메뉴 건너뛰기




Volumn 9, Issue , 2004, Pages 1794-1802

Extracellular virulence factors of group B streptococci

Author keywords

C5a peptidase; CAMP factor; Cytolysin; Group B Streptococcus; Hemolysin; Hyaluronate lyase; Protease; Review; Streptococcus agalactiae; Virulence factor

Indexed keywords

CARBOHYDRATE; CM 101; COMPLEMENT COMPONENT C5A; CYTOLYSIN; EXOTOXIN; HEMOLYSIN; HYALURONIDASE; LYASE; PEPTIDASE; PEPTIDE DERIVATIVE; VIRULENCE FACTOR;

EID: 2442695616     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1296     Document Type: Review
Times cited : (43)

References (87)
  • 1
    • 0035882422 scopus 로고    scopus 로고
    • Group B streptococcal disease in nonpregnant adults
    • Farley M. M.: Group B streptococcal disease in nonpregnant adults. Clin Infect Dis 33, 556-561 (2001)
    • (2001) Clin Infect Dis , vol.33 , pp. 556-561
    • Farley, M.M.1
  • 4
    • 0002053789 scopus 로고    scopus 로고
    • Pathogenic mechanisms and virulence factors of group B streptococci
    • Eds: Fischetti VA, Ferretti JJ, Portnoy DA, Rood JI. ASM Press, Washington, D.C.
    • Nizet V. & C. E. Rubens: Pathogenic mechanisms and virulence factors of group B streptococci. In: The Gram- Positive Pathogens. Eds: Fischetti VA, Ferretti JJ, Portnoy DA, Rood JI. ASM Press, Washington, D.C. 125-136 (2000)
    • (2000) The Gram- Positive Pathogens , pp. 125-136
    • Nizet, V.1    Rubens, C.E.2
  • 5
    • 0001918172 scopus 로고    scopus 로고
    • Surface structures of group B streptococcus important in human immunity
    • Eds: Fischetti VA, Ferretti JJ, Portnoy DA, Rood JI. ASM Press, Washington, D.C.
    • Paoletti L. C., L. C. Madoff & D. L. Kasper: Surface structures of group B streptococcus important in human immunity. In: The Gram-Positive Pathogens. Eds: Fischetti VA, Ferretti JJ, Portnoy DA, Rood JI. ASM Press, Washington, D.C. 137-153 (2000)
    • (2000) The Gram-Positive Pathogens , pp. 137-153
    • Paoletti, L.C.1    Madoff, L.C.2    Kasper, D.L.3
  • 6
    • 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
  • 7
    • 0019787480 scopus 로고
    • Lysis of erythrocytes by a hemolysin produced by a group B Streptococcus sp
    • Marchlewicz B. A. & J. L. Duncan: Lysis of erythrocytes by a hemolysin produced by a group B Streptococcus sp. Infect Immun 34, 787-794 (1981)
    • (1981) Infect Immun , vol.34 , pp. 787-794
    • Marchlewicz, B.A.1    Duncan, J.L.2
  • 8
    • 0026134643 scopus 로고
    • The hemolytic and cytolytic activity of group B streptococcal hemolysin and its possible role in early onset group B streptococcal disease
    • Tapsall J. W. & E. A. Phillips: The hemolytic and cytolytic activity of group B streptococcal hemolysin and its possible role in early onset group B streptococcal disease. Pathology 23, 139-144 (1991)
    • (1991) Pathology , vol.23 , pp. 139-144
    • Tapsall, J.W.1    Phillips, E.A.2
  • 9
    • 0029736682 scopus 로고    scopus 로고
    • Group B streptococcal beta- Hemolysin expression is associated with injury of lung epithelial cells
    • Nizet V., R. L. Gibson, E. Y. Chi, P. E. Framson, M. Hulse & C. E. Rubens: Group B streptococcal beta- hemolysin expression is associated with injury of lung epithelial cells. Infect Immun 64, 3818-3826 (1996)
    • (1996) Infect Immun , vol.64 , pp. 3818-3826
    • Nizet, V.1    Gibson, R.L.2    Chi, E.Y.3    Framson, P.E.4    Hulse, M.5    Rubens, C.E.6
  • 10
