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Volumn 182, Issue 2, 2000, Pages 195-205

Thiol-activated cytolysins: Structure, function and role in pathogenesis

Author keywords

Pathogenesis; Pore formation; Structure; Thiol activation; Toxin

Indexed keywords

BACTERIAL TOXIN; CYTOKINE; CYTOLYSIN; THIOL; VIRULENCE FACTOR;

EID: 0033986813     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00536-4     Document Type: Short Survey
Times cited : (112)

References (56)
  • 1
    • 0019256456 scopus 로고
    • Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin)
    • Alouf J.E. Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol. Ther. 11:1980;661-717.
    • (1980) Pharmacol. Ther. , vol.11 , pp. 661-717
    • Alouf, J.E.1
  • 4
    • 0026587933 scopus 로고
    • Molecular determinants of Listeria monocytogenes pathogenesis
    • Portnoy D.A., Chakraborty T., Goebel W., Cossart P. Molecular determinants of Listeria monocytogenes pathogenesis. Infect. Immun. 60:1992;1263-1267.
    • (1992) Infect. Immun. , vol.60 , pp. 1263-1267
    • Portnoy, D.A.1    Chakraborty, T.2    Goebel, W.3    Cossart, P.4
  • 5
    • 0033003586 scopus 로고    scopus 로고
    • An Arcanobacterium (Actinomyces) pyogenes mutant deficient in production of the pore-forming cytolysin pyolysin has reduced virulence
    • Jost B.H., Songer J.G., Billington S.J. An Arcanobacterium (Actinomyces) pyogenes mutant deficient in production of the pore-forming cytolysin pyolysin has reduced virulence. Infect. Immun. 67:1999;1723-1728.
    • (1999) Infect. Immun. , vol.67 , pp. 1723-1728
    • Jost, B.H.1    Songer, J.G.2    Billington, S.J.3
  • 6
    • 0028945951 scopus 로고
    • Virulence studies on the chromosomal α-toxin and θ-toxin mutants constructed by allelic exchange provide genetic evidence for the essential role of α-toxin in Clostridium perfringens-mediated gas gangrene
    • Awad M.M., Bryant A.E., Stevens D.L., Rood J.I. Virulence studies on the chromosomal α-toxin and θ-toxin mutants constructed by allelic exchange provide genetic evidence for the essential role of α-toxin in Clostridium perfringens-mediated gas gangrene. Mol. Microbiol. 15:1995;191-202.
    • (1995) Mol. Microbiol. , vol.15 , pp. 191-202
    • Awad, M.M.1    Bryant, A.E.2    Stevens, D.L.3    Rood, J.I.4
  • 7
    • 0032785378 scopus 로고    scopus 로고
    • Use of genetically manipulated strains of Clostridium perfringens reveals that both alpha-toxin and theta-toxin are required for vascular leukostasis to occur in experimental gas gangrene
    • Ellemor D.M., Baird R.N., Awad M.M., Boyd R.L., Rood J.I., Emmins J.J. Use of genetically manipulated strains of Clostridium perfringens reveals that both alpha-toxin and theta-toxin are required for vascular leukostasis to occur in experimental gas gangrene. Infect. Immun. 67:1999;4902-4907.
    • (1999) Infect. Immun. , vol.67 , pp. 4902-4907
    • Ellemor, D.M.1    Baird, R.N.2    Awad, M.M.3    Boyd, R.L.4    Rood, J.I.5    Emmins, J.J.6
  • 8
    • 0029917088 scopus 로고    scopus 로고
    • The contribution of pneumolysin to the pathogenicity of Streptococcus pneumoniae
    • Paton J.C. The contribution of pneumolysin to the pathogenicity of Streptococcus pneumoniae. Trends Microbiol. 4:1996;103-106.
    • (1996) Trends Microbiol. , vol.4 , pp. 103-106
    • Paton, J.C.1
  • 9
    • 0027717232 scopus 로고
    • Clostridium perfringens invasiveness is enhanced by effects of theta toxin upon PMNL structure and function: The roles of leukocytotoxicity and expression of CD11/CD18 adherence glycoprotein
    • Bryant A.E., Bergstrom R., Zimmerman G.A., Salyer J.L., Hill H.R., Tweten R.K., Sato H., Stevens D.L. Clostridium perfringens invasiveness is enhanced by effects of theta toxin upon PMNL structure and function: the roles of leukocytotoxicity and expression of CD11/CD18 adherence glycoprotein. FEMS Immunol. Med. Microbiol. 7:1993;321-336.
