메뉴 건너뛰기




Volumn 6, Issue 1, 1999, Pages 133-136

Streptococcal DNase B is immunologically identical to superantigen SpeF but involves separate domains

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE; STREPTOCOCCUS ANTIGEN; STREPTOCOCCUS DEOXYRIBONUCLEASE B; SUPERANTIGEN; SUPERANTIGEN SPEF; UNCLASSIFIED DRUG;

EID: 0032952152     PISSN: 1071412X     EISSN: None     Source Type: Journal    
DOI: 10.1128/cdli.6.1.133-136.1999     Document Type: Article
Times cited : (15)

References (23)
  • 1
    • 0001322321 scopus 로고
    • A proteolytic enzyme produced by group a streptococci with special reference to its effect on the type-specific M antigen
    • Elliot, S. D. 1945. A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen. J. Exp. Med. 81:573-592.
    • (1945) J. Exp. Med. , vol.81 , pp. 573-592
    • Elliot, S.D.1
  • 2
    • 0032426052 scopus 로고    scopus 로고
    • Identification of domains involved in superantigenicity of streptococcal pyrogenic exotoxin F (SpeF)
    • in press
    • Eriksson, A., S. E. Holm, and M. Norgren. Identification of domains involved in superantigenicity of streptococcal pyrogenic exotoxin F (SpeF). Microb. Pathog., in press.
    • Microb. Pathog.
    • Eriksson, A.1    Holm, S.E.2    Norgren, M.3
  • 3
    • 85046518856 scopus 로고    scopus 로고
    • Epidemiology and clinical aspects of invasive streptococcal infections and the streptococcal toxic shock syndrome
    • in press
    • Eriksson, B., J. Andersson, S. E. Holm, and M. Norgren. Epidemiology and clinical aspects of invasive streptococcal infections and the streptococcal toxic shock syndrome. Clin. Infect. Dis., in press.
    • Clin. Infect. Dis.
    • Eriksson, B.1    Andersson, J.2    Holm, S.E.3    Norgren, M.4
  • 4
    • 0009725761 scopus 로고
    • Immune responses to streptococcal infections
    • N. R. Rose, H. Friedman, and J. L. Fahey (ed.), American Society for Microbiology, Washington, D.C.
    • Ferrieri, P. 1986. Immune responses to streptococcal infections, p. 336-341. In N. R. Rose, H. Friedman, and J. L. Fahey (ed.), Manual of clinical immunology, 3rd ed. American Society for Microbiology, Washington, D.C.
    • (1986) Manual of Clinical Immunology, 3rd Ed , pp. 336-341
    • Ferrieri, P.1
  • 5
    • 0025350533 scopus 로고
    • Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor
    • Hauser, A. R., and P. M. Schlievert. 1990. Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor. J. Bacteriol. 172:4536-4542.
    • (1990) J. Bacteriol. , vol.172 , pp. 4536-4542
    • Hauser, A.R.1    Schlievert, P.M.2
  • 6
    • 0018821876 scopus 로고
    • Extremely high titers of serum antibodies against the streptococcal exoenzyme deoxyribonuclease B
    • Hederstedt, B., S. E. Holm, and R. Norberg. 1980. Extremely high titers of serum antibodies against the streptococcal exoenzyme deoxyribonuclease B. J. Clin. Microbiol. 11:720-723.
    • (1980) J. Clin. Microbiol. , vol.11 , pp. 720-723
    • Hederstedt, B.1    Holm, S.E.2    Norberg, R.3
  • 7
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A virulence mechanism
    • Herwald, H., M. Collin, W. Muller-Esterl, and L. Björck. 1996. Streptococcal cysteine proteinase releases kinins: a virulence mechanism. J. Exp. Med. 184:665-673.
    • (1996) J. Exp. Med. , vol.184 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Muller-Esterl, W.3    Björck, L.4
  • 8
    • 0027361378 scopus 로고
    • Cloning, characterization and over-expression of a Streptococcus pyogenes gene encoding a new type of mitogenic factor
    • Iwasaki, M., H. Igarashi, Y. Hinuma, and T. Yutsuda. 1993. Cloning, characterization and over-expression of a Streptococcus pyogenes gene encoding a new type of mitogenic factor. FEMS Lett. 331:187-192.
    • (1993) FEMS Lett. , vol.331 , pp. 187-192
    • Iwasaki, M.1    Igarashi, H.2    Hinuma, Y.3    Yutsuda, T.4
  • 9
    • 0030741106 scopus 로고    scopus 로고
    • The mitogenic factor (MF) secreted from Streptococcus pyogenes is a heat-stable nuclease requiring His122 for activity
    • Iwasaki, M., H. Igarashi, and T. Yutsuda. 1997. The mitogenic factor (MF) secreted from Streptococcus pyogenes is a heat-stable nuclease requiring His122 for activity. Microbiology 143:2449-2455.
    • (1997) Microbiology , vol.143 , pp. 2449-2455
    • Iwasaki, M.1    Igarashi, H.2    Yutsuda, T.3
  • 10
    • 0031965073 scopus 로고    scopus 로고
    • Antistreptolysin O and antideoxyribonuclease B titers: Normal values for children ages 2 to 12 in the United States
    • Kaplan, E. L., C. D. Rothermel, and D. R. Johnson. 1998. Antistreptolysin O and antideoxyribonuclease B titers: normal values for children ages 2 to 12 in the United States. Pediatrics 101:86-88.
    • (1998) Pediatrics , vol.101 , pp. 86-88
    • Kaplan, E.L.1    Rothermel, C.D.2    Johnson, D.R.3
  • 11
    • 0027290733 scopus 로고
