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Volumn 9, Issue , 2004, Pages 1157-1188

Extracellular virulence factors of streptococci associated with animal diseases

Author keywords

Animal Disease; Bacteria; Capsule; M proteins; Microorganism; Review; Streptococci; Toxins; Virulence Factors

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; BACTERIOCIN; CYCLIC AMP; EXOTOXIN; FIBRONECTIN BINDING PROTEIN; FIMBRIA PROTEIN; HEMOLYSIN; HYALURONIDASE; M LIKE PROTEIN; MEMBRANE PROTEIN; PROTEINASE; STREPTOKINASE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 2442713060     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1287     Document Type: Review
Times cited : (30)

References (270)
  • 1
    • 0036779816 scopus 로고    scopus 로고
    • What happened to the streptococci: Overview of taxonomic and nomenclature changes
    • Facklam R.: What happened to the streptococci: overview of taxonomic and nomenclature changes. Clin Microbiol Rev 15, 613-630 (2002)
    • (2002) Clin Microbiol Rev , vol.15 , pp. 613-630
    • Facklam, R.1
  • 2
    • 0031974386 scopus 로고    scopus 로고
    • Identification of Streptococci to species level by sequencing the gene encoding the manganese-dependent superoxide dismutase
    • Poyart C., G. Quesne, S. Coulon, P. Berche & P. Trieu-Cuot: Identification of Streptococci to species level by sequencing the gene encoding the manganese-dependent superoxide dismutase. J Clin Microbiol 36, 41-47 (1998)
    • (1998) J Clin Microbiol , vol.36 , pp. 41-47
    • Poyart, C.1    Quesne, G.2    Coulon, S.3    Berche, P.4    Trieu-Cuot, P.5
  • 3
    • 0025998182 scopus 로고
    • Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences
    • Bentley R. W., J. A. Leigh & M. D. Collins: Intrageneric structure of Streptococcus based on comparative analysis of small-subunit rRNA sequences. Int J Syst Bacteriol 41, 487-494 (1991)
    • (1991) Int J Syst Bacteriol , vol.41 , pp. 487-494
    • Bentley, R.W.1    Leigh, J.A.2    Collins, M.D.3
  • 4
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre W. W. & O. Schneewind: Surface proteins of Gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol Mol Biol Rev 63, 174-229 (1999)
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 5
    • 0033923852 scopus 로고    scopus 로고
    • Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein
    • Collin M. & A. Olsén: Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein. Mol Microbiol 36, 1306-1318 (2000)
    • (2000) Mol Microbiol , vol.36 , pp. 1306-1318
    • Collin, M.1    Olsén, A.2
  • 6
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge A. & L. Björck: Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J Biol Chem 270, 9862-9867 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 9862-9867
    • Berge, A.1    Björck, L.2
  • 7
    • 0001386632 scopus 로고    scopus 로고
    • Streptococcal diseases
    • Eds: Straw B E, D'Allaire S, Mengeling W L, Taylor D J, Iowa State University, Ames
    • Higgins R. & M. Gottschalk: Streptococcal diseases. In: Diseases of swine. Eds: Straw B E, D'Allaire S, Mengeling W L, Taylor D J, Iowa State University, Ames (1999)
    • (1999) Diseases of Swine
    • Higgins, R.1    Gottschalk, M.2
  • 9
    • 0028509851 scopus 로고
    • Serotypes and putative virulence markers of Streptococcus suis isolates from cats and dogs
    • Salasia S. I., C. Lammler & L. A. Devriese: Serotypes and putative virulence markers of Streptococcus suis isolates from cats and dogs. Res Vet Sci 57, 259-261 (1994)
    • (1994) Res Vet Sci , vol.57 , pp. 259-261
    • Salasia, S.I.1    Lammler, C.2    Devriese, L.A.3
  • 11
    • 2542441835 scopus 로고    scopus 로고
    • Isolation of Streptococcus suis from a young wild boar
    • Higgins R., A. Lagace, S. Messier & L. Julien: Isolation of Streptococcus suis from a young wild boar. Can Vet J 38, 114 (1997)
    • (1997) Can Vet J , vol.38 , pp. 114
    • Higgins, R.1    Lagace, A.2    Messier, S.3    Julien, L.4
  • 12
    • 0020596424 scopus 로고
    • Serology of capsulated streptococci pathogenic for pigs: Six new serotypes of Streptococcus suis
    • Perch B., K. B. Pedersen & J. Henrichsen: Serology of capsulated streptococci pathogenic for pigs: six new serotypes of Streptococcus suis. J Clin Microbiol 17, 993-996 (1983)
    • (1983) J Clin Microbiol , vol.17 , pp. 993-996
    • Perch, B.1    Pedersen, K.B.2    Henrichsen, J.3
  • 13
    • 0025461525 scopus 로고
    • An update on Streptococcus suis identification
    • Higgins R. & M. Gottschalk: An update on Streptococcus suis identification. J Vet Diagn Invest 2, 249-252 (1990)
    • (1990) J Vet Diagn Invest , vol.2 , pp. 249-252
    • Higgins, R.1    Gottschalk, M.2
  • 14
    • 0001461628 scopus 로고    scopus 로고
    • The pathogenesis of the meningitis caused by Streptococcus suis: The unresolved questions
    • Gottschalk M. & M. Segura: The pathogenesis of the meningitis caused by Streptococcus suis: the unresolved questions. Vet Microbiol, 75, 59-71 (2000)
    • (2000) Vet Microbiol , vol.75 , pp. 59-71
    • Gottschalk, M.1    Segura, M.2
  • 15
    • 0025346095 scopus 로고
    • Pathogenesis of meningitis caused by Streptococcus suis type 2
    • Williams A. E. & W. F. Blakemore: Pathogenesis of meningitis caused by Streptococcus suis type 2. J Infect Dis 162, 474-481 (1990)
    • (1990) J Infect Dis , vol.162 , pp. 474-481
    • Williams, A.E.1    Blakemore, W.F.2
  • 16
    • 0025152680 scopus 로고
    • The role of bacterial polysaccharide capsules as virulence factors
    • Moxon E. R. & J. S. Kroll: The role of bacterial polysaccharide capsules as virulence factors. Curr Top Microbiol Immunol 150, 65-85 (1990)
    • (1990) Curr Top Microbiol Immunol , vol.150 , pp. 65-85
    • Moxon, E.R.1    Kroll, J.S.2
  • 17
    • 0025298356 scopus 로고
    • Ultrastructural study of surface components of Streptococcus suis
    • Jacques M., M. Gottschalk, B. Foiry & R. Higgins: Ultrastructural study of surface components of Streptococcus suis. J Bacteriol 172, 2833-2838 (1990)
    • (1990) J Bacteriol , vol.172 , pp. 2833-2838
    • Jacques, M.1    Gottschalk, M.2    Foiry, B.3    Higgins, R.4
  • 18
    • 0018249749 scopus 로고
    • The type-specific polysaccharides of Streptococcus suis
    • Elliott S. D. & J. Y. Tai: The type-specific polysaccharides of Streptococcus suis. J Exp Med 148, 1699-1704 (1978)
    • (1978) J Exp Med , vol.148 , pp. 1699-1704
    • Elliott, S.D.1    Tai, J.Y.2
  • 19
    • 0030253290 scopus 로고    scopus 로고
    • Comparative preparation methods of sialylated capsule antigen from Streptococcus suis type 2 with type specific antigenicity
    • Katsumi M., T. Saito, Y. Kataoka, T. Itoh, N. Kikuchi & T. Hiramune: Comparative preparation methods of sialylated capsule antigen from Streptococcus suis type 2 with type specific antigenicity. J Vet Med Sci 58, 947-952 (1996)
    • (1996) J Vet Med Sci , vol.58 , pp. 947-952
    • Katsumi, M.1    Saito, T.2    Kataoka, Y.3    Itoh, T.4    Kikuchi, N.5    Hiramune, T.6
  • 20
    • 0029009432 scopus 로고
    • Agglutination of Streptococcus suis by sialic acid-binding lectins
    • Charland N., J. T. Kellens, F. Caya & M. Gottschalk: Agglutination of Streptococcus suis by sialic acid-binding lectins. J Clin Microbiol 33, 2220-2221 (1995)
    • (1995) J Clin Microbiol , vol.33 , pp. 2220-2221
    • Charland, N.1    Kellens, J.T.2    Caya, F.3    Gottschalk, M.4
  • 21
    • 0030720974 scopus 로고    scopus 로고
    • Characterization and protective activity of a monoclonal antibody against a capsular epitope shared by Streptococcus suis serotypes 1, 2 and 1/2
    • Charland N., M. Jacques, S. Lacouture & M. Gottschalk: Characterization and protective activity of a monoclonal antibody against a capsular epitope shared by Streptococcus suis serotypes 1, 2 and 1/2. Microbiology 143, 3607-3614 (1997)
    • (1997) Microbiology , vol.143 , pp. 3607-3614
    • Charland, N.1    Jacques, M.2    Lacouture, S.3    Gottschalk, M.4
  • 22
    • 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., F. Clifton-Hadley & J. Tai: 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 Lond 85, 275-285 (1980)
    • (1980) J Hyg Lond , vol.85 , pp. 275-285
    • Elliott, S.D.1    Clifton-Hadley, F.2    Tai, J.3
  • 23
    • 0030250181 scopus 로고    scopus 로고
    • Detection of antibodies against Streptococcus suis capsular type 2 using a purified capsular polysaccharide antigen-based indirect ELISA
    • del Campo Sepulveda E. M., E. Altman, M. Kobisch, S. D'Allaire & M. Gottschalk: Detection of antibodies against Streptococcus suis capsular type 2 using a purified capsular polysaccharide antigen-based indirect ELISA. Vet Microbiol 52, 113-125 (1996)
    • (1996) Vet Microbiol , vol.52 , pp. 113-125
    • Del Campo Sepulveda, E.M.1    Altman, E.2    Kobisch, M.3    D'Allaire, S.4    Gottschalk, M.5
  • 24
    • 0014575273 scopus 로고
    • Streptococcal infection in young pigs. III. The immunity of adult pigs investigated by the bactericidal test
    • Agarwal K. K., S. D. Elliott & P. J. Lachmann: Streptococcal infection in young pigs. III. The immunity of adult pigs investigated by the bactericidal test. J Hyg 67, 491-503 (1969)
    • (1969) J Hyg , vol.67 , pp. 491-503
    • Agarwal, K.K.1    Elliott, S.D.2    Lachmann, P.J.3
  • 25
    • 0031936119 scopus 로고    scopus 로고
    • Streptococcus suis serotype 2 mutants deficient in capsular expression
    • Charland N., J. Harel, M. Kobish, S. Lacasse & M. Gottschalk: Streptococcus suis serotype 2 mutants deficient in capsular expression. Microbiology 144, 325-332 (1998)
    • (1998) Microbiology , vol.144 , pp. 325-332
    • Charland, N.1    Harel, J.2    Kobish, M.3    Lacasse, S.4    Gottschalk, M.5
  • 26
    • 0033040620 scopus 로고    scopus 로고
    • Identification and characterization of the cps locus of Streptococcus suis serotype 2: The capsule protects against phagocytosis and is an important virulence factor
    • Smith H. E., M. Damman, J. Van der Velde, F. Wagenaar, H. J. Wisselink, N. Stockhofe-Zurwieden & M. A. Smits: Identification and characterization of the cps locus of Streptococcus suis serotype 2: the capsule protects against phagocytosis and is an important virulence factor. Infect Immun 67, 1750-1756 (1999)
    • (1999) Infect Immun , vol.67 , pp. 1750-1756
    • Smith, H.E.1    Damman, M.2    Van Der Velde, J.3    Wagenaar, F.4    Wisselink, H.J.5    Stockhofe-Zurwieden, N.6    Smits, M.A.7
  • 27
    • 0026197777 scopus 로고
    • Adherence of Streptococcus suis capsular type 2 to porcine lung sections
    • Gottschalk M., S. Petitbois, R. Higgins & M. Jacques: Adherence of Streptococcus suis capsular type 2 to porcine lung sections. Can J Vet Res 55, 302-304 (1991)
    • (1991) Can J Vet Res , vol.55 , pp. 302-304
    • Gottschalk, M.1    Petitbois, S.2    Higgins, R.3    Jacques, M.4
  • 28
    • 0028058022 scopus 로고
    • Increase of capsular material thickness following in vivo growth of virulent Streptococcus suis serotype 2 strains
    • Quessy S., J. D. Dubreuil, M. Jacques, F. Malouin & R. Higgins: Increase of capsular material thickness following in vivo growth of virulent Streptococcus suis serotype 2 strains. FEMS Microbiol Lett 115, 19-26 (1994)
    • (1994) FEMS Microbiol Lett , vol.115 , pp. 19-26
    • Quessy, S.1    Dubreuil, J.D.2    Jacques, M.3    Malouin, F.4    Higgins, R.5
  • 29
    • 0024316972 scopus 로고
    • Definition of a bacterial virulence factor: Sialylation of the group B streptococcal capsule
    • Wessels M. R., C. E. Rubens, V. J. Benedi & D. L. Kasper: Definition of a bacterial virulence factor: sialylation of the group B streptococcal capsule. Proc Natl Acad Sci USA 86, 8983-8987 (1989)
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8983-8987
    • Wessels, M.R.1    Rubens, C.E.2    Benedi, V.J.3    Kasper, D.L.4
  • 30
    • 0030199551 scopus 로고    scopus 로고
    • Role of capsular sialic acid in virulence and resistance to phagocytosis of Streptococcus suis capsular type 2
    • Charland N., M. Kobisch, B. Martineau-Doize, M. Jacques & M. Gottschalk: Role of capsular sialic acid in virulence and resistance to phagocytosis of Streptococcus suis capsular type 2. FEMS Immunol Med Microbiol 14, 195-203 (1996)
    • (1996) FEMS Immunol Med Microbiol , vol.14 , pp. 195-203
    • Charland, N.1    Kobisch, M.2    Martineau-Doize, B.3    Jacques, M.4    Gottschalk, M.5
  • 32
    • 0025813338 scopus 로고
    • A longitudinal study of natural infection of piglets with Streptococcus suis types 1 and 2
    • Robertson I. D., D. K. Blackmore, D. J. Hampson & Z. F. Fu: A longitudinal study of natural infection of piglets with Streptococcus suis types 1 and 2. Epidemiol Infect 107, 119-126 (1991)
    • (1991) Epidemiol Infect , vol.107 , pp. 119-126
    • Robertson, I.D.1    Blackmore, D.K.2    Hampson, D.J.3    Fu, Z.F.4
  • 33
    • 0025827206 scopus 로고
    • Identification of two proteins associated with virulence of Streptococcus suis type 2
    • Vecht U., H. J. Wisselink, M. L. Jellema & H. E. Smith: Identification of two proteins associated with virulence of Streptococcus suis type 2. Infect Immun 59, 3156-3162 (1991)
    • (1991) Infect Immun , vol.59 , pp. 3156-3162
    • Vecht, U.1    Wisselink, H.J.2    Jellema, M.L.3    Smith, H.E.4
  • 34
    • 0024692557 scopus 로고
    • Differences in virulence between two strains of Streptococcus suis type II after experimentally induced infection of newborn germ-free pigs
    • Vecht U., J. P. Arends, E. J. van der Molen & L. A. van Leengoed: Differences in virulence between two strains of Streptococcus suis type II after experimentally induced infection of newborn germ-free pigs. Am J Vet Res 50, 1037-1043 (1989)
    • (1989) Am J Vet Res , vol.50 , pp. 1037-1043
    • Vecht, U.1    Arends, J.P.2    Van Der Molen, E.J.3    Van Leengoed, L.A.4
  • 35
    • 0026316140 scopus 로고
    • Virulence of Streptococcus suis type 2 strains in newborn germfree pigs depends on phenotype
    • Vecht U., H. J. Wisselink, J. E. van Dijk & H. E. Smith: Virulence of Streptococcus suis type 2 strains in newborn germfree pigs depends on phenotype. Infect Immun 60, 550-556 (1992)
