries of spacers and repeats. BMC Bioinformatics 8: 172.
    • (2007) BMC Bioinformatics , vol.8 , pp. 172
    • Grissa, I.1    Vergnaud, G.2    Pourcel, C.3
  • 47
    • 64049118040 scopus 로고    scopus 로고
    • Short motif sequences determine the targets of the prokaryotic CRISPR defence system
    • Mojica FJ, Diez-Villasenor C, Garcia-Martinez J, Almendros C (2009) Short motif sequences determine the targets of the prokaryotic CRISPR defence system. Microbiology 155: 733-740.
    • (2009) Microbiology , vol.155 , pp. 733-740
    • Mojica, F.J.1    Diez-Villasenor, C.2    Garcia-Martinez, J.3    Almendros, C.4
  • 48
    • 34248374277 scopus 로고    scopus 로고
    • A putative RNA-interference-based immune system in prokaryotes: Computational analysis of the predicted enzymatic machinery, functional analogies with eukaryotic RNAi, and hypothetical mechanisms of action
    • Makarova KS, Grishin NV, Shabalina SA, Wolf YI, Koonin EV (2006) A putative RNA-interference-based immune system in prokaryotes: computational analysis of the predicted enzymatic machinery, functional analogies with eukaryotic RNAi, and hypothetical mechanisms of action. Biol Direct 1: 7.
    • (2006) Biol Direct , vol.1 , pp. 7
    • Makarova, K.S.1    Grishin, N.V.2    Shabalina, S.A.3    Wolf, Y.I.4    Koonin, E.V.5
  • 49
    • 34248400310 scopus 로고    scopus 로고
    • A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes
    • Haft DH, Selengut J, Mongodin EF, Nelson KE (2005) A guild of 45 CRISPR-associated (Cas) protein families and multiple CRISPR/Cas subtypes exist in prokaryotic genomes. PLoS Comput Biol 1: e60.
    • (2005) PLoS Comput Biol , vol.1
    • Haft, D.H.1    Selengut, J.2    Mongodin, E.F.3    Nelson, K.E.4
  • 52
    • 1542397137 scopus 로고    scopus 로고
    • Phage integrases: Biology and applications
    • DOI 10.1016/j.jmb.2003.09.082, PII S0022283603013561
    • Groth AC, Calos MP (2004) Phage integrases: biology and applications. J Mol Biol 335: 667-678. (Pubitemid 38352810)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.3 , pp. 667-678
    • Groth, A.C.1    Calos, M.P.2
  • 53
    • 53849090635 scopus 로고    scopus 로고
    • A conserved antirepressor controls horizontal gene transfer by proteolysis
    • Bose B, Auchtung JM, Lee CA, Grossman AD (2008) A conserved antirepressor controls horizontal gene transfer by proteolysis. Mol Microbiol 70: 570-582.
    • (2008) Mol Microbiol , vol.70 , pp. 570-582
    • Bose, B.1    Auchtung, J.M.2    Lee, C.A.3    Grossman, A.D.4
  • 54
    • 80052246919 scopus 로고    scopus 로고
    • Inhibitory activity of Lactobacillus plantarum LMG P-26358 against Listeria innocua when used as an adjunct starter in the manufacture of cheese
    • Mills S, Serrano LM, Griffin C, O'Connor PM, Schaad G, et al. (2011) Inhibitory activity of Lactobacillus plantarum LMG P-26358 against Listeria innocua when used as an adjunct starter in the manufacture of cheese.Microb Cell Fact10: S7.
    • (2011) Microb Cell Fact , vol.10
    • Mills, S.1    Serrano, L.M.2    Griffin, C.3    O'Connor, P.M.4    Schaad, G.5
  • 55
    • 78449236189 scopus 로고    scopus 로고
    • Genome sequence of the temperate bacteriophage PH10 from Streptococcus oralis
    • van der Ploeg JR (2010) Genome sequence of the temperate bacteriophage PH10 from Streptococcus oralis. Virus Genes 41: 450-458.
