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Volumn 7, Issue 4, 1996, Pages 221-229

Thiol-activated cytolysins

Author keywords

Listeriolysin; Membrane damaging toxin; Perfringolysin; Pneumolysin; Streptolysin; Thiol activated cytolysin; Thiol activated toxin

Indexed keywords

BACTERIAL TOXIN; BINDING PROTEIN; CHOLESTEROL; CYTOLYSIN; THIOL;

EID: 0029852034     PISSN: 0954139X     EISSN: None     Source Type: Journal    
DOI: 10.1097/00013542-199610000-00004     Document Type: Review
Times cited : (28)

References (50)
  • 1
    • 0026695462 scopus 로고
    • Differential sensitivity of pneumolysin-induced channels to gating by divalent cations
    • Korchev YE, Bashford CL, Pasternak CA. Differential sensitivity of pneumolysin-induced channels to gating by divalent cations. J Memb Biol 1992; 127: 195-203.
    • (1992) J Memb Biol , vol.127 , pp. 195-203
    • Korchev, Y.E.1    Bashford, C.L.2    Pasternak, C.A.3
  • 2
    • 0026512567 scopus 로고
    • Listeriolysin genes: Complete sequence of ivanolysin from Listeria ivanovii and of listeriolysin from Listeria seeligeri
    • Haas A, Dumbsky M, Kreft J. Listeriolysin genes: complete sequence of ivanolysin from Listeria ivanovii and of listeriolysin from Listeria seeligeri. Biochim Biophys Act 1992; 1130: 81-84.
    • (1992) Biochim Biophys Act , vol.1130 , pp. 81-84
    • Haas, A.1    Dumbsky, M.2    Kreft, J.3
  • 3
    • 0023026162 scopus 로고
    • Use of a monoclonal antibody to determine the mode of transmembrane pore-formation by streptolysin O
    • Hugo F, Reichwein J, Arvand M, Kramer S, Bhakdi S. Use of a monoclonal antibody to determine the mode of transmembrane pore-formation by streptolysin O. Infect Immun 1986; 54: 641-645.
    • (1986) Infect Immun , vol.54 , pp. 641-645
    • Hugo, F.1    Reichwein, J.2    Arvand, M.3    Kramer, S.4    Bhakdi, S.5
  • 4
    • 1842323092 scopus 로고    scopus 로고
    • Functional analysis of pneumolysin by use of monoclonal antibodies
    • de los Toyos JR, Mendez FJ, Aparicio JF et al. Functional analysis of pneumolysin by use of monoclonal antibodies. Infect Immun 1996; 64: 480-484.
    • (1996) Infect Immun , vol.64 , pp. 480-484
    • De Los Toyos, J.R.1    Mendez, F.J.2    Aparicio, J.F.3
  • 5
    • 0002027172 scopus 로고
    • The family of antigenically-related, cholesterol-binding ('sulphydryl-activated') cytolytic toxins
    • Alouf JE, Freer JH, eds. London: Academic Press
    • Alouf JE, Geoffroy C. The family of antigenically-related, cholesterol-binding ('sulphydryl-activated') cytolytic toxins. In: Alouf JE, Freer JH, eds. Sourcebook of bacterial protein toxins. London: Academic Press, 1992, pp 147-186.
    • (1992) Sourcebook of Bacterial Protein Toxins , pp. 147-186
    • Alouf, J.E.1    Geoffroy, C.2
  • 6
    • 0028988973 scopus 로고
    • Interaction of theta-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 theta-toxin (perfringolysin O), a cholesterol-binding cytolysin, with liposomal membranes: change in the aromatic side chains upon binding and insertion. Biochem 1995; 34: 6513-6520.
    • (1995) Biochem , vol.34 , pp. 6513-6520
    • Nakamura, M.1    Sekino, N.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 7
    • 0024407229 scopus 로고
    • Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity
    • Saunders FK, Mitchell TJ, Walker JA, Andrew PW, Boulnois GJ. Pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae, does not require a thiol group for in vitro activity. Infect Immun 1989; 57: 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
  • 8
    • 0020558325 scopus 로고
    • Inhibition of human polymorphonuclear leukocyte respiratory burst, bactericidal activity, and migration by pneumolysin
    • Paton JC, Ferrante A. Inhibition of human polymorphonuclear leukocyte respiratory burst, bactericidal activity, and migration by pneumolysin. Infect Immun 1983; 41: 1212-1216.
