메뉴 건너뛰기




Volumn 56, Issue 3, 2005, Pages 681-695

Mutational analysis of the group A streptococcal operon encoding streptolysin S and its virulence role in invasive infection

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; M PROTEIN; STREPTOLYSIN S;

EID: 17644385827     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04583.x     Document Type: Article
Times cited : (151)

References (73)
  • 1
    • 0024271505 scopus 로고
    • Production, purification, and assay of streptolysin S
    • Alouf, J.E., and Loridan, C. (1988) Production, purification, and assay of streptolysin S. Methods Enzymol 165: 59-64.
    • (1988) Methods Enzymol , vol.165 , pp. 59-64
    • Alouf, J.E.1    Loridan, C.2
  • 2
    • 0032145096 scopus 로고    scopus 로고
    • Molecular analysis of the role of the group A streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection
    • Ashbaugh, C.D., Warren, H.B., Carey, V.J., and Wessels, M.R. (1998) Molecular analysis of the role of the group A streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection. J Clin Invest 102: 550-560.
    • (1998) J Clin Invest , vol.102 , pp. 550-560
    • Ashbaugh, C.D.1    Warren, H.B.2    Carey, V.J.3    Wessels, M.R.4
  • 3
    • 0013911340 scopus 로고
    • Disruption of wall-less bacteria by streptococcal and staphylococcal toxins
    • Bernheimer, A.W. (1966) Disruption of wall-less bacteria by streptococcal and staphylococcal toxins. J Bacteriol 91: 1677-1680.
    • (1966) J Bacteriol , vol.91 , pp. 1677-1680
    • Bernheimer, A.W.1
  • 4
    • 0014094077 scopus 로고
    • Physical behavior of streptolysin S
    • Bernheimer, A.W. (1967) Physical behavior of streptolysin S. J Bacteriol 93: 2024-2025.
    • (1967) J Bacteriol , vol.93 , pp. 2024-2025
    • Bernheimer, A.W.1
  • 5
    • 0032036480 scopus 로고    scopus 로고
    • Reduced virulence of group A streptococcal Tn916 mutants that do not produce streptolysin S
    • Betschel, S.D., Borgia, S.M., Barg, N.L., Low, D.E., and De Azavedo, J.C. (1998) Reduced virulence of group A streptococcal Tn916 mutants that do not produce streptolysin S. Infect Immun 66: 1671-1679.
    • (1998) Infect Immun , vol.66 , pp. 1671-1679
    • Betschel, S.D.1    Borgia, S.M.2    Barg, N.L.3    Low, D.E.4    De Azavedo, J.C.5
  • 6
    • 0037381631 scopus 로고    scopus 로고
    • Molecular basis of group A streptococcal virulence
    • Bisno, A.L., Brito, M.O., and Collins, C.M. (2003) Molecular basis of group A streptococcal virulence. Lancet Infect Dis 3: 191-200.
    • (2003) Lancet Infect Dis , vol.3 , pp. 191-200
    • Bisno, A.L.1    Brito, M.O.2    Collins, C.M.3
  • 7
    • 0034778929 scopus 로고    scopus 로고
    • Generation and surface localization of intact M protein in Streptococcus pyogenes are dependent on sagA
    • Biswas, I., Germon, P., McDade, K., and Scott, J.R. (2001) Generation and surface localization of intact M protein in Streptococcus pyogenes are dependent on sagA. Infect Immun 69: 7029-7038.
    • (2001) Infect Immun , vol.69 , pp. 7029-7038
    • Biswas, I.1    Germon, P.2    McDade, K.3    Scott, J.R.4
  • 8
    • 0030825160 scopus 로고    scopus 로고
    • Cloning of a chromosomal region responsible for streptolysin S production in Streptococcus pyogenes
    • Borgia, S.M., Betschel, S., Low, D.E., and de Azavedo, J.C. (1997) Cloning of a chromosomal region responsible for streptolysin S production in Streptococcus pyogenes. Adv Exp Med Biol 418: 733-736.