    • 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
  • 11
    • 0019196836 scopus 로고
    • Properties of a hemolysin produced by group B streptococci
    • Marchlewicz B. A. & J. L. Duncan: Properties of a hemolysin produced by group B streptococci. Infect Immun 30, 805-813 (1980)
    • (1980) Infect Immun , vol.30 , pp. 805-813
    • Marchlewicz, B.A.1    Duncan, J.L.2
  • 13
    • 0021024063 scopus 로고
    • Effect of carrier molecules on production and properties of extracellular hemolysin produced by Streptococcus agalactiae
    • Tsaihong J. & D. Wennerstrom: Effect of carrier molecules on production and properties of extracellular hemolysin produced by Streptococcus agalactiae. Curr Microbiol 9, 33-338 (1983)
    • (1983) Curr Microbiol , vol.9 , pp. 33-338
    • Tsaihong, J.1    Wennerstrom, D.2
  • 14
    • 0023235593 scopus 로고
    • Relationship between pigment production and haemoysin formation by Lancefield group B streptococci
    • Tapsall J.: Relationship between pigment production and haemoysin formation by Lancefield group B streptococci. J Med Microbiol 24, 83-87 (1987)
    • (1987) J Med Microbiol , vol.24 , pp. 83-87
    • Tapsall, J.1
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0035154927 scopus 로고    scopus 로고
    • Genetic basis for the beta- Haemolytic/cytolytic activity of group B Streptococcus
    • Pritzlaff C. A., J. C. Chang, S. P. Kuo, G. S. Tamura, C. E. Rubens & V. Nizet: Genetic basis for the beta- haemolytic/cytolytic activity of group B Streptococcus. Mol Microbiol 39, 236-247 (2001)
    • (2001) Mol Microbiol , vol.39 , pp. 236-247
    • Pritzlaff, C.A.1    Chang, J.C.2    Kuo, S.P.3    Tamura, G.S.4    Rubens, C.E.5    Nizet, V.6
  • 18
    • 0018727314 scopus 로고
    • Group B streptococcal type Ia sepsis in mice after intranasal inoculation and the effect of infection on lungs
    • Wennerstrom D. E.: Group B streptococcal type Ia sepsis in mice after intranasal inoculation and the effect of infection on lungs. Infect Immun 26, 287-293 (1979)
    • (1979) Infect Immun , vol.26 , pp. 287-293
    • Wennerstrom, D.E.1
  • 19
    • 0030819130 scopus 로고    scopus 로고
    • The role of group B streptococci beta-hemolysin expression in newborn lung injury
    • Nizet V., R. L. Gibson & C. E. Rubens: The role of group B streptococci beta-hemolysin expression in newborn lung injury. Adv Exp Med Biol 418, 627-630 (1997)
    • (1997) Adv Exp Med Biol , vol.418 , pp. 627-630
    • Nizet, V.1    Gibson, R.L.2    Rubens, C.E.3
  • 21
    • 0037097516 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin induces mortality and liver injury in experimental sepsis
    • Ring A., J. S. Braun, J. Pohl, V. Nizet, W. Stremmel & J. L. Shenep: Group B streptococcal beta-hemolysin induces mortality and liver injury in experimental sepsis. J Infect Dis 185, 1745-1753 (2002)
    • (2002) J Infect Dis , vol.185 , pp. 1745-1753
    • Ring, A.1    Braun, J.S.2    Pohl, J.3    Nizet, V.4    Stremmel, W.5    Shenep, J.L.6
  • 22
    • 0032909112 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin promotes injury of lung microvascular endothelial cells
    • Gibson R. L., V. Nizet & C. E. Rubens: Group B streptococcal beta-hemolysin promotes injury of lung microvascular endothelial cells. Pediatr Res 45, 626-634 (1999)
    • (1999) Pediatr Res , vol.45 , pp. 626-634
    • Gibson, R.L.1    Nizet, V.2    Rubens, C.E.3