    • (1983) Infect Immun , vol.41 , pp. 1212-1216
    • Paton, J.C.1    Ferrante, A.2
  • 9
    • 0022999334 scopus 로고
    • Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin
    • Nandoskar M, Ferrante A, Bates EJ et al. Inhibition of human monocyte respiratory burst, degranulation, phospholipid methylation and bactericidal activity by pneumolysin. Immunol 1986; 59: 515-520.
    • (1986) Immunol , vol.59 , pp. 515-520
    • Nandoskar, M.1    Ferrante, A.2    Bates, E.J.3
  • 10
    • 0028176663 scopus 로고
    • Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1-beta by human mononuclear phagocytes
    • Houldsworth S, Andrew PW, Mitchell TJ. Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1-beta by human mononuclear phagocytes. Infect Immun 1994; 62: 1501-1503.
    • (1994) Infect Immun , vol.62 , pp. 1501-1503
    • Houldsworth, S.1    Andrew, P.W.2    Mitchell, T.J.3
  • 11
    • 0028129056 scopus 로고
    • Pneumolysin activates phospholipase a in pulmonary artery endothelial cells
    • Rubins JB, Mitchell TJ, Andrew PW, Niewoehner DE. Pneumolysin activates phospholipase A in pulmonary artery endothelial cells. Infect Immun 1994; 62: 3829-3836.
    • (1994) Infect Immun , vol.62 , pp. 3829-3836
    • Rubins, J.B.1    Mitchell, T.J.2    Andrew, P.W.3    Niewoehner, D.E.4
  • 12
    • 0025613913 scopus 로고
    • The effect of Streptococcus pneumoniae pneumolysin on human respiratory epithelium in vitro
    • Feldman C, Mitchell TJ, Andrew PW et al. The effect of Streptococcus pneumoniae pneumolysin on human respiratory epithelium in vitro. Microb Path 1990; 9: 275-284.
    • (1990) Microb Path , vol.9 , pp. 275-284
    • Feldman, C.1    Mitchell, T.J.2    Andrew, P.W.3
  • 13
    • 0021363204 scopus 로고
    • Activation of human complement by the pneumococcal toxin pneumolysin
    • Paton JC, Rowan KB, Ferrante A. Activation of human complement by the pneumococcal toxin pneumolysin. Infect Immun 1984; 43: 1085-1087.
    • (1984) Infect Immun , vol.43 , pp. 1085-1087
    • Paton, J.C.1    Rowan, K.B.2    Ferrante, A.3
  • 14
    • 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 1985; 48: 713-719.
    • (1985) Infect Immun , vol.48 , pp. 713-719
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 15
    • 0025879875 scopus 로고
    • Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein
    • Mitchell TJ, Andrew PW, Saunders FK, Smith AN, Boulnois GJ. Complement activation and antibody binding by pneumolysin via a region of the toxin homologous to a human acute-phase protein. Mol Microbiol 1991; 5: 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
  • 16
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy DA, Jacks PS, Hinrichs DJ. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med 1988; 167: 1459-1471.
    • (1988) J Exp Med , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 17
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney LG, Portnoy DA. Actin filaments and the growth, movement and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 1989; 109: 1597-1608.
    • (1989) J Cell Biol , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 18
    • 0025329666 scopus 로고
    • Bacillus subtilis expressing a haemolysin gene from Listeria monocytogenes can grow in mammalian cells
    • Bielecki J, Youngman P, Connelly P, Portnoy DA. Bacillus subtilis expressing a haemolysin gene from Listeria monocytogenes can grow in mammalian cells. Nature 1990; 345: 175-176.
    • (1990) Nature , vol.345 , pp. 175-176
    • Bielecki, J.1    Youngman, P.2    Connelly, P.3    Portnoy, D.A.4
  • 19
    • 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 1993; 61: 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
  • 20
    • 0024355265 scopus 로고
    • Reduced virulence of a defined pneumolysin-negative mutant of Streptococcus pneumoniae
    • Berry AM, Yother J, Briles DE, Hansman D, Paton JC. Reduced virulence of a defined pneumolysin-negative mutant of Streptococcus pneumoniae. Infect Immun 1989; 57: 2037-2042.
