메뉴 건너뛰기




Volumn 36, Issue 6, 2000, Pages 1306-1318

Generation of a mature streptococcal cysteine proteinase is dependent on cell wall-anchored M1 protein

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; ENZYME PRECURSOR; M PROTEIN; VIRULENCE FACTOR;

EID: 0033923852     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01942.x     Document Type: Article
Times cited : (92)

References (74)
  • 1
    • 0025372126 scopus 로고
    • Protein H - A novel IgG binding bacterial protein
    • Åkesson, P., Cooney, J., Kishimoto, F., and Björck, L. (1990) Protein H - a novel IgG binding bacterial protein. Mol Immunol 27: 523-531.
    • (1990) Mol Immunol , vol.27 , pp. 523-531
    • Åkesson, P.1    Cooney, J.2    Kishimoto, F.3    Björck, L.4
  • 2
    • 0028331996 scopus 로고
    • M1 protein and protein H: IgGFc- and albumin-binding streptococcal surface proteins encoded by adjacent genes
    • Åkesson, P., Schmidt, K.-H., Cooney, J., and Björck, L. (1994) M1 protein and protein H: IgGFc- and albumin-binding streptococcal surface proteins encoded by adjacent genes. Biochem J 300: 877-886.
    • (1994) Biochem J , vol.300 , pp. 877-886
    • Åkesson, P.1    Schmidt, K.-H.2    Cooney, J.3    Björck, L.4
  • 3
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A.J., and Kirschke, H. (1981) Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol 80: 535-561.
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 4
    • 0028831866 scopus 로고
    • Human kininogens interact with M protein, a bacterial surface protein and virulence determinant
    • Ben Nasr, A., Herwald, H., Müller-Esterl, W., and Björck, L. (1995) Human kininogens interact with M protein, a bacterial surface protein and virulence determinant. Biochem J 305: 173-180.
    • (1995) Biochem J , vol.305 , pp. 173-180
    • Ben Nasr, A.1    Herwald, H.2    Müller-Esterl, W.3    Björck, L.4
  • 5
    • 0028941597 scopus 로고
    • Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
    • Berge, A., and Björck, L. (1995) Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins. J Biol Chem 270: 9862-9867.
    • (1995) J Biol Chem , vol.270 , pp. 9862-9867
    • Berge, A.1    Björck, L.2
  • 6
    • 0027451350 scopus 로고
    • PAM, a novel plasminogen-binding protein from streptococcus pyogenes
    • Berge, A., and Sjöbring, U. (1993) PAM, a novel plasminogen-binding protein from Streptococcus pyogenes. J Biol Chem 268: 25417-25424.
    • (1993) J Biol Chem , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjöbring, U.2
  • 7
    • 0030878839 scopus 로고    scopus 로고
    • Streptococcal protein H forms soluble complement-activating complexes with IgG, but inhibits complement activation by IgG-coated targets
    • Berge, A., Kihlberg, B.-M., Sjöholm, A.G., and Björck, L. (1997) Streptococcal protein H forms soluble complement-activating complexes with IgG, but inhibits complement activation by IgG-coated targets. J Biol Chem 272: 20774-20781.
    • (1997) J Biol Chem , vol.272 , pp. 20774-20781
    • Berge, A.1    Kihlberg, B.-M.2    Sjöholm, A.G.3    Björck, L.4
  • 8
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnbiom, H.C., and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7: 1513-1523.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnbiom, H.C.1    Doly, J.2
  • 9
    • 0030034479 scopus 로고    scopus 로고
    • Streptococcal infection of skin and soft tissue
    • Bisno, A.L., and Stevens, D.L. (1996) Streptococcal infection of skin and soft tissue. N Engl J Med 334: 240-245.
    • (1996) N Engl J Med , vol.334 , pp. 240-245
    • Bisno, A.L.1    Stevens, D.L.2
  • 10
    • 0024546648 scopus 로고
    • Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor
    • Björck, L., Åkesson, P., Bonus, M., Trojnar, J., Abrahamson, M., Olafsson, I., et al. (1989) Bacterial growth blocked by a synthetic peptide based on the structure of a human proteinase inhibitor. Nature 337: 385-386.