  • 24
    • 0033928019 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin induces nitric oxide production in murine macrophages
    • Ring A., J. S. Braun, V. Nizet, W. Stremmel & J. L. Shenep: Group B streptococcal beta-hemolysin induces nitric oxide production in murine macrophages. J Infect Dis 182, 150-157 (2000)
    • (2000) J Infect Dis , vol.182 , pp. 150-157
    • Ring, A.1    Braun, J.S.2    Nizet, V.3    Stremmel, W.4    Shenep, J.L.5
  • 25
    • 0037080038 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8
    • Doran K. S., J. C. Chang, V. M. Benoit, L. Eckmann & V. Nizet: Group B streptococcal beta-hemolysin/cytolysin promotes invasion of human lung epithelial cells and the release of interleukin-8. J Infect Dis 185, 196-203 (2002)
    • (2002) J Infect Dis , vol.185 , pp. 196-203
    • Doran, K.S.1    Chang, J.C.2    Benoit, V.M.3    Eckmann, L.4    Nizet, V.5
  • 26
    • 0141723665 scopus 로고    scopus 로고
    • Group B streptococcal beta- Hemolysin/cytolysin activates neutrophil signaling pathways in brain endothelium and contributes to development of meningitis
    • Doran K, G. Y. Liu, V.: Group B streptococcal beta- hemolysin/cytolysin activates neutrophil signaling pathways in brain endothelium and contributes to development of meningitis. J Clin Invest 112, 736-744 (2003)
    • (2003) J Clin Invest , vol.112 , pp. 736-744
    • Doran, K.1    Liu, G.Y.2
  • 28
    • 0036785637 scopus 로고    scopus 로고
    • Cellular activation, phagocytosis, and bactericidal activity against group B streptococcus involve parallel myeloid differentiation factor 88-dependent and independent signaling pathways
    • Henneke P., O. Takeuchi, R. Malley, E. Lien, R. R. Ingalls, M. W. Freeman, T. Mayadas, V. Nizet, S. Akira, D. L. Kasper & D. T. Golenbock: Cellular activation, phagocytosis, and bactericidal activity against group B streptococcus involve parallel myeloid differentiation factor 88-dependent and independent signaling pathways. J Immunol 169, 3970-3977 (2002)
    • (2002) J Immunol , vol.169 , pp. 3970-3977
    • Henneke, P.1    Takeuchi, O.2    Malley, R.3    Lien, E.4    Ingalls, R.R.5    Freeman, M.W.6    Mayadas, T.7    Nizet, V.8    Akira, S.9    Kasper, D.L.10    Golenbock, D.T.11
  • 29
    • 0035037963 scopus 로고    scopus 로고
    • Immunomodulation by exogenous surfactant: Effect on TNF-alpha secretion and luminol- Enhanced chemiluminescence activity by murine macrophages stimulated with group B streptococci
    • Talati A. J., D. T. Crouse, B. K. English, C. Newman, L. Harrison & E. Meals: Immunomodulation by exogenous surfactant: effect on TNF-alpha secretion and luminol- enhanced chemiluminescence activity by murine macrophages stimulated with group B streptococci. Microbes Infect 3, 267-273 (2001)
    • (2001) Microbes Infect , vol.3 , pp. 267-273
    • Talati, A.J.1    Crouse, D.T.2    English, B.K.3    Newman, C.4    Harrison, L.5    Meals, E.6
  • 30
    • 0033753605 scopus 로고    scopus 로고
    • Surfactant treatment of neonates with respiratory failure and group B streptococcal infection
    • Members of the Collaborative European Multicenter Study Group. discussion 1135
    • Herting E., O. Gefeller, M. Land, L. van Sonderen, K. Harms & B. Robertson: Surfactant treatment of neonates with respiratory failure and group B streptococcal infection. Members of the Collaborative European Multicenter Study Group. Pediatrics 106, 957-964; discussion 1135 (2000)