    • (1997) Adv Exp Med Biol , vol.418 , pp. 733-736
    • Borgia, S.M.1    Betschel, S.2    Low, D.E.3    De Azavedo, J.C.4
  • 9
    • 0023852747 scopus 로고
    • Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line
    • Boukamp, P., Petrussevska, R.T., Breitkreutz, D., Hornung, J., Markham, A., and Fusenig, N.E. (1988) Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line. J Cell Biol 106: 761-771.
    • (1988) J Cell Biol , vol.106 , pp. 761-771
    • Boukamp, P.1    Petrussevska, R.T.2    Breitkreutz, D.3    Hornung, J.4    Markham, A.5    Fusenig, N.E.6
  • 10
    • 0035834742 scopus 로고    scopus 로고
    • Similarities between complement-mediated and streptolysin S-mediated hemolysis
    • Carr, A., Sledjeski, D.D., Podbielski, A., Boyle, M.D., and Kreikemeyer, B. (2001) Similarities between complement-mediated and streptolysin S-mediated hemolysis. J Biol Chem 276: 41790-41796.
    • (2001) J Biol Chem , vol.276 , pp. 41790-41796
    • Carr, A.1    Sledjeski, D.D.2    Podbielski, A.3    Boyle, M.D.4    Kreikemeyer, B.5
  • 11
    • 0032575881 scopus 로고    scopus 로고
    • Blue/white screening of recombinant plasmids in Gram-positive bacteria by interruption of alkaline phosphatase gene (phoZ) expression
    • Chaffin, D.O., and Rubens, C.E. (1998) Blue/white screening of recombinant plasmids in Gram-positive bacteria by interruption of alkaline phosphatase gene (phoZ) expression. Gene 219: 91-99.
    • (1998) Gene , vol.219 , pp. 91-99
    • Chaffin, D.O.1    Rubens, C.E.2
  • 13
    • 0034033679 scopus 로고    scopus 로고
    • Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases
    • Chatellier, S., Ihendyane, N., Kansal, R.G., Khambaty, F., Basma, H., Norrby-Teglund, A., et al. (2000) Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases. Infect Immun 68: 3523-3534.
    • (2000) Infect Immun , vol.68 , pp. 3523-3534
    • Chatellier, S.1    Ihendyane, N.2    Kansal, R.G.3    Khambaty, F.4    Basma, H.5    Norrby-Teglund, A.6
  • 14
    • 0032444198 scopus 로고    scopus 로고
    • A globally disseminated M1 subclone of group A streptococci differs from other subclones by 70 kilobases of prophage DNA and capacity for high-frequency intracellular invasion
    • Cleary, P.P., LaPenta, D., Vessela, R., Lam, H., and Cue, D. (1998) A globally disseminated M1 subclone of group A streptococci differs from other subclones by 70 kilobases of prophage DNA and capacity for high-frequency intracellular invasion. Infect Immun 66: 5592-5597.
    • (1998) Infect Immun , vol.66 , pp. 5592-5597
    • Cleary, P.P.1    LaPenta, D.2    Vessela, R.3    Lam, H.4    Cue, D.5
  • 15
    • 0031014093 scopus 로고    scopus 로고
    • An outbreak of invasive group A streptococcal disease associated with high carriage rates of the invasive clone among school-aged children
    • Cockerill, F.R., 3rd, MacDonald, K.L., Thompson, R.L., Roberson, F., Kohner, P.C., Besser-Wiek, J., et al. (1997) An outbreak of invasive group A streptococcal disease associated with high carriage rates of the invasive clone among school-aged children. JAMA 277: 38-43.
    • (1997) JAMA , vol.277 , pp. 38-43
    • Cockerill III, F.R.1    MacDonald, K.L.2    Thompson, R.L.3    Roberson, F.4    Kohner, P.C.5    Besser-Wiek, J.6
  • 16
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M.W. (2000) Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 13: 470-511.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 17
    • 0036129905 scopus 로고    scopus 로고
    • Antibodies against a synthetic peptide of SagA neutralize the cytolytic activity of streptolysin S from group A streptococci
    • Dale, J.B., Chiang, E.Y., Hasty, D.L., and Courtney, H.S. (2002) Antibodies against a synthetic peptide of SagA neutralize the cytolytic activity of streptolysin S from group A streptococci. Infect Immun 70: 2166-2170.