    • (1989) Infect Immun , vol.57 , pp. 2037-2042
    • Berry, A.M.1    Yother, J.2    Briles, D.E.3    Hansman, D.4    Paton, J.C.5
  • 21
    • 0029016207 scopus 로고
    • The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus
    • Canvin JR, Marvin AP, Sivakumaran M et al. The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus. J Infect Dis 1995; 172: 119-123.
    • (1995) J Infect Dis , vol.172 , pp. 119-123
    • Canvin, J.R.1    Marvin, A.P.2    Sivakumaran, M.3
  • 22
    • 0026261690 scopus 로고
    • Pneumolysin induces the salient features of pneumococcal infection in the rat lung in vivo
    • Feldman C, Munro NC, Jeffrey DK et al. Pneumolysin induces the salient features of pneumococcal infection in the rat lung in vivo. Am J Resp Cell Mol Biol 1991; 5: 416-423.
    • (1991) Am J Resp Cell Mol Biol , vol.5 , pp. 416-423
    • Feldman, C.1    Munro, N.C.2    Jeffrey, D.K.3
  • 23
    • 0028934267 scopus 로고
    • Effect of defined point mutations in the pneumolysin gene on the virulence of Streptococcus pneumoniae
    • Berry AM, Alexander JE, Mitchell TJ, Andrew PW, Hansman D, Paton JC. Effect of defined point mutations in the pneumolysin gene on the virulence of Streptococcus pneumoniae. Infect Immun 1995; 63: 1969-1974.
    • (1995) Infect Immun , vol.63 , pp. 1969-1974
    • Berry, A.M.1    Alexander, J.E.2    Mitchell, T.J.3    Andrew, P.W.4    Hansman, D.5    Paton, J.C.6
  • 24
    • 0029986122 scopus 로고    scopus 로고
    • Distinct role for pneumolysin's cytotoxic and complement activities in the pathogenesis of pneumococcal pneumonia
    • in press
    • Rubins JB, Charboneau D, Fasching C et al. Distinct role for pneumolysin's cytotoxic and complement activities in the pathogenesis of pneumococcal pneumonia. Am J Respir Crit Care Med 1996 (in press).
    • (1996) Am J Respir Crit Care Med
    • Rubins, J.B.1    Charboneau, D.2    Fasching, C.3
  • 25
    • 0028945951 scopus 로고
    • Virulence studies on chromosomal alpha-toxin and theta-toxin mutants constructed by allelic exchange provide genetic-evidence for the essential role of alpha-toxin in Clostridium perfringens-mediated gas-gangrene
    • Awad MM, Bryant AE, Stevens DL, Rood JI. Virulence studies on chromosomal alpha-toxin and theta-toxin mutants constructed by allelic exchange provide genetic-evidence for the essential role of alpha-toxin in Clostridium perfringens-mediated gas-gangrene. Mol Microbiol 1995; 15: 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
  • 26
    • 0023491913 scopus 로고
    • Nucleotide sequence of the streptolysin O (SLO) gene: Structural homologies between SLO and other membrane-damaging, thiol-activated toxins
    • Kehoe MA, Miller L, Walker JA, Boulnois GJ. Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane-damaging, thiol-activated toxins. Infect Immun 1987; 55: 3228-3232.
    • (1987) Infect Immun , vol.55 , pp. 3228-3232
    • Kehoe, M.A.1    Miller, L.2    Walker, J.A.3    Boulnois, G.J.4
  • 27
    • 0023656177 scopus 로고
    • Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens
    • Iwamoto M, Ohno-Iwashita Y, Ando S. Role of the essential thiol group in the thiol-activated cytolysin from Clostridium perfringens. Eur J Biochem 1987; 167: 425-430.
    • (1987) Eur J Biochem , vol.167 , pp. 425-430
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 28
    • 0019618021 scopus 로고
    • Les toxins cytolytiques bacteriennes thiol-dependantes: Streptolysine O et toxines apparentees. Thiol-dependent cytolytic bacterial toxins: streptolysin O and related toxins
    • Tunis
    • Alouf JE. Les toxins cytolytiques bacteriennes thiol-dependantes: streptolysine O et toxines apparentees. Thiol-dependent cytolytic bacterial toxins: streptolysin O and related toxins. Arch Inst Pasteur (Tunis) 1981; 355-373.