    • (2000) Pediatrics , vol.106 , pp. 957-964
    • Herting, E.1    Gefeller, O.2    Land, M.3    Van Sonderen, L.4    Harms, K.5    Robertson, B.6
  • 31
    • 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
  • 32
    • 0029896862 scopus 로고    scopus 로고
    • Compositional analysis of hyaluronan, chondroitin sulfate and dermatan sulfate: HPLC of disaccharides produced from the glycosaminoglycans by solvolysis
    • Tokyo
    • Qui G. N., T. H., T. Toida, I. Koshiishi & I. T: Compositional analysis of hyaluronan, chondroitin sulfate and dermatan sulfate: HPLC of disaccharides produced from the glycosaminoglycans by solvolysis. Chem. Pharm. Bull. (Tokyo) 44, 1017-1020 (1996)
    • (1996) Chem. Pharm. Bull. , vol.44 , pp. 1017-1020
    • Qui, G.N.1    Toida, T.2    Koshiishi, I.3
  • 33
    • 0030713419 scopus 로고    scopus 로고
    • Specificity of the hyaluronate lyase of group-B streptococcus toward unsulphated regions of chondroitin sulphate
    • Baker J. R., H. Yu, K. Morrison, W. F. Averett & D. G. Pritchard: Specificity of the hyaluronate lyase of group-B streptococcus toward unsulphated regions of chondroitin sulphate. Biochem J 327 (Pt 1), 65-71 (1997)
    • (1997) Biochem J , vol.327 , Issue.1 PART , pp. 65-71
    • Baker, J.R.1    Yu, H.2    Morrison, K.3    Averett, W.F.4    Pritchard, D.G.5
  • 34
    • 0034212445 scopus 로고    scopus 로고
    • Action pattern and substrate specificity of the hyaluronan lyase from group B streptococci
    • Baker J. R. & D. G. Pritchard: Action pattern and substrate specificity of the hyaluronan lyase from group B streptococci. Biochem J 348 Pt 2, 465-471 (2000)
    • (2000) Biochem J , vol.348 , Issue.2 PART , pp. 465-471
    • Baker, J.R.1    Pritchard, D.G.2
  • 36
    • 0032577423 scopus 로고    scopus 로고
    • The Streptococcus agalactiae hylB gene encoding hyaluronate lyase: Completion of the sequence and expression analysis
    • Gase K., J. Ozegowski & H. Malke: The Streptococcus agalactiae hylB gene encoding hyaluronate lyase: completion of the sequence and expression analysis. Biochim Biophys Acta 1398, 86-98 (1998)
    • (1998) Biochim Biophys Acta , vol.1398 , pp. 86-98
    • Gase, K.1    Ozegowski, J.2    Malke, H.3
  • 37
    • 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
  • 39
    • 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
  • 40
    • 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
  • 41
    • 0025338724 scopus 로고
    • Hyaluronate can function as a cell adhesion molecule and CD44 participates in hyaluronate recognition
    • Miyake K., C. B. Underhill, J. Lesley & P. W. Kincade: Hyaluronate can function as a cell adhesion molecule and CD44 participates in hyaluronate recognition. J Exp Med 172, 69-75 (1990)
    • (1990) J Exp Med , vol.172 , pp. 69-75
    • Miyake, K.1    Underhill, C.B.2    Lesley, J.3    Kincade, P.W.4
  • 42
    • 0024435017 scopus 로고
    • CD44-a molecule involved in leukocyte adherence and T-cell activation
    • Haynes B. F., M. J. Telen, L. P. Hale & S. M. Denning: CD44-a molecule involved in leukocyte adherence and T-cell activation. Immunol Today 10, 423-428 (1989)
    • (1989) Immunol Today , vol.10 , pp. 423-428
    • Haynes, B.F.1    Telen, M.J.2    Hale, L.P.3    Denning, S.M.4
  • 43
    • 0018176336 scopus 로고