    • (2002) Infect Immun , vol.70 , pp. 2166-2170
    • Dale, J.B.1    Chiang, E.Y.2    Hasty, D.L.3    Courtney, H.S.4
  • 18
    • 0029772572 scopus 로고    scopus 로고
    • Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11
    • Diep, D.B., Havarstein, L.S., and Nes, I.F. (1996) Characterization of the locus responsible for the bacteriocin production in Lactobacillus plantarum C11. J Bacteriol 178: 4472-4483.
    • (1996) J Bacteriol , vol.178 , pp. 4472-4483
    • Diep, D.B.1    Havarstein, L.S.2    Nes, I.F.3
  • 19
    • 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., Chang, J.C., Benoit, V.M., Eckmann, L., and Nizet, V. (2002) 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) 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
  • 20
    • 0034946907 scopus 로고    scopus 로고
    • Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus
    • Dorschner, R.A., Pestonjamasp, V.K., Tamakuwala, S., Ohtake, T., Rudisill, J., Nizet, V., et al. (2001) Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus. J Invest Dermatol 117: 91-97.
    • (2001) J Invest Dermatol , vol.117 , pp. 91-97
    • Dorschner, R.A.1    Pestonjamasp, V.K.2    Tamakuwala, S.3    Ohtake, T.4    Rudisill, J.5    Nizet, V.6
  • 21
    • 19044390231 scopus 로고    scopus 로고
    • Mouse skin passage of a Streptococcus pyogenes Tn917 mutant of sagA/pel restores virulence, beta-hemolysis and sagA/pel expression without altering the position or sequence of the transposon
    • Eberhard, T.H., Sledjeski, D.D., and Boyle, M.D. (2001) Mouse skin passage of a Streptococcus pyogenes Tn917 mutant of sagA/pel restores virulence, beta-hemolysis and sagA/pel expression without altering the position or sequence of the transposon. BMC Microbiol 1: 33.
    • (2001) BMC Microbiol , vol.1 , pp. 33
    • Eberhard, T.H.1    Sledjeski, D.D.2    Boyle, M.D.3
  • 22
    • 0033973453 scopus 로고    scopus 로고
    • Group A streptococci in the 1990s
    • Efstratiou, A. (2000) Group A streptococci in the 1990s. J Antimicrob Chemother 45 (Suppl.): 3-12.
    • (2000) J Antimicrob Chemother , vol.45 , Issue.SUPPL. , pp. 3-12
    • Efstratiou, A.1
  • 23
    • 0842327156 scopus 로고    scopus 로고
    • Contribution of CsrR-regulated virulence factors to the progress and outcome of murine skin infections by Streptococcus pyogenes
    • Engleberg, N.C., Heath, A., Vardaman, K., and DiRita, V.J. (2004) Contribution of CsrR-regulated virulence factors to the progress and outcome of murine skin infections by Streptococcus pyogenes. Infect Immun 72: 623-628.
    • (2004) Infect Immun , vol.72 , pp. 623-628
    • Engleberg, N.C.1    Heath, A.2    Vardaman, K.3    DiRita, V.J.4
  • 24
    • 0033053646 scopus 로고    scopus 로고
    • A response regulator that represses transcription of several virulence operons in the group A streptococcus
    • Federle, M.J., McIver, K.S., and Scott, J.R. (1999) A response regulator that represses transcription of several virulence operons in the group A streptococcus. J Bacteriol 181: 3649-3657.
    • (1999) J Bacteriol , vol.181 , pp. 3649-3657
    • Federle, M.J.1    McIver, K.S.2    Scott, J.R.3
  • 26
    • 0037635056 scopus 로고    scopus 로고
    • Combined contributions of streptolysin O and streptolysin S to virulence of serotype M5 Streptococcus pyogenes strain Manfredo
    • Fontaine, M.C., Lee, J.J., and Kehoe, M.A. (2003) Combined contributions of streptolysin O and streptolysin S to virulence of serotype M5 Streptococcus pyogenes strain Manfredo. Infect Immun 71: 3857-3865.
