메뉴 건너뛰기




Volumn 10, Issue 11, 2011, Pages 5163-5174

Large-scale identification of bacteria-Host crosstalk by affinity chromatography: Capturing the interactions of streptococcus suis proteins with host cells

Author keywords

affinity chromatography; pathogen host crosstalk; shotgun proteomics; Streptococcus suis; virulence factors

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE PROTEIN; RESIN;

EID: 80655147172     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200758q     Document Type: Article
Times cited : (27)

References (71)
  • 1
    • 0034307834 scopus 로고    scopus 로고
    • The pathogenesis of the meningitis caused by Streptococcus suis: The unresolved questions
    • Gottschalk, M.; Segura, M. The pathogenesis of the meningitis caused by Streptococcus suis: the unresolved questions Vet. Microbiol. 2000, 76 (3) 259-72
    • (2000) Vet. Microbiol. , vol.76 , Issue.3 , pp. 259-72
    • Gottschalk, M.1    Segura, M.2
  • 3
    • 0025837442 scopus 로고
    • A case of human endocarditis due to Streptococcus suis in North America
    • Trottier, S.; Higgins, R.; Brochu, G.; Gottschalk, M. A case of human endocarditis due to Streptococcus suis in North America Rev. Infect. Dis. 1991, 13 (6) 1251-2
    • (1991) Rev. Infect. Dis. , vol.13 , Issue.6 , pp. 1251-2
    • Trottier, S.1    Higgins, R.2    Brochu, G.3    Gottschalk, M.4
  • 4
    • 0023673334 scopus 로고
    • Meningitis caused by Streptococcus suis in humans
    • Arends, J. P.; Zanen, H. C. Meningitis caused by Streptococcus suis in humans Rev. Infect. Dis. 1988, 10 (1) 131-7
    • (1988) Rev. Infect. Dis. , vol.10 , Issue.1 , pp. 131-7
    • Arends, J.P.1    Zanen, H.C.2
  • 5
    • 15744401405 scopus 로고    scopus 로고
    • Biochemical analysis, cpn60 and 16S rDNA sequence data indicate that Streptococcus suis serotypes 32 and 34, isolated from pigs, are Streptococcus orisratti
    • DOI 10.1016/j.vetmic.2005.01.003
    • Hill, J. E.; Gottschalk, M.; Brousseau, R.; Harel, J.; Hemmingsen, S. M.; Goh, S. H. Biochemical analysis, cpn60 and 16S rDNA sequence data indicate that Streptococcus suis serotypes 32 and 34, isolated from pigs, are Streptococcus orisratti Vet. Microbiol. 2005, 107 (1-2) 63-9 (Pubitemid 40417530)
    • (2005) Veterinary Microbiology , vol.107 , Issue.1-2 , pp. 63-69
    • Hill, J.E.1    Gottschalk, M.2    Brousseau, R.3    Harel, J.4    Hemmingsen, S.M.5    Goh, S.H.6
  • 7
    • 67349188374 scopus 로고    scopus 로고
    • Characterization of Streptococcus suis isolates from the diseased pigs in China between 2003 and 2007
    • Wei, Z.; Li, R.; Zhang, A.; He, H.; Hua, Y.; Xia, J.; Cai, X.; Chen, H.; Jin, M. Characterization of Streptococcus suis isolates from the diseased pigs in China between 2003 and 2007 Vet. Microbiol. 2009, 137 (1-2) 196-201
    • (2009) Vet. Microbiol. , vol.137 , Issue.1-2 , pp. 196-201
    • Wei, Z.1    Li, R.2    Zhang, A.3    He, H.4    Hua, Y.5    Xia, J.6    Cai, X.7    Chen, H.8    Jin, M.9
  • 8
    • 0034213785 scopus 로고    scopus 로고
    • Distribution of capsular types and production of muramidase-released protein (MRP) and extracellular factor (EF) of Streptococcus suis strains isolated from diseased pigs in seven European countries
    • DOI 10.1016/S0378-1135(00)00188-7, PII S0378113500001887
    • Wisselink, H. J.; Smith, H. E.; Stockhofe-Zurwieden, N.; Peperkamp, K.; Vecht, U. Distribution of capsular types and production of muramidase-released protein (MRP) and extracellular factor (EF) of Streptococcus suis strains isolated from diseased pigs in seven European countries Vet. Microbiol. 2000, 74 (3) 237-48 (Pubitemid 30252029)
    • (2000) Veterinary Microbiology , vol.74 , Issue.3 , pp. 237-248
    • Wisselink, H.J.1    Smith, H.E.2    Stockhofe-Zurwieden, N.3    Peperkamp, K.4    Vecht, U.5
  • 9
    • 77949393600 scopus 로고    scopus 로고
    • Streptococcus suis: A new emerging or an old neglected zoonotic pathogen?
