메뉴 건너뛰기




Volumn 7, Issue 9, 2008, Pages 4132-4142

Identification and characterization of novel immunogenic proteins of Streptococcus suis serotype 2

Author keywords

Cell wall protein; Extracellular protein; Immunoproteomics; Streptococcus suis; Vaccine candidate

Indexed keywords

STREPTOCOCCUS VACCINE; ANTISERUM; BACTERIAL PROTEIN; BACTERIUM ANTIBODY; PRIMER DNA;

EID: 55249105950     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr800196v     Document Type: Article
Times cited : (54)

References (51)
  • 1
    • 0020668995 scopus 로고
    • Streptococcus suis type 2 infections
    • Clifton-Hadley, F. A. Streptococcus suis type 2 infections. Br. Vet. J. 1983, 139 (1), 1-5.
    • (1983) Br. Vet. J , vol.139 , Issue.1 , pp. 1-5
    • Clifton-Hadley, F.A.1
  • 2
    • 0024023118 scopus 로고
    • Isolation of Streptococcus suis from diseased pigs in Canada
    • Touil, F.; Higgins, R.; Nadeau, M. Isolation of Streptococcus suis from diseased pigs in Canada. Vet. Microbiol. 1988, 17 (2), 171-177.
    • (1988) Vet. Microbiol , vol.17 , Issue.2 , pp. 171-177
    • Touil, F.1    Higgins, R.2    Nadeau, M.3
  • 3
    • 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), 131-137.
    • (1988) Rev. Infect. Dis , vol.10 , Issue.1 , pp. 131-137
    • Arends, J.P.1    Zanen, H.C.2
  • 5
    • 0024430038 scopus 로고
    • Occupational exposure to Streptococcus suis type 2
    • Robertson, I. D.; Blackmore, D. K. Occupational exposure to Streptococcus suis type 2. Epidemiol. Infect 1989, 103 (1), 157-164.
    • (1989) Epidemiol. Infect , vol.103 , Issue.1 , pp. 157-164
    • Robertson, I.D.1    Blackmore, D.K.2
  • 8
    • 0028814642 scopus 로고
    • Streptococcus suis infection in Hong Kong
    • Kay, R.; Cheng, A. F.; Tse, C. Y. Streptococcus suis infection in Hong Kong. QJM 1995, 88 (1), 39-47.
    • (1995) QJM , vol.88 , Issue.1 , pp. 39-47
    • Kay, R.1    Cheng, A.F.2    Tse, C.Y.3
  • 10
    • 33744459956 scopus 로고    scopus 로고
    • Invasive disease and toxic shock due to zoonotic Streptococcus suis: An emerging infection in the East?
    • Sriskandan, S.; Slater, J. D. Invasive disease and toxic shock due to zoonotic Streptococcus suis: an emerging infection in the East? PLoS Med. 2006, 3 (5), el87.
    • (2006) PLoS Med , vol.3 , Issue.5
    • Sriskandan, S.1    Slater, J.D.2
  • 11
    • 34247111738 scopus 로고    scopus 로고
    • Potential use of an unencapsulated and aromatic amino acid-auxotrophic Streptococcus suis mutant as a live attenuated vaccine in swine
    • Fittipaldi, N.; Harel, J.; D'Amours, B.; Lacouture, S.; Kobisch, M.; Gottschalk, M. Potential use of an unencapsulated and aromatic amino acid-auxotrophic Streptococcus suis mutant as a live attenuated vaccine in swine. Vaccine 2007, 25 (18), 3524-3535.
    • (2007) Vaccine , vol.25 , Issue.18 , pp. 3524-3535
    • Fittipaldi, N.1    Harel, J.2    D'Amours, B.3    Lacouture, S.4    Kobisch, M.5    Gottschalk, M.6
  • 13
    • 0025177493 scopus 로고
    • Immunisation of pigs with killed cultures of Streptococcus suis type 2
    • Holt, M. E.; Enright, M. R.; Alexander, T. J. Immunisation of pigs with killed cultures of Streptococcus suis type 2. Res. Vet. Sci. 1990, 48 (1), 23-27.