    • Association of elevated levels of extracellular neuraminidase with clinical isolates of type III group B streptococci
    • Milligan T. W., C. J. Baker, D. C. Straus & S. J. Mattingly: Association of elevated levels of extracellular neuraminidase with clinical isolates of type III group B streptococci. Infect Immun 21, 738-746 (1978)
    • (1978) Infect Immun , vol.21 , pp. 738-746
    • Milligan, T.W.1    Baker, C.J.2    Straus, D.C.3    Mattingly, S.J.4
  • 44
  • 45
    • 0023893101 scopus 로고
    • Pulmonary alveolar type II epithelial cells synthesize and secrete proteins of the classical and alternative complement pathways
    • Strunk R. C., D. M. Eidlen & R. J. Mason: Pulmonary alveolar type II epithelial cells synthesize and secrete proteins of the classical and alternative complement pathways. J Clin Invest 81, 1419-1426 (1988)
    • (1988) J Clin Invest , vol.81 , pp. 1419-1426
    • Strunk, R.C.1    Eidlen, D.M.2    Mason, R.J.3
  • 46
    • 0018077302 scopus 로고
    • Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a
    • Fernandez H. N. & T. E. Hugli: Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a. J Biol Chem 253, 6955-6964 (1978)
    • (1978) J Biol Chem , vol.253 , pp. 6955-6964
    • Fernandez, H.N.1    Hugli, T.E.2
  • 47
    • 0017100057 scopus 로고
    • Pneumonia in the neonate associated with group B streptococcal septicemia
    • Hemming V. G., D. W. McCloskey & H. R. Hill: Pneumonia in the neonate associated with group B streptococcal septicemia. Am J Dis Child 130, 1231-1233 (1976)
    • (1976) Am J Dis Child , vol.130 , pp. 1231-1233
    • Hemming, V.G.1    McCloskey, D.W.2    Hill, H.R.3
  • 48
    • 0016127795 scopus 로고
    • Group B beta-hemolytic streptococcal infection in the newborn. I. Early onset infection
    • Quirante J., R. Ceballos & G. Cassady: Group B beta-hemolytic streptococcal infection in the newborn. I. Early onset infection. Am J Dis Child 128, 659-665 (1974)
    • (1974) Am J Dis Child , vol.128 , pp. 659-665
    • Quirante, J.1    Ceballos, R.2    Cassady, G.3
  • 49
    • 0023271891 scopus 로고
    • Biochemical, structural, and functional abnormalities of polymorphonuclear leukocytes in the neonate
    • Hill H. R.: Biochemical, structural, and functional abnormalities of polymorphonuclear leukocytes in the neonate. Pediatr Res 22, 375-382 (1987)
    • (1987) Pediatr Res , vol.22 , pp. 375-382
    • Hill, H.R.1
  • 51
    • 0026086678 scopus 로고
    • Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus
    • Bohnsack J. F., K. W. Mollison, A. M. Buko, J. C. Ashworth & H. R. Hill: Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus. Biochem J 273 (Pt 3), 635-640 (1991)
    • (1991) Biochem J , vol.273 , Issue.3 PART , pp. 635-640
    • Bohnsack, J.F.1    Mollison, K.W.2    Buko, A.M.3    Ashworth, J.C.4    Hill, H.R.5
  • 53
    • 0029884182 scopus 로고    scopus 로고
    • Conservation of the C5a peptidase genes in group A and B streptococci
    • Chmouryguina I., A. Suvorov, P. Ferrieri & P. P. Cleary: Conservation of the C5a peptidase genes in group A and B streptococci. Infect Immun 64, 2387-2390 (1996)
    • (1996) Infect Immun , vol.64 , pp. 2387-2390
    • Chmouryguina, I.1    Suvorov, A.2    Ferrieri, P.3    Cleary, P.P.4
  • 55
    • 0030824688 scopus 로고    scopus 로고
    • Structural and functional similarity of C5a-ase enzymes from group A and B streptococci