    • Gottschalk, M.; Xu, J.; Calzas, C.; Segura, M. Streptococcus suis: a new emerging or an old neglected zoonotic pathogen? Future Microbiol. 2010, 5, 371-91
    • (2010) Future Microbiol. , vol.5 , pp. 371-91
    • Gottschalk, M.1    Xu, J.2    Calzas, C.3    Segura, M.4
  • 10
    • 67249147690 scopus 로고    scopus 로고
    • In vivo transcriptional profiling of Listeria monocytogenes and mutagenesis identify new virulence factors involved in infection
    • Camejo, A.; Buchrieser, C.; Couve, E.; Carvalho, F.; Reis, O.; Ferreira, P.; Sousa, S.; Cossart, P.; Cabanes, D. In vivo transcriptional profiling of Listeria monocytogenes and mutagenesis identify new virulence factors involved in infection PLoS Pathog. 2009, 5 (5) e1000449
    • (2009) PLoS Pathog. , vol.5 , Issue.5 , pp. 1000449
    • Camejo, A.1    Buchrieser, C.2    Couve, E.3    Carvalho, F.4    Reis, O.5    Ferreira, P.6    Sousa, S.7    Cossart, P.8    Cabanes, D.9
  • 11
    • 42149116330 scopus 로고    scopus 로고
    • Regulation of whole bacterial pathogen transcription within infected hosts
    • DOI 10.1111/j.1574-6976.2008.00103.x
    • La, M. V.; Raoult, D.; Renesto, P. Regulation of whole bacterial pathogen transcription within infected hosts FEMS Microbiol. Rev. 2008, 32 (3) 440-60 (Pubitemid 351538745)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.3 , pp. 440-460
    • La, M.-V.1    Raoult, D.2    Renesto, P.3
  • 12
    • 77957679027 scopus 로고    scopus 로고
    • Response of swine spleen to Streptococcus suis infection revealed by transcription analysis
    • Li, R.; Zhang, A.; Chen, B.; Teng, L.; Wang, Y.; Chen, H.; Jin, M. Response of swine spleen to Streptococcus suis infection revealed by transcription analysis BMC Genomics 2010, 11, 556
    • (2010) BMC Genomics , vol.11 , pp. 556
    • Li, R.1    Zhang, A.2    Chen, B.3    Teng, L.4    Wang, Y.5    Chen, H.6    Jin, M.7
  • 14
    • 0036180962 scopus 로고    scopus 로고
    • Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2
    • DOI 10.1128/IAI.70.3.1319-1325.2002
    • de Greeff, A.; Buys, H.; Verhaar, R.; Dijkstra, J.; van Alphen, L.; Smith, H. E. Contribution of fibronectin-binding protein to pathogenesis of Streptococcus suis serotype 2 Infect. Immun. 2002, 70 (3) 1319-25 (Pubitemid 34163407)
    • (2002) Infection and Immunity , vol.70 , Issue.3 , pp. 1319-1325
    • De Greeff, A.1    Buys, H.2    Verhaar, R.3    Dijkstra, J.4    Van Alphen, L.5    Smith, H.E.6
  • 15
    • 3843116600 scopus 로고    scopus 로고
    • Cloning and purification of the Streptococcus suis serotype 2 glyceraldehyde-3-phosphate dehydrogenase and its involvement as an adhesin
    • DOI 10.1016/j.vetmic.2004.05.008, PII S0378113504002068
    • Brassard, J.; Gottschalk, M.; Quessy, S. Cloning and purification of the Streptococcus suis serotype 2 glyceraldehyde-3-phosphate dehydrogenase and its involvement as an adhesin Vet. Microbiol. 2004, 102 (1-2) 87-94 (Pubitemid 39037377)
    • (2004) Veterinary Microbiology , vol.102 , Issue.1-2 , pp. 87-94
    • Brassard, J.1    Gottschalk, M.2    Quessy, S.3
  • 16
    • 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.; Zhao, Y.; Chen, H.; Jin, M. Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2 Vaccine 2009, 27 (9) 1348-53
    • (2009) Vaccine , vol.27 , Issue.9 , pp. 1348-53
    • Zhang, A.1    Chen, B.2    Mu, X.3    Li, R.4    Zheng, P.5    Zhao, Y.6    Chen, H.7    Jin, M.8
  • 18
    • 47049118856 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a cell wall surface protein, 6-phosphogluconate-dehydrogenase, of Streptococcus suis serotype 2
    • Tan, C.; Fu, S.; Liu, M.; Jin, M.; Liu, J.; Bei, W.; Chen, H. Cloning, expression and characterization of a cell wall surface protein, 6-phosphogluconate-dehydrogenase, of Streptococcus suis serotype 2 Vet. Microbiol. 2008, 130 (3-4) 363-70
    • (2008) Vet. Microbiol. , vol.130 , Issue.3-4 , pp. 363-70