    • (1989) Nature , vol.337 , pp. 385-386
    • Björck, L.1    Åkesson, P.2    Bonus, M.3    Trojnar, J.4    Abrahamson, M.5    Olafsson, I.6
  • 11
    • 10244261522 scopus 로고    scopus 로고
    • Activation of a 66-kDa human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine proteinase
    • Burns, E.H., Marciel, A.M., and Musser, J.M. (1996) Activation of a 66-kDa human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine proteinase. Infect Immun 64: 4744-4750.
    • (1996) Infect Immun , vol.64 , pp. 4744-4750
    • Burns, E.H.1    Marciel, A.M.2    Musser, J.M.3
  • 12
    • 0023571164 scopus 로고
    • Identification of a gene that regulates expression of M protein, the major virulence determinant of group A Streptococci
    • Caparon, M.G., and Scott, J.R. (1987) Identification of a gene that regulates expression of M protein, the major virulence determinant of group A Streptococci. Proc Natl Acad Sci USA 84: 8677-8681.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8677-8681
    • Caparon, M.G.1    Scott, J.R.2
  • 13
    • 0028839780 scopus 로고
    • Allosteric and temperature effects on the plasma protein binding by streptococcal M protein family members
    • Cedervall, T., Åkesson, P., Stenberg, L., Herrmann, A., and Åkerström, B. (1995) Allosteric and temperature effects on the plasma protein binding by streptococcal M protein family members. Scand J Immunol 42: 433-441.
    • (1995) Scand J Immunol , vol.42 , pp. 433-441
    • Cedervall, T.1    Åkesson, P.2    Stenberg, L.3    Herrmann, A.4    Åkerström, B.5
  • 14
    • 0030948560 scopus 로고    scopus 로고
    • Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion
    • Chaussee, M.S., Phillips, E.R., and Ferretti, J.J. (1997) Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion. Infect Immun 65: 1956-1959.
    • (1997) Infect Immun , vol.65 , pp. 1956-1959
    • Chaussee, M.S.1    Phillips, E.R.2    Ferretti, J.J.3
  • 15
    • 0028265857 scopus 로고
    • Group A streptococcal immunoglobulin-binding proteins: Adhesins, molecular mimicry or sensory proteins?
    • Cleary, P., and Retnoningrum, D. (1994) Group A streptococcal immunoglobulin-binding proteins: adhesins, molecular mimicry or sensory proteins? Trends Microbiol 2: 131-136.
    • (1994) Trends Microbiol , vol.2 , pp. 131-136
    • Cleary, P.1    Retnoningrum, D.2
  • 16
    • 0027327055 scopus 로고
    • The serotypes of Streptococcus pyogenes present in Britain during 1980-90 and their association with disease
    • Colman, G., Tanna, A., Efstratiou, A., and Gaworzewska, E.T. (1993) The serotypes of Streptococcus pyogenes present in Britain during 1980-90 and their association with disease. J Med Microbiol 39: 165-178.
    • (1993) J Med Microbiol , vol.39 , pp. 165-178
    • Colman, G.1    Tanna, A.2    Efstratiou, A.3    Gaworzewska, E.T.4
  • 17
    • 0031686023 scopus 로고    scopus 로고
    • Streptococcus pyogenes serotype M1 encodes multiple pathways for entry into human epithelial cells
    • Cue, D., Dombek, P.E., Lam, H., and Cleary, P.P. (1998) Streptococcus pyogenes serotype M1 encodes multiple pathways for entry into human epithelial cells. Infect Immun 66: 4593-4601.
    • (1998) Infect Immun , vol.66 , pp. 4593-4601
    • Cue, D.1    Dombek, P.E.2    Lam, H.3    Cleary, P.P.4
  • 18
    • 0032904116 scopus 로고    scopus 로고
    • High-frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements
    • Dombek, P.E., Cue, D., Sedgewick, J., Lam, H., Ruschkowski, S., Finlay, B.B., et al. (1999) High-frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements. Mol Microbiol 31: 859-870.