    • (2010) Virus Genes , vol.41 , pp. 450-458
    • Van Der Ploeg, J.R.1
  • 56
    • 0037125989 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae
    • Tettelin H, Masignani V, Cieslewicz MJ, Eisen JA, Peterson S, et al. (2002) Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae. Proc Natl Acad Sci U S A 99: 12391-12396.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 12391-12396
    • Tettelin, H.1    Masignani, V.2    Cieslewicz, M.J.3    Eisen, J.A.4    Peterson, S.5
  • 58
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • Wang IN, Smith DL, Young R (2000) Holins: the protein clocks of bacteriophage infections. Annu Rev Microbiol 54: 799-825.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 59
    • 34247849321 scopus 로고    scopus 로고
    • YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis
    • DOI 10.1128/JB.01936-06
    • Szurmant H, Mohan MA, Imus PM, Hoch JA (2007) YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis. J Bacteriol 189: 3280-3289. (Pubitemid 46697418)
    • (2007) Journal of Bacteriology , vol.189 , Issue.8 , pp. 3280-3289
    • Szurmant, H.1    Mohan, M.A.2    Imus, P.M.3    Hoch, J.A.4
  • 61
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • DOI 10.1128/MMBR.00020-06
    • Mascher T, Helmann JD, Unden G (2006) Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol Mol Biol Rev 70: 910-938. (Pubitemid 44958261)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.4 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 63
    • 0035794713 scopus 로고    scopus 로고
    • Molecular basis of thermosensing: A two-component signal transduction thermometer in bacillus subtilis
    • DOI 10.1093/emboj/20.7.1681
    • Aguilar PS, Hernandez-Arriaga AM, Cybulski LE, Erazo AC, de Mendoza D (2001) Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis. EMBO J 20: 1681-1691. (Pubitemid 32299405)
    • (2001) EMBO Journal , vol.20 , Issue.7 , pp. 1681-1691
    • Aguilar, P.S.1    Hernandez-Arriaga, A.M.2    Cybulski, L.E.3    Erazo, A.C.4    De Mendoza, D.5
  • 64
    • 1942443703 scopus 로고    scopus 로고
    • The Membrane Fluidity Sensor DesK of Bacillus subtilis Controls the Signal Decay of Its Cognate Response Regulator
    • DOI 10.1128/JB.186.9.2655-2663.2004
    • Albanesi D, Mansilla MC, de Mendoza D (2004) The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator. J Bacteriol 186: 2655-2663. (Pubitemid 38525919)
    • (2004) Journal of Bacteriology , vol.186 , Issue.9 , pp. 2655-2663
    • Albanesi, D.1    Mansilla, M.C.2    De Mendoza, D.3
  • 65
    • 3342944909 scopus 로고    scopus 로고
    • Inactivation of the ciaH gene in Streptococcus mutans diminishes mutacin production and competence development, alters sucrose-dependent biofilm formation, and reduces stress tolerance
    • DOI 10.1128/IAI.72.8.4895-4899.2004
    • Qi F, Merritt J, Lux R, Shi W (2004) Inactivation of the ciaH gene in Streptococcus mutans diminishes mutacin production and competence development, alters sucrose-dependent biofilm formation, and reduces stress tolerance. Infect Immun 72: 4895-4899. (Pubitemid 38989355)
    • (2004) Infection and Immunity , vol.72 , Issue.8 , pp. 4895-4899
    • Qi, F.1    Merritt, J.2    Lux, R.3    Shi, W.4
  • 66
    • 37549063380 scopus 로고    scopus 로고
    • Involvement of sensor kinases in the stress tolerance response of Streptococcus mutans
    • Biswas I, Drake L, Erkina D, Biswas S (2008) Involvement of sensor kinases in the stress tolerance response of Streptococcus mutans. J Bacteriol 190: 68-77.