    • (1993) FEMS Immunol. Med. Microbiol. , vol.7 , pp. 321-336
    • Bryant, A.E.1    Bergstrom, R.2    Zimmerman, G.A.3    Salyer, J.L.4    Hill, H.R.5    Tweten, R.K.6    Sato, H.7    Stevens, D.L.8
  • 10
    • 0013955199 scopus 로고
    • Cytotoxic effects in vitro of highly purified streptolysin O on mouse macrophages cultured in a serum-free medium
    • Fauve R.M., Alouf J.E., Delaunay A., Raynaud M. Cytotoxic effects in vitro of highly purified streptolysin O on mouse macrophages cultured in a serum-free medium. J. Bacteriol. 92:1966;1150-1153.
    • (1966) J. Bacteriol. , vol.92 , pp. 1150-1153
    • Fauve, R.M.1    Alouf, J.E.2    Delaunay, A.3    Raynaud, M.4
  • 12
    • 0030846035 scopus 로고    scopus 로고
    • The mechanism of cell death in Listeria monocytogenes-infected murine macrophages is distinct from apoptosis
    • Barsig J., Kaufmann S.H.E. The mechanism of cell death in Listeria monocytogenes-infected murine macrophages is distinct from apoptosis. Infect. Immun. 65:1997;4075-4081.
    • (1997) Infect. Immun. , vol.65 , pp. 4075-4081
    • Barsig, J.1    Kaufmann, S.H.E.2
  • 13
    • 0030781597 scopus 로고    scopus 로고
    • Are bacterial exotoxins cytokine network regulators?
    • Henderson B., Wilson M., Wren B. Are bacterial exotoxins cytokine network regulators? Trends Microbiol. 11:1997;454-458.
    • (1997) Trends Microbiol. , vol.11 , pp. 454-458
    • Henderson, B.1    Wilson, M.2    Wren, B.3
  • 14
    • 0031973902 scopus 로고    scopus 로고
    • Streptolysin O and adherence synergistically modulate proinflammatory responses of keratinocytes to group A streptococci
    • Ruiz N., Wang B., Pentland A., Caparon M. Streptolysin O and adherence synergistically modulate proinflammatory responses of keratinocytes to group A streptococci. Mol. Microbiol. 27:1998;337-346.
    • (1998) Mol. Microbiol. , vol.27 , pp. 337-346
    • Ruiz, N.1    Wang, B.2    Pentland, A.3    Caparon, M.4
  • 15
    • 0031457628 scopus 로고    scopus 로고
    • Toxin structure: Part of a hole?
    • Bayley H. Toxin structure: part of a hole? Curr. Biol. 7:1997;R763-R767.
    • (1997) Curr. Biol. , vol.7
    • Bayley, H.1
  • 16
    • 0033033378 scopus 로고    scopus 로고
    • Listeriolysin O-dependent activation of endothelial cells during infection with Listeria monocytogenes: Activation of NF-κB and upregulation of adhesion molecules and chemokines
    • Kayal S., Lilienbaum A., Poyart C., Memet S., Israel A., Berche P. Listeriolysin O-dependent activation of endothelial cells during infection with Listeria monocytogenes: activation of NF-κB and upregulation of adhesion molecules and chemokines. Mol. Microbiol. 31:1999;1709-1722.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1709-1722
    • Kayal, S.1    Lilienbaum, A.2    Poyart, C.3    Memet, S.4    Israel, A.5    Berche, P.6
  • 17
    • 0030037296 scopus 로고    scopus 로고
    • Induction of cytokine gene expression by listeriolysin O and roles of macrophages and NK cells
    • Nishibori T., Xiong H., Kawamura I., Arakawa M., Mitsuyama M. Induction of cytokine gene expression by listeriolysin O and roles of macrophages and NK cells. Infect. Immun. 64:1996;3188-3195.