    • (2003) Infect Immun , vol.71 , pp. 3857-3865
    • Fontaine, M.C.1    Lee, J.J.2    Kehoe, M.A.3
  • 27
    • 0030868740 scopus 로고    scopus 로고
    • New genetic techniques for group B streptococci: High-efficiency transformation, maintenance of temperature-sensitive pWV01 plasmids, and mutagenesis with Tn917
    • Framson, P.E., Nittayajarn, A., Merry, J., Youngman, P., and Rubens, C.E. (1997) New genetic techniques for group B streptococci: high-efficiency transformation, maintenance of temperature-sensitive pWV01 plasmids, and mutagenesis with Tn917. Appl Environ Microbiol 63: 3539-3547.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3539-3547
    • Framson, P.E.1    Nittayajarn, A.2    Merry, J.3    Youngman, P.4    Rubens, C.E.5
  • 28
    • 0036785660 scopus 로고    scopus 로고
    • Discovery of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease
    • Fuller, J.D., Camus, A., Duncan, C.L., Nizet, V., Bast, D.J., Thune, R.L., et al. (2002) Discovery of a streptolysin S-associated gene cluster and its role in the pathogenesis of Streptococcus iniae disease. Infect Immu 70: 5730-5739.
    • (2002) Infect Immu , vol.70 , pp. 5730-5739
    • Fuller, J.D.1    Camus, A.2    Duncan, C.L.3    Nizet, V.4    Bast, D.J.5    Thune, R.L.6
  • 29
    • 0032909112 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin promotes injury of lung microvascular endothelial cells
    • Gibson, R.L., Nizet, V., and Rubens, C.E. (1999) Group B streptococcal beta-hemolysin promotes injury of lung microvascular endothelial cells. Pediatr Res 45: 626-634.
    • (1999) Pediatr Res , vol.45 , pp. 626-634
    • Gibson, R.L.1    Nizet, V.2    Rubens, C.E.3
  • 30
    • 0015405443 scopus 로고
    • Mechanisms of cell and tissue injury induced by group A streptococci: Relation to poststreptococcal sequelae
    • Ginsburg, I. (1972) Mechanisms of cell and tissue injury induced by group A streptococci: relation to poststreptococcal sequelae. J Infect Dis 126: 294-340.
    • (1972) J Infect Dis , vol.126 , pp. 294-340
    • Ginsburg, I.1
  • 31
    • 0033396215 scopus 로고    scopus 로고
    • Is streptolysin S of group A streptococci a virulence factor?
    • Ginsburg, I. (1999) Is streptolysin S of group A streptococci a virulence factor? APMIS 107: 1051-1059.
    • (1999) APMIS , vol.107 , pp. 1051-1059
    • Ginsburg, I.1
  • 32
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant, S.G., Jessee, J., Bloom, F.R., and Hanahan, D. (1990) Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc Natl Acad Sci USA 87: 4645-4649.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4645-4649
    • Grant, S.G.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 33
    • 0032856769 scopus 로고    scopus 로고
    • A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B
    • Heath, A., DiRita, V.J., Barg, N.L., and Engleberg, N.C. (1999) A two-component regulatory system, CsrR-CsrS, represses expression of three Streptococcus pyogenes virulence factors, hyaluronic acid capsule, streptolysin S, and pyrogenic exotoxin B. Infect Immun 67: 5298-5305.
    • (1999) Infect Immun , vol.67 , pp. 5298-5305
    • Heath, A.1    DiRita, V.J.2    Barg, N.L.3    Engleberg, N.C.4
  • 34
    • 2942554929 scopus 로고    scopus 로고
    • Localization and functional analysis of Pepl, the immunity peptide of Pep5-producing Staphylococcus epidermidis strain 5
    • Hoffmann, A., Schneider, T., Pag, U., and Sahl, H.G. (2004) Localization and functional analysis of Pepl, the immunity peptide of Pep5-producing Staphylococcus epidermidis strain 5. Appl Environ Microbiol 70: 3263-3271.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3263-3271
    • Hoffmann, A.1    Schneider, T.2    Pag, U.3    Sahl, H.G.4
  • 35
    • 0024345189 scopus 로고
    • High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stablized media
    • Holo, H., and Nes, I.F. (1989) High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stablized media. Appl Environ Microbiol 55: 3119-3123.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 3119-3123
    • Holo, H.1    Nes, I.F.2
  • 36
    • 0017372052 scopus 로고
    • Effect of streptolysin S on human and mouse T and B lymphocytes
    • Hryniewicz, W., and Pryjma, J. (1977) Effect of streptolysin S on human and mouse T and B lymphocytes. Infect Immun 16: 730-733.