    • (2008) J Bacteriol , vol.190 , pp. 68-77
    • Biswas, I.1    Drake, L.2    Erkina, D.3    Biswas, S.4
  • 67
    • 64049107725 scopus 로고    scopus 로고
    • The CiaR response regulator in group B Streptococcus promotes intracellular survival and resistance to innate immune defenses
    • Quach D, van Sorge NM, Kristian SA, Bryan JD, Shelver DW, et al. (2009) The CiaR response regulator in group B Streptococcus promotes intracellular survival and resistance to innate immune defenses. J Bacteriol 191: 2023-2032.
    • (2009) J Bacteriol , vol.191 , pp. 2023-2032
    • Quach, D.1    Van Sorge, N.M.2    Kristian, S.A.3    Bryan, J.D.4    Shelver, D.W.5
  • 69
    • 33846896349 scopus 로고    scopus 로고
    • The Streptococcus mutans vicX gene product modulates gtfB/C expression, biofilm formation, genetic competence, and oxidative stress tolerance
    • DOI 10.1128/JB.01161-06
    • Senadheera MD, Lee AW, Hung DC, Spatafora GA, Goodman SD, et al. (2007) The Streptococcus mutans vicX gene product modulates gtfB/C expression, biofilm formation, genetic competence, and oxidative stress tolerance. J Bacteriol 189: 1451-1458. (Pubitemid 46239767)
    • (2007) Journal of Bacteriology , vol.189 , Issue.4 , pp. 1451-1458
    • Senadheera, M.D.1    Lee, A.W.C.2    Hung, D.C.I.3    Spatafora, G.A.4    Goodman, S.D.5    Cvitkovitch, D.G.6
  • 70
    • 70350438457 scopus 로고    scopus 로고
    • Inactivation of VicK affects acid production and acid survival of Streptococcus mutans
    • Senadheera D, Krastel K, Mair R, Persadmehr A, Abranches J, et al. (2009) Inactivation of VicK affects acid production and acid survival of Streptococcus mutans. J Bacteriol 191: 6415-6424.
    • (2009) J Bacteriol , vol.191 , pp. 6415-6424
    • Senadheera, D.1    Krastel, K.2    Mair, R.3    Persadmehr, A.4    Abranches, J.5
  • 71
    • 0032911313 scopus 로고    scopus 로고
    • Two-component signal transduction in Bacillus subtilis: How one organism sees its world
    • Fabret C, Feher VA, Hoch JA (1999) Two-component signal transduction in Bacillus subtilis: how one organism sees its world. J Bacteriol 181: 1975-1983. (Pubitemid 29164948)
    • (1999) Journal of Bacteriology , vol.181 , Issue.7 , pp. 1975-1983
    • Fabret, C.1    Feher, V.A.2    Hoch, J.A.3
  • 72
    • 80053341745 scopus 로고    scopus 로고
    • Molecular insights into the control of transcription initiation at the Staphylococcus aureus agr operon
    • Reynolds J, Wigneshweraraj S (2011) Molecular insights into the control of transcription initiation at the Staphylococcus aureus agr operon. J Mol Biol 412: 862-881.
    • (2011) J Mol Biol , vol.412 , pp. 862-881
    • Reynolds, J.1    Wigneshweraraj, S.2
  • 74
    • 0004067952 scopus 로고    scopus 로고
    • (the third edition). Beijing: Higher Education Press
    • Wang JY, Zhu SG, Xu CF (2002) Biochemistry (the third edition). Beijing: Higher Education Press. 151p.