    • Chmouryguina, II, A. N. Suvorov, B. Carlson & P. Cleary: Structural and functional similarity of C5a-ase enzymes from group A and B streptococci. Adv Exp Med Biol 418, 757-759 (1997)
    • (1997) Adv Exp Med Biol , vol.418 , pp. 757-759
    • Chmouryguina II1    Suvorov, A.N.2    Carlson, B.3    Cleary, P.4
  • 57
    • 0026565386 scopus 로고
    • Bacterial evasion of the antibody response: Human IgG antibodies neutralize soluble but not bacteria-associated group B streptococcal C5a-ase
    • Bohnsack J. F., X. N. Zhou, J. N. Gustin, C. E. Rubens, C. J. Parker & H. R. Hill: Bacterial evasion of the antibody response: human IgG antibodies neutralize soluble but not bacteria-associated group B streptococcal C5a-ase. J Infect Dis 165, 315-321 (1992)
    • (1992) J Infect Dis , vol.165 , pp. 315-321
    • Bohnsack, J.F.1    Zhou, X.N.2    Gustin, J.N.3    Rubens, C.E.4    Parker, C.J.5    Hill, H.R.6
  • 59
    • 0027537685 scopus 로고
    • Restricted ability of group B streptococcal C5a-ase to inactivate C5a prepared from different animal species
    • Bohnsack J. F., J. K. Chang & H. R. Hill: Restricted ability of group B streptococcal C5a-ase to inactivate C5a prepared from different animal species. Infect Immun 61, 1421-1426 (1993)
    • (1993) Infect Immun , vol.61 , pp. 1421-1426
    • Bohnsack, J.F.1    Chang, J.K.2    Hill, H.R.3
  • 61
    • 0024420563 scopus 로고
    • Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors
    • Kishimoto T. K., M. A. Jutila, E. L. Berg & E. C. Butcher: Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors. Science 245, 1238-1241 (1989)
    • (1989) Science , vol.245 , pp. 1238-1241
    • Kishimoto, T.K.1    Jutila, M.A.2    Berg, E.L.3    Butcher, E.C.4
  • 62
    • 0036117970 scopus 로고    scopus 로고
    • The group B streptococcal C5a peptidase is both a specific protease and an invasin
    • Cheng Q., D. Stafslien, S. S. Purushothaman & P. Cleary: The group B streptococcal C5a peptidase is both a specific protease and an invasin. Infect Immun 70, 2408-2413 (2002)
    • (2002) Infect Immun , vol.70 , pp. 2408-2413
    • Cheng, Q.1    Stafslien, D.2    Purushothaman, S.S.3    Cleary, P.4
  • 63
    • 0036266052 scopus 로고    scopus 로고
    • Identification of novel adhesins from Group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding
    • Beckmann C., J. D. Waggoner, T. O. Harris, G. S. Tamura & C. E. Rubens: Identification of novel adhesins from Group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding. Infect Immun 70, 2869-2876 (2002)
    • (2002) Infect Immun , vol.70 , pp. 2869-2876
    • Beckmann, C.1    Waggoner, J.D.2    Harris, T.O.3    Tamura, G.S.4    Rubens, C.E.5
  • 64
    • 0031230887 scopus 로고    scopus 로고
    • Arg-Gly-Asp(RGD) peptides inhibit Streptococcus mitis to adhere to fibronectin
    • Sugano N., H. Tanaka, K. Ito & S. Murai: Arg-Gly-Asp(RGD) peptides inhibit Streptococcus mitis to adhere to fibronectin. J Nihon Univ Sch Dent 39, 154-155 (1997)
    • (1997) J Nihon Univ Sch Dent , vol.39 , pp. 154-155
    • Sugano, N.1    Tanaka, H.2    Ito, K.3    Murai, S.4
  • 65
    • 0036841265 scopus 로고    scopus 로고
    • Immunization with C5a peptidase or peptidase-type III polysaccharide conjugate vaccines enhances clearance of group B streptococci from lungs of infected mice
