메뉴 건너뛰기




Volumn 6, Issue 1, 2004, Pages 79-88

Enolase from Streptococcus sobrinus is an immunosuppressive protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIGEN; BACTERIUM ANTIBODY; CYTOKINE; ENOLASE; FLUORIDE; GAMMA INTERFERON; GENE PRODUCT; HISTIDINE; IMMUNOSUPPRESSIVE ACID PROTEIN; INTERLEUKIN 10; POLYPEPTIDE; RECOMBINANT ENZYME;

EID: 1642431995     PISSN: 14625814     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1462-5822.2003.00344.x     Document Type: Article
Times cited : (50)

References (50)
  • 3
    • 0018677353 scopus 로고
    • Evidence for the synthesis and release of strongly immunosuppressive noncytotoxic substances by Streptococcus intermedius
    • Arala-Chaves, M., Higerd, T.B., Porto, M.T., Munoz, J., Goust, J.M., and Fudenberg, H.H. (1979) Evidence for the synthesis and release of strongly immunosuppressive noncytotoxic substances by Streptococcus intermedius. J Clin Invest 64: 871-873.
    • (1979) J. Clin. Invest. , vol.64 , pp. 871-873
    • Arala-Chaves, M.1    Higerd, T.B.2    Porto, M.T.3    Munoz, J.4    Goust, J.M.5    Fudenberg, H.H.6
  • 4
    • 0024120138 scopus 로고
    • Correlation between B cell mitogenicity and immunosuppressor effect of a protein released by porcine monocytes infected with African swine fever virus
    • Arala-Chaves, M.P., Ribeiro, A.S., Vilanova, M., Porto, M.T., Santarem, M.M.G., and Lima, M. (1988) Correlation between B cell mitogenicity and immunosuppressor effect of a protein released by porcine monocytes infected with African swine fever virus. Am J Vet Res 49: 1955-1961.
    • (1988) Am. J. Vet. Res. , vol.49 , pp. 1955-1961
    • Arala-Chaves, M.P.1    Ribeiro, A.S.2    Vilanova, M.3    Porto, M.T.4    Santarem, M.M.G.5    Lima, M.6
  • 5
    • 0016031737 scopus 로고
    • Antibody formation in mouse bone marrow. I. Evidence for the development of plaque forming cells in situ
    • Benner, R., Meina, F., Van der Meulen, G.M., and Muiswinkel, W.B.V. (1974) Antibody formation in mouse bone marrow. I. Evidence for the development of plaque forming cells in situ. Immunology 26: 247-255.
    • (1974) Immunology , vol.26 , pp. 247-255
    • Benner, R.1    Meina, F.2    Van der Meulen, G.M.3    Muiswinkel, W.B.V.4
  • 6
    • 0034931519 scopus 로고    scopus 로고
    • a-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergman, S., Rohde, M., Chhatwal, G.S., and Hammerschmidt, S. (2001) a-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40: 1273-1287.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1273-1287
    • Bergman, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 7
    • 0027193999 scopus 로고
    • Infection with Mycobacterium avium induces production of interleukin-10 (IL-10), and administration of anti-IL-10 antibody is associated with enhanced resistance to infection in mice
    • Bermudez, L.E., and Champsi, J. (1993) Infection with Mycobacterium avium induces production of interleukin-10 (IL-10), and administration of anti-IL-10 antibody is associated with enhanced resistance to infection in mice. Infect Immun 61: 3093-3097.
    • (1993) Infect. Immun. , vol.61 , pp. 3093-3097
    • Bermudez, L.E.1    Champsi, J.2
  • 9
    • 0034964334 scopus 로고    scopus 로고
    • Mechanisms for induction of immunosuppression during experimental cryptococcosis: Role of glucuronoxylomannan
    • Chiapello, L., Iribarren, P., Cervi, L., Rubinstein, H., and Masih, D.T. (2001) Mechanisms for induction of immunosuppression during experimental cryptococcosis: role of glucuronoxylomannan. Clin Immunol 100: 96-106.
    • (2001) Clin. Immunol. , vol.100 , pp. 96-106
    • Chiapello, L.1    Iribarren, P.2    Cervi, L.3    Rubinstein, H.4    Masih, D.T.5
  • 10
    • 0026578175 scopus 로고
    • Natural transmission of Streptococcus sobrinus. rats: Saliva and serum antibody responses to colonization
    • Cole, M.F., Hsu, S.D., Sheridan, M.J., and Stiles, H.M. (1992) Natural transmission of Streptococcus sobrinus. rats: saliva and serum antibody responses to colonization. Infect Immun 60: 778-783.