    • (1992) Infect Immun , vol.60 , pp. 550-556
    • Vecht, U.1    Wisselink, H.J.2    Van Dijk, J.E.3    Smith, H.E.4
  • 36
    • 0027272260 scopus 로고
    • Repeats in an extracellular protein of weakly pathogenic strains of Streptococcus suis type 2 are absent in pathogenic strains
    • Smith H. E., F. H. Reek, U. Vecht, A. L. Gielkens & M. A. Smits: Repeats in an extracellular protein of weakly pathogenic strains of Streptococcus suis type 2 are absent in pathogenic strains. Infect Immun 61, 3318-3326 (1993)
    • (1993) Infect Immun , vol.61 , pp. 3318-3326
    • Smith, H.E.1    Reek, F.H.2    Vecht, U.3    Gielkens, A.L.4    Smits, M.A.5
  • 37
    • 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
    • Wisselink H. J., H. E. Smith, N. Stockhofe-Zurwieden, K. Peperkamp & U. Vecht: 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 74, 237-248 (2000)
    • (2000) Vet Microbiol , vol.74 , pp. 237-248
    • Wisselink, H.J.1    Smith, H.E.2    Stockhofe-Zurwieden, N.3    Peperkamp, K.4    Vecht, U.5
  • 38
    • 0031607123 scopus 로고    scopus 로고
    • Production of virulence-related proteins by Canadian strains of Streptococcus suis capsular type 2
    • Gottschalk M., A. Lebrun, H. Wisselink, J. D. Dubreuil, H. Smith & U. Vecht: Production of virulence-related proteins by Canadian strains of Streptococcus suis capsular type 2. Can J Vet Res 62, 75-79 (1998)
    • (1998) Can J Vet Res , vol.62 , pp. 75-79
    • Gottschalk, M.1    Lebrun, A.2    Wisselink, H.3    Dubreuil, J.D.4    Smith, H.5    Vecht, U.6
  • 39
    • 0026725379 scopus 로고
    • Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2
    • Smith H. E., U. Vecht, A. L. Gielkens & M. A. Smits: Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2. Infect Immun 60, 2361-2367 (1992)
    • (1992) Infect Immun , vol.60 , pp. 2361-2367
    • Smith, H.E.1    Vecht, U.2    Gielkens, A.L.3    Smits, M.A.4
  • 40
    • 0029796644 scopus 로고    scopus 로고
    • Mutants of Streptococcus suis types 1 and 2 impaired in expression of muramidase-released protein and extracellular protein induce disease in newborn germfree pigs
    • Smith H. E., U. Vecht, H. J. Wisselink, N. Stockhofe-Zurwieden, Y. Biermann & M. A. Smits: Mutants of Streptococcus suis types 1 and 2 impaired in expression of muramidase-released protein and extracellular protein induce disease in newborn germfree pigs. Infect Immun 64, 4409-4412 (1996)
    • (1996) Infect Immun , vol.64 , pp. 4409-4412
    • Smith, H.E.1    Vecht, U.2    Wisselink, H.J.3    Stockhofe-Zurwieden, N.4    Biermann, Y.5    Smits, M.A.6
  • 41
    • 0032961029 scopus 로고    scopus 로고
    • Relatedness of Streptococcus suis serotype 2 isolates from different geographic origins as evaluated by molecular fingerprinting and phenotyping
    • Chatellier S., M. Gottschalk, R. Higgins, R. Brousseau & J. Harel: Relatedness of Streptococcus suis serotype 2 isolates from different geographic origins as evaluated by molecular fingerprinting and phenotyping. J Clin Microbiol 37, 362-366 (1999)
    • (1999) J Clin Microbiol , vol.37 , pp. 362-366
    • Chatellier, S.1    Gottschalk, M.2    Higgins, R.3    Brousseau, R.4    Harel, J.5
  • 42
    • 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., U. Vecht, N. Stockhofe-Zurwieden & H. E. Smith: Protection of pigs against challenge with virulent Streptococcus suis serotype 2 strains by a muramidase-released protein and extracellular factor vaccine. Vet Rec 148, 473-477 (2001)
    • (2001) Vet Rec , vol.148 , pp. 473-477
    • Wisselink, H.J.1    Vecht, U.2    Stockhofe-Zurwieden, N.3    Smith, H.E.4
  • 43
    • 0040162342 scopus 로고    scopus 로고
    • Production of muraminidase-released protein (MRP), extracellular factor (EF) and suilysin by field isolates of Streptococcus suis capsular types 2, 1/2, 9, 7 and 3 isolated from swine in France
    • Berthelot-Hérault F., H. Morvan, A.-M. Kéribin, M. Gottschalk & M. Kobisch: Production of muraminidase-released protein (MRP), extracellular factor (EF) and suilysin by field isolates of Streptococcus suis capsular types 2, 1/2, 9, 7 and 3 isolated from swine in France. Vet Res 31, 473-479 (2000)
    • (2000) Vet Res , vol.31 , pp. 473-479
    • Berthelot-Hérault, F.1    Morvan, H.2    Kéribin, A.-M.3    Gottschalk, M.4    Kobisch, M.5
  • 44
    • 0029680642 scopus 로고    scopus 로고
    • Prevalence of various phenotypes of Streptococcus suis isolated from swine in the U.S.A. based on the presence of muraminidase-released protein and extracellular factor
    • Galina L., U. Vecht, H. J. Wisselink & C. Pijoan: Prevalence of various phenotypes of Streptococcus suis isolated from swine in the U.S.A. based on the presence of muraminidase-released protein and extracellular factor. Can J Vet Res 60, 72-74 (1996)
    • (1996) Can J Vet Res , vol.60 , pp. 72-74
    • Galina, L.1    Vecht, U.2    Wisselink, H.J.3    Pijoan, C.4
  • 45
    • 0028231216 scopus 로고
    • Identification, purification, and characterization of a thiol-activated hemolysin (suilysin) of Streptococcus suis
    • Jacobs A. A., P. L. Loeffen, A. J. van den Berg & P. K. Storm: Identification, purification, and characterization of a thiol-activated hemolysin (suilysin) of Streptococcus suis. Infect Immun 62, 1742-1748 (1994)
    • (1994) Infect Immun , vol.62 , pp. 1742-1748
    • Jacobs, A.A.1    Loeffen, P.L.2    Van Den Berg, A.J.3    Storm, P.K.4
  • 46
    • 0028895636 scopus 로고
    • Characterization of Streptococcus suis capsular type 2 haemolysin
    • Gottschalk M. G., S. Lacouture & J. D. Dubreuil: Characterization of Streptococcus suis capsular type 2 haemolysin. Microbiology 141, 189-195 (1995)
    • (1995) Microbiology , vol.141 , pp. 189-195
    • Gottschalk, M.G.1    Lacouture, S.2    Dubreuil, J.D.3
  • 47
    • 0034877296 scopus 로고    scopus 로고
    • The family of thiol-activated, cholesterol-binding cytolysins
    • Palmer M.: The family of thiol-activated, cholesterol-binding cytolysins. Toxicon 39, 1681-1689 (2001)
    • (2001) Toxicon , vol.39 , pp. 1681-1689
    • Palmer, M.1
  • 48
    • 0002027172 scopus 로고
    • The family of the antigenically-related cholesterol-binding ("sulphydryl-activated") cytolytic toxins
    • Eds: Alouf J E, New York Academic Press, New York
    • Alouf J. E. & C. Geoffroy: The family of the antigenically-related cholesterol-binding ("sulphydryl-activated") cytolytic toxins. In: Sourcebook of Bacterial Protein Toxins. Eds: Alouf J E, New York Academic Press, New York (1991)
    • (1991) Sourcebook of Bacterial Protein Toxins
    • Alouf, J.E.1    Geoffroy, C.2
  • 49
    • 0031752825 scopus 로고    scopus 로고
    • Characterisation of the gene encoding suilysin from Streptococcus suis and expression in field strains
    • Segers R. P., T. Kenter, L. A. M. de Haan & A. A. C. Jacobs: Characterisation of the gene encoding suilysin from Streptococcus suis and expression in field strains. FEMS Microbiol Lett 167, 255-261 (1998)
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 255-261
    • Segers, R.P.1    Kenter, T.2    De Haan, L.A.M.3    Jacobs, A.A.C.4
  • 51
    • 0033963551 scopus 로고    scopus 로고
    • Streptococcus suis serotype 2 interactions with human brain microvascular endothelial cells
    • Charland N., V. Nizet, C. Rubens, K. S. Kim, S. Lacouture & M. Gottschalk: Streptococcus suis serotype 2 interactions with human brain microvascular endothelial cells. Infect Immun 68, 637-643 (2000)
    • (2000) Infect Immun , vol.68 , pp. 637-643
    • Charland, N.1    Nizet, V.2    Rubens, C.3    Kim, K.S.4    Lacouture, S.5    Gottschalk, M.6
  • 52
    • 0033870279 scopus 로고    scopus 로고
    • Interactions between Streptococcus suis serotype 2 and different epithelial cell lines
    • Lalonde M., M. Segura, S. Lacouture & M. Gottschalk: Interactions between Streptococcus suis serotype 2 and different epithelial cell lines. Microbiology 146, 1913-1921 (2000)
    • (2000) Microbiology , vol.146 , pp. 1913-1921
    • Lalonde, M.1    Segura, M.2    Lacouture, S.3    Gottschalk, M.4
  • 53
    • 0032883924 scopus 로고    scopus 로고
    • Epithelial invasion and cell lysis by virulent strains of Streptococcus suis is enhanced by the presence of suilysin
    • Norton P. M., C. Rolph, P. N. Ward, R. W. Bentley & J. A. Leigh: Epithelial invasion and cell lysis by virulent strains of Streptococcus suis is enhanced by the presence of suilysin. FEMS Immunol Med Microbiol 26, 25-35 (1999)
    • (1999) FEMS Immunol Med Microbiol , vol.26 , pp. 25-35
    • Norton, P.M.1    Rolph, C.2    Ward, P.N.3    Bentley, R.W.4    Leigh, J.A.5
  • 54
    • 0036073871 scopus 로고    scopus 로고
    • Streptococcus suis interactions with the murine macrophage cell line J774: Adhesion and cytotoxicity
    • Segura M. & M. Gottschalk: Streptococcus suis interactions with the murine macrophage cell line J774: adhesion and cytotoxicity. Infect immun 70, 4312-4322 (2002)
    • (2002) Infect Immun , vol.70 , pp. 4312-4322
    • Segura, M.1    Gottschalk, M.2
  • 55
    • 0037458527 scopus 로고    scopus 로고
    • Pro-inflammatory cytokine and chemokine release by human brain microvascular endothelial cells stimulated by Streptococcus suis serotype 2
    • Vadeboncoeur N., M. Segura, D. Al-Numani, G. Vanier & M. Gottschalk: Pro-inflammatory cytokine and chemokine release by human brain microvascular endothelial cells stimulated by Streptococcus suis serotype 2. FEMS Immunol Med Microbiol 35, 49-58 (2003)
    • (2003) FEMS Immunol Med Microbiol , vol.35 , pp. 49-58
    • Vadeboncoeur, N.1    Segura, M.2    Al-Numani, D.3    Vanier, G.4    Gottschalk, M.5
  • 56
    • 0037215998 scopus 로고    scopus 로고
    • Role of suilysin in pathogenesis of Streptococcus suis capsular serotype 2
    • Lun S., J. Perez-Casal, W. Connor & P. J. Willson: Role of suilysin in pathogenesis of Streptococcus suis capsular serotype 2. Microb Pathog 34, 27-37 (2003)
    • (2003) Microb Pathog , vol.34 , pp. 27-37
    • Lun, S.1    Perez-Casal, J.2    Connor, W.3    Willson, P.J.4
  • 57
    • 0038047059 scopus 로고    scopus 로고
    • Up-regulation of ICAM-1, CD11a/CD18 and CD11c/CD18 on human THP-I monocytes stimulated by Streptococcus suis serotype 2
    • Al-Numani D., M. Segura, M. Doré & M. Gottschalk: Up-regulation of ICAM-1, CD11a/CD18 and CD11c/CD18 on human THP-I monocytes stimulated by Streptococcus suis serotype 2. Clin Exp Immunol 133, 67-77 (2002)
    • (2002) Clin Exp Immunol , vol.133 , pp. 67-77
    • Al-Numani, D.1    Segura, M.2    Doré, M.3    Gottschalk, M.4
  • 59
    • 0029838726 scopus 로고    scopus 로고
    • Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis
    • Jacobs A. A., A. J. van den Berg & P. L. Loeffen: Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis. Vet Rec 139, 225-228 (1996)
    • (1996) Vet Rec , vol.139 , pp. 225-228
    • Jacobs, A.A.1    Van Den Berg, A.J.2    Loeffen, P.L.3
  • 60
    • 0029646404 scopus 로고
    • Production of suilysin, the thiol-activated haemolysin of Streptococcus suis, by field isolates from diseased pigs
    • Jacobs A. A., A. J. van den Berg, J. C. Baars, B. Nielsen & L. W. Johannsen: Production of suilysin, the thiol-activated haemolysin of Streptococcus suis, by field isolates from diseased pigs. Vet Rec 137, 295-296 (1995)
    • (1995) Vet Rec , vol.137 , pp. 295-296
    • Jacobs, A.A.1    Van Den Berg, A.J.2    Baars, J.C.3    Nielsen, B.4    Johannsen, L.W.5
  • 61
    • 0032746044 scopus 로고    scopus 로고
    • Hybridization analysis of the gene encoding a hemolysin (suilysin) of Streptococcus suis type 2: Evidence for the absence of the gene in some isolates
    • Okwumabua O., O. Abdelmagid & M. M. Chengappa: Hybridization analysis of the gene encoding a hemolysin (suilysin) of Streptococcus suis type 2: evidence for the absence of the gene in some isolates. FEMS Microbiol Lett 181, 113-121 (1999)
    • (1999) FEMS Microbiol Lett , vol.181 , pp. 113-121
    • Okwumabua, O.1    Abdelmagid, O.2    Chengappa, M.M.3
  • 62
    • 0032701076 scopus 로고    scopus 로고
    • Presence of the Streptococcus suis suilysin gene and expression of MRP and EF correlates with high virulence in Streptococcus suis type 2 isolates
    • Staats J., P. Brandon, G. Stewart & M. M. Chengappa: Presence of the Streptococcus suis suilysin gene and expression of MRP and EF correlates with high virulence in Streptococcus suis type 2 isolates. Vet Microbiol 70, 201-211 (1999)
    • (1999) Vet Microbiol , vol.70 , pp. 201-211
    • Staats, J.1    Brandon, P.2    Stewart, G.3    Chengappa, M.M.4
  • 63
    • 0035129356 scopus 로고    scopus 로고
    • Relatedness of Streptococcus suis isolates of various serotypes and clinical backgrounds as evaluated by macrorestriction analysis and expression of potential virulence traits
    • Allgaier A., R. Goethe, H. J. Wisselink, H. E. Smith & P. Valentin-Weigand: Relatedness of Streptococcus suis isolates of various serotypes and clinical backgrounds as evaluated by macrorestriction analysis and expression of potential virulence traits. J Clin Microbiol 39, 445-453 (2001)
    • (2001) J Clin Microbiol , vol.39 , pp. 445-453
    • Allgaier, A.1    Goethe, R.2    Wisselink, H.J.3    Smith, H.E.4    Valentin-Weigand, P.5
  • 64
    • 0026208919 scopus 로고
    • Beta-hemolytic streptococci from pigs: Bacteriological diagnosis
    • Hommez J., L. A. Devriese, F. Castryck & C. Miry: Beta-hemolytic streptococci from pigs: bacteriological diagnosis. J Vet Med B 38, 441-444 (1991)
    • (1991) J Vet Med B , vol.38 , pp. 441-444
    • Hommez, J.1    Devriese, L.A.2    Castryck, F.3    Miry, C.4
  • 65
    • 0028641577 scopus 로고
    • A cytotoxic factor of Streptococcus suis isolated from a septicemia patient
    • Yamaguchi M., M. Miyake, H. Nishiya & M. Noda: A cytotoxic factor of Streptococcus suis isolated from a septicemia patient. Jpn J Med Sci Biol 47, 318-319 (1994)
    • (1994) Jpn J Med Sci Biol , vol.47 , pp. 318-319
    • Yamaguchi, M.1    Miyake, M.2    Nishiya, H.3    Noda, M.4
  • 66