    • (1990) Res. Vet. Sci , vol.48 , Issue.1 , pp. 23-27
    • Holt, M.E.1    Enright, M.R.2    Alexander, T.J.3
  • 14
    • 0024996552 scopus 로고
    • Isolation and characterization of temperature-sensitive mutants of Streptococcus suis: Efficacy trial of the mutant vaccine in mice
    • Kebede, M.; Chengappa, M. M.; Stuart, J. G. Isolation and characterization of temperature-sensitive mutants of Streptococcus suis: efficacy trial of the mutant vaccine in mice. Vet. Microbiol. 1990, 22 (2-3), 249-257.
    • (1990) Vet. Microbiol , vol.22 , Issue.2-3 , pp. 249-257
    • Kebede, M.1    Chengappa, M.M.2    Stuart, J.G.3
  • 15
    • 0019210683 scopus 로고
    • Streptococcal infection in young pigs. V. An immunogenic polysaccharide from Streptococcus suis type 2 with particular reference to vaccination against streptococcal meningitis in pigs
    • Elliott, S. D.; Clifton-Hadley, F.; Tai, J. Streptococcal infection in young pigs. V. An immunogenic polysaccharide from Streptococcus suis type 2 with particular reference to vaccination against streptococcal meningitis in pigs. J. Hyg. (London) 1980, 85 (2), 275-285.
    • (1980) J. Hyg. (London) , vol.85 , Issue.2 , pp. 275-285
    • Elliott, S.D.1    Clifton-Hadley, F.2    Tai, J.3
  • 16
    • 0035858032 scopus 로고    scopus 로고
    • Protection of pigs against challenge with virulent Streptococcus suis serotype 2 strains by a muramidase-released protein and extracellular factor vaccine
    • Wisselink, H. J.; Vecht, U.; Stockhofe-Zurwieden, N.; Smith, H. E. Protection of pigs against challenge with virulent Streptococcus suis serotype 2 strains by a muramidase-released protein and extracellular factor vaccine. Vet. Rec. 2001, 148 (15), 473-477.
    • (2001) Vet. Rec , vol.148 , Issue.15 , pp. 473-477
    • Wisselink, H.J.1    Vecht, U.2    Stockhofe-Zurwieden, N.3    Smith, H.E.4
  • 17
    • 0029838726 scopus 로고    scopus 로고
    • Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis
    • Jacobs, A. A.; van den Berg, A. J.; Loeffen, P. L. Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis. Vet. Rec. 1996, 139 (10), 225-228.
    • (1996) Vet. Rec , vol.139 , Issue.10 , pp. 225-228
    • Jacobs, A.A.1    van den Berg, A.J.2    Loeffen, P.L.3
  • 18
    • 5644277479 scopus 로고    scopus 로고
    • Rapid screening of highly efficient vaccine candidates by immunoproteomics
    • Chen, Z.; Peng, B.; Wang, S.; Peng, X. Rapid screening of highly efficient vaccine candidates by immunoproteomics. Proteomics 2004, 4 (10), 3203-3213.
    • (2004) Proteomics , vol.4 , Issue.10 , pp. 3203-3213
    • Chen, Z.1    Peng, B.2    Wang, S.3    Peng, X.4
  • 19
    • 0036249166 scopus 로고    scopus 로고
    • Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis
    • Vytvytska, O.; Nagy, E.; Bluggel, M.; Meyer, H. E.; Kurzbauer, R.; Huber, L. A.; Klade, C. S. Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis. Proteomics 2002, 2 (5), 580-590.
    • (2002) Proteomics , vol.2 , Issue.5 , pp. 580-590
    • Vytvytska, O.1    Nagy, E.2    Bluggel, M.3    Meyer, H.E.4    Kurzbauer, R.5    Huber, L.A.6    Klade, C.S.7
  • 21
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre, W. W.; Schneewind, O. Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol. Mol. Biol. Rev. 1999, 63 (1), 174-229.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , Issue.1 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 22
    • 17844401762 scopus 로고    scopus 로고
    • Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species
    • Trost, M.; Wehmhoner, D.; Karst, U.; Dieterich, G.; Wehland, J.; Jansch, L. Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species. Proteomics 2005, 5 (6), 1544-1557.