    • (1999) Mol Microbiol , vol.31 , pp. 859-870
    • Dombek, P.E.1    Cue, D.2    Sedgewick, J.3    Lam, H.4    Ruschkowski, S.5    Finlay, B.B.6
  • 19
    • 0033168439 scopus 로고    scopus 로고
    • Autocatalytic processing of the streptococcal cysteine protease zymogen: Processing mechanism and characterization of the autoproteolytic cleavage sites
    • Doran, J.D., Nomizu, M., Takebe, S., Menard, R., Griffith, D., and Ziomek, E. (1999) Autocatalytic processing of the streptococcal cysteine protease zymogen: processing mechanism and characterization of the autoproteolytic cleavage sites. Eur J Biochem 263: 145-151.
    • (1999) Eur J Biochem , vol.263 , pp. 145-151
    • Doran, J.D.1    Nomizu, M.2    Takebe, S.3    Menard, R.4    Griffith, D.5    Ziomek, E.6
  • 20
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman, P., and Begg, G. (1967) A protein sequenator. Eur J Biochem 1: 80-91.
    • (1967) Eur J Biochem , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 21
    • 0001322321 scopus 로고
    • A proteolytic enzyme produced by group A streptococci with special reference to its effect on the type-specific M antigen
    • Elliott, 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
    • Elliott, S.D.1
  • 22
    • 0000647519 scopus 로고
    • An inactive precursor of streptococcal proteinase
    • Elliott, S.D., and Dole, V.P. (1947) An inactive precursor of streptococcal proteinase. J Exp Med 85: 305-320.
    • (1947) J Exp Med , vol.85 , pp. 305-320
    • Elliott, S.D.1    Dole, V.P.2
  • 23
    • 0025937405 scopus 로고
    • A simple preparative procedure to extract and purify protein G from group G streptococci
    • Faulmann, E.L., and Boyle, M.D. (1991) A simple preparative procedure to extract and purify protein G from group G streptococci. Prep Biochem 21: 75-86.
    • (1991) Prep Biochem , vol.21 , pp. 75-86
    • Faulmann, E.L.1    Boyle, M.D.2
  • 24
    • 0024412074 scopus 로고
    • Streptococcal M protein: Molecular design and biological behavior
    • Fischetti, V.A. (1989) Streptococcal M protein: molecular design and biological behavior. Clin Microbiol Rev 2: 285-314.
    • (1989) Clin Microbiol Rev , vol.2 , pp. 285-314
    • Fischetti, V.A.1
  • 25
    • 0025077034 scopus 로고
    • Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram-positive cocci
    • Fischetti, V.A., Pancholi, V., and Schneewind, O. (1990) Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram-positive cocci. Mol Microbiol 4: 1603-1605.
    • (1990) Mol Microbiol , vol.4 , pp. 1603-1605
    • Fischetti, V.A.1    Pancholi, V.2    Schneewind, O.3
  • 26
    • 0029030848 scopus 로고
    • Protein H- a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains
    • Frick, I.-M., Crossin, K.L., Edelman, G.E., and Björck, L. (1995) Protein H- a bacterial surface protein with affinity for both immunoglobulin and fibronectin type III domains. EMBO J 14: 1674-1679.
    • (1995) EMBO J , vol.14 , pp. 1674-1679
    • Frick, I.-M.1    Crossin, K.L.2    Edelman, G.E.3    Björck, L.4
  • 27
    • 0021016755 scopus 로고
    • Isolation and characterization of erythrogenic toxins V. Communication: Identity of erythrogenic toxin type B and streptococcal proteinase precursor
    • Gerlach, D., Knöll, H., Köhler, W., Ozegowski, J.-H., and Hribalova, V. (1983) Isolation and characterization of erythrogenic toxins V. Communication: identity of erythrogenic toxin type B and streptococcal proteinase precursor. Zbl Bakt Hyg, I Abt Orig A 225: 221-233.
    • (1983) Zbl Bakt Hyg, I Abt Orig A , vol.225 , pp. 221-233
    • Gerlach, D.1    Knöll, H.2    Köhler, W.3    Ozegowski, J.-H.4    Hribalova, V.5
  • 28
    • 0000925011 scopus 로고
    • Analysis of protein conformation by gel electrophoresis
    • Creighton, T.E. (ed.). Oxford: IRL Press
    • Goldenberg, D.P. (1989) Analysis of protein conformation by gel electrophoresis. In Protein Structure: a Practical Approach. Creighton, T.E. (ed.). Oxford: IRL Press, pp. 225-250.