    • (1996) Infect. Immun. , vol.64 , pp. 3188-3195
    • Nishibori, T.1    Xiong, H.2    Kawamura, I.3    Arakawa, M.4    Mitsuyama, M.5
  • 19
    • 0033017538 scopus 로고    scopus 로고
    • Effect of tumor necrosis factor α and interleukin 1-α On the adherance of Streptococcus pneumoniae to chinchilla tracheal epithelium
    • Tong H.H., Fisher L.M., Kosunick G.M., DeMaria T.F. Effect of tumor necrosis factor α and interleukin 1-α on the adherance of Streptococcus pneumoniae to chinchilla tracheal epithelium. Acta Otolaryngol. 119:1999;78-92.
    • (1999) Acta Otolaryngol. , vol.119 , pp. 78-92
    • Tong, H.H.1    Fisher, L.M.2    Kosunick, G.M.3    Demaria, T.F.4
  • 21
    • 0025879875 scopus 로고
    • Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein
    • Mitchell T.J., Andrew P.W., Saunders F.K., Smith A.N., Boulnois G.J. Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein. Mol. Microbiol. 5:1991;1883-1888.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1883-1888
    • Mitchell, T.J.1    Andrew, P.W.2    Saunders, F.K.3    Smith, A.N.4    Boulnois, G.J.5
  • 22
    • 0021796923 scopus 로고
    • Complement activation and attack on autologous cell membranes induced by streptolysin-O
    • Bhakdi S., Tranum-Jensen J. Complement activation and attack on autologous cell membranes induced by streptolysin-O. Infect. Immun. 48:1985;713-719.
    • (1985) Infect. Immun. , vol.48 , pp. 713-719
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 23
    • 0030920430 scopus 로고    scopus 로고
    • The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family
    • Billington S.J., Jost B.H., Cuevas W.A., Bright K.R., Songer J.G. The Arcanobacterium (Actinomyces) pyogenes hemolysin, pyolysin, is a novel member of the thiol-activated cytolysin family. J. Bacteriol. 179:1997;6100-6106.
    • (1997) J. Bacteriol. , vol.179 , pp. 6100-6106
    • Billington, S.J.1    Jost, B.H.2    Cuevas, W.A.3    Bright, K.R.4    Songer, J.G.5
  • 24
    • 0030007941 scopus 로고    scopus 로고
    • Superior efficacy of secreted over somatic antigen display in recombinant Salmonella vaccine induced protection against listeriosis
    • Hess J., Gentschev I., Miko D., Welzel M., Ladel C., Goebel W., Kaufmann S.H.E. Superior efficacy of secreted over somatic antigen display in recombinant Salmonella vaccine induced protection against listeriosis. Proc. Natl. Acad. Sci. USA. 93:1996;1458-1463.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1458-1463
    • Hess, J.1    Gentschev, I.2    Miko, D.3    Welzel, M.4    Ladel, C.5    Goebel, W.6    Kaufmann, S.H.E.7
  • 25
    • 0029838726 scopus 로고    scopus 로고
    • Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis
    • Jacobs A.A., van den Berg A.J.G., Loeffen P.L.W. Protection of experimentally infected pigs by suilysin, the thiol-activated haemolysin of Streptococcus suis. Vet. Rec. 139:1996;225-228.
    • (1996) Vet. Rec. , vol.139 , pp. 225-228
    • Jacobs, A.A.1    Van Den Berg, A.J.G.2    Loeffen, P.L.W.3
  • 26
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J., Feil S.C., McKinstry W.J., Tweten R.K., Parker M.W. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell. 89:1997;685-692.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 28
    • 0033612389 scopus 로고    scopus 로고
    • Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
    • Gilbert R.J.C., Jimenez J.L., Chen S., Tickle I.J., Rossjohn J., Parker M., Andrew P.W., Saibil H.R. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Cell. 97:1999;647-655.