    • Tan, C.1    Fu, S.2    Liu, M.3    Jin, M.4    Liu, J.5    Bei, W.6    Chen, H.7
  • 19
    • 77956362798 scopus 로고    scopus 로고
    • ApuA, a multifunctional alpha-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus
    • Ferrando, M. L.; Fuentes, S.; de Greeff, A.; Smith, H.; Wells, J. M. ApuA, a multifunctional alpha-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus Microbiology 2010, 156 (Pt 9) 2818-28
    • (2010) Microbiology , vol.156 , Issue.PART 9 , pp. 2818-28
    • Ferrando, M.L.1    Fuentes, S.2    De Greeff, A.3    Smith, H.4    Wells, J.M.5
  • 20
    • 0029736717 scopus 로고    scopus 로고
    • The galactosyl-(α1-4)-galactose-binding adhesin of Streptococcus suis: Occurrence in strains of different hemagglutination activities and induction of opsonic antibodies
    • Tikkanen, K.; Haataja, S.; Finne, J. The galactosyl-(alpha 1-4)-galactose-binding adhesin of Streptococcus suis: occurrence in strains of different hemagglutination activities and induction of opsonic antibodies Infect. Immun. 1996, 64 (9) 3659-65 (Pubitemid 26298690)
    • (1996) Infection and Immunity , vol.64 , Issue.9 , pp. 3659-3665
    • Tikkanen, K.1    Haataja, S.2    Finne, J.3
  • 21
    • 0029741635 scopus 로고    scopus 로고
    • The GALα1-4GAL-binding adhesin of Streptococcus suis, a gram-positive meningitis-associated bacterium
    • Haataja, S.; Tikkanen, K.; Hytonen, J.; Finne, J. The Gal alpha 1-4 Gal-binding adhesin of Streptococcus suis, a gram-positive meningitis-associated bacterium Adv. Exp. Med. Biol. 1996, 408, 25-34 (Pubitemid 26331049)
    • (1996) Advances in Experimental Medicine and Biology , vol.408 , pp. 25-34
    • Haataja, S.1    Tikkanen, K.2    Hytonen, J.3    Finne, J.4
  • 22
    • 0028973095 scopus 로고
    • Purification of a galactosyl-alpha1-4-galactose-binding adhesin from the Gram-Positive meningitis-associated bacterium Streptococcus suis
    • DOI 10.1074/jbc.270.48.28874
    • Tikkanen, K.; Haataja, S.; Francois-Gerard, C.; Finne, J. Purification of a galactosyl-alpha 1-4-galactose-binding adhesin from the gram-positive meningitis-associated bacterium Streptococcus suis J. Biol. Chem. 1995, 270 (48) 28874-8 (Pubitemid 3016853)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.48 , pp. 28874-28878
    • Tikkanen, K.1    Haataja, S.2    Francois-Gerard, C.3    Finne, J.4
  • 23
    • 0028172418 scopus 로고
    • Oligosaccharide-receptor interaction of the Gal alpha 1-4Gal binding adhesin of Streptococcus suis. Combining site architecture and characterization of two variant adhesin specificities
    • Haataja, S.; Tikkanen, K.; Nilsson, U.; Magnusson, G.; Karlsson, K. A.; Finne, J. Oligosaccharide-receptor interaction of the Gal alpha 1-4Gal binding adhesin of Streptococcus suis. Combining site architecture and characterization of two variant adhesin specificities J. Biol. Chem. 1994, 269 (44) 27466-72
    • (1994) J. Biol. Chem. , vol.269 , Issue.44 , pp. 27466-72
    • Haataja, S.1    Tikkanen, K.2    Nilsson, U.3    Magnusson, G.4    Karlsson, K.A.5    Finne, J.6
  • 24
    • 0027513149 scopus 로고
    • Characterization of a novel bacterial adhesion specificity of Streptococcus suis recognizing blood group P receptor oligosaccharides
    • Haataja, S.; Tikkanen, K.; Liukkonen, J.; Francois-Gerard, C.; Finne, J. Characterization of a novel bacterial adhesion specificity of Streptococcus suis recognizing blood group P receptor oligosaccharides J. Biol. Chem. 1993, 268 (6) 4311-7 (Pubitemid 23072973)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.6 , pp. 4311-4317
    • Haataja, S.1    Tikkanen, K.2    Liukkonen, J.3    Francois-Gerard, C.4    Finne, J.5
  • 25
    • 0034931519 scopus 로고    scopus 로고
    • α-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, G. S.; Hammerschmidt, S. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface Mol. Microbiol. 2001, 40 (6) 1273-87 (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