    • (1989) Protein Structure: A Practical Approach , pp. 225-250
    • Goldenberg, D.P.1
  • 29
    • 0025334854 scopus 로고
    • The gene sequence and some properties of protein H - A novel IgG binding protein
    • Gomi, H., Hozumi, T., Hattori, S., Tagawa, C., Kishimoto, F., and Björck, L. (1990) The gene sequence and some properties of protein H - a novel IgG binding protein. J Immunol 144: 4046-4052.
    • (1990) J Immunol , vol.144 , pp. 4046-4052
    • Gomi, H.1    Hozumi, T.2    Hattori, S.3    Tagawa, C.4    Kishimoto, F.5    Björck, L.6
  • 30
    • 0031930829 scopus 로고    scopus 로고
    • Expression and characterization of group A streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes
    • Gubba, S., Low, D.E., and Musser, J.M. (1998) Expression and characterization of group A streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes. Infect Immun 66: 765-770.
    • (1998) Infect Immun , vol.66 , pp. 765-770
    • Gubba, S.1    Low, D.E.2    Musser, J.M.3
  • 31
    • 0025832204 scopus 로고
    • Lactococcal proteinase maturation protein PrtM is a lipoprotein
    • Haandrikman, A.J., Kok, J., and Venema, G. (1991) Lactococcal proteinase maturation protein PrtM is a lipoprotein. J Bacteriol 173: 4517-4525.
    • (1991) J Bacteriol , vol.173 , pp. 4517-4525
    • Haandrikman, A.J.1    Kok, J.2    Venema, G.3
  • 32
    • 0027067804 scopus 로고
    • Bradykinin receptors: Pharmacological properties and biological roles
    • Hall, J.M. (1992) Bradykinin receptors: pharmacological properties and biological roles. Pharmacol Ther 56: 131-190.
    • (1992) Pharmacol Ther , vol.56 , pp. 131-190
    • Hall, J.M.1
  • 34
    • 0027281174 scopus 로고
    • Nucleotide substitutions and small-scale insertion produce size and antigenic variation in group A streptococcal M1 protein
    • Harbaugh, M.P., Podbielski, A., Hügl, S., and Cleary, P.P. (1993) Nucleotide substitutions and small-scale insertion produce size and antigenic variation in group A streptococcal M1 protein. Mol Microbiol 8: 981-991.
    • (1993) Mol Microbiol , vol.8 , pp. 981-991
    • Harbaugh, M.P.1    Podbielski, A.2    Hügl, S.3    Cleary, P.P.4
  • 35
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988) Antibodies: a Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 36
    • 0025350533 scopus 로고
    • Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and streptococcal proteinase precursor
    • Hauser, A.R., and Schlievert, P.M. (1990) Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and streptococcal proteinase precursor. J Bacteriol 172: 4536-4542.
    • (1990) J Bacteriol , vol.172 , pp. 4536-4542
    • Hauser, A.R.1    Schlievert, P.M.2
  • 37
    • 0029788388 scopus 로고    scopus 로고
    • Streptococcal cysteine proteinase releases kinins: A novel virulence mechanism
    • Herwald, H., Collin, M., Müller-Esterl, W., and Björck, L. (1996) Streptococcal cysteine proteinase releases kinins: a novel virulence mechanism. J Exp Med 184: 665-673.
    • (1996) J Exp Med , vol.184 , pp. 665-673
    • Herwald, H.1    Collin, M.2    Müller-Esterl, W.3    Björck, L.4
  • 38
    • 0343017792 scopus 로고
    • Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H
    • Horstmann, R.D., Sievertsen, H.J., Knobloch, J., and Fischetti, V.A. (1988) Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H. Proc Natl Acad Sci USA 85: 1657-1661.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1657-1661
    • Horstmann, R.D.1    Sievertsen, H.J.2    Knobloch, J.3    Fischetti, V.A.4
  • 39
    • 0002431274 scopus 로고
    • Radioimmunoassay
    • Weir, D.M. (ed.). Oxford: Blackwell Scientific Publications
    • Hunter, W.M. (1978) Radioimmunoassay In Handbook of Experimental Immunology. Weir, D.M. (ed.). Oxford: Blackwell Scientific Publications, pp. 14.1-14.40.
