메뉴 건너뛰기




Volumn 165, Issue 2, 1996, Pages 73-79

Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: Prototypes of pore-forming bacterial cytolysins

Author keywords

Alpha toxin; Escherichia coli hemolysin; Microbial pathogenesis; Streptolysin O; Transmembrane pores

Indexed keywords

ALPHA TOXIN; BACTERIOCIN; CYTOTOXIN; HEMOLYSIN; STREPTOLYSIN O;

EID: 0029916264     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050300     Document Type: Review
Times cited : (264)

References (45)
  • 1
    • 0002027172 scopus 로고
    • The family of the antigenically related, cholesterol-binding ("sulphydryl-activated") cytolytic toxins
    • Alouf JE, Freer JH (ed) Academic Press, New York London
    • Alouf JE, Geoffrey C (1991) The family of the antigenically related, cholesterol-binding ("sulphydryl-activated") cytolytic toxins. In: Alouf JE, Freer JH (ed) Sourcebook of bacterial protein toxins, Academic Press, New York London, pp 147-186
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 147-186
    • Alouf, J.E.1    Geoffrey, C.2
  • 2
    • 0028020468 scopus 로고
    • Triggers and switches in self-assembling pore-forming proteins
    • Bayley H (1994) Triggers and switches in self-assembling pore-forming proteins. J Cell Biochem 56:177-182
    • (1994) J Cell Biochem , vol.56 , pp. 177-182
    • Bayley, H.1
  • 3
    • 0024505102 scopus 로고
    • Pore formation by the Escherichia coli hemolysin: Evidence for an association-dissociation equilibrium of the pore-forming aggregates
    • Benz R, Schmid A, Wagner W, Goebel W (1989) Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates. Infect Immun 57:887-893
    • (1989) Infect Immun , vol.57 , pp. 887-893
    • Benz, R.1    Schmid, A.2    Wagner, W.3    Goebel, W.4
  • 4
    • 0023901550 scopus 로고
    • Damage to cell membranes by pore-forming bacterial cytolysins
    • Bhakdi S, Tranum-Jensen J (1988) Damage to cell membranes by pore-forming bacterial cytolysins. Prog Allergy 40:1-43
    • (1988) Prog Allergy , vol.40 , pp. 1-43
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 5
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • Bhakdi S, Tranum-Jensen J (1991) Alpha-toxin of Staphylococcus aureus. Microbiol Rev 55:733-751
    • (1991) Microbiol Rev , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 6
    • 77955095800 scopus 로고
    • Staphylococcal alpha-toxin: Oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles
    • Bhakdi S, Füssle R, Tranum-Jensen J (1981) Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles. Proc Natl Acad Sci USA 78:5475-5479
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 5475-5479
    • Bhakdi, S.1    Füssle, R.2    Tranum-Jensen, J.3
  • 8
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi S, Weller U, Walev I, Martin E, Jonas D, Palmer M (1993) A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med Microbiol Immun 182:167-175
    • (1993) Med Microbiol Immun , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 9
    • 0028106748 scopus 로고
    • Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: The unknown connection
    • Bhakdi S, Grimminger F, Suttorp N, Walmrath D, Seeger W (1994) Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: the unknown connection. Med Microbiol Immun 183:119-144
    • (1994) Med Microbiol Immun , vol.183 , pp. 119-144
    • Bhakdi, S.1    Grimminger, F.2    Suttorp, N.3    Walmrath, D.4    Seeger, W.5
  • 10
    • 0025288364 scopus 로고
    • Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes
    • Boehm DF, Welch RA, Snyder IS (1990) Domains of Escherichia coli hemolysin (HlyA) involved in binding of calcium and erythrocyte membranes. Infect Immun 58:1959-1964
    • (1990) Infect Immun , vol.58 , pp. 1959-1964
    • Boehm, D.F.1    Welch, R.A.2    Snyder, I.S.3
  • 11
    • 0020614630 scopus 로고