    • 0037436490 scopus 로고    scopus 로고
    • Identification and characterization of four proteases produced by Streptococcus suis
    • Jobin M.-C. & D. Grenier: Identification and characterization of four proteases produced by Streptococcus suis. FEMS Microbiol Lett 220, 113-119 (2003)
    • (2003) FEMS Microbiol Lett , vol.220 , pp. 113-119
    • Jobin, M.-C.1    Grenier, D.2
  • 67
    • 0033619675 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides
    • Mentlein R.: Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul Pept 85, 9-24 (1999)
    • (1999) Regul Pept , vol.85 , pp. 9-24
    • Mentlein, R.1
  • 68
    • 0026424245 scopus 로고
    • Superoxide dismutases of pathogenic and non-pathogenic Streptococcus suis type 2 isolates
    • Langford P., A. E. Williams & J. S. Kroll: Superoxide dismutases of pathogenic and non-pathogenic Streptococcus suis type 2 isolates. FEMS Microbiol Lett 61, 347-350 (1991)
    • (1991) FEMS Microbiol Lett , vol.61 , pp. 347-350
    • Langford, P.1    Williams, A.E.2    Kroll, J.S.3
  • 69
    • 0033306553 scopus 로고    scopus 로고
    • Effects of iron and manganese availability on growth and production of Superoxide dismutase by Streptococcus suis
    • Niven D. F., A. Ekins & A. A. W. Al-Samaurai: Effects of iron and manganese availability on growth and production of Superoxide dismutase by Streptococcus suis. Can J Microbiol 45, 1027-1032 (1999)
    • (1999) Can J Microbiol , vol.45 , pp. 1027-1032
    • Niven, D.F.1    Ekins, A.2    Al-Samaurai, A.A.W.3
  • 70
    • 0019412005 scopus 로고
    • Bacterial adherence: Adhesin-receptor interactions mediating the attachment of bacteria to mucosal surfaces
    • Beachey E. H.: Bacterial adherence: adhesin-receptor interactions mediating the attachment of bacteria to mucosal surfaces. J Infect Dis 143, 325-345 (1981)
    • (1981) J Infect Dis , vol.143 , pp. 325-345
    • Beachey, E.H.1
  • 72
    • 0028990155 scopus 로고
    • Bacteriocins of gram-positive bacteria
    • Jack R. W., J. R. Tagg & B. Ray: Bacteriocins of gram-positive bacteria. Microbiol Rev 59, 171-200 (1995)
    • (1995) Microbiol Rev , vol.59 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 73
    • 0042029585 scopus 로고    scopus 로고
    • Production and properties of bacteriocin-like inhibitory substances from the swine pathogen Streptococcus suis serotype 2
    • Mélançon D. & D. Grenier: Production and properties of bacteriocin-like inhibitory substances from the swine pathogen Streptococcus suis serotype 2. Appl Environ Microbiol 69, 4482-4488 (2003)
    • (2003) Appl Environ Microbiol , vol.69 , pp. 4482-4488
    • Mélançon, D.1    Grenier, D.2
  • 74
    • 0022977009 scopus 로고
    • Biology of the group E streptococci: A review
    • Wessman G. E.: Biology of the group E streptococci: a review. Vet Microbiol 12, 297-328 (1986)
    • (1986) Vet Microbiol , vol.12 , pp. 297-328
    • Wessman, G.E.1
  • 75
    • 0032058561 scopus 로고    scopus 로고
    • Studies on biochemical, serological and further characteristics of Streptococcus porcinus
    • Laminler C., N. Cirak & J. Smola: Studies on biochemical, serological and further characteristics of Streptococcus porcinus. J Vet Med B 45, 235-243 (1998)
    • (1998) J Vet Med B , vol.45 , pp. 235-243
    • Laminler, C.1    Cirak, N.2    Smola, J.3
  • 76
    • 0028869793 scopus 로고
    • Identification of Streptococcus porcinus from human sources
    • Facklam R., J. Elliott, N. Pigott & A. R. Franklin: Identification of Streptococcus porcinus from human sources. J Clin Microbiol 33, 385-388 (1995)
    • (1995) J Clin Microbiol , vol.33 , pp. 385-388
    • Facklam, R.1    Elliott, J.2    Pigott, N.3    Franklin, A.R.4
  • 77
    • 0036299316 scopus 로고    scopus 로고
    • Specificity role of the streptokinase C-terminal domain in plasminogen activation
    • Kim D. M., S. J. Lee, S. K. Yoon & S. M. Byun: Specificity role of the streptokinase C-terminal domain in plasminogen activation. Biochem Biophys Res Commun 290, 585-588 (2002)
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 585-588
    • Kim, D.M.1    Lee, S.J.2    Yoon, S.K.3    Byun, S.M.4
  • 79
    • 0031607564 scopus 로고    scopus 로고
    • Biochemical and serological examination of beta-hemolytic streptococci isolated from slaughtered pigs
    • Katsumi M., Y. Kataoka, T. Takahashi, N. Kikuchi & T. Hiramune: Biochemical and serological examination of beta-hemolytic streptococci isolated from slaughtered pigs. J Vet Med Sci 60, 129-131 (1998)
    • (1998) J Vet Med Sci , vol.60 , pp. 129-131
    • Katsumi, M.1    Kataoka, Y.2    Takahashi, T.3    Kikuchi, N.4    Hiramune, T.5
  • 80
    • 0020695698 scopus 로고
    • Bacteriocin-like activity of group B and group C streptococci of human and of animal origin
    • Schofield C. R. & J. R. Tagg: Bacteriocin-like activity of group B and group C streptococci of human and of animal origin. J Hyg (Lond) 90, 7-18 (1983)
    • (1983) J Hyg (Lond) , vol.90 , pp. 7-18
    • Schofield, C.R.1    Tagg, J.R.2
  • 81
    • 0033856431 scopus 로고    scopus 로고
    • Haemolysin-deficient variants of Streptococcus pyogenes and S. dysgalactiae subsp. equisimilis may be overlooked as aetiological agents of pharyngitis
    • Dierksen K. P. & J. R. Tagg: Haemolysin-deficient variants of Streptococcus pyogenes and S. dysgalactiae subsp. equisimilis may be overlooked as aetiological agents of pharyngitis. J Med Microbiol 49, 811-816 (2000)
    • (2000) J Med Microbiol , vol.49 , pp. 811-816
    • Dierksen, K.P.1    Tagg, J.R.2
  • 82
    • 0027246044 scopus 로고
    • Purification and characterization of streptolysin O secreted by Streptococcus equisimilis (group C)
    • Gerlach D., W. Kohler, E. Gunther & K. Mann: Purification and characterization of streptolysin O secreted by Streptococcus equisimilis (group C). Infect Immun 61, 2727-2731 (1993)
    • (1993) Infect Immun , vol.61 , pp. 2727-2731
    • Gerlach, D.1    Kohler, W.2    Gunther, E.3    Mann, K.4
  • 83
    • 0030868813 scopus 로고    scopus 로고
    • M proteins of Streptococcus equisimilis strains isolated from pharyngitis patients
    • Bisno A. L., C. Collins & J. C. Turner: M proteins of Streptococcus equisimilis strains isolated from pharyngitis patients. Adv Exp Med Biol 418, 745-748 (1997)
    • (1997) Adv Exp Med Biol , vol.418 , pp. 745-748
    • Bisno, A.L.1    Collins, C.2    Turner, J.C.3
  • 84
    • 0037063971 scopus 로고    scopus 로고
    • Superantigen-like gene(s) in human pathogenic Streptococcus dysgalactiae, subsp equisimilis: Genomic localisation of the gene encoding streptococcal pyrogenic exotoxin G (speG(dys))
    • Sachse S., P. Seidel, D. Gerlach, E. Gunther, J. Rodel, E. Straube & K. H. Schmidt: Superantigen-like gene(s) in human pathogenic Streptococcus dysgalactiae, subsp equisimilis: genomic localisation of the gene encoding streptococcal pyrogenic exotoxin G (speG(dys)). FEMS Immunol Med Microbiol 34, 159-167 (2002)
    • (2002) FEMS Immunol Med Microbiol , vol.34 , pp. 159-167
    • Sachse, S.1    Seidel, P.2    Gerlach, D.3    Gunther, E.4    Rodel, J.5    Straube, E.6    Schmidt, K.H.7
  • 85
    • 0025988405 scopus 로고
    • Streptokinases produced by pathogenic group C streptococci demonstrate species specificity plasminogen activation
    • McCoy H. E., C. C. Broder & R. Lottenberg: Streptokinases produced by pathogenic group C streptococci demonstrate species specificity plasminogen activation. J Infect Dis 164, 515-521 (1991)
    • (1991) J Infect Dis , vol.164 , pp. 515-521
    • McCoy, H.E.1    Broder, C.C.2    Lottenberg, R.3
  • 86
    • 0032744287 scopus 로고    scopus 로고
    • Cloning, expression, sequence analysis, and characterization of streptokinases secreted by porcine and equine isolates of Streptococcus equisimilis
    • Caballero A. R., R. Lottenberg & K. H. Johnston: Cloning, expression, sequence analysis, and characterization of streptokinases secreted by porcine and equine isolates of Streptococcus equisimilis. Infect Immun 67, 6478-6486 (1999)
    • (1999) Infect Immun , vol.67 , pp. 6478-6486
    • Caballero, A.R.1    Lottenberg, R.2    Johnston, K.H.3
  • 87
    • 0032752642 scopus 로고    scopus 로고
    • Species specificity of plasminogen activation and acquisition of surface-associated proteolytic activity by Group C Streptococci grown in plasma
    • Schroeder B., M. D. P. Boyle, B. R. Sheerin, A. C. Asbury & R. Lottenberg: Species specificity of plasminogen activation and acquisition of surface-associated proteolytic activity by Group C Streptococci grown in plasma. Infect Immun 67, 6487-6495 (1999)
    • (1999) Infect Immun , vol.67 , pp. 6487-6495
    • Schroeder, B.1    Boyle, M.D.P.2    Sheerin, B.R.3    Asbury, A.C.4    Lottenberg, R.5
  • 88
    • 0028133589 scopus 로고
    • Characterization of a novel streptokinase produced by Streptococcus equisimilis of non-human origin
    • Nowicki S. T., D. Minning-Wenz, K. H. Johnston & R. Lottenberg: Characterization of a novel streptokinase produced by Streptococcus equisimilis of non-human origin. Thromb Haemost 72, 595-603 (1994)
    • (1994) Thromb Haemost , vol.72 , pp. 595-603
    • Nowicki, S.T.1    Minning-Wenz, D.2    Johnston, K.H.3    Lottenberg, R.4
  • 90
    • 0032520623 scopus 로고    scopus 로고
    • Potential virulence factors of Streptococcus dysgalactiae associated with bovine mastitis
    • Calvinho L. F., R. A. Almeida & S. P. Oliver: Potential virulence factors of Streptococcus dysgalactiae associated with bovine mastitis. Vet Microbiol 61, 93-110 (1998)
    • (1998) Vet Microbiol , vol.61 , pp. 93-110
    • Calvinho, L.F.1    Almeida, R.A.2    Oliver, S.P.3
  • 91
    • 0030180379 scopus 로고    scopus 로고
    • Influence of Streptococcus dysgalactiae surface hydrophobicity on adherence to mammary epithelial cells and phagocytosis by mammary macrophages
    • Calvinho L. F., R. A. Almeida & S. P. Oliver: Influence of Streptococcus dysgalactiae surface hydrophobicity on adherence to mammary epithelial cells and phagocytosis by mammary macrophages. Zentralbl Veterinarmed [B] 43, 257-266 (1996)
    • (1996) Zentralbl Veterinarmed [B] , vol.43 , pp. 257-266
    • Calvinho, L.F.1    Almeida, R.A.2    Oliver, S.P.3
  • 92
    • 0009830859 scopus 로고
    • Streptococcal M proteins
    • Fishetti V. A.: Streptococcal M proteins. Sci Am 264, 32-39 (1991)
    • (1991) Sci Am , vol.264 , pp. 32-39
    • Fishetti, V.A.1
  • 93
    • 0023229936 scopus 로고
    • Binding of fibronectin, fibrinogen and type 11 collagen to streptococci isolated from bovine mastitis
    • Mamo W., G. Fröman, A. Sundås & T. Wadström: Binding of fibronectin, fibrinogen and type 11 collagen to streptococci isolated from bovine mastitis. Microb Pathog 2, 417-424 (1987)
    • (1987) Microb Pathog , vol.2 , pp. 417-424
    • Mamo, W.1    Fröman, G.2    Sundås, A.3    Wadström, T.4
  • 94
    • 0028876382 scopus 로고
    • Phenotypic characterization of Streptococcus dysgalactiae isolates from bovine mastitis by their binding to host derived proteins
    • Rantamäki L. K. & H. P. Müller: Phenotypic characterization of Streptococcus dysgalactiae isolates from bovine mastitis by their binding to host derived proteins. Vet Microbiol 46, 415-426 (1995)
    • (1995) Vet Microbiol , vol.46 , pp. 415-426
    • Rantamäki, L.K.1    Müller, H.P.2
  • 96
    • 0025912412 scopus 로고
    • Inhibitory effects of fibrinogen on phagocytic killing of streptococcal isolates from humans, cattle and horses
    • Traore M. Y., P. Valentin-Weigand, G. S. Chhatwal & H. Blobel: Inhibitory effects of fibrinogen on phagocytic killing of streptococcal isolates from humans, cattle and horses. Vet Microbiol 28, 295-302 (1991)
    • (1991) Vet Microbiol , vol.28 , pp. 295-302
    • Traore, M.Y.1    Valentin-Weigand, P.2    Chhatwal, G.S.3    Blobel, H.4
  • 97
    • 0029679927 scopus 로고    scopus 로고
    • Taxonomic study of Lancefield streptococcal groups C, G, and L (Streptococcus dysgalactiae) and proposal of S. dysgalactiae subsp. equisimilis subsp. nov.
    • Vandamme P., B. Pot, E. Falsen, K. Kersters & L. A. Devriese: Taxonomic study of Lancefield streptococcal groups C, G, and L (Streptococcus dysgalactiae) and proposal of S. dysgalactiae subsp. equisimilis subsp. nov. Int J Syst Bacterial 46, 774-781 (1996)
    • (1996) Int J Syst Bacterial , vol.46 , pp. 774-781
    • Vandamme, P.1    Pot, B.2    Falsen, E.3    Kersters, K.4    Devriese, L.A.5
  • 98
    • 0032520615 scopus 로고    scopus 로고
    • The interaction of Streptococcus dysgalactiae with plasmin and plasminogen
    • Leigh J. A., S. M. Hodgkindson & R. A. Lincoln: The interaction of Streptococcus dysgalactiae with plasmin and plasminogen. Vet Microbiol 61, 121-135 (1998)
    • (1998) Vet Microbiol , vol.61 , pp. 121-135
    • Leigh, J.A.1    Hodgkindson, S.M.2    Lincoln, R.A.3
  • 99
    • 0025319341 scopus 로고
    • Isolation and characterization of hyaluronidases from Streptococcus dysgalactiae, S. zooepidemicus and S. equi
    • Sting R., P. Schaufuss & H. Blobel: Isolation and characterization of hyaluronidases from Streptococcus dysgalactiae, S. zooepidemicus and S. equi. Zentralbl Bakteriol 272, 276-282 (1990)
    • (1990) Zentralbl Bakteriol , vol.272 , pp. 276-282
    • Sting, R.1    Schaufuss, P.2    Blobel, H.3
  • 100
    • 0037346432 scopus 로고    scopus 로고
    • Streptococcus dysgalactiae-denved mitogen (SDM), a novel bacterial superantigen: Characterization of its biological activity and predicted tertiary structure
    • Miyoshi-Akiyama T., J. Zhao, H. Kato, K. Kikuchi, K. Totsuka, Y. Kataoka, M. Katsumi & T. Uchiyama: Streptococcus dysgalactiae-denved mitogen (SDM), a novel bacterial superantigen: characterization of its biological activity and predicted tertiary structure. Mol Microbiol 47, 1589-1599 (2003)
    • (2003) Mol Microbiol , vol.47 , pp. 1589-1599
    • Miyoshi-Akiyama, T.1    Zhao, J.2    Kato, H.3    Kikuchi, K.4    Totsuka, K.5    Kataoka, Y.6    Katsumi, M.7    Uchiyama, T.8
  • 101
    • 0032923136 scopus 로고    scopus 로고
    • Streptococcus uberis: A permanent barrier to the control of bovine mastitis?