    • (1999) Cell , vol.97 , pp. 647-655
    • Gilbert, R.J.C.1    Jimenez, J.L.2    Chen, S.3    Tickle, I.J.4    Rossjohn, J.5    Parker, M.6    Andrew, P.W.7    Saibil, H.R.8
  • 29
    • 0023783454 scopus 로고
    • Protease-nicked theta-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes
    • Ohno-Iwashita Y., Iwamoto M., Mitsui K., Ando S., Nagai Y. Protease-nicked theta-toxin of Clostridium perfringens, a new membrane probe with no cytolytic effect, reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes. Eur. J. Biochem. 176:1988;95-101.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 95-101
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Mitsui, K.3    Ando, S.4    Nagai, Y.5
  • 30
    • 0028001461 scopus 로고
    • A role in the cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae
    • Owen R.H.G., Boulnois G.J., Andrew P.W., Mitchell T.J. A role in the cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae. FEMS Microbiol. Lett. 121:1994;217-222.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 217-222
    • Owen, R.H.G.1    Boulnois, G.J.2    Andrew, P.W.3    Mitchell, T.J.4
  • 31
    • 0033603558 scopus 로고    scopus 로고
    • C-terminal amino acid residues are required for the folding and cholesterol binding property of perfringolysin O, a pore-forming cytolysin
    • Shimada Y., Nakamura M., Naito Y., Nomura K., Ohno-Iwashita Y. C-terminal amino acid residues are required for the folding and cholesterol binding property of perfringolysin O, a pore-forming cytolysin. J. Biol. Chem. 274:1999;18536-18542.
    • (1999) J. Biol. Chem , vol.274 , pp. 18536-18542
    • Shimada, Y.1    Nakamura, M.2    Naito, Y.3    Nomura, K.4    Ohno-Iwashita, Y.5
  • 32
    • 0025244264 scopus 로고
    • Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis
    • Iwamoto M., Ohno-Iwashita Y., Ando S. Effect of isolated C-terminal fragment of theta-toxin (perfringolysin O) on toxin assembly and membrane lysis. Eur. J. Biochem. 194:1990;25-31.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 25-31
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 33
    • 0028988973 scopus 로고
    • Interaction of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: Change in the aromatic side chains upon binding and insertion
    • Nakamura M., Sekino N., Iwamoto M., Ohno-Iwashita Y. Interaction of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion. Biochemistry. 34:1995;6513-6520.
    • (1995) Biochemistry , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 34
    • 0031749207 scopus 로고    scopus 로고
    • Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes
    • Nakamura M., Sekino-Suzuki N., Mitsui K.-I., Ohno-Iwashita Y. Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes. J. Biochem. (Tokyo). 123:1998;1145-1155.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1145-1155
    • Nakamura, M.1    Sekino-Suzuki, N.2    Mitsui, K.-I.3    Ohno-Iwashita, Y.4
  • 35
    • 0032536856 scopus 로고    scopus 로고
    • Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
    • Palmer M., Harris R., Freytag C., Kehoe M., Tranum-Jensen J., Bhakdi S. Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization. EMBO J. 17:1998;1598-1605.
    • (1998) EMBO J. , vol.17 , pp. 1598-1605
    • Palmer, M.1    Harris, R.2    Freytag, C.3    Kehoe, M.4    Tranum-Jensen, J.5    Bhakdi, S.6
  • 36
    • 0027169048 scopus 로고
    • A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane
    • Sekiya K., Satoh R., Danbara H., Futaesaku Y. A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane. J. Bacteriol. 175:1993;5953-5961.
    • (1993) J. Bacteriol. , vol.175 , pp. 5953-5961
    • Sekiya, K.1    Satoh, R.2    Danbara, H.3    Futaesaku, Y.4
  • 37
    • 0025989653 scopus 로고
    • Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae
    • Boulnois G.J., Paton J.C., Mitchell T.J., Andrew P.W. Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. Mol. Microbiol. 5:1991;2611-2616.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2611-2616
    • Boulnois, G.J.1    Paton, J.C.2    Mitchell, T.J.3    Andrew, P.W.4
  • 38
    • 0025685253 scopus 로고
    • Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitution in listeriolysin O
    • Michel E., Reich K.A., Favier R., Berche P., Cossart P. Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitution in listeriolysin O. Mol. Microbiol. 4:1990;2167-2178.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2167-2178
    • Michel, E.1    Reich, K.A.2    Favier, R.3    Berche, P.4    Cossart, P.5
  • 39
    • 0029972377 scopus 로고    scopus 로고
    • Contribution of individual tryptophan residues to the structure and activity of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin
    • Sekino-Suzuki N., Nakamura M., Mitsui K.-I., Ohno-Iwashita Y. Contribution of individual tryptophan residues to the structure and activity of θ-toxin (perfringolysin O), a cholesterol-binding cytolysin. Eur. J. Biochem. 241:1996;941-947.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 941-947
    • Sekino-Suzuki, N.1    Nakamura, M.2    Mitsui, K.-I.3    Ohno-Iwashita, Y.4
  • 40
    • 0024407229 scopus 로고
    • Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity
    • Saunders F.K., Mitchell T.J., Walker J.A., Andrew P.W., Boulnois G.J. Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity. Infect. Immun. 57:1989;2547-2552.