    • (2005) Proteomics , vol.5 , Issue.6 , pp. 1544-1557
    • Trost, M.1    Wehmhoner, D.2    Karst, U.3    Dieterich, G.4    Wehland, J.5    Jansch, L.6
  • 24
    • 36349021369 scopus 로고    scopus 로고
    • Improved solubilization of surface proteins from Listeria monocytogenes for 2-DE
    • Mujahid, S.; Pechan, T.; Wang, C. Improved solubilization of surface proteins from Listeria monocytogenes for 2-DE. Electrophoresis 2007, 28 (21), 3998-4007.
    • (2007) Electrophoresis , vol.28 , Issue.21 , pp. 3998-4007
    • Mujahid, S.1    Pechan, T.2    Wang, C.3
  • 25
    • 34548380916 scopus 로고    scopus 로고
    • Immunoproteomic assay of membrane-associated proteins of Streptococcus suis type 2 China vaccine strain HA9801
    • Zhang, W.; Lu, C. P. Immunoproteomic assay of membrane-associated proteins of Streptococcus suis type 2 China vaccine strain HA9801. Zoonoses Public Health 2007, 54 (6-7), 253-259.
    • (2007) Zoonoses Public Health , vol.54 , Issue.6-7 , pp. 253-259
    • Zhang, W.1    Lu, C.P.2
  • 26
    • 0036955884 scopus 로고    scopus 로고
    • Identification and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the Arginine Deiminase system of Streptococcus pyogenes
    • Winterhoff, N.; Goethe, R.; Gruening, P.; Rohde, M.; Kalisz, H.; Smith, H. E.; Valentin-Weigand, P. Identification and characterization of two temperature-induced surface-associated proteins of Streptococcus suis with high homologies to members of the Arginine Deiminase system of Streptococcus pyogenes. J. Bacteriol. 2002, 184 (24), 6768-6776.
    • (2002) J. Bacteriol , vol.184 , Issue.24 , pp. 6768-6776
    • Winterhoff, N.1    Goethe, R.2    Gruening, P.3    Rohde, M.4    Kalisz, H.5    Smith, H.E.6    Valentin-Weigand, P.7
  • 28
    • 29544436727 scopus 로고    scopus 로고
    • Ying, T.; Wang, H.; Li, M.; Wang, J.; Wang, J.; Shi, Z.; Feng, E.; Liu, X.; Su, G.; Wei, K.; Zhang, X.; Huang, P; Huang, L. Immunopro-teomics of outer membrane proteins and extracellular proteins of Shigella flexneri 2a 2457T. Proteomics 2005, 5 (18), 4777-4793.
    • Ying, T.; Wang, H.; Li, M.; Wang, J.; Wang, J.; Shi, Z.; Feng, E.; Liu, X.; Su, G.; Wei, K.; Zhang, X.; Huang, P; Huang, L. Immunopro-teomics of outer membrane proteins and extracellular proteins of Shigella flexneri 2a 2457T. Proteomics 2005, 5 (18), 4777-4793.
  • 30
    • 29644439702 scopus 로고    scopus 로고
    • Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs
    • Li, Y.; Martinez, G.; Gottschalk, M.; Lacouture, S.; Willson, P.; Dubreuil, J. D.; Jacques, M.; Harel, J. Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs. Infect. Immun. 2006, 74 (1), 305-312.
    • (2006) Infect. Immun , vol.74 , Issue.1 , pp. 305-312
    • Li, Y.1    Martinez, G.2    Gottschalk, M.3    Lacouture, S.4    Willson, P.5    Dubreuil, J.D.6    Jacques, M.7    Harel, J.8
  • 32
  • 33
    • 3843116600 scopus 로고    scopus 로고
    • 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.
    • 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.
  • 34
    • 35948951215 scopus 로고    scopus 로고
    • Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits
    • Antikainen, J.; Kuparinen, V.; Lahteenmaki, K.; Korhonen, T. K. Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits. FEMS Immunol. Med. Microbiol. 2007, 51 (3), 526-534.
    • (2007) FEMS Immunol. Med. Microbiol , vol.51 , Issue.3 , pp. 526-534
    • Antikainen, J.1    Kuparinen, V.2    Lahteenmaki, K.3    Korhonen, T.K.4
  • 35
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (Lal) to human intestinal cells and mucins
    • Granato, D.; Bergonzelli, G. E.; Pridmore, R. D.; Marvin, L.; Rouvet, M.; Corthesy-Theulaz, I. E. Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (Lal) to human intestinal cells and mucins. Infect. Immun. 2004, 72 (4), 2160-2169.