    • Leigh J. A.: Streptococcus uberis: a permanent barrier to the control of bovine mastitis? Vet J 157, 225-238 (1999)
    • (1999) Vet J , vol.157 , pp. 225-238
    • Leigh, J.A.1
  • 102
    • 0031062339 scopus 로고    scopus 로고
    • Patterns of clinical mastitis manifestations in Danish organic dairy herds
    • Vaarst M. & C. Enevoldsen: Patterns of clinical mastitis manifestations in Danish organic dairy herds. J Dairy Res 64, 23-37 (1997)
    • (1997) J Dairy Res , vol.64 , pp. 23-37
    • Vaarst, M.1    Enevoldsen, C.2
  • 103
    • 0028724209 scopus 로고
    • Pathologic findings of experimentally induced Streptococcus uberis infection in the mammary gland of cows
    • Thomas L. H., W. Haider, A. W. Hill & R. S. Cook: Pathologic findings of experimentally induced Streptococcus uberis infection in the mammary gland of cows. Am J Vet Res 55, 1723-1728 (1994)
    • (1994) Am J Vet Res , vol.55 , pp. 1723-1728
    • Thomas, L.H.1    Haider, W.2    Hill, A.W.3    Cook, R.S.4
  • 104
    • 0032192871 scopus 로고    scopus 로고
    • Virulence factors of Streptococcus uberis isolated from cows with mastitis
    • Oliver S. P., R. A. Almeida & L. F. Calvinho: Virulence factors of Streptococcus uberis isolated from cows with mastitis. Zentralbl Veterinarmed [B] 45, 461-471 (1998)
    • (1998) Zentralbl Veterinarmed [B] , vol.45 , pp. 461-471
    • Oliver, S.P.1    Almeida, R.A.2    Calvinho, L.F.3
  • 105
    • 0024117979 scopus 로고
    • Pathogenicity of two strains of Streptococcus uberis infused into lactating and non-lactating bovine mammary glands
    • Hill A. W.: Pathogenicity of two strains of Streptococcus uberis infused into lactating and non-lactating bovine mammary glands. Res Vet Sci 45, 400-404 (1988)
    • (1988) Res Vet Sci , vol.45 , pp. 400-404
    • Hill, A.W.1
  • 106
    • 0025456435 scopus 로고
    • Two strains of Streptococcus uberis, of differing ability to cause clinical mastitis, differ in their ability to resist some host defence factors
    • Leigh J. A., T. R. Field & M. R. Williams: Two strains of Streptococcus uberis, of differing ability to cause clinical mastitis, differ in their ability to resist some host defence factors. Res Vet Sci 49, 85-87 (1990)
    • (1990) Res Vet Sci , vol.49 , pp. 85-87
    • Leigh, J.A.1    Field, T.R.2    Williams, M.R.3
  • 107
    • 0028266395 scopus 로고
    • Streptococcus uberis resists the bactericidal action of bovine neutrophils despite the presence of bound immunoglobulin
    • Leigh J. A. & T. R. Field: Streptococcus uberis resists the bactericidal action of bovine neutrophils despite the presence of bound immunoglobulin. Infect Immun 62, 1854-1859 (1994)
    • (1994) Infect Immun , vol.62 , pp. 1854-1859
    • Leigh, J.A.1    Field, T.R.2
  • 108
    • 0027727704 scopus 로고
    • Growth curve, capsule expression and characterization of the capsular material of selected strains of Streptococcus uberis
    • Almeida R. A. & S. P. Oliver: Growth curve, capsule expression and characterization of the capsular material of selected strains of Streptococcus uberis. Zentralbl Veterinarmed [B] 40, 697-706 (1993)
    • (1993) Zentralbl Veterinarmed [B] , vol.40 , pp. 697-706
    • Almeida, R.A.1    Oliver, S.P.2
  • 109
    • 0026083526 scopus 로고
    • Killing of Streptococcus uberis by bovine neutrophils following growth in chemically defined media
    • Leigh J. A. & T. R. Field: Killing of Streptococcus uberis by bovine neutrophils following growth in chemically defined media. Vet Res Commun 15, 1-6 (1991)
    • (1991) Vet Res Commun , vol.15 , pp. 1-6
    • Leigh, J.A.1    Field, T.R.2
  • 110
    • 0035167308 scopus 로고    scopus 로고
    • Identification and disruption of two discrete loci encoding hyaluronic acid capsule biosynthesis genes hasA, hasB, and hasC in Streptococcus uberis
    • Ward P. N., T. R. Field, W. G. Ditcham, E. Maguin & J. A. Leigh: Identification and disruption of two discrete loci encoding hyaluronic acid capsule biosynthesis genes hasA, hasB, and hasC in Streptococcus uberis. Infect Immun 69, 392-399 (2001)
    • (2001) Infect Immun , vol.69 , pp. 392-399
    • Ward, P.N.1    Field, T.R.2    Ditcham, W.G.3    Maguin, E.4    Leigh, J.A.5
  • 111
    • 0031656714 scopus 로고    scopus 로고
    • Molecular analysis of the capsule gene region of group A Streptococcus: The hasAB genes are sufficient for capsule expression
    • Ashbaugh C. D., S. Alberti & M. R. Wessels: Molecular analysis of the capsule gene region of group A Streptococcus: the hasAB genes are sufficient for capsule expression. J Bacteriol 190, 4955-4959 (1998)
    • (1998) J Bacteriol , vol.190 , pp. 4955-4959
    • Alberti, A.C.D.S.1    Wessels, M.R.2
  • 112
    • 0027767807 scopus 로고
    • Antiphagocytic effect of the capsule of Streptococcus uberis
    • Almeida R. A. & S. P. Oliver: Antiphagocytic effect of the capsule of Streptococcus uberis. Zentralbl Veterinarmed [B] 40, 707-714 (1993)
    • (1993) Zentralbl Veterinarmed [B] , vol.40 , pp. 707-714
    • Almeida, R.A.1    Oliver, S.P.2
  • 113
    • 0029349680 scopus 로고
    • Phagocytosis of Streptococcus uberis by bovine mammary macrophages:opsonizing effect of bovine antiserum
    • Almeida R. A. & S. P. Oliver: Phagocytosis of Streptococcus uberis by bovine mammary macrophages:opsonizing effect of bovine antiserum. Zentralbl Veterinarmed [B] 42, 331-337 (1995)
    • (1995) Zentralbl Veterinarmed [B] , vol.42 , pp. 331-337
    • Almeida, R.A.1    Oliver, S.P.2
  • 114
    • 0030628660 scopus 로고    scopus 로고
    • Phagocytosis of Streptococcus uberis by bovine mammary gland macrophages
    • Grant R. G. & J. M. Finch: Phagocytosis of Streptococcus uberis by bovine mammary gland macrophages. Res Vet Sci 62, 74-78 (1996)
    • (1996) Res Vet Sci , vol.62 , pp. 74-78
    • Grant, R.G.1    Finch, J.M.2
  • 115
    • 0037220436 scopus 로고    scopus 로고
    • The hyaluronic acid capsule of Streptococcus uberis is not required for the development of infection and clinical mastitis
    • Field T. R., P. N. Ward, L. H. Pedersen & J. A. Leigh: The hyaluronic acid capsule of Streptococcus uberis is not required for the development of infection and clinical mastitis. Infect Immun 71, 132-139 (2003)
    • (2003) Infect Immun , vol.71 , pp. 132-139
    • Field, T.R.1    Ward, P.N.2    Pedersen, L.H.3    Leigh, J.A.4
  • 116
    • 0027384693 scopus 로고
    • Activation of bovine plasminogen by Streptococcus uberis
    • Leigh J. A.: Activation of bovine plasminogen by Streptococcus uberis. FEMS Microbiol Lett 114, 67-71 (1993)
    • (1993) FEMS Microbiol Lett , vol.114 , pp. 67-71
    • Leigh, J.A.1
  • 117
    • 0028306612 scopus 로고
    • Purification of a plasminogen activator from Streptococcus uberis
    • Leigh J. A.: Purification of a plasminogen activator from Streptococcus uberis. FEMS Microbiol Lett 118, 153-158 (1994)
    • (1994) FEMS Microbiol Lett , vol.118 , pp. 153-158
    • Leigh, J.A.1
  • 118
    • 0030821761 scopus 로고    scopus 로고
    • Characterization of a novel plasminogen activator from Streptococcus uberis
    • Lincoln R. A. & J. A. Leigh: Characterization of a novel plasminogen activator from Streptococcus uberis. Adv Exp Med Biol 418, 643-645 (1997)
    • (1997) Adv Exp Med Biol , vol.418 , pp. 643-645
    • Lincoln, R.A.1    Leigh, J.A.2
  • 119
    • 0033052674 scopus 로고    scopus 로고
    • Purification and cloning of a streptokinase from Streptococcus uberis
    • Johnsen L. B., K. Poulsen, M. Kilian & T. E. Petersen: Purification and cloning of a streptokinase from Streptococcus uberis. Infect Immun 67, 1072-1078 (1999)
    • (1999) Infect Immun , vol.67 , pp. 1072-1078
    • Johnsen, L.B.1    Poulsen, K.2    Kilian, M.3    Petersen, T.E.4
  • 121
    • 0035918292 scopus 로고    scopus 로고
    • The mechanism of a bacterial plasminogen activator intermediate between streptokinase and staphylokinase
    • Sazonova I. Y., A. K. Houng, S. A. Chowdhry, B. R. Robinson, L. Hedstrom & G. L. Reed: The mechanism of a bacterial plasminogen activator intermediate between streptokinase and staphylokinase. J Biol Chem 276, 12609-12613 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 12609-12613
    • Sazonova, I.Y.1    Houng, A.K.2    Chowdhry, S.A.3    Robinson, B.R.4    Hedstrom, L.5    Reed, G.L.6
  • 122
    • 0034733025 scopus 로고    scopus 로고
    • Kinetic and structural characterization of a two-domain streptokinase: Dissection of domain functionality
    • Johnsen L. B., L. K. Rasmussen, T. E. Petersen, M. Etzerodt & S. N. Fedosov: Kinetic and structural characterization of a two-domain streptokinase: dissection of domain functionality. Biochemistry 39, 6440-6448 (2000)
    • (2000) Biochemistry , vol.39 , pp. 6440-6448
    • Johnsen, L.B.1    Rasmussen, L.K.2    Petersen, T.E.3    Etzerodt, M.4    Fedosov, S.N.5
  • 123
    • 0036135477 scopus 로고    scopus 로고
    • Characterization of PauB, a novel broad-spectrum plasminogen activator from Streptococcus uberis
    • Ward P. N. & J. A. Leigh: Characterization of PauB, a novel broad-spectrum plasminogen activator from Streptococcus uberis. J Bacteriol 184, 119-125 (2002)
    • (2002) J Bacteriol , vol.184 , pp. 119-125
    • Ward, P.N.1    Leigh, J.A.2
  • 124
    • 0030959780 scopus 로고    scopus 로고
    • Streptococcus uberis acquires plasmin activity following growth in the presence of bovine plasminogen through the action of its specific plasminogen activator
    • Leigh J. A. & R. A. Lincoln: Streptococcus uberis acquires plasmin activity following growth in the presence of bovine plasminogen through the action of its specific plasminogen activator. FEMS Microbiol Lett 154, 123-129 (1997)
    • (1997) FEMS Microbiol Lett , vol.154 , pp. 123-129
    • Leigh, J.A.1    Lincoln, R.A.2
  • 125
    • 0030867317 scopus 로고    scopus 로고
    • The auxotrophic nature of Streptococcus uberis. The acquisition of essential acids from plasmin derived casein peptides
    • Kitt A. J. & J. A. Leigh: The auxotrophic nature of Streptococcus uberis. The acquisition of essential acids from plasmin derived casein peptides. Adv Exp Med Biol 418, 647-650 (1997)
    • (1997) Adv Exp Med Biol , vol.418 , pp. 647-650
    • Kitt, A.J.1    Leigh, J.A.2
  • 126
    • 0024370641 scopus 로고
    • Isolation and characterization of hyaluronidase from Streptococcus uberis
    • Schaufuss P., R. Sting, W. Schaeg & H. Blobel: Isolation and characterization of hyaluronidase from Streptococcus uberis. Zentralbl Bakteriol 271, 46-53 (1989)
    • (1989) Zentralbl Bakteriol , vol.271 , pp. 46-53
    • Schaufuss, P.1    Sting, R.2    Schaeg, W.3    Blobel, H.4
  • 127
    • 0028527434 scopus 로고
    • Proliferation of a bovine mammary epithelial cell line in the presence of bacterial virulence factors
    • Matthews K. R., J. J. Rejman, J. D. Turner & S. P. Oliver: Proliferation of a bovine mammary epithelial cell line in the presence of bacterial virulence factors. J Dairy Sci 77, 2959-2964 (1994)
    • (1994) J Dairy Sci , vol.77 , pp. 2959-2964
    • Matthews, K.R.1    Rejman, J.J.2    Turner, J.D.3    Oliver, S.P.4
  • 128
    • 0026291492 scopus 로고
    • Biochemical and serological properties of Streptococcus uberis
    • Lammler C.: Biochemical and serological properties of Streptococcus uberis. Zentralbl Veterinarmed [B] 38, 737-742 (1991)
    • (1991) Zentralbl Veterinarmed [B] , vol.38 , pp. 737-742
    • Lammler, C.1
  • 129
    • 0028970487 scopus 로고
    • Partial characterization of the cohemolytic factor produced by Streptococcus uberis and comparison with the CAMP-factor
    • Lopes M. F., V. L. Merquior, J. M. Peralta & L. M. Teixeira: Partial characterization of the cohemolytic factor produced by Streptococcus uberis and comparison with the CAMP-factor. FEMS Immunol Med Microbiol 12, 205-212 (1995)
    • (1995) FEMS Immunol Med Microbiol , vol.12 , pp. 205-212
    • Lopes, M.F.1    Merquior, V.L.2    Peralta, J.M.3    Teixeira, L.M.4
  • 130
    • 0033769357 scopus 로고    scopus 로고
    • Identification of streptococci isolated from various sources by determination of cfb gene and other CAMP-factor genes
    • Hassan A. A., A. Abdulmawjood, A. O. Yildirim, K. Fink, C. Lammler & R. Schlenstedt: Identification of streptococci isolated from various sources by determination of cfb gene and other CAMP-factor genes. Can J Microbiol 46, 946-951 (2000)
    • (2000) Can J Microbiol , vol.46 , pp. 946-951
    • Hassan, A.A.1    Abdulmawjood, A.2    Yildirim, A.O.3    Fink, K.4    Lammler, C.5    Schlenstedt, R.6
  • 131
    • 0029930799 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the CAMP factor gene of Streptococcus uberis
    • Jiang M., L. A. Babiuk & A. A. Potter: Cloning, sequencing and expression of the CAMP factor gene of Streptococcus uberis. Microb Pathog 20, 297-307 (1996)
    • (1996) Microb Pathog , vol.20 , pp. 297-307
    • Jiang, M.1    Babiuk, L.A.2    Potter, A.A.3
  • 132
    • 0019406305 scopus 로고
    • Lethal effect of CAMP-factor and Uberis-factor: A new finding about diffusible exosubstances of Streptococcus agalactiae and Streptococcus uberis
    • Shalka B. & J. Smola: Lethal effect of CAMP-factor and Uberis-factor: a new finding about diffusible exosubstances of Streptococcus agalactiae and Streptococcus uberis. Zentralbl Bakteriol 249, 190-194 (1981)
    • (1981) Zentralbl Bakteriol , vol.249 , pp. 190-194
    • Shalka, B.1    Smola, J.2
  • 133
    • 0032529967 scopus 로고    scopus 로고
    • Protein expression by Streptococcus uberis in co-culture with bovine mammary epithelial cells