    • (2002) Biochemistry , pp. 151
    • Wang, J.Y.1    Zhu, S.G.2    Xu, C.F.3
  • 76
    • 0344393465 scopus 로고    scopus 로고
    • Physiological Characterization of a Heme-Deficient Mutant of Staphylococcus aureus by a Proteomic Approach
    • DOI 10.1128/JB.185.23.6928-6937.2003
    • Kohler C, von Eiff C, Peters G, Proctor RA, Hecker M, et al. (2003) Physiological characterization of a heme-deficient mutant of Staphylococcus aureus by a proteomic approach. J Bacteriol 185: 6928-6937. (Pubitemid 37444495)
    • (2003) Journal of Bacteriology , vol.185 , Issue.23 , pp. 6928-6937
    • Kohler, C.1    Von Eiff, C.2    Peters, G.3    Proctor, R.A.4    Hecker, M.5    Engelmann, S.6
  • 77
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • DOI 10.1016/0304-4157(95)00017-8
    • Moller JV, Juul B, leMaire M (1996) Structural organization, ion transport, and energy transduction of P-type ATPases. Bba-Rev Biomembranes 1286: 1-51. (Pubitemid 26188366)
    • (1996) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1286 , Issue.1 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Le, M.M.3
  • 79
    • 0033886560 scopus 로고    scopus 로고
    • Families of transmembrane transporters selective for amino acids and their derivatives
    • Saier MH (2000) Families of transmembrane transporters selective for amino acids and their derivatives. Microbiology 146: 1775-1795.
    • (2000) Microbiology , vol.146 , pp. 1775-1795
    • Saier, M.H.1
  • 80
    • 0024198129 scopus 로고
    • Evidence for high-affinity binding-protein dependent transport-systems in Gram-positive bacteria and in mycoplasma
    • Gilson E, Alloing G, Schmidt T, Claverys JP, Dudler R, et al. (1988) Evidence for high-affinity binding-protein dependent transport-systems in Gram-positive bacteria and in mycoplasma. Embo J7: 3971-3974.
    • (1988) Embo , vol.J7 , pp. 3971-3974
    • Gilson, E.1    Alloing, G.2    Schmidt, T.3    Claverys, J.P.4    Dudler, R.5
  • 81
    • 84862234673 scopus 로고    scopus 로고
    • Antibiotic transport in resistant bacteria: Synchrotron UV fluorescence microscopy to determine antibiotic accumulation with single cell resolution
    • Kascakova S, Maigre L, Chevalier J, Refregiers M, Pages JM (2012) Antibiotic transport in resistant bacteria: synchrotron UV fluorescence microscopy to determine antibiotic accumulation with single cell resolution. Plos One 7: e38624.
    • (2012) Plos One , vol.7
    • Kascakova, S.1    Maigre, L.2    Chevalier, J.3    Refregiers, M.4    Pages, J.M.5
  • 82
    • 33749575659 scopus 로고    scopus 로고
    • Manganese transport and the role of manganese in virulence
    • DOI 10.1146/annurev.micro.60.080805.142149
    • Papp-Wallace KM, Maguire ME (2006) Manganese transport and the role of manganese in virulence. Annu Rev Microbiol 60: 187-209. (Pubitemid 44627946)
    • (2006) Annual Review of Microbiology , vol.60 , pp. 187-209
    • Papp-Wallace, K.M.1    Maguire, M.E.2
  • 85
    • 27944435773 scopus 로고    scopus 로고
    • Utilization of putrescine by Streptococcus pneumoniae during growth in choline-limited medium
    • Ware D, Watt J, Swiatlo E (2005) Utilization of putrescine by Streptococcus pneumoniae during growth in choline-limited medium. J Microbiol 43: 398-405. (Pubitemid 41666878)
    • (2005) Journal of Microbiology , vol.43 , Issue.5 , pp. 398-405
    • Ware, D.1    Watt, J.2    Swiatlo, E.3
  • 86
    • 84861904854 scopus 로고    scopus 로고
    • VFDB 2012 update: Toward the genetic diversity and molecular evolution of bacterial virulence factors
    • Chen LH, Xiong ZH, Sun LL, Yang J, Jin Q (2012) VFDB 2012 update: toward the genetic diversity and molecular evolution of bacterial virulence factors. Nucleic Acids Res 40: D641-D645.