    • Cheng Q., S. Debol, H. Lam, R. Eby, L. Edwards, Y. Matsuka, S. B. Olmsted & P. P. Cleary: Immunization with C5a peptidase or peptidase-type III polysaccharide conjugate vaccines enhances clearance of group B streptococci from lungs of infected mice. Infect Immun 70, 6409-6415 (2002)
    • (2002) Infect Immun , vol.70 , pp. 6409-6415
    • Cheng, Q.1    Debol, S.2    Lam, H.3    Eby, R.4    Edwards, L.5    Matsuka, Y.6    Olmsted, S.B.7    Cleary, P.P.8
  • 66
    • 0035077539 scopus 로고    scopus 로고
    • Antibody against surface-bound C5a peptidase is opsonic and initiates macrophage killing of group B streptococci
    • Cheng Q., B. Carlson, S. Pillai, R. Eby, L. Edwards, S. B. Olmsted & P. Cleary: Antibody against surface-bound C5a peptidase is opsonic and initiates macrophage killing of group B streptococci. Infect Immun 69, 2302-2308 (2001)
    • (2001) Infect Immun , vol.69 , pp. 2302-2308
    • Cheng, Q.1    Carlson, B.2    Pillai, S.3    Eby, R.4    Edwards, L.5    Olmsted, S.B.6    Cleary, P.7
  • 68
    • 0018383398 scopus 로고
    • Nature and mechanism of action of the CAMP protein of group B streptococci
    • Bernheimer A. W., R. Linder & L. S. Avigad: Nature and mechanism of action of the CAMP protein of group B streptococci. Infect Immun 23, 838-844 (1979)
    • (1979) Infect Immun , vol.23 , pp. 838-844
    • Bernheimer, A.W.1    Linder, R.2    Avigad, L.S.3
  • 70
    • 0023759423 scopus 로고
    • Cloning and expression of the CAMP factor of group B streptococci in Escherichia coli
    • Schneewind O., K. Friedrich & R. Lutticken: Cloning and expression of the CAMP factor of group B streptococci in Escherichia coli. Infect Immun 56, 2174-2179 (1988)
    • (1988) Infect Immun , vol.56 , pp. 2174-2179
    • Schneewind, O.1    Friedrich, K.2    Lutticken, R.3
  • 71
    • 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
  • 72
    • 0032774762 scopus 로고    scopus 로고
    • Identification, cloning, and expression of the CAMP factor gene (cfa) of group A streptococci
    • Gase K., J. J. Ferretti, C. Primeaux & W. M. McShan: Identification, cloning, and expression of the CAMP factor gene (cfa) of group A streptococci. Infect Immun 67, 4725-4731 (1999)
    • (1999) Infect Immun , vol.67 , pp. 4725-4731
    • Gase, K.1    Ferretti, J.J.2    Primeaux, C.3    McShan, W.M.4
  • 73
    • 0141755375 scopus 로고    scopus 로고
    • Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin
    • Lang S. & M. Palmer: Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin. J Biol Chem 2003)
    • (2003) J Biol Chem
    • Lang, S.1    Palmer, M.2
  • 74
    • 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
  • 75
    • 0019406305 scopus 로고
    • Lethal effect of CAMP-factor and UBERIS-factor - A new finding about diffusible exosubstances of Streptococcus agalactiae and Streptococcus uberis
    • Skalka 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 A 249, 190-194 (1981)
    • (1981) Zentralbl Bakteriol A , vol.249 , pp. 190-194
    • Skalka, B.1    Smola, J.2
  • 76
    • 0028149749 scopus 로고
    • Cell-associated collagenolytic activity by group B streptococci
    • Jackson R. J., M. L. Dao & D. V. Lim: Cell-associated collagenolytic activity by group B streptococci. Infect Immun 62, 5647-5651 (1994)
    • (1994) Infect Immun , vol.62 , pp. 5647-5651
    • Jackson, R.J.1    Dao, M.L.2    Lim, D.V.3
  • 78
    • 0019506980 scopus 로고
    • Studies on group B beta- Hemolytic Streptococcus. I. Isolation and partial characterization of an extracellular toxin