    • (1992) Infect. Immun. , vol.60 , pp. 778-783
    • Cole, M.F.1    Hsu, S.D.2    Sheridan, M.J.3    Stiles, H.M.4
  • 13
    • 0023903777 scopus 로고
    • Correlation between specific immunosuppression and polyclonal B cell activation induced by a protein secreted by Streptococcus mutans
    • Ferreira, P., Soares. R., Ribeiro, A., and Arala-Chaves, M.P. (1988) Correlation between specific immunosuppression and polyclonal B cell activation induced by a protein secreted by Streptococcus mutans. Scand J Immunol 27: 549-554.
    • (1988) Scand. J. Immunol. , vol.27 , pp. 549-554
    • Ferreira, P.1    Soares, R.2    Ribeiro, A.3    Arala-Chaves, M.P.4
  • 14
    • 0030844105 scopus 로고    scopus 로고
    • Purification, biochemical and biological characterization of an immunosuppressive and lymphocyte mitogenic protein secreted by Streptococcus sobrinus
    • Ferreira, P., Brás, A., Tavares, D., Vilanova, M., Ribeiro, A., Videira, A., and Arala-Chaves, M. (1997) Purification, biochemical and biological characterization of an immunosuppressive and lymphocyte mitogenic protein secreted by Streptococcus sobrinus. Int Immunol 11: 1735-1743.
    • (1997) Int. Immunol. , vol.11 , pp. 1735-1743
    • Ferreira, P.1    Brás, A.2    Tavares, D.3    Vilanova, M.4    Ribeiro, A.5    Videira, A.6    Arala-Chaves, M.7
  • 15
    • 0026768249 scopus 로고
    • Characterization of the interaction of yeast enolase with polynucleotides
    • 1159
    • al-Giery, A.G., and Brewer, J.M. (1992) Characterization of the interaction of yeast enolase with polynucleotides. Biochim Biophys Acta 1159: 134-140.
    • (1992) Biochim. Biophys. Acta , pp. 134-140
    • al-Giery, A.G.1    Brewer, J.M.2
  • 16
    • 0017440273 scopus 로고
    • Effects of fluoride on the enzymatic regulation of bacterial carbohydrate metabolism
    • Hamilton, I.R. (1977) Effects of fluoride on the enzymatic regulation of bacterial carbohydrate metabolism. Caries Res 11: 262-291.
    • (1977) Caries Res. , vol.11 , pp. 262-291
    • Hamilton, I.R.1
  • 17
    • 0034026315 scopus 로고    scopus 로고
    • Current understanding of the cause of dental caries
    • Hanada, N. (2000) Current understanding of the cause of dental caries. Jpn J Infect Dis 53: 1-5.
    • (2000) Jpn. J. Infect. Dis. , vol.53 , pp. 1-5
    • Hanada, N.1
  • 18
    • 0035200159 scopus 로고    scopus 로고
    • The effects of interleukin-10 depletion in vivo on the immune response to Porphyromonas gingivalis. a murine model
    • Herminajeng, E., Sosroseno, W., Bird, P.S., and Seymour, G.J. (2001) The effects of interleukin-10 depletion in vivo on the immune response to Porphyromonas gingivalis. a murine model. Periodontol 72: 1527-1534.
    • (2001) Periodontol. , vol.72 , pp. 1527-1534
    • Herminajeng, E.1    Sosroseno, W.2    Bird, P.S.3    Seymour, G.J.4
  • 19
    • 0027347042 scopus 로고
    • Close association between Streptococcus sobrinus. the saliva of young children and smooth-surface caries increment
    • Hirose, H., Hirose, K., Isogai, E., Miura, H., and Ueda, I. (1993) Close association between Streptococcus sobrinus. the saliva of young children and smooth-surface caries increment. Caries Res 27: 292-297.
    • (1993) Caries Res. , vol.27 , pp. 292-297
    • Hirose, H.1    Hirose, K.2    Isogai, E.3    Miura, H.4    Ueda, I.5
  • 20
    • 0025217794 scopus 로고
    • Isolation, Characterization, and inhibition kinetics of enolase from Streptococcus rattus FA-1
    • Huther, F.J., Psarros, N., and Duschner, H. (1990) Isolation, Characterization, and inhibition kinetics of enolase from Streptococcus rattus FA-1. Infect Immun 58: 1043-1047.