    • (2012) Nucleic Acids Res , vol.40
    • Chen, L.H.1    Xiong, Z.H.2    Sun, L.L.3    Yang, J.4    Jin, Q.5
  • 88
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham MW (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
  • 89
    • 77956362798 scopus 로고    scopus 로고
    • ApuA, a multifunctional alpha-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus
    • Ferrando ML, Fuentes S, de Greeff A, Smith H, Wells JM (2010) ApuA, a multifunctional alpha-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus. Microbiology 156: 2818-2828.
    • (2010) Microbiology , vol.156 , pp. 2818-2828
    • Ferrando, M.L.1    Fuentes, S.2    De Greeff, A.3    Smith, H.4    Wells, J.M.5
  • 90
    • 0343962600 scopus 로고    scopus 로고
    • Biological roles of two new murein hydrolases of Streptococcus pneumoniae representing examples of module shuffling
    • DOI 10.1016/S0923-2508(00)00172-8
    • Lopez R, Gonzalez MP, Garcia E, Garcia JL, Garcia P (2000) Biological roles of two new murein hydrolases of Streptococcus pneumoniae representing examples of module shuffling. Res Microbiol 151: 437-443. (Pubitemid 30619795)
    • (2000) Research in Microbiology , vol.151 , Issue.6 , pp. 437-443
    • Lopez, R.1    P, G.M.2    Garcia, E.3    L, G.J.4    Garcia, P.5
  • 91
    • 19744378673 scopus 로고    scopus 로고
    • Identification and characterization of an autolysin-e cncoding gene of Streptococcus mutans
    • DOI 10.1128/IAI.73.6.3512-3520.2005
    • Shibata Y, Kawada M, Nakano Y, Toyoshima K, Yamashita Y (2005) Identification and characterization of an autolysin-encoding gene of Streptococcus mutans. Infect Immun 73: 3512-3520. (Pubitemid 40745895)
    • (2005) Infection and Immunity , vol.73 , Issue.6 , pp. 3512-3520
    • Shibata, Y.1    Kawada, M.2    Nakano, Y.3    Toyoshima, K.4    Yamashita, Y.5
  • 92
    • 0019214958 scopus 로고
    • Antibiotic-tolerant mutants of Streptococcus pneumoniae that are not deficient in autolytic activity
    • Williamson R, Tomasz A (1980) Antibiotic-tolerant mutants of Streptococcus pneumoniae that are not deficient in autolytic activity. J Bacteriol 144: 105-113. (Pubitemid 11208812)
    • (1980) Journal of Bacteriology , vol.144 , Issue.1 , pp. 105-113
    • Williamson, R.1    Tomasz, A.2
  • 93
    • 48649083759 scopus 로고    scopus 로고
    • The IL-8 protease SpyCEP/ScpC of group A Streptococcus promotes resistance to neutrophil killing
    • Zinkernagel AS, Timmer AM, Pence MA, Locke JB, Buchanan JT, et al. (2008) The IL-8 protease SpyCEP/ScpC of group A Streptococcus promotes resistance to neutrophil killing. Cell Host Microbe 4: 170-178.
    • (2008) Cell Host Microbe , vol.4 , pp. 170-178
    • Zinkernagel, A.S.1    Timmer, A.M.2    Pence, M.A.3    Locke, J.B.4    Buchanan, J.T.5
  • 94
    • 0032476656 scopus 로고    scopus 로고
    • A role for Trigger Factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • DOI 10.1093/emboj/17.21.6263
    • Lyon WR, Gibson CM, Caparon MG (1998) A role for trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. Embo Journal 17: 6263-6275. (Pubitemid 28497799)
    • (1998) EMBO Journal , vol.17 , Issue.21 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 95
    • 0038623056 scopus 로고    scopus 로고
    • Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease
    • DOI 10.1128/JB.185.12.3661-3667.2003
    • Lyon WR, Caparon MG (2003) Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease. J Bacteriol 185: 3661-3667. (Pubitemid 36676433)
    • (2003) Journal of Bacteriology , vol.185 , Issue.12 , pp. 3661-3667
    • Lyon, W.R.1    Caparon, M.G.2
  • 96
    • 0141755375 scopus 로고    scopus 로고
    • Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin
    • Lang SH, Palmer M (2003) Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin. J Biol Chem278: 38167-38173.