    • Hellerqvist C. G., J. Rojas, R. S. Green, S. Sell, H. Sundell & M. T. Stahlman: Studies on group B beta- hemolytic Streptococcus. I. Isolation and partial characterization of an extracellular toxin. Pediatr Res 15, 892-898 (1981)
    • (1981) Pediatr Res , vol.15 , pp. 892-898
    • Hellerqvist, C.G.1    Rojas, J.2    Green, R.S.3    Sell, S.4    Sundell, H.5    Stahlman, M.T.6
  • 79
    • 0021015244 scopus 로고
    • Pulmonary hemodynamic and ultrastructural changes associated with Group B streptococcal toxemia in adult sheep and newborn lambs
    • Rojas J., L. E. Larsson, C. G. Hellerqvist, K. L. Brigham, M. E. Gray & M. T. Stahlman: Pulmonary hemodynamic and ultrastructural changes associated with Group B streptococcal toxemia in adult sheep and newborn lambs. Pediatr Res 17, 1002-1008 (1983)
    • (1983) Pediatr Res , vol.17 , pp. 1002-1008
    • Rojas, J.1    Larsson, L.E.2    Hellerqvist, C.G.3    Brigham, K.L.4    Gray, M.E.5    Stahlman, M.T.6
  • 80
    • 0023108832 scopus 로고
    • Molecular basis for group B beta-hemolytic streptococcal disease
    • Hellerqvist C. G., H. Sundell & P. Gettins: Molecular basis for group B beta-hemolytic streptococcal disease. Proc Natl Acad Sci U S A 84, 51-55 (1987)
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 51-55
    • Hellerqvist, C.G.1    Sundell, H.2    Gettins, P.3
  • 83
    • 0033977389 scopus 로고    scopus 로고
    • Evaluation of the virulence of a Streptococcus pneumoniae neuraminidase-deficient mutant in nasopharyngeal colonization and development of otitis media in the chinchilla model
    • Tong H. H., L. E. Blue, M. A. James & T. F. DeMaria: Evaluation of the virulence of a Streptococcus pneumoniae neuraminidase-deficient mutant in nasopharyngeal colonization and development of otitis media in the chinchilla model. Infect Immun 68, 921-924 (2000)
    • (2000) Infect Immun , vol.68 , pp. 921-924
    • Tong, H.H.1    Blue, L.E.2    James, M.A.3    DeMaria, T.F.4
  • 84
    • 0034786512 scopus 로고    scopus 로고
    • The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence
    • Holmes A. R., R. McNab, K. W. Millsap, M. Rohde, S. Hammerschmidt, J. L. Mawdsley & H. F. Jenkinson: The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol Microbiol 41, 1395-1408 (2001)
    • (2001) Mol Microbiol , vol.41 , pp. 1395-1408
    • Holmes, A.R.1    McNab, R.2    Millsap, K.W.3    Rohde, M.4    Hammerschmidt, S.5    Mawdsley, J.L.6    Jenkinson, H.F.7
  • 85
    • 0036568587 scopus 로고    scopus 로고
    • Anchorless adhesins and invasins of Gram-positive bacteria: A new class of virulence factors
    • Chhatwal G. S.: Anchorless adhesins and invasins of Gram-positive bacteria: a new class of virulence factors. Trends Microbiol 10, 205-208 (2002)
    • (2002) Trends Microbiol , vol.10 , pp. 205-208
    • Chhatwal, G.S.1
  • 86
    • 0033775014 scopus 로고    scopus 로고
    • Identification of Streptococcus agalactiae virulence genes in the neonatal rat sepsis model using signature-tagged mutagenesis
    • Jones A. L., K. M. Knoll & C. E. Rubens: Identification of Streptococcus agalactiae virulence genes in the neonatal rat sepsis model using signature-tagged mutagenesis. Mol Microbiol 37, 1444-1455 (2000)
    • (2000) Mol Microbiol , vol.37 , pp. 1444-1455
    • Jones, A.L.1    Knoll, K.M.2    Rubens, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.