  • 26
    • 34247854961 scopus 로고    scopus 로고
    • Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis
    • DOI 10.1128/JB.01966-06
    • Knaust, A.; Weber, M. V.; Hammerschmidt, S.; Bergmann, S.; Frosch, M.; Kurzai, O. Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis J. Bacteriol. 2007, 189 (8) 3246-55 (Pubitemid 46697415)
    • (2007) Journal of Bacteriology , vol.189 , Issue.8 , pp. 3246-3255
    • Knaust, A.1    Weber, M.V.R.2    Hammerschmidt, S.3    Bergmann, S.4    Frosch, M.5    Kurzai, O.6
  • 27
    • 77951586997 scopus 로고    scopus 로고
    • The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: Surface localization and role in host cell adhesion
    • Tunio, S. A.; Oldfield, N. J.; Berry, A.; Ala'Aldeen, D. A.; Wooldridge, K. G.; Turner, D. P. The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: surface localization and role in host cell adhesion Mol. Microbiol. 2010, 76 (3) 605-15
    • (2010) Mol. Microbiol. , vol.76 , Issue.3 , pp. 605-15
    • Tunio, S.A.1    Oldfield, N.J.2    Berry, A.3    Ala'Aldeen, D.A.4    Wooldridge, K.G.5    Turner, D.P.6
  • 28
    • 33746903479 scopus 로고    scopus 로고
    • The protein secretion systems in Listeria: Inside out bacterial virulence
    • DOI 10.1111/j.1574-6976.2006.00035.x
    • Desvaux, M.; Hebraud, M. The protein secretion systems in Listeria: inside out bacterial virulence FEMS Microbiol. Rev. 2006, 30 (5) 774-805 (Pubitemid 44199350)
    • (2006) FEMS Microbiology Reviews , vol.30 , Issue.5 , pp. 774-805
    • Desvaux, M.1    Hebraud, M.2
  • 29
    • 70349323594 scopus 로고    scopus 로고
    • Capturing host-pathogen interactions by protein microarrays: Identification of novel streptococcal proteins binding to human fibronectin, fibrinogen, and C4BP
    • Margarit, I.; Bonacci, S.; Pietrocola, G.; Rindi, S.; Ghezzo, C.; Bombaci, M.; Nardi-Dei, V.; Grifantini, R.; Speziale, P.; Grandi, G. Capturing host-pathogen interactions by protein microarrays: identification of novel streptococcal proteins binding to human fibronectin, fibrinogen, and C4BP FASEB J. 2009, 23 (9) 3100-12
    • (2009) FASEB J. , vol.23 , Issue.9 , pp. 3100-12
    • Margarit, I.1    Bonacci, S.2    Pietrocola, G.3    Rindi, S.4    Ghezzo, C.5    Bombaci, M.6    Nardi-Dei, V.7    Grifantini, R.8    Speziale, P.9    Grandi, G.10
  • 31
    • 58149328654 scopus 로고    scopus 로고
    • Overcoming function annotation errors in the Gram-positive pathogen Streptococcus suis by a proteomics-driven approach
    • Rodriguez-Ortega, M. J.; Luque, I.; Tarradas, C.; Barcena, J. A. Overcoming function annotation errors in the Gram-positive pathogen Streptococcus suis by a proteomics-driven approach BMC Genomics 2008, 9, 588
    • (2008) BMC Genomics , vol.9 , pp. 588
    • Rodriguez-Ortega, M.J.1    Luque, I.2    Tarradas, C.3    Barcena, J.A.4
  • 33
    • 79551469739 scopus 로고    scopus 로고
    • Reduced virulence is an important characteristic of biofilm infection of Streptococcus suis
    • Wang, Y.; Zhang, W.; Wu, Z.; Lu, C. Reduced virulence is an important characteristic of biofilm infection of Streptococcus suis FEMS Microbiol. Lett. 2011, 316 (1) 36-43
    • (2011) FEMS Microbiol. Lett. , vol.316 , Issue.1 , pp. 36-43
    • Wang, Y.1    Zhang, W.2    Wu, Z.3    Lu, C.4
  • 34
    • 79952306782 scopus 로고    scopus 로고
    • Contribution of the Rgg Transcription Regulator to Metabolism and Virulence of Streptococcus suis Serotype 2
    • Zheng, F.; Ji, H.; Cao, M.; Wang, C.; Feng, Y.; Li, M.; Pan, X.; Wang, J.; Qin, Y.; Hu, F.; Tang, J. Contribution of the Rgg Transcription Regulator to Metabolism and Virulence of Streptococcus suis Serotype 2 Infect. Immun. 2011, 79 (3) 1319-1328
    • (2011) Infect. Immun. , vol.79 , Issue.3 , pp. 1319-1328