    • (1977) Infect Immun , vol.16 , pp. 730-733
    • Hryniewicz, W.1    Pryjma, J.2
  • 37
    • 0037065568 scopus 로고    scopus 로고
    • Streptolysin S and necrotising infections produced by group G streptococcus
    • Humar, D., Datta, V., Bast, D.J., Beall, B., De Azavedo, J.C., and Nizet, V. (2002) Streptolysin S and necrotising infections produced by group G streptococcus. Lancet 359: 124-129.
    • (2002) Lancet , vol.359 , pp. 124-129
    • Humar, D.1    Datta, V.2    Bast, D.J.3    Beall, B.4    De Azavedo, J.C.5    Nizet, V.6
  • 38
    • 0028211139 scopus 로고
    • Elucidation of the structure of SA-FF22, a lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22
    • Jack, R.W., Carne, A., Metzger, J., Stefanovic, S., Sahl, H.G., Jung, G., and Tagg, J. (1994) Elucidation of the structure of SA-FF22, a lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22. Eur J Biochem 220: 455-462.
    • (1994) Eur J Biochem , vol.220 , pp. 455-462
    • Jack, R.W.1    Carne, A.2    Metzger, J.3    Stefanovic, S.4    Sahl, H.G.5    Jung, G.6    Tagg, J.7
  • 39
    • 0028990155 scopus 로고
    • Bacteriocins of gram-positive bacteria
    • Jack, R.W., Tagg, J.R., and Ray, B. (1995) Bacteriocins of gram-positive bacteria. Microbiol Rev 59: 171-200.
    • (1995) Microbiol Rev , vol.59 , pp. 171-200
    • Jack, R.W.1    Tagg, J.R.2    Ray, B.3
  • 40
    • 0037315055 scopus 로고    scopus 로고
    • Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX
    • Jeng, A., Sakota, V., Li, Z., Datta, V., Beall, B., and Nizet, V. (2003) Molecular genetic analysis of a group A Streptococcus operon encoding serum opacity factor and a novel fibronectin-binding protein, SfbX. J Bacteriol 185: 1208-1217.
    • (2003) J Bacteriol , vol.185 , pp. 1208-1217
    • Jeng, A.1    Sakota, V.2    Li, Z.3    Datta, V.4    Beall, B.5    Nizet, V.6
  • 41
    • 0033791996 scopus 로고    scopus 로고
    • Inverse relation between disease severity and expression of the streptococcal cysteine protease, SpeB, among clonal M1T1 isolates recovered from invasive group A streptococcal infection cases
    • Kansal, R.G., McGeer, A., Low, D.E., Norrby-Teglund, A., and Kotb, M. (2000) Inverse relation between disease severity and expression of the streptococcal cysteine protease, SpeB, among clonal M1T1 isolates recovered from invasive group A streptococcal infection cases. Infect Immun 68: 6362-6369.
    • (2000) Infect Immun , vol.68 , pp. 6362-6369
    • Kansal, R.G.1    McGeer, A.2    Low, D.E.3    Norrby-Teglund, A.4    Kotb, M.5
  • 42
    • 0000916747 scopus 로고
    • Studies on lysosomes. IV. Solubilization of enzymes during mitochondrial swelling and disruptions of lysosomes by streptolysins and other hemolytic agents
    • Keiser, H., Weissmann, G., and Bernheimer, A.W. (1964) Studies on lysosomes. IV. Solubilization of enzymes during mitochondrial swelling and disruptions of lysosomes by streptolysins and other hemolytic agents. J Cell Biol 22: 101.