    • (1978) Handbook of Experimental Immunology , pp. 141-1440
    • Hunter, W.M.1
  • 40
    • 0022643093 scopus 로고
    • Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution
    • James, M.N.G., and Sielecki, A.R. (1986) Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution. Nature 319: 33-38.
    • (1986) Nature , vol.319 , pp. 33-38
    • James, M.N.G.1    Sielecki, A.R.2
  • 41
    • 0030267784 scopus 로고    scopus 로고
    • A highly variable region in members of the streptococcal M protein family binds the human complement regulator C4BP
    • Johnsson, E., Thern, A., Dahlbäck, B., Hedén, L.-O., Wikström, M., and Lindahl, G. (1996) A highly variable region in members of the streptococcal M protein family binds the human complement regulator C4BP. J Immunol 157: 3021-3029.
    • (1996) J Immunol , vol.157 , pp. 3021-3029
    • Johnsson, E.1    Thern, A.2    Dahlbäck, B.3    Hedén, L.-O.4    Wikström, M.5    Lindahl, G.6
  • 42
    • 0034058370 scopus 로고    scopus 로고
    • Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: An integrin-binding cysteine protease
    • Kagawa, T.F., Cooney, J.C., Baker, H.M., McSweeney, S., Liu, M., Gubba, S., et al. (2000) Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: an integrin-binding cysteine protease. Proc Natl Acad Sci USA 97: 2235-2240.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2235-2240
    • Kagawa, T.F.1    Cooney, J.C.2    Baker, H.M.3    McSweeney, S.4    Liu, M.5    Gubba, S.6
  • 43
    • 78651183624 scopus 로고
    • Fibrinogen precipitation by streptococcal M protein
    • Kantor, F.S. (1965) Fibrinogen precipitation by streptococcal M protein. J Exp Med 121: 849-859.
    • (1965) J Exp Med , vol.121 , pp. 849-859
    • Kantor, F.S.1
  • 44
    • 0027893017 scopus 로고
    • A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin
    • Kapur, V., Topouzis, S., Majesky, M.W., Li, L.-L., Hamrick, M.R., Hamill, R.J., et al. (1993a) A conserved Streptococcus pyogenes extracellular cysteine protease cleaves human fibronectin and degrades vitronectin. Microb Pathog 15: 327-346.
    • (1993) Microb Pathog , vol.15 , pp. 327-346
    • Kapur, V.1    Topouzis, S.2    Majesky, M.W.3    Li, L.-L.4    Hamrick, M.R.5    Hamill, R.J.6
  • 45
    • 0027290733 scopus 로고
    • Cleavage of interleukin 1β (IL-1β) precursor to produce active IL-1β by a conserved extracellular cysteine proteinase from Streptococcus pyogenes
    • Kapur, V., Malesky, M.W., Li, L.-L., Black, R.A., and Musser, J.M. (1993b) Cleavage of interleukin 1β (IL-1β) precursor to produce active IL-1β by a conserved extracellular cysteine proteinase 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    Malesky, M.W.2    Li, L.-L.3    Black, R.A.4    Musser, J.M.5
  • 46
    • 0027931766 scopus 로고
    • Vaccination with streptococcal extracellular cysteine proteinase (interleukin-1β convertase) protects mice against challenge with heterologous group A streptococci
    • Kapur, V., Maffei, J.T., Greer, R., Li, L.-L., Adams, G.J., and Musser, J.M. (1994) Vaccination with streptococcal extracellular cysteine proteinase (interleukin-1β convertase) protects mice against challenge with heterologous group A streptococci. Microb Pathog 16: 443-450.