    • (1989) Infect. Immun. , vol.57 , pp. 2547-2552
    • Saunders, F.K.1    Mitchell, T.J.2    Walker, J.A.3    Andrew, P.W.4    Boulnois, G.J.5
  • 41
    • 0024720325 scopus 로고
    • The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity
    • Pinkney M., Beachey E., Kehoe M. The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity. Infect. Immun. 57:1989;2553-2558.
    • (1989) Infect. Immun. , vol.57 , pp. 2553-2558
    • Pinkney, M.1    Beachey, E.2    Kehoe, M.3
  • 42
    • 0029902726 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies against listeriolysin: Mapping of epitopes involved in pore formation
    • Darji A., Niebuhr K., Hense M., Wehland J., Chakraborty T., Weiss S. Neutralizing monoclonal antibodies against listeriolysin: mapping of epitopes involved in pore formation. Infect. Immun. 64:1996;2356-2358.
    • (1996) Infect. Immun. , vol.64 , pp. 2356-2358
    • Darji, A.1    Niebuhr, K.2    Hense, M.3    Wehland, J.4    Chakraborty, T.5    Weiss, S.6
  • 44
    • 0029909653 scopus 로고    scopus 로고
    • Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
    • Palmer M., Saweljew P., Vulicevic I., Valeva A., Kehoe M., Bhakdi S. Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis. J. Biol. Chem. 271:1996;26664-26667.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26664-26667
    • Palmer, M.1    Saweljew, P.2    Vulicevic, I.3    Valeva, A.4    Kehoe, M.5    Bhakdi, S.6
  • 45
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An α-helical to β-sheet transition identified by fluorescence spectroscopy
    • Shepard L.A., Heuck A.P., Hamman B.D., Rossjohn J., Parker M.W., Ryan K.R., Johnson A.E., Tweten R.K. Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an α-helical to β-sheet transition identified by fluorescence spectroscopy. Biochemistry. 37:1998;14563-14574.
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 47
    • 0022266614 scopus 로고
    • Membrane damage by channel-forming proteins: Staphylococcal α-toxin, streptolysin O and the C5b-9 complement complex
    • Bhakdi S., Tranum-Jensen J. Membrane damage by channel-forming proteins: staphylococcal α-toxin, streptolysin O and the C5b-9 complement complex. Biochem. Soc. Symp. 50:1985;221-233.
    • (1985) Biochem. Soc. Symp. , vol.50 , pp. 221-233
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 48
    • 0031137686 scopus 로고    scopus 로고
    • Streptococcal cytolysins
    • Nagamune H. Streptococcal cytolysins. Seikagaku. 69:1997;343-348.
    • (1997) Seikagaku , vol.69 , pp. 343-348
    • Nagamune, H.1
  • 49
    • 0032007852 scopus 로고    scopus 로고
    • A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers
    • Korchev Y.E., Bashford C.L., Pederzolli C., Pasternak C.A., Morgan P.J., Andrew P.W., Mitchell T.J. A conserved tryptophan in pneumolysin is a determinant of the characteristics of channels formed by pneumolysin in cells and planar lipid bilayers. Biochem. J. 329:1998;571-577.