    • (1981) Arch Inst Pasteur , pp. 355-373
    • Alouf, J.E.1
  • 29
    • 0000537298 scopus 로고
    • Molecular studies of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae as an aid to vaccine design
    • Gustav Fischer, Stuttgart
    • Mitchell TJ, Andrew PW, Boulnois GJ, Lee C-J, Lock RA, Paton JC. Molecular studies of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae as an aid to vaccine design. In: Bacterial protein toxins. Gustav Fischer, Stuttgart: 1992, pp 429-437.
    • (1992) Bacterial Protein Toxins , pp. 429-437
    • Mitchell, T.J.1    Andrew, P.W.2    Boulnois, G.J.3    Lee, C.-J.4    Lock, R.A.5    Paton, J.C.6
  • 30
    • 0028001461 scopus 로고
    • A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae
    • Owen RHG, Boulnois GJ, Andrew PW, Mitchell TJ. A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae. FEMS Microbiol Lett 1994; 121: 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
    • 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 1990; 194: 25-31.
    • (1990) Eur J Biochem , vol.194 , pp. 25-31
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 32
    • 0023757453 scopus 로고
    • Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: Significant homology with the genes for streptolysin O and pneumolysin
    • Tweten RK. Nucleotide sequence of the gene for perfringolysin O (theta-toxin) from Clostridium perfringens: significant homology with the genes for streptolysin O and pneumolysin. Infect Immun 1988; 56: 3235-3240.
    • (1988) Infect Immun , vol.56 , pp. 3235-3240
    • Tweten, R.K.1
  • 33
    • 0030043134 scopus 로고    scopus 로고
    • Aerolysin - The ins and cuts of a model channel-forming toxin
    • Parker MW, van der Goot FG, Buckley JT. Aerolysin - the ins and cuts of a model channel-forming toxin. Mol Microbiol 1996; 19: 205-212.
    • (1996) Mol Microbiol , vol.19 , pp. 205-212
    • Parker, M.W.1    Van Der Goot, F.G.2    Buckley, J.T.3
  • 34
    • 0027768921 scopus 로고
    • Characterization of the solution properties and conformation of pneumolysin, the membrane-damaging toxin of Streptococcus pneumoniae
    • Morgan PJ, Varley PG, Rowe AJ, Andrew PW, Mitchell TJ. Characterization of the solution properties and conformation of pneumolysin, the membrane-damaging toxin of Streptococcus pneumoniae. Biochem J 1993; 296: 671-674.
    • (1993) Biochem J , vol.296 , pp. 671-674
    • Morgan, P.J.1    Varley, P.G.2    Rowe, A.J.3    Andrew, P.W.4    Mitchell, T.J.5
  • 35
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • Morgan PJ, Hyman SC, Byron O, Andrew PW, Mitchell TJ, Rowe AJ. Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J Biol Chem 1994; 269: 25315-25320.
    • (1994) J Biol Chem , vol.269 , pp. 25315-25320
    • Morgan, P.J.1    Hyman, S.C.2    Byron, O.3    Andrew, P.W.4    Mitchell, T.J.5    Rowe, A.J.6
  • 37
    • 0016715847 scopus 로고
    • Effect of streptolysin O on erythrocyte membranes, liposomes and lipid dispersions
    • Duncan JL, Schlegel R. Effect of streptolysin O on erythrocyte membranes, liposomes and lipid dispersions. J Cell Biol 1975; 67: 160-173.
    • (1975) J Cell Biol , vol.67 , pp. 160-173
    • Duncan, J.L.1    Schlegel, R.2
  • 38
    • 0027526035 scopus 로고
    • The projection structure of perfringolysin O (Clostridium perfringens theta-toxin)
    • Olofsson A, Hebert H, Thelestam M. The projection structure of perfringolysin O (Clostridium perfringens theta-toxin). FEBS Lett 1993; 319: 125-127.
    • (1993) FEBS Lett , vol.319 , pp. 125-127
    • Olofsson, A.1    Hebert, H.2    Thelestam, M.3
  • 39
    • 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 1993; 175: 5953-5961.