    • Fang W., D. A. Luther & S. P. Olivier: Protein expression by Streptococcus uberis in co-culture with bovine mammary epithelial cells. FEMS Microbiol Lett 166, 237-242 (1998)
    • (1998) FEMS Microbiol Lett , vol.166 , pp. 237-242
    • Fang, W.1    Luther, D.A.2    Olivier, S.P.3
  • 134
    • 0031278063 scopus 로고    scopus 로고
    • Induction of surface-associated proteins of Streptococcus uberis by cultivation with extracellular matrix components and bovine mammary epithelial cells
    • Gilbert F. B., D. A. Luther & S. P. Olivier: Induction of surface-associated proteins of Streptococcus uberis by cultivation with extracellular matrix components and bovine mammary epithelial cells. FEMS Microbiol Lett 156, 161-164 (1997)
    • (1997) FEMS Microbiol Lett , vol.156 , pp. 161-164
    • Gilbert, F.B.1    Luther, D.A.2    Olivier, S.P.3
  • 135
    • 3142710239 scopus 로고    scopus 로고
    • Molecular epidemiology of Streptococcus agalactiae (group B Streptococcus)
    • Manning S. D.: Molecular epidemiology of Streptococcus agalactiae (group B Streptococcus). Front Biosci 8, S1-18 (2003)
    • (2003) Front Biosci , vol.8
    • Manning, S.D.1
  • 136
    • 0033637467 scopus 로고    scopus 로고
    • Pathogenesis of neonatal Streptococcus agalactiae infections
    • Spellerberg B.: Pathogenesis of neonatal Streptococcus agalactiae infections. Microbes Infect 2, 1733-1742 (2000)
    • (2000) Microbes Infect , vol.2 , pp. 1733-1742
    • Spellerberg, B.1
  • 137
    • 0031183482 scopus 로고    scopus 로고
    • Streptococcus agalactiae mastitis: A review
    • Keefe G. P.: Streptococcus agalactiae mastitis: a review. Can Vet J 38, 429-437 (1997)
    • (1997) Can Vet J , vol.38 , pp. 429-437
    • Keefe, G.P.1
  • 140
    • 0032876761 scopus 로고    scopus 로고
    • M protein of a Streptococcus dysgalactiae human wound isolate shows multiple binding to different plasma proteins and shares epitopes with keratin and human cartilage
    • Geyer A., A. Roth, S. Vettermann, E. Gunther, A. Groh, E. Straube & K. Schmidt: M protein of a Streptococcus dysgalactiae human wound isolate shows multiple binding to different plasma proteins and shares epitopes with keratin and human cartilage. FEMS Immunol Med Microbiol 26, 11-24 (1999)
    • (1999) FEMS Immunol Med Microbiol , vol.26 , pp. 11-24
    • Geyer, A.1    Roth, A.2    Vettermann, S.3    Gunther, E.4    Groh, A.5    Straube, E.6    Schmidt, K.7
  • 141
    • 0037008124 scopus 로고    scopus 로고
    • Pheno- and genotypic properties of streptococci of serological group B of canine and feline origin
    • Yildirim A. O., C. Lammler, R. Weiss & P. Kopp: Pheno- and genotypic properties of streptococci of serological group B of canine and feline origin. FEMS Microbiol Lett 212, 187-192 (2002)
    • (2002) FEMS Microbiol Lett , vol.212 , pp. 187-192
    • Yildirim, A.O.1    Lammler, C.2    Weiss, R.3    Kopp, P.4
  • 142
    • 0021971602 scopus 로고
    • Virulence of human and bovine isolates of group B streptococci (types Ia and III) in experimental pregnant mouse models
    • Poutrel B. & J. Dore: Virulence of human and bovine isolates of group B streptococci (types Ia and III) in experimental pregnant mouse models. Infect Immun 47, 94-97 (1985)
    • (1985) Infect Immun , vol.47 , pp. 94-97
    • Poutrel, B.1    Dore, J.2
  • 143
    • 0021200690 scopus 로고
    • Human and bovine group B streptococci: Two distinct populations
    • Finch L. A. & D. R. Martin: Human and bovine group B streptococci: two distinct populations. J Appl Bacteriol 57, 273-278 (1984)
    • (1984) J Appl Bacteriol , vol.57 , pp. 273-278
    • Finch, L.A.1    Martin, D.R.2
  • 144
    • 0021342628 scopus 로고
    • Type-specific capsular antigen is associated with virulence in late-onset group B streptococcal type III disease
    • Klegerman M. E., K. M. Boyer, C. K. Papierniak, L. Levine & S. P. Gotoff: Type-specific capsular antigen is associated with virulence in late-onset group B streptococcal type III disease. Infect Immun 44, 124-129 (1984)
    • (1984) Infect Immun , vol.44 , pp. 124-129
    • Klegerman, M.E.1    Boyer, K.M.2    Papierniak, C.K.3    Levine, L.4    Gotoff, S.P.5
  • 145
    • 0033986714 scopus 로고    scopus 로고
    • Characterization of Streptococcus agalactiae isolates of bovine and human origin by randomly amplified polymorphic DNA analysis
    • Martinez G., J. Harel, R. Higgins, S. Lacouture, D. Daignault & M. Gottschalk: Characterization of Streptococcus agalactiae isolates of bovine and human origin by randomly amplified polymorphic DNA analysis. J Clin Microbiol 38, 71-78 (2000)
    • (2000) J Clin Microbiol , vol.38 , pp. 71-78
    • Martinez, G.1    Harel, J.2    Higgins, R.3    Lacouture, S.4    Daignault, D.5    Gottschalk, M.6
  • 146
    • 0344588809 scopus 로고    scopus 로고
    • Streptococcus suis and group B Streptococcus differ in their interactions with murine macrophages
    • Segura M. A., P. Cléroux & M. Gottschalk: Streptococcus suis and group B Streptococcus differ in their interactions with murine macrophages. FEMS Immunol Med Microbiol 21, 189-195 (1998)
    • (1998) FEMS Immunol Med Microbiol , vol.21 , pp. 189-195
    • Segura, M.A.1    Cléroux, P.2    Gottschalk, M.3
  • 147
    • 0023429307 scopus 로고
    • Transposon mutagenesis of group B streptococcal type III capsular polysaccharide: Correlation of capsule expression with virulence
    • Rubens C. E., M. R. Wessels, L. M. Heggen & D. L. Kasper: Transposon mutagenesis of group B streptococcal type III capsular polysaccharide: correlation of capsule expression with virulence. Proc Natl Acad Sci USA 84, 7208-7212 (1987)
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7208-7212
    • Rubens, C.E.1    Wessels, M.R.2    Heggen, L.M.3    Kasper, D.L.4
  • 148
    • 0024078436 scopus 로고
    • Ingestion and killing of Streptococcus agalactiae by bovine granulocytes in the presence of natural opsonins
    • Rainard P., Y. Lautrou & B. Poutrel: Ingestion and killing of Streptococcus agalactiae by bovine granulocytes in the presence of natural opsonins. Vet Microbiol 18, 41-50 (1988)
    • (1988) Vet Microbiol , vol.18 , pp. 41-50
    • Rainard, P.1    Lautrou, Y.2    Poutrel, B.3
  • 149
    • 0028651957 scopus 로고
    • Phase variation in streptococci of serological group B. Characteristic properties of isolates from human and bovine infection
    • Salasia S. I., I. W. Wibawan, C. Lammler & M. Sellin: Phase variation in streptococci of serological group B. Characteristic properties of isolates from human and bovine infection. APMIS 102, 925-930 (1994)
    • (1994) APMIS , vol.102 , pp. 925-930
    • Salasia, S.I.1    Wibawan, I.W.2    Lammler, C.3    Sellin, M.4
  • 150
    • 0029069117 scopus 로고
    • In vivo hemolytic activity of group B Streptococcus is dependent on erythrocyte-bacteria contact and independent of a carrier molecule
    • Platt M. W.: In vivo hemolytic activity of group B Streptococcus is dependent on erythrocyte-bacteria contact and independent of a carrier molecule. Curr Microbiol 31, 5-9 (1995)
    • (1995) Curr Microbiol , vol.31 , pp. 5-9
    • Platt, M.W.1
  • 151
    • 0020522325 scopus 로고
    • Hemolysin produced by group B Streptococcus agalactiae
    • Dal M. C. & H. Monteil: Hemolysin produced by group B Streptococcus agalactiae. FEMS Microbiol Lett 16, 89-94 (1983)
    • (1983) FEMS Microbiol Lett , vol.16 , pp. 89-94
    • Dal, M.C.1    Monteil, H.2
  • 152
    • 0032935929 scopus 로고    scopus 로고
    • Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition
    • Spellerberg B., B. Pohl, G. Haase, S. Martin, J. Weber-Heynemann & R. Lutticken: Identification of genetic determinants for the hemolytic activity of Streptococcus agalactiae by ISS1 transposition. J Bacteriol 181, 3212-3219 (1999)
    • (1999) J Bacteriol , vol.181 , pp. 3212-3219
    • Spellerberg, B.1    Pohl, B.2    Haase, G.3    Martin, S.4    Weber-Heynemann, J.5    Lutticken, R.6
  • 153
    • 0034662445 scopus 로고    scopus 로고
    • The cyl genes of Streptococcus agalactiae are involved in the production of pigment
    • Spellerberg B., S. Martin, C. Brandt & R. Lutticken: The cyl genes of Streptococcus agalactiae are involved in the production of pigment. FEMS Microbiol Lett 188, 125-128 (2000)
    • (2000) FEMS Microbiol Lett , vol.188 , pp. 125-128
    • Spellerberg, B.1    Martin, S.2    Brandt, C.3    Lutticken, R.4
  • 154
    • 0025004750 scopus 로고
    • Kinetics of hemolysin production in bovine group B streptococci
    • Griffiths B. B.: Kinetics of hemolysin production in bovine group B streptococci. J Basic Microbiol 30, 241-250 (1990)
    • (1990) J Basic Microbiol , vol.30 , pp. 241-250
    • Griffiths, B.B.1
  • 155
    • 0027256040 scopus 로고
    • Group B streptococcal toxic shock-like syndrome: Report of a case and purification of an associated pyrogenic toxin
    • Schlievert P. M., J. E. Gocke & J. R. Deringer: Group B streptococcal toxic shock-like syndrome: report of a case and purification of an associated pyrogenic toxin. Clin Infect Dis 17, 26-31 (1993)
    • (1993) Clin Infect Dis , vol.17 , pp. 26-31
    • Schlievert, P.M.1    Gocke, J.E.2    Deringer, J.R.3
  • 157
    • 0027216327 scopus 로고
    • Group B streptococcal neuraminidase is actually a hyaluronidase
    • Pritchard D. G. & B. Lin: Group B streptococcal neuraminidase is actually a hyaluronidase. Infect Immun 61, 3234-3239 (1993)
    • (1993) Infect Immun , vol.61 , pp. 3234-3239
    • Pritchard, D.G.1    Lin, B.2
  • 158
    • 0028397834 scopus 로고
    • Purification and characterization of hyaluronidase from Streptococcus agalactiae
    • Ozegowski J. H., E. Gunther & W. Reichardt: Purification and characterization of hyaluronidase from Streptococcus agalactiae. Zentralbl Bakteriol 280, 497-506 (1994)
    • (1994) Zentralbl Bakteriol , vol.280 , pp. 497-506
    • Ozegowski, J.H.1    Gunther, E.2    Reichardt, W.3
  • 160
    • 0019765975 scopus 로고
    • Hyaluronidase production, lactose and salicin fermentation and phagetypability in bovine group B Streptococci
    • Haug R. H., O. Olsvik & O. Hushovd: Hyaluronidase production, lactose and salicin fermentation and phagetypability in bovine group B Streptococci. NIPH Ann 4, 69-73 (1981)
    • (1981) NIPH Ann , vol.4 , pp. 69-73
    • Haug, R.H.1    Olsvik, O.2    Hushovd, O.3
  • 161
    • 0037176776 scopus 로고    scopus 로고
    • Identification and characterization of Streptococcus agalactiae isolated from horses
    • Yildirim A. O., C. Lammler & R. Weiss: Identification and characterization of Streptococcus agalactiae isolated from horses. Vet Microbiol 85, 31-35 (2002)
    • (2002) Vet Microbiol , vol.85 , pp. 31-35
    • Yildirim, A.O.1    Lammler, C.2    Weiss, R.3
  • 163
    • 0037183993 scopus 로고    scopus 로고
    • Structure and flexibility of Streptococcus agalactiae hyaluronate lyase complex with its substrate. Insights into the mechanism of processive degradation of hyaluronan
    • Mello L. V., B. L. De Groot, S. Li & M. J. Jedrzejas: Structure and flexibility of Streptococcus agalactiae hyaluronate lyase complex with its substrate. Insights into the mechanism of processive degradation of hyaluronan. J Biol Chem 277, 36678-36688 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 36678-36688
    • Mello, L.V.1    De Groot, B.L.2    Li, S.3    Jedrzejas, M.J.4
  • 164
    • 0035798695 scopus 로고    scopus 로고
    • Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase
    • Li S. & M. J. Jedrzejas: Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase. J Biol Chem 276, 41407-41416 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 41407-41416
    • Li, S.1    Jedrzejas, M.J.2
  • 165
    • 0021361641 scopus 로고
    • Group B streptococci: Extracellular neuraminidase production and virulence in mouse
    • Orefici G., A. De Stasio, M. Guarino, A. Martini & N. Orsi: Group B streptococci: extracellular neuraminidase production and virulence in mouse. Microbiologica 7, 75-78 (1984)
    • (1984) Microbiologica , vol.7 , pp. 75-78
    • Orefici, G.1    De Stasio, A.2    Guarino, M.3    Martini, A.4    Orsi, N.5
  • 166
    • 0028585787 scopus 로고
    • Molecular characterization of the cfb gene encoding group B streptococcal CAMP-factor
    • Podbielski A., O. Blankenstein & R. Lutticken: Molecular characterization of the cfb gene encoding group B streptococcal CAMP-factor. Med Microbiol Immunol (Berl) 183, 239-256 (1994)
    • (1994) Med Microbiol Immunol (Berl) , vol.183 , pp. 239-256
    • Podbielski, A.1    Blankenstein, O.2    Lutticken, R.3
  • 167
    • 0036293020 scopus 로고    scopus 로고
    • Molecular characterization of phenotypically CAMP-negative Streptococcus agalactiae isolated from bovine mastitis
    • Hassan A. A., O. Akineden, C. Lammler & R. Huber-Schlenstedt: Molecular characterization of phenotypically CAMP-negative Streptococcus agalactiae isolated from bovine mastitis. J Vet Med B 49, 257-259 (2002)
    • (2002) J Vet Med B , vol.49 , pp. 257-259
    • Hassan, A.A.1    Akineden, O.2    Lammler, C.3    Huber-Schlenstedt, R.4
  • 168
    • 0023265348 scopus 로고
    • Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity
    • Jurgens D., B. Sterzik & F. J. Fehrenbach: Unspecific binding of group B streptococcal cocytolysin (CAMP factor) to immunoglobulins and its possible role in pathogenicity. J Exp Med 165, 720-732 (1987)
    • (1987) J Exp Med , vol.165 , pp. 720-732
    • Jurgens, D.1    Sterzik, B.2    Fehrenbach, F.J.3
  • 170
    • 0141755375 scopus 로고    scopus 로고
    • Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin
    • June 30, [Epub ahead of print]