    • (1964) J Cell Biol , vol.22 , pp. 101
    • Keiser, H.1    Weissmann, G.2    Bernheimer, A.W.3
  • 43
    • 0029572448 scopus 로고
    • Biological properties of a Streptococcus pyogenes mutant generated by Tn976 insertion in mga
    • Kihlberg, B.M., Cooney, J., Caparon, M.G., Olsen, A., and Bjorck, L. (1995) Biological properties of a Streptococcus pyogenes mutant generated by Tn976 insertion 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    Olsen, A.4    Bjorck, L.5
  • 45
    • 0000508182 scopus 로고
    • Biochemical studies on streptolysin S II. Properties of a polypeptide component and its role in the toxin activity
    • Koyama, J. (1963) Biochemical studies on streptolysin S II. Properties of a polypeptide component and its role in the toxin activity. J Biochem 54: 146-151.
    • (1963) J Biochem , vol.54 , pp. 146-151
    • Koyama, J.1
  • 48
    • 0028046519 scopus 로고
    • Group A streptococci efficiently invade human respiratory epithelial cells
    • LaPenta, D., Rubens, C., Chi, E., and Cleary, P.P. (1994) Group A streptococci efficiently invade human respiratory epithelial cells. Proc Natl Acad Sci USA 91: 12115-12119.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12115-12119
    • LaPenta, D.1    Rubens, C.2    Chi, E.3    Cleary, P.P.4
  • 49
    • 0026782639 scopus 로고
    • Molecular, genetic, and functional analysis of the basic replicon of pVA380-1, a plasmid of oral streptococcal origin
    • LeBlanc, D.J., Lee, L.N., and Abu-Al-Jaibat, A. (1992) Molecular, genetic, and functional analysis of the basic replicon of pVA380-1, a plasmid of oral streptococcal origin. Plasmid 28: 130-145.
    • (1992) Plasmid , vol.28 , pp. 130-145
    • LeBlanc, D.J.1    Lee, L.N.2    Abu-Al-Jaibat, A.3
  • 50
    • 0032822538 scopus 로고    scopus 로고
    • Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins
    • Li, Z., Sledjeski, D.D., Kreikemeyer, B., Podbielski, A., and Boyle, M.D. (1999) Identification of pel, a Streptococcus pyogenes locus that affects both surface and secreted proteins. J Bacteriol 181: 6019-6027.
    • (1999) J Bacteriol , vol.181 , pp. 6019-6027
    • Li, Z.1    Sledjeski, D.D.2    Kreikemeyer, B.3    Podbielski, A.4    Boyle, M.D.5
  • 51
    • 0031023072 scopus 로고    scopus 로고
    • The leader peptide is essential for the posttranslational modification of the DNA-gyrase inhibitor microcin B17
    • Madison, L.L., Vivas, E.I., Li, Y.M., Walsh, C.T., and Kolter, R. (1997) The leader peptide is essential for the posttranslational modification of the DNA-gyrase inhibitor microcin B17. Mol Microbiol 23: 161-168.
    • (1997) Mol Microbiol , vol.23 , pp. 161-168
    • Madison, L.L.1    Vivas, E.I.2    Li, Y.M.3    Walsh, C.T.4    Kolter, R.5
  • 52
    • 0026801262 scopus 로고
    • New thermosensitive plasmid for gram-positive bacteria
    • Maguin, E., Duwat, P., Hege, T., Ehrlich, D., and Gruss, A. (1992) New thermosensitive plasmid for gram-positive bacteria. J Bacteriol 174: 5633-5638.
    • (1992) J Bacteriol , vol.174 , pp. 5633-5638
    • Maguin, E.1    Duwat, P.2    Hege, T.3    Ehrlich, D.4    Gruss, A.5
  • 53
    • 0028648266 scopus 로고
    • Protective immunity to the group A Streptococcus may be only strain specific
    • de Malmanche, S.A., and Martin, D.R. (1994) Protective immunity to the group A Streptococcus may be only strain specific. Med Microbiol Immunol (Berl) 183: 299-306.