    • (1994) Microb Pathog , vol.16 , pp. 443-450
    • Kapur, V.1    Maffei, J.T.2    Greer, R.3    Li, L.-L.4    Adams, G.J.5    Musser, J.M.6
  • 47
    • 77956818241 scopus 로고
    • Cell-wall-associated proteins in Gram-positive bacteria
    • Ghuysen, J.-M., and Hakenbeck, R. (eds). Amsterdam: Elsevier Science
    • Kehoe, M.A. (1994) Cell-wall-associated proteins in Gram-positive bacteria. In Bacterial Cell Wall. 27. Ghuysen, J.-M., and Hakenbeck, R. (eds). Amsterdam: Elsevier Science, pp. 217-261.
    • (1994) Bacterial Cell Wall , vol.27 , pp. 217-261
    • Kehoe, M.A.1
  • 48
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan, A.R., and James, M.N. (1998) Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci 7: 815-836.
    • (1998) Protein Sci , vol.7 , pp. 815-836
    • Khan, A.R.1    James, M.N.2
  • 49
    • 0029572448 scopus 로고
    • Biological properties of a streptococcus pyogenes generated by Tn916 insertions in mga
    • Kihlberg, B.-M., Cooney, J., Caparon, M.G., Olsén, A., and Björck, L. (1995) Biological properties of a Streptococcus pyogenes generated by Tn916 insertions in mga. Microb Pathog 19: 299-315.
    • (1995) Microb Pathog , vol.19 , pp. 299-315
    • Kihlberg, B.-M.1    Cooney, J.2    Caparon, M.G.3    Olsén, A.4    Björck, L.5
  • 50
    • 0032055570 scopus 로고    scopus 로고
    • Identification of a domain in human factor H and factor H-like protein-1 required for the interaction with streptococcal M proteins
    • Kotarsky, H., Hellwage, J., Johnsson, E., Skerka, C., Svensson, H.G., Lindahl, G., et al. (1998) Identification of a domain in human factor H and factor H-like protein-1 required for the interaction with streptococcal M proteins. J Immunol 160: 3349-3354.
    • (1998) J Immunol , vol.160 , pp. 3349-3354
    • Kotarsky, H.1    Hellwage, J.2    Johnsson, E.3    Skerka, C.4    Svensson, H.G.5    Lindahl, G.6
  • 51
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 52
    • 0024449598 scopus 로고
    • Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro
    • Lecker, S., Lill, R., Ziegelhoffer, T., Georgopoulos, C., Bassford, P.J., Jr, Kumamoto, C.A., et al. (1989) Three pure chaperone proteins of Escherichia coli-SecB, trigger factor and GroEL-form soluble complexes with precursor proteins in vitro. EMBO J 8: 2703-2709.
    • (1989) EMBO J , vol.8 , pp. 2703-2709
    • Lecker, S.1    Lill, R.2    Ziegelhoffer, T.3    Georgopoulos, C.4    Bassford P.J., Jr.5    Kumamoto, C.A.6
  • 53
    • 0000686715 scopus 로고
    • Streptococcal proteinase: The zymogen to enzyme transformation
    • Liu, T.-Y., and Elliott, S.D. (1965) Streptococcal proteinase: the zymogen to enzyme transformation. J Biol Chem 240: 1138-1142.
    • (1965) J Biol Chem , vol.240 , pp. 1138-1142
    • Liu, T.-Y.1    Elliott, S.D.2
  • 54
    • 0030960001 scopus 로고    scopus 로고
    • Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains
    • Lukomski, S., Sreevatsan, S., Amberg, A., Reichardt, W., Woischnik, M., Podbielski, A., et al. (1997) Inactivation of Streptococcus pyogenes extracellular cysteine protease significantly decreases mouse lethality of serotype M3 and M49 strains. J Clin Invest 99: 2574-2580.
    • (1997) J Clin Invest , vol.99 , pp. 2574-2580
    • Lukomski, S.1    Sreevatsan, S.2    Amberg, A.3    Reichardt, W.4    Woischnik, M.5    Podbielski, A.6
  • 55
    • 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., Burns, E.H. Jr, Wyde, P.R., Podbielski, A., Rurangirwa, J., Moore-Poveda, D.K., et al. (1998) 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) Infect Immun , vol.66 , pp. 771-776
    • Lukomski, S.1    Burns E.H., Jr.2    Wyde, P.R.3    Podbielski, A.4    Rurangirwa, J.5    Moore-Poveda, D.K.6
  • 56
    • 0033042528 scopus 로고    scopus 로고
    • Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice
    • Lukomski, S., Montgomery, C.A., Rurangirwa, J., Geske, R.S., Barrish, J.P., Adams, G.J., et al. (1999) Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice. Infect Immun 67: 1779-1788.