    • Zheng, F.1    Ji, H.2    Cao, M.3    Wang, C.4    Feng, Y.5    Li, M.6    Pan, X.7    Wang, J.8    Qin, Y.9    Hu, F.10    Tang, J.11
  • 35
    • 79551680752 scopus 로고    scopus 로고
    • The two-component regulatory system CiaRH contributes to the virulence of Streptococcus suis 2
    • Li, J.; Tan, C.; Zhou, Y.; Fu, S.; Hu, L.; Hu, J.; Chen, H.; Bei, W. The two-component regulatory system CiaRH contributes to the virulence of Streptococcus suis 2 Vet. Microbiol. 2011, 148 (1) 99-104
    • (2011) Vet. Microbiol. , vol.148 , Issue.1 , pp. 99-104
    • Li, J.1    Tan, C.2    Zhou, Y.3    Fu, S.4    Hu, L.5    Hu, J.6    Chen, H.7    Bei, W.8
  • 36
    • 4444347083 scopus 로고    scopus 로고
    • Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells
    • DOI 10.1111/j.1462-5822.2004.00409.x
    • Benga, L.; Goethe, R.; Rohde, M.; Valentin-Weigand, P. Non-encapsulated strains reveal novel insights in invasion and survival of Streptococcus suis in epithelial cells Cell Microbiol. 2004, 6 (9) 867-81 (Pubitemid 39162628)
    • (2004) Cellular Microbiology , vol.6 , Issue.9 , pp. 867-881
    • Benga, L.1    Goethe, R.2    Rohde, M.3    Valentin-Weigand, P.4
  • 38
    • 77951959305 scopus 로고    scopus 로고
    • Evaluation of the protective efficacy of a newly identified immunogenic protein, HP0272, of Streptococcus suis
    • Chen, B.; Zhang, A.; Li, R.; Mu, X.; He, H.; Chen, H.; Jin, M. Evaluation of the protective efficacy of a newly identified immunogenic protein, HP0272, of Streptococcus suis FEMS Microbiol. Lett. 2010, 307 (1) 12-8
    • (2010) FEMS Microbiol. Lett. , vol.307 , Issue.1 , pp. 12-8
    • Chen, B.1    Zhang, A.2    Li, R.3    Mu, X.4    He, H.5    Chen, H.6    Jin, M.7
  • 39
    • 0023231138 scopus 로고
    • Biotin binding to avidin. Oligosaccharide side chain not required for ligand association
    • Hiller, Y.; Gershoni, J. M.; Bayer, E. A.; Wilchek, M. Biotin binding to avidin. Oligosaccharide side chain not required for ligand association Biochem. J. 1987, 248 (1) 167-71 (Pubitemid 17161037)
    • (1987) Biochemical Journal , vol.248 , Issue.1 , pp. 167-171
    • Hiller, Y.1    Gershoni, J.M.2    Bayer, E.A.3    Wilchek, M.4
  • 40
    • 58149314321 scopus 로고    scopus 로고
    • Identification and Experimental Verification of Protective Antigens Against Streptococcus suis Serotype 2 Based on Genome Sequence Analysis
    • Liu, L.; Cheng, G.; Wang, C.; Pan, X.; Cong, Y.; Pan, Q.; Wang, J.; Zheng, F.; Hu, F.; Tang, J. Identification and Experimental Verification of Protective Antigens Against Streptococcus suis Serotype 2 Based on Genome Sequence Analysis Curr. Microbiol. 2009, 58 (1) 11-7
    • (2009) Curr. Microbiol. , vol.58 , Issue.1 , pp. 11-7
    • Liu, L.1    Cheng, G.2    Wang, C.3    Pan, X.4    Cong, Y.5    Pan, Q.6    Wang, J.7    Zheng, F.8    Hu, F.9    Tang, J.10
  • 41
    • 34249303833 scopus 로고    scopus 로고
    • Adhesion activity of glyceraldehyde-3-phosphate dehydrogenase in a Chinese Streptococcus suis type 2 strain
    • DOI 10.2376/0005-9366-120-207
    • Wang, K.; Lu, C. Adhesion activity of glyceraldehyde-3-phosphate dehydrogenase in a Chinese Streptococcus suis type 2 strain Berl. Munch. Tierarztl. Wochenschr. 2007, 120 (5-6) 207-9 (Pubitemid 46806496)
    • (2007) Berliner und Munchener Tierarztliche Wochenschrift , vol.120 , Issue.5-6 , pp. 207-209
    • Wang, K.1    Lu, C.2
  • 42
    • 53449101619 scopus 로고    scopus 로고
    • Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis
    • Esgleas, M.; Li, Y.; Hancock, M. A.; Harel, J.; Dubreuil, J. D.; Gottschalk, M. Isolation and characterization of alpha-enolase, a novel fibronectin-binding protein from Streptococcus suis Microbiology 2008, 154 (Pt 9) 2668-79
    • (2008) Microbiology , vol.154 , Issue.PART 9 , pp. 2668-79
    • Esgleas, M.1    Li, Y.2    Hancock, M.A.3    Harel, J.4    Dubreuil, J.D.5    Gottschalk, M.6
  • 43