    • (1994) Med Microbiol Immunol (Berl) , vol.183 , pp. 299-306
    • De Malmanche, S.A.1    Martin, D.R.2
  • 54
    • 4444351650 scopus 로고    scopus 로고
    • Synthesis of group A streptococcal virulence factors is controlled by a regulatory RNA molecule
    • Mangold, M., Siller, M., Roppenser, B., Vlaminckx, B.J., Penfound, T.A., Klein, R., et al. (2004) Synthesis of group A streptococcal virulence factors is controlled by a regulatory RNA molecule. Mol Microbiol 53: 1515-1527.
    • (2004) Mol Microbiol , vol.53 , pp. 1515-1527
    • Mangold, M.1    Siller, M.2    Roppenser, B.3    Vlaminckx, B.J.4    Penfound, T.A.5    Klein, R.6
  • 55
    • 0032989690 scopus 로고    scopus 로고
    • Emergence and spread of a new clone of M type 1 group A Streptococcus coincident with the increase in invasive diseases in Japan
    • Murono, K., Fujita, K., Saijo, M., Hirano, Y., Zhang, J., and Murai, T. (1999) Emergence and spread of a new clone of M type 1 group A Streptococcus coincident with the increase in invasive diseases in Japan. Pediatr Infect Dis J 18: 254-257.
    • (1999) Pediatr Infect Dis J , vol.18 , pp. 254-257
    • Murono, K.1    Fujita, K.2    Saijo, M.3    Hirano, Y.4    Zhang, J.5    Murai, T.6
  • 56
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and Horton, P. (1999) PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24: 34-36.
    • (1999) Trends Biochem Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 57
    • 0036966408 scopus 로고    scopus 로고
    • Streptococcal beta-hemolysins: Genetics and role in disease pathogenesis
    • Nizet, V. (2002) Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol 10: 575-580.
    • (2002) Trends Microbiol , vol.10 , pp. 575-580
    • Nizet, V.1
  • 58
    • 0029736682 scopus 로고    scopus 로고
    • Group B streptococcal beta-hemolysin expression is associated with injury of lung epithelial cells
    • Nizet, V., Gibson, R.L., Chi, E.Y., Framson, P.E., Hulse, M., and Rubens, C.E. (1996) Group B streptococcal beta-hemolysin expression is associated with injury of lung epithelial cells. Infect Immun 64: 3818-3826.
    • (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
  • 60
    • 0035936156 scopus 로고    scopus 로고
    • Innate antimicrobial peptide protects the skin from invasive bacterial infection
    • Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R.A., et al. (2001) Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414: 454-457.
    • (2001) Nature , vol.414 , pp. 454-457
    • Nizet, V.1    Ohtake, T.2    Lauth, X.3    Trowbridge, J.4    Rudisill, J.5    Dorschner, R.A.6
  • 61
    • 0025188767 scopus 로고
    • Inability of toxin inhibitors to neutralize enhanced toxicity caused by bacteria adherent to tissue culture cells
    • Ofek, I., Zafriri, D., Goldhar, J., and Eisenstein, B.I. (1990) Inability of toxin inhibitors to neutralize enhanced toxicity caused by bacteria adherent to tissue culture cells. Infect Immun 58: 3737-3742.
    • (1990) Infect Immun , vol.58 , pp. 3737-3742
    • Ofek, I.1    Zafriri, D.2    Goldhar, J.3    Eisenstein, B.I.4
  • 62
    • 0035154927 scopus 로고    scopus 로고
    • Genetic basis for the beta-haemolytic/cytolytic activity of group B Streptococcus
    • Pritzlaff, C.A., Chang, J.C., Kuo, S.P., Tamura, G.S., Rubens, C.E., and Nizet, V. (2001) Genetic basis for the beta-haemolytic/cytolytic activity of group B Streptococcus. Mol Microbiol 39: 236-247.
    • (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
  • 63
    • 0024283925 scopus 로고
    • The nucleotide sequence of pACYC184
    • Rose, R.E. (1988) The nucleotide sequence of pACYC184. Nucleic Acids Res 16: 355.