    • Lang S. & M. Palmer: Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin. J Biol Chem June 30, [Epub ahead of print] (2003)
    • (2003) J Biol Chem
    • Lang, S.1    Palmer, M.2
  • 171
    • 0031578913 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of the superoxide dismutase gene from Streptococcus agalacliae
    • Caillot O., C. Poyart, P. Berche & P. Trieu-Cuot: Molecular characterization and expression analysis of the superoxide dismutase gene from Streptococcus agalacliae. Gene 204, 213-218 (1997)
    • (1997) Gene , vol.204 , pp. 213-218
    • Caillot, O.1    Poyart, C.2    Berche, P.3    Trieu-Cuot, P.4
  • 172
    • 0029975360 scopus 로고    scopus 로고
    • Entry and intracellular survival of group B Streptococci in J774 macrophages
    • Valentin-Weigand P., P. Benkel, M. Rohde & G. S. Chhatwal: Entry and intracellular survival of group B Streptococci in J774 macrophages. Infect Immun 64, 2467-2473 (1996)
    • (1996) Infect Immun , vol.64 , pp. 2467-2473
    • Valentin-Weigand, P.1    Benkel, P.2    Rohde, M.3    Chhatwal, G.S.4
  • 173
    • 0034924910 scopus 로고    scopus 로고
    • Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae
    • Poyart C., E. Pellegrini, O. Caillot, C. Boumaila, M. Baptista & P. Trieu-Cuot: Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae. Infect Immun 69, 5098-5106 (2001)
    • (2001) Infect Immun , vol.69 , pp. 5098-5106
    • Poyart, C.1    Pellegrini, E.2    Caillot, O.3    Boumaila, C.4    Baptista, M.5    Trieu-Cuot, P.6
  • 174
    • 0023273680 scopus 로고
    • Human infection with Streptococcus zooepidemicus (Lancefield group C): Three case reports
    • Barnham M., A. Ljunggren & M. McIntyre: Human infection with Streptococcus zooepidemicus (Lancefield group C): three case reports. Epidemiol Infect 98, 183-190 (1987)
    • (1987) Epidemiol Infect , vol.98 , pp. 183-190
    • Ljunggren, B.M.A.1    McIntyre, M.2
  • 175
    • 0036005857 scopus 로고    scopus 로고
    • A case of zoonosis associated with Streptococcus equi ssp. zooepidemicus
    • Boucher C., R. Higgins, M. Nadeau & C. Vincent: [A case of zoonosis associated with Streptococcus equi ssp. zooepidemicus]. Can Vet J 43, 123-124 (2002)
    • (2002) Can Vet J , vol.43 , pp. 123-124
    • Boucher, C.1    Higgins, R.2    Nadeau, M.3    Vincent, C.4
  • 176
    • 0033109970 scopus 로고    scopus 로고
    • Pulsed-field gel electrophoresis and distribution of the genes zag and fnz in isolates of Streptococcus equi
    • Lindmark H., P. Jonsson, E. Engvall & B. Guss: Pulsed-field gel electrophoresis and distribution of the genes zag and fnz in isolates of Streptococcus equi. Res Vet Sci 66, 93-99 (1999)
    • (1999) Res Vet Sci , vol.66 , pp. 93-99
    • Lindmark, H.1    Jonsson, P.2    Engvall, E.3    Guss, B.4
  • 177
    • 0028541098 scopus 로고
    • Genetic structure of populations of -haemolytic Lancefield group C streptococci from horses and their association with disease
    • Jorm L. R., D. N. Love, G. D. Bailey, G. M. Bailey & D. A. Briscoe: Genetic structure of populations of -haemolytic Lancefield group C streptococci from horses and their association with disease. Res Vet Sci 57, 292-299 (1994)
    • (1994) Res Vet Sci , vol.57 , pp. 292-299
    • Jorm, L.R.1    Love, D.N.2    Bailey, G.D.3    Bailey, G.M.4    Briscoe, D.A.5
  • 178
    • 0031414098 scopus 로고    scopus 로고
    • Streptococci and enterococci as animal pathogens
    • Chanter N.: Streptococci and enterococci as animal pathogens. J Appl Microbiol Symp Suppl 83, 100S-109S (1997)
    • (1997) J Appl Microbiol Symp Suppl , vol.83
    • Chanter, N.1
  • 180
    • 0036220868 scopus 로고    scopus 로고
    • The molecular basis of Streptococcus equi infection and disease
    • Harrington D. J., I. C. Sutcliffe & N. Chanter: The molecular basis of Streptococcus equi infection and disease. Microbes Infect 4, 501-510 (2002)
    • (2002) Microbes Infect , vol.4 , pp. 501-510
    • Harrington, D.J.1    Sutcliffe, I.C.2    Chanter, N.3
  • 181
    • 0032793192 scopus 로고    scopus 로고
    • In vivo pathogenicity and resistance to phagocytosis of Streptococcus equi strains with different levels of capsule expression
    • Anzai T., J. Timoney, Y. Kuwamoto, Y. Fujita, R. Wada & T. Inoue: In vivo pathogenicity and resistance to phagocytosis of Streptococcus equi strains with different levels of capsule expression. Vet Microbiol 67, 277-286 (1999)
    • (1999) Vet Microbiol , vol.67 , pp. 277-286
    • Anzai, T.1    Timoney, J.2    Kuwamoto, Y.3    Fujita, Y.4    Wada, R.5    Inoue, T.6
  • 182
    • 0022038199 scopus 로고
    • Production and biological properties of M-protein of Streptococcus equi
    • Srivastava S. K., D. A. Barnum & J. F. Prescott: Production and biological properties of M-protein of Streptococcus equi. Res Vet Sci 38, 184-188 (1985)
    • (1985) Res Vet Sci , vol.38 , pp. 184-188
    • Srivastava, S.K.1    Barnum, D.A.2    Prescott, J.F.3
  • 183
    • 0037032398 scopus 로고    scopus 로고
    • Construction of a stable non-mucoid deletion mutant of the Streptococcus equi. Pinnacle vaccine strain
    • Walker J. & J. Timoney: Construction of a stable non-mucoid deletion mutant of the Streptococcus equi. Pinnacle vaccine strain. Vet Microbiol 89, 311 (2002)
    • (2002) Vet Microbiol , vol.89 , pp. 311
    • Walker, J.1    Timoney, J.2
  • 184
    • 0027141962 scopus 로고
    • The protective M proteins of the equine group C streptococci
    • Timoney J. & M. M. Mukhtar: The protective M proteins of the equine group C streptococci. Vet Microbiol 37, 389-395 (1993)
    • (1993) Vet Microbiol , vol.37 , pp. 389-395
    • Timoney, J.1    Mukhtar, M.M.2
  • 185
    • 0032872878 scopus 로고    scopus 로고
    • Recombinant hyaluronate associated protein as a protective immunogen against Streptococcus equi and Streptococcus zooepidemicus challenge in mice
    • Chanter N., C. L. Ward, N. C. Collin, J. A. Flanagan, M. Binns, S. B. Houghton, K. C. Smith & J. A. Mumford: Recombinant hyaluronate associated protein as a protective immunogen against Streptococcus equi and Streptococcus zooepidemicus challenge in mice. Microb Pathog 27, 133-143 (1999)
    • (1999) Microb Pathog , vol.27 , pp. 133-143
    • Chanter, N.1    Ward, C.L.2    Collin, N.C.3    Flanagan, J.A.4    Binns, M.5    Houghton, S.B.6    Smith, K.C.7    Mumford, J.A.8
  • 186
    • 0021083828 scopus 로고
    • Adherence of Streptococcus equi on tongue, cheek and nasal epithelial cells of ponies
    • Srivastava S. K. & D. A. Barnum: Adherence of Streptococcus equi on tongue, cheek and nasal epithelial cells of ponies. Vet Microbiol 8, 493-504 (1983)
    • (1983) Vet Microbiol , vol.8 , pp. 493-504
    • Srivastava, S.K.1    Barnum, D.A.2
  • 187
    • 0030884041 scopus 로고    scopus 로고
    • Comparison of the sequences and functions of Streptococcus equi M-like proteins SeM and SzPSe
    • Timoney J. F., S. C. Artiushin & J. S. Boschwitz: Comparison of the sequences and functions of Streptococcus equi M-like proteins SeM and SzPSe. Infect Immun 65, 3600-3605 (1997)
    • (1997) Infect Immun , vol.65 , pp. 3600-3605
    • Timoney, J.F.1    Artiushin, S.C.2    Boschwitz, J.S.3
  • 188
    • 0031979211 scopus 로고    scopus 로고
    • Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with Streptococcus equi subsp. equi
    • Meehan M., P. Nowlan & P. Owen: Affinity purification and characterization of a fibrinogen-binding protein complex which protects mice against lethal challenge with Streptococcus equi subsp. equi. Microbiology 144, 993-1003 (1998)
    • (1998) Microbiology , vol.144 , pp. 993-1003
    • Meehan, M.1    Nowlan, P.2    Owen, P.3
  • 189
    • 0035217484 scopus 로고    scopus 로고
    • The fibrinogen-binding protein of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model
    • Meehan M., Y. Lynagh, C. Woods & P. Owen: The fibrinogen-binding protein of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model. Microbiology 147, 3311-3322 (2001)
    • (2001) Microbiology , vol.147 , pp. 3311-3322
    • Meehan, M.1    Lynagh, Y.2    Woods, C.3    Owen, P.4
  • 190
    • 0034106122 scopus 로고    scopus 로고
    • Localization and characterization of the ligand-binding domain of the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi
    • Meehan M., D. A. Muldowney, N. J. Watkins & P. Owen: Localization and characterization of the ligand-binding domain of the fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi. Microbiology 146, 1187-1194 (2000)
    • (2000) Microbiology , vol.146 , pp. 1187-1194
    • Meehan, M.1    Muldowney, D.A.2    Watkins, N.J.3    Owen, P.4
  • 191
    • 0027993049 scopus 로고
    • Characterization of the antiphagocytic activity of equine fibrinogen for Streptococcus equi subsp. equi
    • Boschwitz J. S. & J. F. Timoney: Characterization of the antiphagocytic activity of equine fibrinogen for Streptococcus equi subsp. equi. Microb Pathog 17, 121-129 (1994)
    • (1994) Microb Pathog , vol.17 , pp. 121-129
    • Boschwitz, J.S.1    Timoney, J.F.2
  • 192
    • 0027991837 scopus 로고
    • Inhibition of C3 deposition on Streptococcus equi subsp. equi by M protein: A mechanism for survival in equine blood
    • Boschwitz J. S. & J. F. Timoney: Inhibition of C3 deposition on Streptococcus equi subsp. equi by M protein: a mechanism for survival in equine blood. Infect Immun 62, 3515-3520 (1994)
    • (1994) Infect Immun , vol.62 , pp. 3515-3520
    • Boschwitz, J.S.1    Timoney, J.F.2
  • 193
    • 0034120702 scopus 로고    scopus 로고
    • Streptococcus equi with truncated M-proteins isolated from outwardly healthy horses
    • Chanter N., N. C. Talbot, J. R. Newton, D. Hewson & K. Verheyen: Streptococcus equi with truncated M-proteins isolated from outwardly healthy horses. Microbiology 146, 1361-1369 (2000)
    • (2000) Microbiology , vol.146 , pp. 1361-1369
    • Chanter, N.1    Talbot, N.C.2    Newton, J.R.3    Hewson, D.4    Verheyen, K.5
  • 194
    • 0032900509 scopus 로고    scopus 로고
    • SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibits the binding between fibronectin and collagen
    • Lindmark H. & B. Guss: SFS, a novel fibronectin-binding protein from Streptococcus equi, inhibits the binding between fibronectin and collagen. Infect Immun 67, 2383-2388 (1999)
    • (1999) Infect Immun , vol.67 , pp. 2383-2388
    • Lindmark, H.1    Guss, B.2
  • 195
    • 0035055230 scopus 로고    scopus 로고
    • Comparison of the fibronectin-binding protein FNE from Streptococcus equi subspecies equi with FNZ from S. equi subspecies zooepidemicus reveals a major and conserved difference
    • Lindmark H., M. Nilsson & B. Guss: Comparison of the fibronectin-binding protein FNE from Streptococcus equi subspecies equi with FNZ from S. equi subspecies zooepidemicus reveals a major and conserved difference. Infect Immun 69, 3159-3163 (2001)
    • (2001) Infect Immun , vol.69 , pp. 3159-3163
    • Nilsson, L.H.M.1    Guss, B.2
  • 197
    • 0033593827 scopus 로고    scopus 로고
    • Streptococcus equi but not Streptococcus zooepidemicus produces potent mitogenic responses from equine peripheral blood mononuclear cells
    • Anzai T., A. S. Sheoran, Y. Kuwamoto, T. Kondo, R. Wada, T. Inoue & J. Timoney: Streptococcus equi but not Streptococcus zooepidemicus produces potent mitogenic responses from equine peripheral blood mononuclear cells. Vet Immunol Immunopathol 67, 235-246 (1999)
    • (1999) Vet Immunol Immunopathol , vol.67 , pp. 235-246
    • Anzai, T.1    Sheoran, A.S.2    Kuwamoto, Y.3    Kondo, T.4    Wada, R.5    Inoue, T.6    Timoney, J.7
  • 198
    • 0036353004 scopus 로고    scopus 로고
    • Characterization and immunogenicity of pyrogenic mitogens SePE-H and SePE-I of Streptococcus equi
    • Artiushin S. C., J. F. Timoney, A. S. Sheoran & S. K. Muthupalani: Characterization and immunogenicity of pyrogenic mitogens SePE-H and SePE-I of Streptococcus equi. Microb Pathog 32, 71-85 (2002)
    • (2002) Microb Pathog , vol.32 , pp. 71-85
    • Artiushin, S.C.1    Timoney, J.F.2    Sheoran, A.S.3    Muthupalani, S.K.4
  • 199
    • 0002349478 scopus 로고
    • The family of mitogenic shock-inducing and superantigenic toxins from staphylococci and streptococci
    • Eds: Alouf J E, Freer J H, Academic Press, London
    • Alouf J. E., H. Knoll & W. Kohler: The family of mitogenic shock-inducing and superantigenic toxins from staphylococci and streptococci. In: Sourcebook of bacterial protein toxins. Eds: Alouf J E, Freer J H, Academic Press, London (1991)
    • (1991) Sourcebook of Bacterial Protein Toxins
    • Alouf, J.E.1    Knoll, H.2    Kohler, W.3
  • 200
    • 0037372650 scopus 로고    scopus 로고
    • Two novel superantigens found in both Group A and Group C Streptococcus
    • Proft T., P. D. Webb, V. Handley & F. J. D.: Two novel superantigens found in both Group A and Group C Streptococcus. Infect Immun 71, 1361-1369 (2003)
    • (2003) Infect Immun , vol.71 , pp. 1361-1369
    • Proft, T.1    Webb, P.D.2    Handley, V.3
  • 201
    • 0021766558 scopus 로고
    • Lysogeny and the immunologically reactive proteins of Streptococcus equi
    • Timoney J. F., P. J. Timoney & K. L. Strickland: Lysogeny and the immunologically reactive proteins of Streptococcus equi. Vet Rec 115, 148-149 (1984)
    • (1984) Vet Rec , vol.115 , pp. 148-149
    • Timoney, J.F.1    Timoney, P.J.2    Strickland, K.L.3
  • 202
    • 85037968974 scopus 로고    scopus 로고
    • Detection and characterisation of Streptococcus equi and Streptococcus zooepidemicus proteases to identify potential protective immunogens
    • Dubai, United Arab Emirates