    • (2003) J Biol Chem , vol.278 , pp. 38167-38173
    • Lang, S.H.1    Palmer, M.2
  • 97
    • 0023265348 scopus 로고
    • Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity
    • DOI 10.1084/jem.165.3.720
    • Jurgens D, Sterzik B, Fehrenbach FJ (1987) Unspecific binding of Group-B Streptococcal cocytolysin (Camp Factor) to immunoglobulins and its possible role in pathogenicity. J Exp Med165: 720-732. (Pubitemid 17059449)
    • (1987) Journal of Experimental Medicine , vol.165 , Issue.3 , pp. 720-732
    • Jurgens, D.1    Sterzik, B.2    Fehrenbach, F.J.3
  • 99
    • 0034931519 scopus 로고    scopus 로고
    • alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • DOI 10.1046/j.1365-2958.2001.02448.x
    • Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S (2001) alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40: 1273-1287. (Pubitemid 32635298)
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 100
    • 53449101619 scopus 로고    scopus 로고
    • Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis
    • Esgleas M, Li Y, Hancock MA, Harel J, Dubreuil JD, et al. (2008) Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis. Microbiology 154: 2668-2679.
    • (2008) Microbiology , vol.154 , pp. 2668-2679
    • Esgleas, M.1    Li, Y.2    Hancock, M.A.3    Harel, J.4    Dubreuil, J.D.5
  • 101
    • 0346445147 scopus 로고    scopus 로고
    • Extracellular virulence factors of Streptococcus pneumoniae
    • Jedrzejas MJ (2004) Extracellular virulence factors of Streptococcus pneumoniae. Front Biosci 9: 891-914.
    • (2004) Front Biosci , vol.9 , pp. 891-914
    • Jedrzejas, M.J.1
  • 102
    • 80052704944 scopus 로고    scopus 로고
    • Differential secretomics of Streptococcus pyogenes reveals a novel peroxide regulator (PerR)-regulated extracellular virulence factor mitogen factor 3 (MF3)
    • Wen YT, Tsou CC, Kuo HT, Wang JS, Wu JJ, et al. (2011) Differential secretomics of Streptococcus pyogenes reveals a novel peroxide regulator (PerR)-regulated extracellular virulence factor mitogen factor 3 (MF3). Mol Cell Proteomics 10: M110 007013.
    • (2011) Mol Cell Proteomics , vol.10
    • Wen, Y.T.1    Tsou, C.C.2    Kuo, H.T.3    Wang, J.S.4    Wu, J.J.5
  • 103
    • 0038647338 scopus 로고    scopus 로고
    • Effect of Varidase (streptodornase) on biofilm formed by Pseudomonas aeruginosa
    • DOI 10.1159/000070617
    • Nemoto K, Hirota K, Murakami K, Taniguti K, Murata H, et al. (2003) Effect of Varidase (streptodornase) on biofilm formed by Pseudomonas aeruginosa. Chemotherapy 49: 121-125. (Pubitemid 36736932)
    • (2003) Chemotherapy , vol.49 , Issue.3 , pp. 121-125
    • Nemoto, K.1    Hirota, K.2    Murakami, K.3    Taniguti, K.4    Murata, H.5    Viducic, D.6    Miyake, Y.7
  • 104
    • 80051471277 scopus 로고    scopus 로고
    • Exposure of Thomsen-Friedenreich antigen in Streptococcus pneumoniae infection is dependent on pneumococcal neuraminidase A
    • Coats MT, Murphy T, Paton JC, Gray B, Briles DE (2011) Exposure of Thomsen-Friedenreich antigen in Streptococcus pneumoniae infection is dependent on pneumococcal neuraminidase A. Microb Pathogenesis 50: 343-349.