    • 49849083653 scopus 로고    scopus 로고
    • Dexamethasone prevents alteration of tight junction-associated proteins and barrier function in porcine choroid plexus epithelial cells after infection with Streptococcus suis in vitro
    • Tenenbaum, T.; Matalon, D.; Adam, R.; Seibt, A.; Wewer, C.; Schwerk, C.; Galla, H. J.; Schroten, H. Dexamethasone prevents alteration of tight junction-associated proteins and barrier function in porcine choroid plexus epithelial cells after infection with Streptococcus suis in vitro Brain Res. 2008, 1229, 1-17
    • (2008) Brain Res. , vol.1229 , pp. 1-17
    • Tenenbaum, T.1    Matalon, D.2    Adam, R.3    Seibt, A.4    Wewer, C.5    Schwerk, C.6    Galla, H.J.7    Schroten, H.8
  • 44
    • 51649090331 scopus 로고    scopus 로고
    • Polysaccharide capsule and suilysin contribute to extracellular survival of Streptococcus suis co-cultivated with primary porcine phagocytes
    • Benga, L.; Fulde, M.; Neis, C.; Goethe, R.; Valentin-Weigand, P. Polysaccharide capsule and suilysin contribute to extracellular survival of Streptococcus suis co-cultivated with primary porcine phagocytes Vet. Microbiol. 2008, 132 (1-2) 211-9
    • (2008) Vet. Microbiol. , vol.132 , Issue.1-2 , pp. 211-9
    • Benga, L.1    Fulde, M.2    Neis, C.3    Goethe, R.4    Valentin-Weigand, P.5
  • 45
    • 0036073871 scopus 로고    scopus 로고
    • Streptococcus suis interactions with the murine macrophage cell line J774: Adhesion and cytotoxicity
    • DOI 10.1128/IAI.70.8.4312-4322.2002
    • Segura, M.; Gottschalk, M. Streptococcus suis interactions with the murine macrophage cell line J774: adhesion and cytotoxicity Infect. Immun. 2002, 70 (8) 4312-22 (Pubitemid 34790940)
    • (2002) Infection and Immunity , vol.70 , Issue.8 , pp. 4312-4322
    • Segura, M.1    Gottschalk, M.2
  • 46
    • 13844307110 scopus 로고    scopus 로고
    • Streptococcus suis serotype 2 binding to extracellular matrix proteins
    • DOI 10.1016/j.femsle.2005.01.017
    • Esgleas, M.; Lacouture, S.; Gottschalk, M. Streptococcus suis serotype 2 binding to extracellular matrix proteins FEMS Microbiol. Lett. 2005, 244 (1) 33-40 (Pubitemid 40261176)
    • (2005) FEMS Microbiology Letters , vol.244 , Issue.1 , pp. 33-40
    • Esgleas, M.1    Lacouture, S.2    Gottschalk, M.3
  • 47
    • 46049089600 scopus 로고    scopus 로고
    • The role of complex carbohydrate catabolism in the pathogenesis of invasive streptococci
    • Shelburne, S. A.; Davenport, M. T.; Keith, D. B.; Musser, J. M. The role of complex carbohydrate catabolism in the pathogenesis of invasive streptococci Trends Microbiol. 2008, 16 (7) 318-25
    • (2008) Trends Microbiol. , vol.16 , Issue.7 , pp. 318-25
    • Shelburne, S.A.1    Davenport, M.T.2    Keith, D.B.3    Musser, J.M.4
  • 49
    • 48249105088 scopus 로고    scopus 로고
    • A large scale analysis of protein-protein interactions in the nitrogen-fixing bacterium Mesorhizobium loti
    • Shimoda, Y.; Shinpo, S.; Kohara, M.; Nakamura, Y.; Tabata, S.; Sato, S. A large scale analysis of protein-protein interactions in the nitrogen-fixing bacterium Mesorhizobium loti DNA Res. 2008, 15 (1) 13-23
    • (2008) DNA Res. , vol.15 , Issue.1 , pp. 13-23
    • Shimoda, Y.1    Shinpo, S.2    Kohara, M.3    Nakamura, Y.4    Tabata, S.5    Sato, S.6
  • 52
    • 58149229162 scopus 로고    scopus 로고
    • An in vitro microfluidic approach to generating protein-interaction networks
    • Gerber, D.; Maerkl, S. J.; Quake, S. R. An in vitro microfluidic approach to generating protein-interaction networks Nat. Methods 2009, 6 (1) 71-4
    • (2009) Nat. Methods , vol.6 , Issue.1 , pp. 71-4
    • Gerber, D.1    Maerkl, S.J.2    Quake, S.R.3
  • 53
    • 78651431723 scopus 로고    scopus 로고
    • Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guerin