    • (1993) J Bacteriol , vol.175 , pp. 5953-5961
    • Sekiya, K.1    Satoh, R.2    Danbara, H.3    Futaesaku, Y.4
  • 41
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilisation of cell membranes
    • Berl
    • Bhakdi S, Weller U, Walev I, Martin E, Jonas D, Palmer M. A guide to the use of pore-forming toxins for controlled permeabilisation of cell membranes. Med Microbiol Immunol (Berl) 1993; 182: 167-175.
    • (1993) Med Microbiol Immunol , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 42
    • 0029079747 scopus 로고
    • Efficient gene delivery and expression in mammalian cells using DNA coupled with perfringolysin O
    • Gottschalk S, Tweten RK, Smith LC, Woo SLC. Efficient gene delivery and expression in mammalian cells using DNA coupled with perfringolysin O. Gene Therapy 1995; 2: 498-503.
    • (1995) Gene Therapy , vol.2 , pp. 498-503
    • Gottschalk, S.1    Tweten, R.K.2    Smith, L.C.3    Woo, S.L.C.4
  • 44
    • 0020638911 scopus 로고
    • Effect of immunization with pneumolysin on survival time of mice challenged with Streptococcus pneumoniae
    • Paton JC, Lock RA, Hansman DJ. Effect of immunization with pneumolysin on survival time of mice challenged with Streptococcus pneumoniae. Infect Immun 1983; 40: 548-552.
    • (1983) Infect Immun , vol.40 , pp. 548-552
    • Paton, J.C.1    Lock, R.A.2    Hansman, D.J.3
  • 45
    • 0028028168 scopus 로고
    • Immunization of mice with pneumolysin toxoid confers a significant degree of protection against at least nine serotypes of Streptococcus pneumoniae
    • Alexander JE, Lock RA, Peeters C et al. Immunization of mice with pneumolysin toxoid confers a significant degree of protection against at least nine serotypes of Streptococcus pneumoniae. Infect Immun 1994; 62: 5683-5688.
    • (1994) Infect Immun , vol.62 , pp. 5683-5688
    • Alexander, J.E.1    Lock, R.A.2    Peeters, C.3
  • 46
    • 0023251174 scopus 로고
    • Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae
    • Walker JA, Allen RL, Falmagne P et al. Molecular cloning, characterization, and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae. Infect. Immun. 1987; 55: 1184-1189.
    • (1987) Infect. Immun. , vol.55 , pp. 1184-1189
    • Walker, J.A.1    Allen, R.L.2    Falmagne, P.3
  • 47
    • 0023930894 scopus 로고
    • Expression of Escherichia coli and sequence analysis of the listeriolysin O determinant of Listeria monocytogenes
    • Mengaud J, Vicente MF, Chenevert J et al. Expression of Escherichia coli and sequence analysis of the listeriolysin O determinant of Listeria monocytogenes. Infect Immun 1988; 56: 766-772.
    • (1988) Infect Immun , vol.56 , pp. 766-772
    • Mengaud, J.1    Vicente, M.F.2    Chenevert, J.3
  • 48
    • 0020517091 scopus 로고
    • Cloning and expression in Escherichia coli and Bacillus subtilis of the hemolysin (cereolysin) determinant from Bacillus cereus
    • Kreft J, Berger H, Hartlein M, Muller B, Weidinger G, Goebel W. Cloning and expression in Escherichia coli and Bacillus subtilis of the hemolysin (cereolysin) determinant from Bacillus cereus. J Bacteriol 1983; 155: 681-689.
    • (1983) J Bacteriol , vol.155 , pp. 681-689
    • Kreft, J.1    Berger, H.2    Hartlein, M.3    Muller, B.4    Weidinger, G.5    Goebel, W.6
  • 50
    • 0025640782 scopus 로고
    • Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine
    • Geoffroy C, Mengaud J, Alouf JE, Cossart P. Alveolysin, the thiol-activated toxin of Bacillus alvei, is homologous to listeriolysin O, perfringolysin O, pneumolysin, and streptolysin O and contains a single cysteine. J Bacteriol 1990; 172: 7301-7305.
    • (1990) J Bacteriol , vol.172 , pp. 7301-7305
    • Geoffroy, C.1    Mengaud, J.2    Alouf, J.E.3    Cossart, P.4


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