    • (1998) Biochem. J. , vol.329 , pp. 571-577
    • Korchev, Y.E.1    Bashford, C.L.2    Pederzolli, C.3    Pasternak, C.A.4    Morgan, P.J.5    Andrew, P.W.6    Mitchell, T.J.7
  • 50
    • 0030037295 scopus 로고    scopus 로고
    • Intermedilysin, a novel cytotoxin specific for human cells, secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess
    • Nagamune H., Ohnishi C., Katsuura A., Fushitani K., Whiley R.A., Tsuji A., Matsuda Y. Intermedilysin, a novel cytotoxin specific for human cells, secreted by Streptococcus intermedius UNS46 isolated from a human liver abscess. Infect. Immun. 64:1996;3093-3100.
    • (1996) Infect. Immun. , vol.64 , pp. 3093-3100
    • Nagamune, H.1    Ohnishi, C.2    Katsuura, A.3    Fushitani, K.4    Whiley, R.A.5    Tsuji, A.6    Matsuda, Y.7
  • 51
    • 0015947871 scopus 로고
    • Streptolysin O inhibition of neutrophil chemotaxis and mobility: Nonimmune phenomenon with species specificity
    • Van Epps D.E., Andersen B.R. Streptolysin O inhibition of neutrophil chemotaxis and mobility: nonimmune phenomenon with species specificity. Infect. Immun. 9:1974;27-33.
    • (1974) Infect. Immun. , vol.9 , pp. 27-33
    • Van Epps, D.E.1    Andersen, B.R.2
  • 52
    • 0026596550 scopus 로고
    • Streptococcal shock syndrome: Synthesis of tumor necrosis factor and interleukin-1 by monocytes stimulated with pyrogenic exotoxin A and streptolysin O
    • Hackett S.P., Stevens D.L. Streptococcal shock syndrome: synthesis of tumor necrosis factor and interleukin-1 by monocytes stimulated with pyrogenic exotoxin A and streptolysin O. J. Infect. Dis. 165:1992;879-885.
    • (1992) J. Infect. Dis. , vol.165 , pp. 879-885
    • Hackett, S.P.1    Stevens, D.L.2
  • 53
    • 0028176663 scopus 로고
    • Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1β by human mononuclear phagocytes
    • Houldsworth S., Andrew P.W., Mitchell T.J. Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1β by human mononuclear phagocytes. Infect. Immun. 62:1994;1501-1503.
    • (1994) Infect. Immun. , vol.62 , pp. 1501-1503
    • Houldsworth, S.1    Andrew, P.W.2    Mitchell, T.J.3
  • 54
    • 0032768658 scopus 로고    scopus 로고
    • Pneumolysin, a protein toxin of Streptococcus pneumoniae, induces nitric oxide production from macrophages
    • Braun J.S., Novak R., Gao G., Murray P.J., Shenep J.L. Pneumolysin, a protein toxin of Streptococcus pneumoniae, induces nitric oxide production from macrophages. Infect. Immun. 67:1999;3750-3756.
    • (1999) Infect. Immun. , vol.67 , pp. 3750-3756
    • Braun, J.S.1    Novak, R.2    Gao, G.3    Murray, P.J.4    Shenep, J.L.5
  • 55
    • 0027463286 scopus 로고
    • Membrane damage and interleukin-1 production in murine macrophages exposed to listeriolysin O
    • Yoshikawa H., Kawamura I., Fujita M., Tsukada H., Arakawa M., Mitsuyama M. Membrane damage and interleukin-1 production in murine macrophages exposed to listeriolysin O. Infect. Immun. 61:1993;1334-1339.
    • (1993) Infect. Immun. , vol.61 , pp. 1334-1339
    • Yoshikawa, H.1    Kawamura, I.2    Fujita, M.3    Tsukada, H.4    Arakawa, M.5    Mitsuyama, M.6
  • 56
    • 0028029781 scopus 로고
    • Activation of human effector cells by different bacterial toxins (leukocidin, alveolysin, and erythrogenic toxin A): Generation of interleukin-8
    • Konig B., Koller M., Prevost G., Piemont Y., Alouf J.E., Schreiner A., Konig W. Activation of human effector cells by different bacterial toxins (leukocidin, alveolysin, and erythrogenic toxin A): generation of interleukin-8. Infect. Immun. 62:1994;4831-4837.
    • (1994) Infect. Immun. , vol.62 , pp. 4831-4837
    • Konig, B.1    Koller, M.2    Prevost, G.3    Piemont, Y.4    Alouf, J.E.5    Schreiner, A.6    Konig, W.7


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