    • Zheng, J.; Wei, C.; Zhao, L.; Liu, L.; Leng, W.; Li, W.; Jin, Q. Combining blue native polyacrylamide gel electrophoresis with liquid chromatography tandem mass spectrometry as an effective strategy for analyzing potential membrane protein complexes of Mycobacterium bovis bacillus Calmette-Guerin BMC Genomics 2011, 12, 40
    • (2011) BMC Genomics , vol.12 , pp. 40
    • Zheng, J.1    Wei, C.2    Zhao, L.3    Liu, L.4    Leng, W.5    Li, W.6    Jin, Q.7
  • 54
    • 33645102186 scopus 로고    scopus 로고
    • An evaluation of in vitro protein-protein interaction techniques: Assessing contaminating background proteins
    • Howell, J. M.; Winstone, T. L.; Coorssen, J. R.; Turner, R. J. An evaluation of in vitro protein-protein interaction techniques: assessing contaminating background proteins Proteomics 2006, 6 (7) 2050-69
    • (2006) Proteomics , vol.6 , Issue.7 , pp. 2050-69
    • Howell, J.M.1    Winstone, T.L.2    Coorssen, J.R.3    Turner, R.J.4
  • 57
    • 33947310877 scopus 로고    scopus 로고
    • Proteomic analysis of macrophages: A new way to identify novel cell-surface antigens
    • DOI 10.1016/j.jim.2007.01.009, PII S0022175907000282
    • Zhang, L.; Lun, Y.; Yan, D.; Yu, L.; Ma, W.; Du, B.; Zhu, X. Proteomic analysis of macrophages: a new way to identify novel cell-surface antigens J. Immunol. Methods 2007, 321 (1-2) 80-5 (Pubitemid 46441199)
    • (2007) Journal of Immunological Methods , vol.321 , Issue.1-2 , pp. 80-85
    • Zhang, L.1    Lun, Y.2    Yan, D.3    Yu, L.4    Ma, W.5    Du, B.6    Zhu, X.7
  • 58
    • 0036624537 scopus 로고    scopus 로고
    • Shotgun proteomics: Tools for the analysis of complex biological systems
    • Wu, C. C.; MacCoss, M. J. Shotgun proteomics: tools for the analysis of complex biological systems Curr. Opin. Mol. Ther. 2002, 4 (3) 242-50 (Pubitemid 35282870)
    • (2002) Current Opinion in Molecular Therapeutics , vol.4 , Issue.3 , pp. 242-250
    • Wu, C.C.1    MacCoss, M.J.2
  • 59
    • 38649106736 scopus 로고    scopus 로고
    • Disruption of srtA gene in Streptococcus suis results in decreased interactions with endothelial cells and extracellular matrix proteins
    • DOI 10.1016/j.vetmic.2007.08.032, PII S0378113507004439
    • Vanier, G.; Sekizaki, T.; Dominguez-Punaro, M. C.; Esgleas, M.; Osaki, M.; Takamatsu, D.; Segura, M.; Gottschalk, M. Disruption of srtA gene in Streptococcus suis results in decreased interactions with endothelial cells and extracellular matrix proteins Vet. Microbiol. 2008, 127 (3-4) 417-24 (Pubitemid 351173520)
    • (2008) Veterinary Microbiology , vol.127 , Issue.3-4 , pp. 417-424
    • Vanier, G.1    Sekizaki, T.2    Dominguez-Punaro, M.C.3    Esgleas, M.4    Osaki, M.5    Takamatsu, D.6    Segura, M.7    Gottschalk, M.8
  • 60
    • 36048997622 scopus 로고    scopus 로고
    • Cloning and characterization of an α-enolase of the oral pathogen Streptococcus mutans that binds human plasminogen
    • DOI 10.1016/j.bbrc.2007.10.098, PII S0006291X07022644
    • Jones, M. N.; Holt, R. G. Cloning and characterization of an alpha-enolase of the oral pathogen Streptococcus mutans that binds human plasminogen Biochem. Biophys. Res. Commun. 2007, 364 (4) 924-9 (Pubitemid 350087889)
    • (2007) Biochemical and Biophysical Research Communications , vol.364 , Issue.4 , pp. 924-929
    • Jones, M.N.1    Holt, R.G.2
  • 61
    • 0032486286 scopus 로고    scopus 로고
    • α-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • DOI 10.1074/jbc.273.23.14503
    • Pancholi, V.; Fischetti, V. A. alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci J. Biol. Chem. 1998, 273 (23) 14503-15 (Pubitemid 28319172)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.23 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 62
    • 1642431995 scopus 로고    scopus 로고
    • Enolase from Streptococcus sobrinus is an immunosuppressive protein
    • DOI 10.1046/j.1462-5822.2003.00344.x