    • (2004) Infect. Immun , vol.72 , Issue.4 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthesy-Theulaz, I.E.6
  • 36
    • 34249886795 scopus 로고    scopus 로고
    • Identification of in vivo-expressed immunogenic proteins by serological proteome analysis of the Bacillus anthracis secretome
    • Chitlaru, T.; Gat, O.; Grosfeld, H.; Inbar, I.; Gozlan, Y.; Shafferman, A. Identification of in vivo-expressed immunogenic proteins by serological proteome analysis of the Bacillus anthracis secretome. Infect. Immun. 2007, 75 (6), 2841-2852.
    • (2007) Infect. Immun , vol.75 , Issue.6 , pp. 2841-2852
    • Chitlaru, T.1    Gat, O.2    Grosfeld, H.3    Inbar, I.4    Gozlan, Y.5    Shafferman, A.6
  • 37
    • 38049015834 scopus 로고    scopus 로고
    • Immunoproteomics of extracellular proteins of Chinese virulent strains of Streptococcus suis type 2
    • Zhang, W.; Lu, C. P. Immunoproteomics of extracellular proteins of Chinese virulent strains of Streptococcus suis type 2. Proteomics 2007, 7 (24), 4468-4476.
    • (2007) Proteomics , vol.7 , Issue.24 , pp. 4468-4476
    • Zhang, W.1    Lu, C.P.2
  • 38
    • 0027442464 scopus 로고
    • Cell wall sorting signals in surface proteins of gram-positive bacteria
    • Schneewind, O.; Mihaylova-Petkov, D.; Model, P. Cell wall sorting signals in surface proteins of gram-positive bacteria. EMBO J. 1993, 12 (12), 4803-4811.
    • (1993) EMBO J , vol.12 , Issue.12 , pp. 4803-4811
    • Schneewind, O.1    Mihaylova-Petkov, D.2    Model, P.3
  • 40
    • 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.; Feldman, G.; Portnoi, M.; Dagan, R.; Overweg, K.; Mulholland, F.; Chalifa-Caspi, V.; Wells, J.; Mizrachi-Nebenzahl, Y. 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. 2004, 138 (2), 290-298.
    • (2004) Clin. Exp. Immunol , vol.138 , Issue.2 , pp. 290-298
    • Ling, E.1    Feldman, G.2    Portnoi, M.3    Dagan, R.4    Overweg, K.5    Mulholland, F.6    Chalifa-Caspi, V.7    Wells, J.8    Mizrachi-Nebenzahl, Y.9
  • 41
    • 34147146425 scopus 로고    scopus 로고
    • Contributions of pneumolysin, pneumococcal surface protein A (PspA), and PspC to pathogenicity of Streptococcus pneumoniae D39 in a mouse model
    • Ogunniyi, A. D.; LeMessurier, K. S.; Graham, R. M.; Watt, J. M.; Briles, D. E.; Stroeher, U. H.; Paton, J. C. Contributions of pneumolysin, pneumococcal surface protein A (PspA), and PspC to pathogenicity of Streptococcus pneumoniae D39 in a mouse model. Infect. Immun. 2007, 75 (4), 1843-1851.
    • (2007) Infect. Immun , vol.75 , Issue.4 , pp. 1843-1851
    • Ogunniyi, A.D.1    LeMessurier, K.S.2    Graham, R.M.3    Watt, J.M.4    Briles, D.E.5    Stroeher, U.H.6    Paton, J.C.7
  • 42
    • 2142646463 scopus 로고    scopus 로고
    • Pneumococcal surface protein C contributes to sepsis caused by Streptococcus pneumoniae in mice
    • Iannelli, F.; Chiavolini, D.; Ricci, S.; Oggioni, M. R.; Pozzi, G. Pneumococcal surface protein C contributes to sepsis caused by Streptococcus pneumoniae in mice. Infect. Immun. 2004, 72 (5), 3077-3080.