    • (1990) Infect. Immun. , vol.58 , pp. 1043-1047
    • Huther, F.J.1    Psarros, N.2    Duschner, H.3
  • 21
    • 0020525576 scopus 로고
    • Removal of Gram-negative endotoxin from solution by affinity chromatography
    • Issekutz, A.C. (1983) Removal of Gram-negative endotoxin from solution by affinity chromatography. J Immunol Meth 61: 275-281.
    • (1983) J. Immunol. Meth. , vol.61 , pp. 275-281
    • Issekutz, A.C.1
  • 23
    • 0026586872 scopus 로고
    • Purification, characterization and inhibition by fluoride of enolase from Streptococcus mutans DSM 320523
    • Kaufmann, M., and Bartholmes, P. (1992) Purification, characterization and inhibition by fluoride of enolase from Streptococcus mutans DSM 320523. Caries Res 26: 110-116.
    • (1992) Caries Res. , vol.26 , pp. 110-116
    • Kaufmann, M.1    Bartholmes, P.2
  • 24
    • 0026709730 scopus 로고
    • Protective effect of a T-cell dependent immunosuppressive B cell mitogenic protein (F3′ EP-Si, or p90) produced by Streptococcus intermedius
    • Lima, M., Bandeira, A., Portnoi, D., Ribeiro, A., and Arala-Chaves, M. P. (1992) Protective effect of a T-cell dependent immunosuppressive B cell mitogenic protein (F3′ EP-Si, or p90) produced by Streptococcus intermedius. Infect Immun 60: 3571-3578.
    • (1992) Infect. Immun. , vol.60 , pp. 3571-3578
    • Lima, M.1    Bandeira, A.2    Portnoi, D.3    Ribeiro, A.4    Arala-Chaves, M.P.5
  • 25
    • 0022993292 scopus 로고
    • Role of Streptococcus mutans in human dental decay
    • Loesche, W.J. (1986) Role of Streptococcus mutans in human dental decay. Microbiol Rev 50: 353-380.
    • (1986) Microbiol. Rev. , vol.50 , pp. 353-380
    • Loesche, W.J.1
  • 26
    • 0028089206 scopus 로고
    • Capturing host plasmin (ogen): A common mechanism for invasive pathogens
    • Lottenberg, R., Minning-Wenz, D., and Boyle, M.D. (1994) Capturing host plasmin (ogen): a common mechanism for invasive pathogens. Trends Microbiol 2: 20-24.
    • (1994) Trends Microbiol. , vol.2 , pp. 20-24
    • Lottenberg, R.1    Minning-Wenz, D.2    Boyle, M.D.3
  • 27
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Rosebrough, New York
    • Lowry, O.H., Rosebrough, New York, Farr, A.L., and Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Farr, A.L.2    Randall, R.J.3
  • 29
    • 0141494459 scopus 로고
    • 2nd edn. Baltimore: Williams & Wilkins
    • Newbrun, E. (1983) Cariology, 2nd edn. Baltimore: Williams & Wilkins.
    • (1983) Cariology
    • Newbrun, E.1
  • 30
    • 0032486286 scopus 로고    scopus 로고
    • α-Enolase, a novel strong plasmin (ogen) binding protein on the surface of pathogenic Streptococci
    • Pancholi, V., and Fischetti, V.A. (1998) α-Enolase, a novel strong plasmin (ogen) binding protein on the surface of pathogenic Streptococci. J Biol Chem 273: 14503-14515.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 31
    • 0028297672 scopus 로고
    • Neutralization of IL-10 up-regulates nitric oxide production and protects susceptible mice from challenge with Candida albicans
    • Romani, L., Puccetti, P., Mencacci, A., Cenci, E., Spaccapelo, R., Tonnetti, L., et al. (1994) Neutralization of IL-10 up-regulates nitric oxide production and protects susceptible mice from challenge with Candida albicans. J Immunol 153: 3514-3521.
    • (1994) J. Immunol. , vol.153 , pp. 3514-3521
    • Romani, L.1    Puccetti, P.2    Mencacci, A.3    Cenci, E.4    Spaccapelo, R.5    Tonnetti, L.6
  • 33
    • 0023515657 scopus 로고
    • Semi-purification of an immunosuppressor substance secreted by Streptococcus mutans which plays a role in the protection of the bacterium in the host
    • Santarem, M.M.G., Porto, M.T., Ferreira, P., Soares, R., and Arala-Chaves, M.P. (1987) Semi-purification of an immunosuppressor substance secreted by Streptococcus mutans which plays a role in the protection of the bacterium in the host. Scand J Immunol 26: 755-761.