    • Collin N. C., N. Chanter & J. A. Mumford: Detection and characterisation of Streptococcus equi and Streptococcus zooepidemicus proteases to identify potential protective immunogens. Presented at the Equine Infectious Diseases VIII: Proceedings of the Eighth International Conference, Dubai, United Arab Emirates, (1998)
    • (1998) Equine Infectious Diseases VIII: Proceedings of the Eighth International Conference
    • Collin, N.C.1    Chanter, N.2    Mumford, J.A.3
  • 203
    • 0029654015 scopus 로고
    • S. zooepidemicus infection and bovine mastitis
    • Sharp M. W., M. J. Prince & J. Gibbens: S. zooepidemicus infection and bovine mastitis. Vet Rec 137, 128 (1995)
    • (1995) Vet Rec , vol.137 , pp. 128
    • Sharp, M.W.1    Prince, M.J.2    Gibbens, J.3
  • 204
    • 0034133758 scopus 로고    scopus 로고
    • Comparison of the phenotypes of Streptococcus zooepidemicus isolated from tonsils of healthy horses and specimens obtained from foals and donkeys with pneumonia
    • Anzai T., J. A. Walker, M. B. Blair, T. M. Chambers & J. F. Timoney: Comparison of the phenotypes of Streptococcus zooepidemicus isolated from tonsils of healthy horses and specimens obtained from foals and donkeys with pneumonia. Am J Vet Res 61, 162-166 (2000)
    • (2000) Am J Vet Res , vol.61 , pp. 162-166
    • Anzai, T.1    Walker, J.A.2    Blair, M.B.3    Chambers, T.M.4    Timoney, J.F.5
  • 205
    • 0027469724 scopus 로고
    • Ozone-enhanced pulmonary infection with Streptococcus zooepidemicus in mice. The role of alveolar macrophage function and capsular virulence factors
    • Gilmour M. I., P. Park & M. K. Selgrade: Ozone-enhanced pulmonary infection with Streptococcus zooepidemicus in mice. The role of alveolar macrophage function and capsular virulence factors. Am Rev Respir Dis 147, 753-760 (1993)
    • (1993) Am Rev Respir Dis , vol.147 , pp. 753-760
    • Gilmour, M.I.1    Park, P.2    Selgrade, M.K.3
  • 206
    • 0033208699 scopus 로고    scopus 로고
    • The role of hyaluronic acid capsular material of Streptococcus equi subsp. zooepidemicus in mediating adherence to HeLa cells and in resisting phagocytosis
    • Wibawan I. W., F. H. Pasaribu, I. H. Utama, A. Abdulmawjood & C. Lammler: The role of hyaluronic acid capsular material of Streptococcus equi subsp. zooepidemicus in mediating adherence to HeLa cells and in resisting phagocytosis. Res Vet Sci 67, 131-135 (1999)
    • (1999) Res Vet Sci , vol.67 , pp. 131-135
    • Wibawan, I.W.1    Pasaribu, F.H.2    Utama, I.H.3    Abdulmawjood, A.4    Lammler, C.5
  • 207
    • 0032161833 scopus 로고    scopus 로고
    • Molecular basis of variation in protective SzP proteins of Streptococcus zooepidemicus
    • Walker J. & J. F. Timoney: Molecular basis of variation in protective SzP proteins of Streptococcus zooepidemicus. Am J Vet Res 59, 1129-1133 (1998)
    • (1998) Am J Vet Res , vol.59 , pp. 1129-1133
    • Walker, J.1    Timoney, J.F.2
  • 208
    • 0028916094 scopus 로고
    • Cloning and sequence analysis of a protective M-like protein gene from Streptococcus equi subsp. zooepidemicus
    • Timoney J. F., J. Walker, M. Zhou & J. Ding: Cloning and sequence analysis of a protective M-like protein gene from Streptococcus equi subsp. zooepidemicus. Infect Immun 63, 1440-1445 (1995)
    • (1995) Infect Immun , vol.63 , pp. 1440-1445
    • Timoney, J.F.1    Walker, J.2    Zhou, M.3    Ding, J.4
  • 209
    • 0021961671 scopus 로고
    • Hyalurodinase activity of beta-hemolytic streptococci of the Lancefield group C
    • Balke E., R. Weiss & A. Seipp: [Hyalurodinase activity of beta-hemolytic streptococci of the Lancefield group C]. Zentralbl Bakteriol Mikrobiol Hyg [A] 259, 194-200 (1985)
    • (1985) Zentralbl Bakteriol Mikrobiol Hyg [A] , vol.259 , pp. 194-200
    • Balke, E.1    Weiss, R.2    Seipp, A.3
  • 211
    • 0030984605 scopus 로고    scopus 로고
    • Cloning and sequence analysis of zoo A, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin
    • Simmonds R. S., W. J. Simpson & J. R. Tagg: Cloning and sequence analysis of zoo A, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin. Gene 189, 255-261 (1997)
    • (1997) Gene , vol.189 , pp. 255-261
    • Simmonds, R.S.1    Simpson, W.J.2    Tagg, J.R.3
  • 212
    • 0029909725 scopus 로고    scopus 로고
    • Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881
    • Simmonds R. S., L. Pearson, R. C. Kennedy & J. R. Tagg: Mode of action of a lysostaphin-like bacteriolytic agent produced by Streptococcus zooepidemicus 4881. Appl Environ Microbiol 62, 4536-4541 (1996)
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4536-4541
    • Simmonds, R.S.1    Pearson, L.2    Kennedy, R.C.3    Tagg, J.R.4
  • 213
    • 0032102862 scopus 로고    scopus 로고
    • Zoocin a immunity factor: A femA-like gene found in a group C Streptococcus
    • Beatson S. A., G. L. Sloan & R. S. Simmonds: Zoocin A immunity factor: a femA-like gene found in a group C Streptococcus. FEMS Microbiol Lett 163, 73-77 (1998)
    • (1998) FEMS Microbiol Lett , vol.163 , pp. 73-77
    • Beatson, S.A.1    Sloan, G.L.2    Simmonds, R.S.3
  • 214
    • 0037167472 scopus 로고    scopus 로고
    • Functional characterization of domains found within a lytic enzyme produced by Streptococcus equi subsp. zooepidemicus
    • Lai A. C., S. Tran & R. S. Simmonds: Functional characterization of domains found within a lytic enzyme produced by Streptococcus equi subsp. zooepidemicus. FEMS Microbiol Lett 215, 133-138 (2002)
    • (2002) FEMS Microbiol Lett , vol.215 , pp. 133-138
    • Lai, A.C.1    Tran, S.2    Simmonds, R.S.3
  • 215
    • 0033866076 scopus 로고    scopus 로고
    • Virulence factors and the pathogenesis of disease caused by Streptococcus pneumoniae
    • Mitchell T. J.: Virulence factors and the pathogenesis of disease caused by Streptococcus pneumoniae. Res Microbiol 151, 413-419 (2000)
    • (2000) Res Microbiol , vol.151 , pp. 413-419
    • Mitchell, T.J.1
  • 216
    • 8144231515 scopus 로고    scopus 로고
    • Molecular pathogenesis of pneumococcal pneumonia
    • McCullers J. A. & E. I. Tuomanen: Molecular pathogenesis of pneumococcal pneumonia. Front Biosci 6, D877-8889 (2001)
    • (2001) Front Biosci , vol.6
    • McCullers, J.A.1    Tuomanen, E.I.2
  • 217
    • 0028189398 scopus 로고
    • Streptococcus pneumoniae and equine disease
    • Chanter N.: Streptococcus pneumoniae and equine disease. Equine Vet J 26, 5-6 (1994)
    • (1994) Equine Vet J , vol.26 , pp. 5-6
    • Chanter, N.1
  • 218
    • 0022715254 scopus 로고
    • Isolation of Streptococcus pneumoniae from the respiratory tract of horses
    • Burrell M. H., M. E. Mackintosh & C. E. Taylor: Isolation of Streptococcus pneumoniae from the respiratory tract of horses. Equine Vet J 18, 183-186 (1986)
    • (1986) Equine Vet J , vol.18 , pp. 183-186
    • Burrell, M.H.1    Mackintosh, M.E.2    Taylor, C.E.3
  • 219
    • 0032986490 scopus 로고    scopus 로고
    • Molecular characterization of equine Isolates of Streptococcus pneumoniae: Natural disruption of genes encoding the virulence factors pneumolysin and autolysin
    • Whatmore A. M., S. J. King, N. C. Doherty, D. Sturgeon, N. Chanter & C. G. Dowson: Molecular characterization of equine Isolates of Streptococcus pneumoniae: natural disruption of genes encoding the virulence factors pneumolysin and autolysin. Infect Immun 67, 2776-2782 (1999)
    • (1999) Infect Immun , vol.67 , pp. 2776-2782
    • Whatmore, A.M.1    King, S.J.2    Doherty, N.C.3    Sturgeon, D.4    Chanter, N.5    Dowson, C.G.6
  • 220
    • 0037013407 scopus 로고    scopus 로고
    • Streptococcus iniae infections in Red Sea cage-cultured and wild fishes
    • Colorni A., A. Diamant, A. Eldar, H. Kvitt & A. Zlotkin: Streptococcus iniae infections in Red Sea cage-cultured and wild fishes. Dis Aquat Org 49, 165-170 (2002)
    • (2002) Dis Aquat Org , vol.49 , pp. 165-170
    • Colorni, A.1    Diamant, A.2    Eldar, A.3    Kvitt, H.4    Zlotkin, A.5
  • 221
    • 0000990241 scopus 로고    scopus 로고
    • Emerging bacterial fish pathogens
    • Austin B.: Emerging bacterial fish pathogens. Bull Eur Assoc Fish Pathol 19, 231-234 (1999)
    • (1999) Bull Eur Assoc Fish Pathol , vol.19 , pp. 231-234
    • Austin, B.1
  • 222
    • 0002909511 scopus 로고
    • Streptococcal Infections
    • Eds: Inglis V, Roberts R J, Bromage N R, Blackwell, Oxford
    • Kitao T.: Streptococcal Infections. In: Bacterial diseases of fish. Eds: Inglis V, Roberts R J, Bromage N R, Blackwell, Oxford (1993)
    • (1993) Bacterial Diseases of Fish
    • Kitao, T.1
  • 223
    • 0017125616 scopus 로고
    • Streptococcus iniae sp. nov., a beta-hemolytic streptococcus isolated from an Amazon freshwater dolphin, Inia geoffrensis
    • Peir G. B. & S. H. Madin: Streptococcus iniae sp. nov., a beta-hemolytic streptococcus isolated from an Amazon freshwater dolphin, Inia geoffrensis. Int J Syst Bacteriol 26, 545-553 (1976)
    • (1976) Int J Syst Bacteriol , vol.26 , pp. 545-553
    • Peir, G.B.1    Madin, S.H.2
  • 224
    • 0028325142 scopus 로고
    • Streptococcus shiloi and Streptococcus difficile: Two new Streptococcal species causing a meningoencephalitis in fish
    • Eldar A., Y. Bejerano & H. Bercovier: Streptococcus shiloi and Streptococcus difficile: two new Streptococcal species causing a meningoencephalitis in fish. Curr Microbiol 28, 139-143 (1994)
    • (1994) Curr Microbiol , vol.28 , pp. 139-143
    • Eldar, A.1    Bejerano, Y.2    Bercovier, H.3
  • 226
    • 0035261211 scopus 로고    scopus 로고
    • Prevalence of Streptococcus iniae in tilapia, hybrid striped bass, and channel catfish on commercial fish farms in the United States
    • Shoemaker C. A., P. H. Klesius & J. J. Evans: Prevalence of Streptococcus iniae in tilapia, hybrid striped bass, and channel catfish on commercial fish farms in the United States. Am J Vet Res 62, 174-177 (2001)
    • (2001) Am J Vet Res , vol.62 , pp. 174-177
    • Shoemaker, C.A.1    Klesius, P.H.2    Evans, J.J.3
  • 227
    • 0018089475 scopus 로고
    • Isolation and characterization of a second isolate of Streptococcus iniae
    • Peir G. B. & S. H. Madin: Isolation and characterization of a second isolate of Streptococcus iniae. Int J Syst Bacteriol 28, 311-314 (1978)
    • (1978) Int J Syst Bacteriol , vol.28 , pp. 311-314
    • Peir, G.B.1    Madin, S.H.2
  • 228
    • 0033620673 scopus 로고    scopus 로고
    • Streptococcus iniae, a bacterial infection in barramundi Lates calcarifer
    • Bromage E. S., A. Thomas & L. Owens: Streptococcus iniae, a bacterial infection in barramundi Lates calcarifer. Dis Aquat Organ 36, 177-181 (1999)
    • (1999) Dis Aquat Organ , vol.36 , pp. 177-181
    • Bromage, E.S.1    Thomas, A.2    Owens, L.3
  • 229
    • 0033620694 scopus 로고    scopus 로고
    • Lactococcus garvieae and Streptococcus iniae infections in rainbow trout Oncorhynchus mykiss: Similar, but different diseases
    • Eldar A. & C. Ghittino: Lactococcus garvieae and Streptococcus iniae infections in rainbow trout Oncorhynchus mykiss: similar, but different diseases. Dis Aquat Org 36, 227-231 (1999)
    • (1999) Dis Aquat Org , vol.36 , pp. 227-231
    • Eldar, A.1    Ghittino, C.2
  • 230
    • 0036081383 scopus 로고    scopus 로고
    • Streptococcus-zebrafish model of bacterial pathogenesis
    • Neely M. N., J. D. Pfeifer & M. Caparon: Streptococcus-zebrafish model of bacterial pathogenesis. Infect Immun 70, 3904-3914 (2002)
    • (2002) Infect Immun , vol.70 , pp. 3904-3914
    • Neely, M.N.1    Pfeifer, J.D.2    Caparon, M.3
  • 231
    • 0035086370 scopus 로고    scopus 로고
    • Streptococcus iniae Virulence Is Associated with a Distinct Genetic Profile
    • Fuller J. D., D. J. Bast, V. Nizet, D. E. Low & J. C. S. de Azavedo: Streptococcus iniae Virulence Is Associated with a Distinct Genetic Profile. Infect Immun 69, 1994-2000 (2001)
    • (2001) Infect Immun , vol.69 , pp. 1994-2000
    • Fuller, J.D.1    Bast, D.J.2    Nizet, V.3    Low, D.E.4    De Azavedo, J.C.S.5
  • 232
    • 0036785660 scopus 로고    scopus 로고
    • Identification of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease
    • Fuller J. D., A. C. Camus, C. L. Duncan, V. Nizet, D. J. Bast, R. L. Thune, D. E. Low & J. C. De Azavedo: Identification of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease. Infect Immun 70, 5730-5739 (2002)
    • (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    Thune, R.L.6    Low, D.E.7    De Azavedo, J.C.8
  • 234
    • 0037468277 scopus 로고    scopus 로고
    • Streptococcus iniae: Serological differences, presence of capsule and resistance to immune serum killing
    • Barnes A. C., F. M. Young, M. T. Horne & A. E. Ellis: Streptococcus iniae: serological differences, presence of capsule and resistance to immune serum killing. Dis Aquat Org 53, 241-247 (2003)
    • (2003) Dis Aquat Org , vol.53 , pp. 241-247
    • Barnes, A.C.1    Young, F.M.2    Horne, M.T.3    Ellis, A.E.4
  • 235
    • 0035434675 scopus 로고    scopus 로고
    • Recovery of Streptococcus iniae from diseased fish previuosly vaccinated with a Streptococcus vaccine
    • Bachrach G., A. Zlotkin, A. Hurvitz, D. L. Evans & A. Eldar: Recovery of Streptococcus iniae from diseased fish previuosly vaccinated with a Streptococcus vaccine. Appl Environ Microbiol 67, 3756-3758 (2001)
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3756-3758
    • Bachrach, G.1    Zlotkin, A.2    Hurvitz, A.3    Evans, D.L.4    Eldar, A.5
  • 236
    • 0031906945 scopus 로고    scopus 로고