    • (1999) Infect Immun , vol.67 , pp. 1779-1788
    • Lukomski, S.1    Montgomery, C.A.2    Rurangirwa, J.3    Geske, R.S.4    Barrish, J.P.5    Adams, G.J.6
  • 57
    • 0032476656 scopus 로고    scopus 로고
    • A role for Trigger Factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W.R., Gibson, C.M., and Caparon, M.G. (1998) A role for Trigger Factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J 17: 6263-6275.
    • (1998) EMBO J , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 58
    • 0032785373 scopus 로고    scopus 로고
    • Fibrinogen cleavage by the Streptococcus pyogenes extracellular cysteine protease and generation of antibodies that inhibit enzyme proteolytic activity
    • Matsuka, Y.V., Pillai, S., Gubba, S., Musser, J.M., and Olmsted, S.B. (1999) Fibrinogen cleavage by the Streptococcus pyogenes extracellular cysteine protease and generation of antibodies that inhibit enzyme proteolytic activity. Infect Immun 67: 4326-4333.
    • (1999) Infect Immun , vol.67 , pp. 4326-4333
    • Matsuka, Y.V.1    Pillai, S.2    Gubba, S.3    Musser, J.M.4    Olmsted, S.B.5
  • 59
    • 0030753825 scopus 로고    scopus 로고
    • Role of mga in growth phase regulation of virulence genes of the group A streptococcus
    • McIver, K.S., and Scott, J.R. (1997) Role of mga in growth phase regulation of virulence genes of the group A streptococcus. J Bacteriol 179: 5178-5187.
    • (1997) J Bacteriol , vol.179 , pp. 5178-5187
    • McIver, K.S.1    Scott, J.R.2
  • 60
    • 0031147637 scopus 로고    scopus 로고
    • Streptococcal superantigen, mitogenic factor, and pyrogenic exotoxin B expressed by Streptococcus pyogenes. Structure and function
    • Musser, J.M. (1997) Streptococcal superantigen, mitogenic factor, and pyrogenic exotoxin B expressed by Streptococcus pyogenes. Structure and function. Prep Biochem Biotechnol 27: 143-172.
    • (1997) Prep Biochem Biotechnol , vol.27 , pp. 143-172
    • Musser, J.M.1
  • 61
    • 0029889570 scopus 로고    scopus 로고
    • Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes cysteine proteinase (interleukin 1β convertase) alters proteolytic activity and ablates zymogen processing
    • Musser, J.M., Stockbauer, K., Kapur, V., and Rudgers, G.W. (1996) Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes cysteine proteinase (interleukin 1β convertase) alters proteolytic activity and ablates zymogen processing. Infect Immun 64: 1913-1917.
    • (1996) Infect Immun , vol.64 , pp. 1913-1917
    • Musser, J.M.1    Stockbauer, K.2    Kapur, V.3    Rudgers, G.W.4
  • 62
    • 0026479070 scopus 로고
    • A non radioactive biochemical characterization of membrane proteins using enhanced chemiluminescence
    • Nesbitt, S.A., and Horton, M.A. (1992) A non radioactive biochemical characterization of membrane proteins using enhanced chemiluminescence. Anal Biochem 206: 267-272.
    • (1992) Anal Biochem , vol.206 , pp. 267-272
    • Nesbitt, S.A.1    Horton, M.A.2
  • 63
    • 0028229883 scopus 로고
    • Flesh-eating bacteria: Not new, but still worrisome
    • Nowak, R. (1994) Flesh-eating bacteria: not new, but still worrisome. Science 264: 1655.
    • (1994) Science , vol.264 , pp. 1655
    • Nowak, R.1
  • 64
    • 0030476579 scopus 로고    scopus 로고
    • What is the size of the group A streptococcal vir regulon? the Mga regulator affects expression of secreted and surface virulence factors
    • Podbielski, A., Woischnik, M., Pohl, B., and Schmidt, K.H. (1996a) What is the size of the group A streptococcal vir regulon? The Mga regulator affects expression of secreted and surface virulence factors. Med Microbiol Immunol 185: 171-181.