    • (2004) Infect. Immun , vol.72 , Issue.5 , pp. 3077-3080
    • Iannelli, F.1    Chiavolini, D.2    Ricci, S.3    Oggioni, M.R.4    Pozzi, G.5
  • 43
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von, H. G. The structure of signal peptides from bacterial lipoproteins. Protein Eng. 1989, 2 (7), 531-534.
    • (1989) Protein Eng , vol.2 , Issue.7 , pp. 531-534
    • von, H.G.1
  • 44
    • 0034087259 scopus 로고    scopus 로고
    • Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate
    • Keenan, J.; Oliaro, J.; Domigan, N.; Potter, H.; Aitken, G.; Allardyce, R.; Roake, J. Immune response to an 18-kilodalton outer membrane antigen identifies lipoprotein 20 as a Helicobacter pylori vaccine candidate. Infect. Immun. 2000, 68 (6), 3337-3343.
    • (2000) Infect. Immun , vol.68 , Issue.6 , pp. 3337-3343
    • Keenan, J.1    Oliaro, J.2    Domigan, N.3    Potter, H.4    Aitken, G.5    Allardyce, R.6    Roake, J.7
  • 46
    • 42149107012 scopus 로고    scopus 로고
    • Analysis of the protective capacity of three Streptococcus suis proteins induced under divalent cation-limited conditions
    • Aranda,J.; Garrido, M. E.; Cortes, P.; Llagostera, M.; Barbe, J. Analysis of the protective capacity of three Streptococcus suis proteins induced under divalent cation-limited conditions. Infect. Immun. 2008, 76 (4), 1590-1598.
    • (2008) Infect. Immun , vol.76 , Issue.4 , pp. 1590-1598
    • Aranda, J.1    Garrido, M.E.2    Cortes, P.3    Llagostera, M.4    Barbe, J.5
  • 47
    • 0034064780 scopus 로고    scopus 로고
    • Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment
    • Fenno, J. C.; Tamura, M.; Hannam, P. M.; Wong, G. W.; Chan, R. A.; McBride, B. C. Identification of a Treponema denticola OppA homologue that binds host proteins present in the subgingival environment. Infect. Immun. 2000, 68 (4), 1884-1892.
    • (2000) Infect. Immun , vol.68 , Issue.4 , pp. 1884-1892
    • Fenno, J.C.1    Tamura, M.2    Hannam, P.M.3    Wong, G.W.4    Chan, R.A.5    McBride, B.C.6
  • 48
    • 0032855674 scopus 로고    scopus 로고
    • The adherence-associated lipoprotein P100, encoded by an opp operon structure, functions as the oligopeptide-binding domain OppA of a putative oligopeptide transport system in Mycoplasma hominis
    • Henrich, B.; Hopfe, M.; Kitzerow, A.; Hadding, U. The adherence-associated lipoprotein P100, encoded by an opp operon structure, functions as the oligopeptide-binding domain OppA of a putative oligopeptide transport system in Mycoplasma hominis. J. Bacteriol. 1999, 181 (16), 4873-4878.
    • (1999) J. Bacteriol , vol.181 , Issue.16 , pp. 4873-4878
    • Henrich, B.1    Hopfe, M.2    Kitzerow, A.3    Hadding, U.4
  • 50
    • 33745197348 scopus 로고    scopus 로고
    • Serologic proteome analysis of Borrelia burgdorferi membrane-associated proteins
    • Nowalk, A.J.; Gilmore, R. D., Jr.; Carroll, J. A. Serologic proteome analysis of Borrelia burgdorferi membrane-associated proteins. Infect. Immun. 2006, 74 (7), 3864-3873.
    • (2006) Infect. Immun , vol.74 , Issue.7 , pp. 3864-3873
    • Nowalk, A.J.1    Gilmore Jr., R.D.2    Carroll, J.A.3
  • 51
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    • Lei, B.; Mackie, S.; Lukomski, S.; Musser, J. M. Identification and immunogenicity of group A Streptococcus culture supernatant proteins. Infect. Immun. 2000, 68 (12), 6807-6818.
    • (2000) Infect. Immun , vol.68 , Issue.12 , pp. 6807-6818
    • Lei, B.1    Mackie, S.2    Lukomski, S.3    Musser, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.