    • (2011) Microb Pathogenesis , vol.50 , pp. 343-349
    • Coats, M.T.1    Murphy, T.2    Paton, J.C.3    Gray, B.4    Briles, D.E.5
  • 106
    • 3142640828 scopus 로고    scopus 로고
    • Development of antibodies against pneumococcal proteins alpha-enolase, immunoglobulin A1 protease, streptococcal lipoprotein rotamase A, and putative proteinase maturation protein a in relation to pneumococcal carriage and Otitis Media
    • DOI 10.1016/j.vaccine.2004.01.042, PII S0264410X04001124
    • Adrian PV, Bogaert D, Oprins M, Rapola S, Lahdenkari M, et al. (2004) Development of antibodies against pneumococcal proteins alpha-enolase, immunoglobulin A1 protease, streptococcal lipoprotein rotamase A, and putative proteinase maturation protein A in relation to pneumococcal carriage and Otitis Media. Vaccine 22: 2737-2742. (Pubitemid 38900648)
    • (2004) Vaccine , vol.22 , Issue.21-22 , pp. 2737-2742
    • Adrian, P.V.1    Bogaert, D.2    Oprins, M.3    Rapola, S.4    Lahdenkari, M.5    Kilpi, T.6    De Groot, R.7    Kayhty, H.8    Hermans, P.W.M.9
  • 107
    • 58749094631 scopus 로고    scopus 로고
    • Oral therapeutic vaccination with Streptococcus sobrinus recombinant enolase confers protection against dental caries in rats
    • Dinis M, Tavares D, Veiga-Malta I, Fonseca AJ, Andrade EB, et al. (2009) Oral therapeutic vaccination with Streptococcus sobrinus recombinant enolase confers protection against dental caries in rats. J Infect Dis 199: 116-123.
    • (2009) J Infect Dis , vol.199 , pp. 116-123
    • Dinis, M.1    Tavares, D.2    Veiga-Malta, I.3    Fonseca, A.J.4    Andrade, E.B.5
  • 108
    • 59649104375 scopus 로고    scopus 로고
    • Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2
    • Zhang A, Chen B, Mu X, Li R, Zheng P, et al. (2009) Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2. Vaccine 27: 1348-1353.
    • (2009) Vaccine , vol.27 , pp. 1348-1353
    • Zhang, A.1    Chen, B.2    Mu, X.3    Li, R.4    Zheng, P.5
  • 109
    • 0029946701 scopus 로고    scopus 로고
    • Recombinant neuraminidase vaccine protects against lethal influenza
    • DOI 10.1016/0264-410X(95)00157-V
    • Deroo T, Jou WM, Fiers W (1996) Recombinant neuraminidase vaccine protects against lethal influenza. Vaccine 14: 561-569. (Pubitemid 26173757)
    • (1996) Vaccine , vol.14 , Issue.6 , pp. 561-569
    • Deroo, T.1    Min, J.W.2    Fiers, W.3
  • 111
    • 3042687630 scopus 로고    scopus 로고
    • Immunization with native or recombinant Streptococcus pneumoniae neuraminidase affords protection in the chinchilla otitis media model
    • DOI 10.1128/IAI.72.7.4309-4313.2004
    • Long JP, Tong HH, DeMaria TF (2004) Immunization with native or recombinant Streptococcus pneumoniae neuraminidase affords protection in the chinchilla otitis media model. Infect Immun 72: 4309-4313. (Pubitemid 38821951)
    • (2004) Infection and Immunity , vol.72 , Issue.7 , pp. 4309-4313
    • Long, J.P.1    Tong, H.H.2    DeMaria, T.F.3


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