    • (1988) Nucleic Acids Res , vol.16 , pp. 355
    • Rose, R.E.1
  • 64
    • 0027279657 scopus 로고
    • Isolation and characterization of the lantibiotic salivaricin A and its structural gene sa/A from Streptococcus salivarius 20P3
    • Ross, K.F., Ronson, C.W., and Tagg, J.R. (1993) Isolation and characterization of the lantibiotic salivaricin A and its structural gene sa/A from Streptococcus salivarius 20P3. Appl Environ Microbiol 59: 2014-2021.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2014-2021
    • Ross, K.F.1    Ronson, C.W.2    Tagg, J.R.3
  • 65
    • 0031782954 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria
    • Sahl, H.G., and Bierbaum, G. (1998) Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria. Annu Rev Microbiol 52: 41-79.
    • (1998) Annu Rev Microbiol , vol.52 , pp. 41-79
    • Sahl, H.G.1    Bierbaum, G.2
  • 67
    • 0037222981 scopus 로고    scopus 로고
    • Cytotoxic effects of streptolysin o and streptolysin s enhance the virulence of poorly encapsulated group a streptococci
    • Sierig, G., Cywes, C., Wessels, M.R., and Ashbaugh, C.D. (2003) Cytotoxic effects of streptolysin o and streptolysin s enhance the virulence of poorly encapsulated group a streptococci. Infect Immun 71: 446-455.
    • (2003) Infect Immun , vol.71 , pp. 446-455
    • Sierig, G.1    Cywes, C.2    Wessels, M.R.3    Ashbaugh, C.D.4
  • 68
    • 0025823750 scopus 로고
    • Electrotransformation of Streptococcus pyogenes with plasmid and linear DNA
    • Simon, D., and Ferretti, J.J. (1991) Electrotransformation of Streptococcus pyogenes with plasmid and linear DNA. FEMS Microbiol Lett 66: 219-224.
    • (1991) FEMS Microbiol Lett , vol.66 , pp. 219-224
    • Simon, D.1    Ferretti, J.J.2
  • 69
    • 4244092996 scopus 로고    scopus 로고
    • The flesh-eating bacterium: What's next?
    • Stevens, D.L. (1999) The flesh-eating bacterium: what's next? J Infect Dis 179 (Suppl. 2): S366-S374.
    • (1999) J Infect Dis , vol.179 , Issue.SUPPL. 2
    • Stevens, D.L.1
  • 70
    • 0013958207 scopus 로고
    • Cytolytic effect of streptolysin S complex on Ehrlich ascites tumor cells
    • Taketo, Y., and Taketo, A. (1966) Cytolytic effect of streptolysin S complex on Ehrlich ascites tumor cells. J Biochem (Tokyo) 60: 357-362.
    • (1966) J Biochem (Tokyo) , vol.60 , pp. 357-362
    • Taketo, Y.1    Taketo, A.2
  • 71
    • 0022917641 scopus 로고
    • Host/vector interactions which affect the viability of recombinant phage lambda clones
    • Wertman, K.F., Wyman, A.R., and Botstein, D. (1986) Host/vector interactions which affect the viability of recombinant phage lambda clones. Gene 49: 253-262.
    • (1986) Gene , vol.49 , pp. 253-262
    • Wertman, K.F.1    Wyman, A.R.2    Botstein, D.3
  • 72
    • 0038220969 scopus 로고    scopus 로고
    • Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes
    • Wescombe, P.A., and Tagg, J.R. (2003) Purification and characterization of streptin, a type A1 lantibiotic produced by Streptococcus pyogenes. Appl Environ Microbiol 69: 2737-2747.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 2737-2747
    • Wescombe, P.A.1    Tagg, J.R.2
  • 73
    • 0024594736 scopus 로고
    • Quantitative evaluation of Escherichia coli host strains for tolerance to cytosine methylation in plasmid and phage recombinants
    • Woodcock, D.M., Crowther, P.J., Doherty, J., Jefferson, S., DeCruz, E., Noyer-Weidner, M., et al. (1989) Quantitative evaluation of Escherichia coli host strains for tolerance to cytosine methylation in plasmid and phage recombinants. Nucleic Acids Res 17: 3469-3478.
    • (1989) Nucleic Acids Res , vol.17 , pp. 3469-3478
    • Woodcock, D.M.1    Crowther, P.J.2    Doherty, J.3    Jefferson, S.4    DeCruz, E.5    Noyer-Weidner, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.