    • Cleavage of interleukin 1β(IL-1β) precursor to produce active IL-1β by a conserved extracellular cysteine protease from Streptococcus pyogenes
    • Kapur, V., M. W. Majesky, L. Ling-Ling, R. A. Black, and J. M. Musser. 1993. Cleavage of interleukin 1β(IL-1β) precursor to produce active IL-1β by a conserved extracellular cysteine protease from Streptococcus pyogenes. Proc. Natl. Acad. Sci. USA 90:7676-7680.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7676-7680
    • Kapur, V.1    Majesky, M.W.2    Ling-Ling, L.3    Black, R.A.4    Musser, J.M.5
  • 12
    • 0030761504 scopus 로고    scopus 로고
    • The superantigen streptococcal pyrogenic exotoxin C (SPE-C) exhibits a novel mode of action
    • Li, P.-L., R. E. Tiedemann, S. L. Moffat, and J. D. Fraser. 1997. The superantigen streptococcal pyrogenic exotoxin C (SPE-C) exhibits a novel mode of action. J. Exp. Med. 186:375-383.
    • (1997) J. Exp. Med. , vol.186 , pp. 375-383
    • Li, P.-L.1    Tiedemann, R.E.2    Moffat, S.L.3    Fraser, J.D.4
  • 13
    • 0027248876 scopus 로고
    • Tetanus toxin and botulinum neurotoxins a new group of zinc proteases
    • Montecucco, C., and G. Schiavo. 1993. Tetanus toxin and botulinum neurotoxins a new group of zinc proteases. Trends Biochem. Sci. 18:324-327.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 324-327
    • Montecucco, C.1    Schiavo, G.2
  • 14
    • 0030915389 scopus 로고    scopus 로고
    • Streptococcal superantigens and their role in the pathogenesis of severe infections
    • Norgren, M., and A. Eriksson. 1997. Streptococcal superantigens and their role in the pathogenesis of severe infections. J. Toxicol. Toxin Rev. 16:1-32.
    • (1997) J. Toxicol. Toxin Rev. , vol.16 , pp. 1-32
    • Norgren, M.1    Eriksson, A.2
  • 16
    • 0027943375 scopus 로고
    • Superantigenic properties of the group a streptococcal exotoxin SpeF (MF)
    • Norrby-Teglund, A., D. Newton, M. Kotb, S. E. Holm, and M. Norgren. 1994. Superantigenic properties of the group A streptococcal exotoxin SpeF (MF). Infect. Immun. 62:5227-5233.
    • (1994) Infect. Immun. , vol.62 , pp. 5227-5233
    • Norrby-Teglund, A.1    Newton, D.2    Kotb, M.3    Holm, S.E.4    Norgren, M.5
  • 17
    • 0028021477 scopus 로고
    • Relation between low capacity of human sera to inhibit streptococcal mitogens and serious manifestation of disease
    • Norrby-Teglund, A., K. Pauksens, S. E. Holm, and M. Norgren. 1994. Relation between low capacity of human sera to inhibit streptococcal mitogens and serious manifestation of disease. J. Infect. Dis. 170:585-591.
    • (1994) J. Infect. Dis. , vol.170 , pp. 585-591
    • Norrby-Teglund, A.1    Pauksens, K.2    Holm, S.E.3    Norgren, M.4
  • 18
    • 0029645282 scopus 로고
    • Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site
    • Papageorgiou, A. C., K. R. Acharya, R. Shapiro, E. F. Passalacqua, R. D. Brehm, and H. S. Tranter. 1995. Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site. Structure 3:769-779.
    • (1995) Structure , vol.3 , pp. 769-779
    • Papageorgiou, A.C.1    Acharya, K.R.2    Shapiro, R.3    Passalacqua, E.F.4    Brehm, R.D.5    Tranter, H.S.6
  • 19
    • 0029851715 scopus 로고    scopus 로고
    • Molecular characterization of a major serotype M49 group a streptococcal DNase gene (sdaD)
    • Podbielski, A., I. Zarges, A. Flosdorff, and J. Weber-Heynemann. 1996. Molecular characterization of a major serotype M49 group A streptococcal DNase gene (sdaD). Infect. Immun. 64:5349-5356.
    • (1996) Infect. Immun. , vol.64 , pp. 5349-5356
    • Podbielski, A.1    Zarges, I.2    Flosdorff, A.3    Weber-Heynemann, J.4
  • 22
    • 0017230016 scopus 로고
    • Leucine amino peptidase (bovine lens). the relative binding of cobalt and zinc to leucine amino peptidase and the effect of cobalt substitution on specific activity
    • Thompson, G. A., and F. H. Carpenter. 1976. Leucine amino peptidase (bovine lens). The relative binding of cobalt and zinc to leucine amino peptidase and the effect of cobalt substitution on specific activity. J. Biol. Chem. 251:1618-1624.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1618-1624
    • Thompson, G.A.1    Carpenter, F.H.2
  • 23
    • 0026051852 scopus 로고
    • Isolation, sequence, and expression in Escherichia coli, Bacillus subtilis, and Lactococcus lactis of the DNase (streptodornase)-encoding gene from Streptococcus equimilis H46A
    • Wolinowska, R., P. Ceglowski, J. Kok, and G. Venema. 1991. Isolation, sequence, and expression in Escherichia coli, Bacillus subtilis, and Lactococcus lactis of the DNase (streptodornase)-encoding gene from Streptococcus equimilis H46A. Gene 106:115-119.
    • (1991) Gene , vol.106 , pp. 115-119
    • Wolinowska, R.1    Ceglowski, P.2    Kok, J.3    Venema, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.