    • Genetic inactivation of an extracellular cysteine protease (SpeB) expressed by Streptococcus pyogenes decreases resistance to phagocytosis and dissemination to organs
    • Lukomski S., J. Burns, E. H., P. R. Wyde, A. Podbielski, J. Rurangirwa, D. K. Moore-Poveda & J. M. Musser: Genetic inactivation of an extracellular cysteine protease (SpeB) expressed by Streptococcus pyogenes decreases resistance to phagocytosis and dissemination to organs. Infect Immun 66, 771-776 (1998)
    • (1998) Infect Immun , vol.66 , pp. 771-776
    • Lukomski, S.1    Burns, J.2    Wyde, P.R.3    Podbielski, A.4    Rurangirwa, J.5    Moore-Poveda, D.K.6    Musser, J.M.7
  • 237
    • 0035934075 scopus 로고    scopus 로고
    • Streptococcus iniae inhibition of apoptosis of nonspecific cytotoxic cells: A mechanism of activation of innate immunity in teleosts
    • Taylor S. L., L. Jaso-Friedmann, A. B. Allison, A. Eldar & D. L. Evans: Streptococcus iniae inhibition of apoptosis of nonspecific cytotoxic cells: a mechanism of activation of innate immunity in teleosts. Dis Aquat Org 46, 15-21 (2001)
    • (2001) Dis Aquat Org , vol.46 , pp. 15-21
    • Taylor, S.L.1    Jaso-Friedmann, L.2    Allison, A.B.3    Eldar, A.4    Evans, D.L.5
  • 238
    • 0034216271 scopus 로고    scopus 로고
    • In vivo activation of tilapia nonspecific cytotoxic cells by Streptococcus iniae and amplification with apoptosis regulatory factor(s)
    • Evans D. L., S. L. Taylor, J. H. Leary III, G. R. Bishop, A. Eldar & L. Jaso-Friedmann: In vivo activation of tilapia nonspecific cytotoxic cells by Streptococcus iniae and amplification with apoptosis regulatory factor(s). Fish Shellfish Immunol 10, 419-434 (2000)
    • (2000) Fish Shellfish Immunol , vol.10 , pp. 419-434
    • Evans, D.L.1    Taylor, S.L.2    Leary III, J.H.3    Bishop, G.R.4    Eldar, A.5    Jaso-Friedmann, L.6
  • 242
    • 0031045039 scopus 로고    scopus 로고
    • Septicemia caused by Streptococcus canis in a human
    • Bert F. & N. Lambert-Zechovsky: Septicemia caused by Streptococcus canis in a human. J Clin Microbiol 35, 777-779 (1997)
    • (1997) J Clin Microbiol , vol.35 , pp. 777-779
    • Bert, F.1    Lambert-Zechovsky, N.2
  • 243
    • 0032735184 scopus 로고    scopus 로고
    • Virulence of Streptococcus canis from canine streptococcal toxic shock syndrome and necrotising fasciitis
    • DeWinter L. M., D. E. Low & J. F. Prescott: Virulence of Streptococcus canis from canine streptococcal toxic shock syndrome and necrotising fasciitis. Vet Microbiol 70, 95-110 (1999)
    • (1999) Vet Microbiol , vol.70 , pp. 95-110
    • DeWinter, L.M.1    Low, D.E.2    Prescott, J.F.3
  • 245
    • 0025916805 scopus 로고
    • Virulent human strains of group G streptococci express a C5a peptidase enzyme similar to that produced by group A streptococci
    • Cleary P. P., J. Peterson, C. Chen & C. Nelson: Virulent human strains of group G streptococci express a C5a peptidase enzyme similar to that produced by group A streptococci. Infect Immun 59, 2305-2310 (1991)
    • (1991) Infect Immun , vol.59 , pp. 2305-2310
    • Cleary, P.P.1    Peterson, J.2    Chen, C.3    Nelson, C.4
  • 246
    • 0028106320 scopus 로고
    • The gene encoding a new mitogenic factor in a Streptococcus pyogenes strain is distributed only in group A streptococci
    • Yutsudo T., K. Okumura, M. Iwasaki, A. Hara, S. Kamitani, W. Minamide, H. Igarashi & Y. Hinuma: The gene encoding a new mitogenic factor in a Streptococcus pyogenes strain is distributed only in group A streptococci. Infect Immun 62, 4000-4004 (1994)
    • (1994) Infect Immun , vol.62 , pp. 4000-4004
    • Yutsudo, T.1    Okumura, K.2    Iwasaki, M.3    Hara, A.4    Kamitani, S.5    Minamide, W.6    Igarashi, H.7    Hinuma, Y.8
  • 247
    • 0023514955 scopus 로고
    • Evidence for group A-related M protein genes in human but not animal-associated group G streptococcal pathogens
    • Simpson W. J., J. C. Robbins & P. P. Cleary: Evidence for group A-related M protein genes in human but not animal-associated group G streptococcal pathogens. Microb Pathog 3, 339-350 (1987)
    • (1987) Microb Pathog , vol.3 , pp. 339-350
    • Simpson, W.J.1    Robbins, J.C.2    Cleary, P.P.3
  • 249
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti V. A.: Streptococcal M protein: molecular design and biological behavior. Clin Microbiol Rev 2, 285-314 (1989)
    • (1989) Clin Microbiol Rev , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 250
    • 0026547147 scopus 로고
    • Two types of receptors for human plasminogen on group G streptococci
    • Ullberg M., I. Karlsson, B. Wiman & G. Kronvall: Two types of receptors for human plasminogen on group G streptococci. APMIS 100, 21-28 (1992)
    • (1992) APMIS , vol.100 , pp. 21-28
    • Ullberg, M.1    Karlsson, I.2    Wiman, B.3    Kronvall, G.4
  • 251
    • 0023695486 scopus 로고
    • Binding activity of Streptococcus canis for albumin and other plasma proteins
    • Lammler C., C. Frede, K. Gurturk, A. Hildebrand & H. Blobel: Binding activity of Streptococcus canis for albumin and other plasma proteins. J Gen Microbiol 134(Pt 8), 2317-2323 (1988)
    • (1988) J Gen Microbiol , vol.134 , Issue.8 PART , pp. 2317-2323
    • Lammler, C.1    Frede, C.2    Gurturk, K.3    Hildebrand, A.4    Blobel, H.5
  • 252
    • 0033111786 scopus 로고    scopus 로고
    • Relatedness of Streptococcus canis from canine Streptococcal toxic shock syndrome and necrotizing fasciitis
    • DeWinter L. M. & J. F. Prescott: Relatedness of Streptococcus canis from canine Streptococcal toxic shock syndrome and necrotizing fasciitis. Can J Vet Res 63, 90-95 (1999)
    • (1999) Can J Vet Res , vol.63 , pp. 90-95
    • DeWinter, L.M.1    Prescott, J.F.2
  • 253
    • 0030280155 scopus 로고    scopus 로고
    • Comparative studies on streptococci of serological group G isolated from various origins
    • Soedarmanto I. & C. Lammler: Comparative studies on streptococci of serological group G isolated from various origins. Zentralbl Veterinarmed [B] 43, 513-523 (1996)
    • (1996) Zentralbl Veterinarmed [B] , vol.43 , pp. 513-523
    • Soedarmanto, I.1    Lammler, C.2
  • 254
    • 0021175792 scopus 로고
    • Biotyping and exoenzyme profiling as an aid in the differentiation of human from bovine group G streptococci
    • Clark R. B., J. F. Berrafati, J. M. Janda & E. J. Bottone: Biotyping and exoenzyme profiling as an aid in the differentiation of human from bovine group G streptococci. J Clin Microbiol 20, 706-710 (1984)
    • (1984) J Clin Microbiol , vol.20 , pp. 706-710
    • Clark, R.B.1    Berrafati, J.F.2    Janda, J.M.3    Bottone, E.J.4
  • 255
    • 0021347442 scopus 로고
    • Streptococcus pyogenes streptolysin O as a cause of false-positive CAMP reactions
    • Tapsall J. W. & E. A. Phillips: Streptococcus pyogenes streptolysin O as a cause of false-positive CAMP reactions. J Clin Microbiol 19, 534-537 (1984)
    • (1984) J Clin Microbiol , vol.19 , pp. 534-537
    • Tapsall, J.W.1    Phillips, E.A.2
  • 256
    • 0025113214 scopus 로고
    • Purification and partial characterization of a cohaemolysin (CAMP-factor) produced by Streptococcus canis
    • Gurturk K. & C. Lammler: Purification and partial characterization of a cohaemolysin (CAMP-factor) produced by Streptococcus canis. FEMS Microbiol Immunol 2, 97-102 (1990)
    • (1990) FEMS Microbiol Immunol , vol.2 , pp. 97-102
    • Gurturk, K.1    Lammler, C.2
  • 257
    • 0000868078 scopus 로고
    • Other streptococci
    • Eds: Sneath P H A, Mair N S, Sharpe M E, Holt J G, Williams & Wilkins, Baltimore
    • Hardie J. M.: Other streptococci. In: Bergey's manual of systematic bacteriology. Eds: Sneath P H A, Mair N S, Sharpe M E, Holt J G, Williams & Wilkins, Baltimore (1986)
    • (1986) Bergey's Manual of Systematic Bacteriology
    • Hardie, J.M.1
  • 258
    • 0021710858 scopus 로고
    • Taxonomic studies on Streptococcus bovis and Streptococcus equinus: Description of Streptococcus alactolyticus sp. nov. and Streptococcus saccharolyticus sp. nov
    • Farrow J. A. E., J. Kruze, B. A. Phillips, A. J. Bramley & M. D. Collins: Taxonomic studies on Streptococcus bovis and Streptococcus equinus: description of Streptococcus alactolyticus sp. nov. and Streptococcus saccharolyticus sp. nov. Syst Appl Microbiol 5, 467-482 (1984)
    • (1984) Syst Appl Microbiol , vol.5 , pp. 467-482
    • Farrow, J.A.E.1    Kruze, J.2    Phillips, B.A.3    Bramley, A.J.4    Collins, M.D.5
  • 260
    • 0029062306 scopus 로고
    • Streptococcus gallolyticus sp. nov.; gallate degrading organisms formerly assigned to Streptococcus bovis
    • Osawa R., T. Fujisawa & L. I. Sly: Streptococcus gallolyticus sp. nov.; gallate degrading organisms formerly assigned to Streptococcus bovis. Syst Appl Microbiol 18, 74-78 (1995)
    • (1995) Syst Appl Microbiol , vol.18 , pp. 74-78
    • Osawa, R.1    Fujisawa, T.2    Sly, L.I.3
  • 261
    • 0030836683 scopus 로고    scopus 로고
    • The tannin-degrading species Streptococcus gallolyticus and Streptococcus caprinus are subjective synonyms
    • Sly L. I., M. M. Cahill, R. Osawa & T. Fujisawa: The tannin-degrading species Streptococcus gallolyticus and Streptococcus caprinus are subjective synonyms. Int J Syst Bacteriol 47, 893-894 (1997)
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 893-894
    • Sly, L.I.1    Cahill, M.M.2    Osawa, R.3    Fujisawa, T.4
  • 262
    • 0031784950 scopus 로고    scopus 로고
    • Differentiation between Streptococcus gallolyticus Strains of Human Clinical and Veterinary Origins and Streptococcus bovis Strains from the Intestinal Tracts of Ruminants
    • Devriese L. A., P. Vandamme, B. Pot, M. Vanrobaeys, K. Kersters & F. Haesebrouck: Differentiation between Streptococcus gallolyticus Strains of Human Clinical and Veterinary Origins and Streptococcus bovis Strains from the Intestinal Tracts of Ruminants. J Clin Microbiol 36, 3520-3523 (1998)
    • (1998) J Clin Microbiol , vol.36 , pp. 3520-3523
    • Devriese, L.A.1    Vandamme, P.2    Pot, B.3    Vanrobaeys, M.4    Kersters, K.5    Haesebrouck, F.6
  • 263
    • 0003185856 scopus 로고    scopus 로고
    • The rumen bacteria
    • Eds: Hobson P N, Stewart C S, Blackie Academic and Professional, London
    • Stewart C. S., H. J. Flint & M. P. Bryant: The rumen bacteria. In: The rumen microbial ecosystem. Eds: Hobson P N, Stewart C S, Blackie Academic and Professional, London (1997)
    • (1997) The Rumen Microbial Ecosystem
    • Stewart, C.S.1    Flint, H.J.2    Bryant, M.P.3
  • 264
    • 0029550861 scopus 로고
    • Differentiation of ruminai and human Streptococcus bovis strains by DNA homology and 16S rRNA probes
    • Nelms L. F., D. A. Odelson, T. R. Whitehead & R. B. Hespell: Differentiation of ruminai and human Streptococcus bovis strains by DNA homology and 16S rRNA probes. Curr Microbiol 31, 294-300 (1995)
    • (1995) Curr Microbiol , vol.31 , pp. 294-300
    • Nelms, L.F.1    Odelson, D.A.2    Whitehead, T.R.3    Hespell, R.B.4
  • 266
    • 19244375410 scopus 로고    scopus 로고
    • Secreted antigens as virulence associated markers in Streptococcus bovis strains from pigeons
    • Vanrobaeys M., P. De Herdt, F. Haesebrouck, R. Ducatelle & L. A. Devriese: Secreted antigens as virulence associated markers in Streptococcus bovis strains from pigeons. Vet Microbiol 53, 339-348 (1996)
    • (1996) Vet Microbiol , vol.53 , pp. 339-348
    • Vanrobaeys, M.1    De Herdt, P.2    Haesebrouck, F.3    Ducatelle, R.4    Devriese, L.A.5
  • 267
    • 0031422949 scopus 로고    scopus 로고
    • Extracellular proteins and virulence of Streptococcus bovis isolates from pigeons
    • Vanrobaeys M., P. De Herdt, R. Ducatelle, W. Creten & F. Haesebrouck: Extracellular proteins and virulence of Streptococcus bovis isolates from pigeons. Vet Microbiol 59, 59-66 (1997)
    • (1997) Vet Microbiol , vol.59 , pp. 59-66
    • Vanrobaeys, M.1    De Herdt, P.2    Ducatelle, R.3    Creten, W.4    Haesebrouck, F.5
  • 268
    • 0034636399 scopus 로고    scopus 로고
    • Identification of virulence associated markers in the cell wall of pigeon Streptococcus gallolyticus strains
    • Vanrobaeys M., F. Haesebrouck, R. Ducatelle & P. De Herdt: Identification of virulence associated markers in the cell wall of pigeon Streptococcus gallolyticus strains. Vet Microbiol 73, 319-325 (2000)
    • (2000) Vet Microbiol , vol.73 , pp. 319-325
    • Vanrobaeys, M.1    Haesebrouck, F.2    Ducatelle, R.3    De Herdt, P.4
  • 269
    • 0033065407 scopus 로고    scopus 로고
    • Ultrastructure of surface components of Streptococcus gallolyticus (S. bovis) strains of differing virulence isolated from pigeons
    • Vanrobaeys M., P. De Herdt, G. Charlier, R. Ducatelle & F. Haesebrouck: Ultrastructure of surface components of Streptococcus gallolyticus (S. bovis) strains of differing virulence isolated from pigeons. Microbiology 145(Pt 2), 335-342 (1999)
    • (1999) Microbiology , vol.145 , Issue.2 PART , pp. 335-342
    • Vanrobaeys, M.1    De Herdt, P.2    Charlier, G.3    Ducatelle, R.4    Haesebrouck, F.5
  • 270
    • 0034746484 scopus 로고    scopus 로고
    • Identification of bacteriocin-like inhibitors from rumen Streptococcus spp. and isolation and characterization of Bovicin 255
    • Whitford M. F., M. A. McPherson, R. J. Forster & R. M. Teather: Identification of bacteriocin-like inhibitors from rumen Streptococcus spp. and isolation and characterization of Bovicin 255. Appl Environ Microbiol 67, 569-574 (2001)
    • (2001) Appl Environ Microbiol , vol.67 , pp. 569-574
    • Whitford, M.F.1    McPherson, M.A.2    Forster, R.J.3    Teather, R.M.4


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