    • (1987) Scand. J. Immunol. , vol.26 , pp. 755-761
    • Santarem, M.M.G.1    Porto, M.T.2    Ferreira, P.3    Soares, R.4    Arala-Chaves, M.P.5
  • 34
    • 0036467351 scopus 로고    scopus 로고
    • Yersinia enterocolitica evasion of the host innate immune response by V antigen-induced IL-10 production of macrophages is abrogated in IL-10-deficient mice
    • Sing, A., Roggenkamp, A., Geiger, A.M., and Heesemann, J. (2002) Yersinia enterocolitica evasion of the host innate immune response by V antigen-induced IL-10 production of macrophages is abrogated in IL-10-deficient mice. J Immunol 168: 1315-1321.
    • (2002) J. Immunol. , vol.168 , pp. 1315-1321
    • Sing, A.1    Roggenkamp, A.2    Geiger, A.M.3    Heesemann, J.4
  • 35
    • 0023972041 scopus 로고
    • Tooth decay in the developing world: Could a vaccine help prevent caries?
    • Smith, G.E. (1988) Tooth decay in the developing world: could a vaccine help prevent caries? Perspect Biol Med 31: 440-453.
    • (1988) Perspect. Biol. Med. , vol.31 , pp. 440-453
    • Smith, G.E.1
  • 37
    • 0028019545 scopus 로고
    • Cloning and DNA sequencing of the dextranase inhibitor gene (dei) from Streptococcus sobrinus
    • Sun, J., Wanda, S., Camilli, A., and Curtiss, R. III (1994) Cloning and DNA sequencing of the dextranase inhibitor gene (dei) from Streptococcus sobrinus. J Bacteriol 176: 7213-7222.
    • (1994) J. Bacteriol. , vol.176 , pp. 7213-7222
    • Sun, J.1    Wanda, S.2    Camilli, A.3    Curtiss III, R.4
  • 38
    • 0026738431 scopus 로고
    • Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant immunodominant glycolytic enzyme
    • Sundstrom, P., and Aliaga, G.R. (1992) Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant immunodominant glycolytic enzyme. J Bacteriol 174: 6789-6799.
    • (1992) J. Bacteriol. , vol.174 , pp. 6789-6799
    • Sundstrom, P.1    Aliaga, G.R.2
  • 39
    • 0028047655 scopus 로고
    • A subset of proteins found in culture supernatants of Candida albicans includes the abundant, immunodominant, glycolytic enzyme enolase
    • Sundstrom, P., and Aliaga, G.R. (1994) A subset of proteins found in culture supernatants of Candida albicans includes the abundant, immunodominant, glycolytic enzyme enolase. J Infect Dis 169: 452-456.
    • (1994) J. Infect. Dis. , vol.169 , pp. 452-456
    • Sundstrom, P.1    Aliaga, G.R.2
  • 40
    • 0027339306 scopus 로고
    • CD69 expression during selection and maturation of CD4+8+ thymocytes
    • Swat, W., Dessing, M., von Boehmer, H., and Kisielow, P. (1993) CD69 expression during selection and maturation of CD4+8+ thymocytes. Eur J Immunol 23: 739-744.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 739-744
    • Swat, W.1    Dessing, M.2    von Boehmer, H.3    Kisielow, P.4
  • 41
    • 0025945872 scopus 로고
    • Neuronal survival factor from bovine brain is identical to neuron-specific enolase
    • Takei, N., Kondo, J., Nagaike, K., Oshawa, K., Kato, K., and Kohsaka, S. (1991) Neuronal survival factor from bovine brain is identical to neuron-specific enolase. J Neurochem 57: 1178-1184.
    • (1991) J. Neurochem. , vol.57 , pp. 1178-1184
    • Takei, N.1    Kondo, J.2    Nagaike, K.3    Oshawa, K.4    Kato, K.5    Kohsaka, S.6
  • 42
    • 0027173916 scopus 로고
    • Immunological activities of a Candida albicans protein which play an important role in the survival of the microorganism in the host
    • Tavares, D., Salvador, A., Ferreira, P., and Arala-Chaves, M.P. (1993) Immunological activities of a Candida albicans protein which play an important role in the survival of the microorganism in the host. Infect Immun 61: 1881-1888.