    • (1996) Med Microbiol Immunol , vol.185 , pp. 171-181
    • Podbielski, A.1    Woischnik, M.2    Pohl, B.3    Schmidt, K.H.4
  • 65
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., Spellerberg, B., Woischnik, M., Pohl, B., and Lütticken, R. (1996b) Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177: 137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lütticken, R.5
  • 66
    • 0028308484 scopus 로고
    • Type M12 protein from Streptococcus pyogenes is a receptor for immunoglobulin G3 and human albumin
    • Retnoningrum, D.S., Podbielski, A., and Cleary, P.P. (1993) Type M12 protein from Streptococcus pyogenes is a receptor for immunoglobulin G3 and human albumin. Infect Immun 62: 2387-2394.
    • (1993) Infect Immun , vol.62 , pp. 2387-2394
    • Retnoningrum, D.S.1    Podbielski, A.2    Cleary, P.P.3
  • 68
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller, G., Rucknagel, K.P., Nierhaus, K.H., Schmid, F.X., Fischer, G., and Rahfeld, J.U. (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J 14: 4939-4948.
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rucknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 69
    • 0017226398 scopus 로고
    • Primary structure of streptococcal proteinase
    • Tai, J.Y., Kortt, A.A., Liu, T.-Y., and Elliott, S.D. (1976) Primary structure of streptococcal proteinase. J Biol Chem 251: 1955-1959.
    • (1976) J Biol Chem , vol.251 , pp. 1955-1959
    • Tai, J.Y.1    Kortt, A.A.2    Liu, T.-Y.3    Elliott, S.D.4
  • 70
    • 0027288421 scopus 로고
    • Association of phenotypic and genotypic characteristics of invasive Streptococcus pyogenes isolates with clinical components of streptococcal toxic shock syndrome
    • Talkington, D.F.B.S., Black, C.M., Todd, J.K.J.E., Breiman, R.F., and Facklam, R.R. (1993) Association of phenotypic and genotypic characteristics of invasive Streptococcus pyogenes isolates with clinical components of streptococcal toxic shock syndrome. Infect Immun 61: 3369-3374.
    • (1993) Infect Immun , vol.61 , pp. 3369-3374
    • Talkington, D.F.B.S.1    Black, C.M.2    Todd, J.K.J.E.3    Breiman, R.F.4    Facklam, R.R.5
  • 71
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 72
    • 0032037719 scopus 로고    scopus 로고
    • Effect of group A streptococcal cysteine proteinase on invasion of epithelial cells
    • Tsai, P.-J., Kuo, C.-F., Lin, K.-Y., Lin, Y.-S., Lei, H.-Y., Chen, F.-F., et al. (1998) Effect of group A streptococcal cysteine proteinase on invasion of epithelial cells. Infect Immun 66: 1460-1466.
    • (1998) Infect Immun , vol.66 , pp. 1460-1466
    • Tsai, P.-J.1    Kuo, C.-F.2    Lin, K.-Y.3    Lin, Y.-S.4    Lei, H.-Y.5    Chen, F.-F.6
  • 73
    • 0024538493 scopus 로고
    • A maturation protein is essential for production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope
    • Vos, P., van Asseldonk, M., van Jeveren, F., Siezen, R., Simons, G., and de Vos, W.M. (1989) A maturation protein is essential for production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope. J Bacteriol 171: 2795-2802.
    • (1989) J Bacteriol , vol.171 , pp. 2795-2802
    • Vos, P.1    Van Asseldonk, M.2    Van Jeveren, F.3    Siezen, R.4    Simons, G.5    De Vos, W.M.6
  • 74
    • 0020052104 scopus 로고
    • Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci
    • Whitnack, E., and Beachey, E.H. (1982) Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci. J Clin Invest 69: 1042-1045.
    • (1982) J Clin Invest , vol.69 , pp. 1042-1045
    • Whitnack, E.1    Beachey, E.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.