    • Veiga-Malta, I.; Duarte, M.; Dinis, M.; Tavares, D.; Videira, A.; Ferreira, P. Enolase from Streptococcus sobrinus is an immunosuppressive protein Cell Microbiol. 2004, 6 (1) 79-88 (Pubitemid 38111590)
    • (2004) Cellular Microbiology , vol.6 , Issue.1 , pp. 79-88
    • Veiga-Malta, I.1    Duarte, M.2    Dinis, M.3    Tavares, D.4    Videira, A.5    Ferreira, P.6
  • 63
    • 52649114317 scopus 로고    scopus 로고
    • Identification of immunogenic cell wall-associated proteins of Streptococcus suis serotype 2
    • Zhang, A.; Xie, C.; Chen, H.; Jin, M. Identification of immunogenic cell wall-associated proteins of Streptococcus suis serotype 2 Proteomics 2008, 8 (17) 3506-15
    • (2008) Proteomics , vol.8 , Issue.17 , pp. 3506-15
    • Zhang, A.1    Xie, C.2    Chen, H.3    Jin, M.4
  • 64
    • 34948857581 scopus 로고    scopus 로고
    • Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis
    • DOI 10.1002/pmic.200600876
    • Xolalpa, W.; Vallecillo, A. J.; Lara, M.; Mendoza-Hernandez, G.; Comini, M.; Spallek, R.; Singh, M.; Espitia, C. Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis Proteomics 2007, 7 (18) 3332-41 (Pubitemid 47517948)
    • (2007) Proteomics , vol.7 , Issue.18 , pp. 3332-3341
    • Xolalpa, W.1    Vallecillo, A.J.2    Lara, M.3    Mendoza-Hernandez, G.4    Comini, M.5    Spallek, R.6    Singh, M.7    Espitia, C.8
  • 65
    • 0028106317 scopus 로고
    • Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci
    • Courtney, H. S.; Li, Y.; Dale, J. B.; Hasty, D. L. Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci Infect. Immun. 1994, 62 (9) 3937-46 (Pubitemid 24264340)
    • (1994) Infection and Immunity , vol.62 , Issue.9 , pp. 3937-3946
    • Courtney, H.S.1    Li, Y.2    Dale, J.B.3    Hasty, D.L.4
  • 66
    • 0842283891 scopus 로고    scopus 로고
    • Investigation of a Novel DNase of Streptococcus suis Serotype 2
    • DOI 10.1128/IAI.72.2.774-781.2004
    • Fontaine, M. C.; Perez-Casal, J.; Willson, P. J. Investigation of a novel DNase of Streptococcus suis serotype 2 Infect. Immun. 2004, 72 (2) 774-81 (Pubitemid 38166655)
    • (2004) Infection and Immunity , vol.72 , Issue.2 , pp. 774-781
    • Fontaine, M.C.1    Perez-Casal, J.2    Willson, P.J.3
  • 67
    • 76849115257 scopus 로고    scopus 로고
    • Characterization of a virulence-associated and cell-wall-located DNase of Streptococcus pyogenes
    • Hasegawa, T.; Minami, M.; Okamoto, A.; Tatsuno, I.; Isaka, M.; Ohta, M. Characterization of a virulence-associated and cell-wall-located DNase of Streptococcus pyogenes Microbiology 2010, 156 (Pt 1) 184-90
    • (2010) Microbiology , vol.156 , Issue.PART 1 , pp. 184-90
    • Hasegawa, T.1    Minami, M.2    Okamoto, A.3    Tatsuno, I.4    Isaka, M.5    Ohta, M.6
  • 68
    • 0031038834 scopus 로고    scopus 로고
    • The divIVA minicell locus of Bacillus subtilis
    • Cha, J. H.; Stewart, G. C. The divIVA minicell locus of Bacillus subtilis J. Bacteriol. 1997, 179 (5) 1671-83 (Pubitemid 27100457)
    • (1997) Journal of Bacteriology , vol.179 , Issue.5 , pp. 1671-1683
    • Cha, J.-H.1    Stewart, G.C.2
  • 70
    • 0033857054 scopus 로고    scopus 로고
    • Role of ribosomal protein L12 in gonococcal invasion of Hec1B cells
    • Spence, J. M.; Clark, V. L. Role of ribosomal protein L12 in gonococcal invasion of Hec1B cells Infect. Immun. 2000, 68 (9) 5002-10
    • (2000) Infect. Immun. , vol.68 , Issue.9 , pp. 5002-10
    • Spence, J.M.1    Clark, V.L.2
  • 71
    • 78651338358 scopus 로고    scopus 로고
    • Asc1p, a ribosomal protein, plays a pivotal role in cellular adhesion and virulence in Candida albicans
    • Kim, S. W.; Joo, Y. J.; Kim, J. Asc1p, a ribosomal protein, plays a pivotal role in cellular adhesion and virulence in Candida albicans J. Microbiol. 2010, 48 (6) 842-8
    • (2010) J. Microbiol. , vol.48 , Issue.6 , pp. 842-8
    • Kim, S.W.1    Joo, Y.J.2    Kim, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.