    • (1993) Infect. Immun. , vol.61 , pp. 1881-1888
    • Tavares, D.1    Salvador, A.2    Ferreira, P.3    Arala-Chaves, M.P.4
  • 43
    • 0033914467 scopus 로고    scopus 로고
    • Increased resistence to systemic candidiasis in athymic or interleukin-10 depleted mice
    • Tavares, D., Ferreira, P., and Arala-Chaves, M. (2000) Increased resistence to systemic candidiasis in athymic or interleukin-10 depleted mice. J Infect Dis 182: 266-273.
    • (2000) J. Infect. Dis. , vol.182 , pp. 266-273
    • Tavares, D.1    Ferreira, P.2    Arala-Chaves, M.3
  • 44
    • 0025309621 scopus 로고
    • Molecular cloning of subunits of complex I from Neurospora crassa. Primary structure and in vitro expression of a 22-kDa polypeptide
    • Videira, A., Tropschug, M., Wachter, E., Schneider, H., and Werner, S. (1990) Molecular cloning of subunits of complex I from Neurospora crassa. Primary structure and in vitro expression of a 22-kDa polypeptide. J Biol Chem 265: 13060-13065.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13060-13065
    • Videira, A.1    Tropschug, M.2    Wachter, E.3    Schneider, H.4    Werner, S.5
  • 45
    • 0033016792 scopus 로고    scopus 로고
    • The biological effects induced in mice by p36, a proteinaceous factor of virulence produced by African swine fever virus, are mediated by interleukin-4 and also to a lesser extent by interleukin-10
    • Vilanova, M., Ferreira, P., Ribeiro, A., and Arala-Chaves, M. (1999) The biological effects induced in mice by p36, a proteinaceous factor of virulence produced by African swine fever virus, are mediated by interleukin-4 and also to a lesser extent by interleukin-10. Immunology 96: 389-395.
    • (1999) Immunology , vol.96 , pp. 389-395
    • Vilanova, M.1    Ferreira, P.2    Ribeiro, A.3    Arala-Chaves, M.4
  • 46
    • 1642574943 scopus 로고
    • National health care expenditure study. Dental services: Use, expenditures, and source of payment
    • Data Review 8. USDHHS Publishers no. 82. Washington, DC: Department of Health and Human Services
    • Walden, D.C., and Wilensky, G.R. (1982) National health care expenditure study. Dental services: use, expenditures, and source of payment. Data Review 8. USDHHS Publishers no. 82. Washington, DC: Department of Health and Human Services.
    • (1982)
    • Walden, D.C.1    Wilensky, G.R.2
  • 47
    • 0025864925 scopus 로고
    • Detection of circulating candida enolase by immunoassay in patients with cancer and invasive candidiasis
    • Walsh, T.J., Hathorn, J.W., Sobel, J.D., Merz, W.G., Sanchez, V., Maret, S.M., et al. (1991) Detection of circulating candida enolase by immunoassay in patients with cancer and invasive candidiasis. N Engl J Med 324: 1026-1031.
    • (1991) N. Engl. J. Med. , vol.324 , pp. 1026-1031
    • Walsh, T.J.1    Hathorn, J.W.2    Sobel, J.D.3    Merz, W.G.4    Sanchez, V.5    Maret, S.M.6
  • 48
    • 0022295671 scopus 로고
    • tau-Crystallin from the turtle lens: Purification and partial characterization
    • Williams, L.A., Ding, L., Horwitz, J., and Piatigorsky, J. (1985) tau-Crystallin from the turtle lens: purification and partial characterization. Exp Eye Res 40: 741-749.
    • (1985) Exp. Eye Res. , vol.40 , pp. 741-749
    • Williams, L.A.1    Ding, L.2    Horwitz, J.3    Piatigorsky, J.4
  • 50
    • 0023774341 scopus 로고
    • Characterization of a cell surface-expressed disulphide-linked dimer involved in murine T cell activation
    • Yokoyama, W.M., Koning, F., Kehn, P.J., Pereura, G.M., Stinge, G., Coligan, J.E., and Shevach, E.M. (1988) Characterization of a cell surface-expressed disulphide-linked dimer involved in murine T cell activation. J Immunol 141: 369-376.
    • (1988) J. Immunol. , vol.141 , pp. 369-376
    • Yokoyama, W.M.1    Koning, F.2    Kehn, P.J.3    Pereura, G.M.4    Stinge, G.5    Coligan, J.E.6    Shevach, E.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.