    • Approximate dimensions of membrane lesions produced by streptolysin-S and streptolysin-O
    • Buckingham L, Duncan JL (1983) Approximate dimensions of membrane lesions produced by streptolysin-S and streptolysin-O. Biochim Biophys Acta 729:115-122
    • (1983) Biochim Biophys Acta , vol.729 , pp. 115-122
    • Buckingham, L.1    Duncan, J.L.2
  • 12
    • 0028951608 scopus 로고
    • Breakdown of the round window membrane permeability barrier evoked by streptolysin O: Possible etiologic role in development of sensorineural hearing loss in acute otitis media
    • Engel F, Blatz R, Kellner J, Palmer M, Weller U, Bhakdi S (1995) Breakdown of the round window membrane permeability barrier evoked by streptolysin O: possible etiologic role in development of sensorineural hearing loss in acute otitis media. Infect Immun 63:1305-1310
    • (1995) Infect Immun , vol.63 , pp. 1305-1310
    • Engel, F.1    Blatz, R.2    Kellner, J.3    Palmer, M.4    Weller, U.5    Bhakdi, S.6
  • 13
    • 0024041944 scopus 로고
    • Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion
    • Felmlee T, Welch RA (1988) Alterations of amino acid repeats in the Escherichia coli hemolysin affect cytolytic activity and secretion. Proc Natl Acad Sci USA 85:5269-5273
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5269-5273
    • Felmlee, T.1    Welch, R.A.2
  • 14
    • 0022260426 scopus 로고
    • Nucleotide sequence of an Escherichia coli chromosomal hemolysin
    • Felmlee T, Pellet S, Welch RA (1985) Nucleotide sequence of an Escherichia coli chromosomal hemolysin. J Bacteriol 163:94-105
    • (1985) J Bacteriol , vol.163 , pp. 94-105
    • Felmlee, T.1    Pellet, S.2    Welch, R.A.3
  • 16
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux JE, Braha O, Hobaugh MR, Song L, Cheley S, Shustak C, Bayley H (1994) Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc Natl Acad Sci USA 91:12828-12831
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 17
    • 0021747672 scopus 로고
    • Primary sequence of the alpha-toxin gene from Staphylococcus aureus Wood 46
    • Gray GS, Kehoe M (1984) Primary sequence of the alpha-toxin gene from Staphylococcus aureus Wood 46. Infect Immun 46:615-618
    • (1984) Infect Immun , vol.46 , pp. 615-618
    • Gray, G.S.1    Kehoe, M.2
  • 18
    • 0025947639 scopus 로고
    • Staphylococcus aureas α-toxin dual mechanisms of binding to target cells
    • Hildebrand A, Pohl M, Bhakdi S (1991) Staphylococcus aureas α-toxin dual mechanisms of binding to target cells. J Biol Chem 266:17195-17200
    • (1991) J Biol Chem , vol.266 , pp. 17195-17200
    • Hildebrand, A.1    Pohl, M.2    Bhakdi, S.3
  • 19
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel J-P, Koronakis V, Hughes C (1991) Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351:759-761
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.-P.1    Koronakis, V.2    Hughes, C.3
  • 20
    • 0025244264 scopus 로고
    • Effect of isolated C-terminal fragment of θ-toxin (perfringolysin O) on toxin assembly and membrane lysis
    • Iwamoto M, Ohno-Iwashita Y, Ando S (1990) Effect of isolated C-terminal fragment of θ-toxin (perfringolysin O) on toxin assembly and membrane lysis. Eur J Biochem 194:25-31
    • (1990) Eur J Biochem , vol.194 , pp. 25-31
    • Iwamoto, M.1    Ohno-Iwashita, Y.2    Ando, S.3
  • 21
    • 0028324930 scopus 로고
    • Small transmembrane pores created by staphylococcal alpha-toxin in T lymphocytes evoke internucleosomal DNA-degradation
    • Jonas D, Walev I, Berger T, Liebetrau M, Palmer M, Bhakdi S (1994) Small transmembrane pores created by staphylococcal alpha-toxin in T lymphocytes evoke internucleosomal DNA-degradation. Infect Immun 62:1304-1312
    • (1994) Infect Immun , vol.62 , pp. 1304-1312
    • Jonas, D.1    Walev, I.2    Berger, T.3    Liebetrau, M.4    Palmer, M.5    Bhakdi, S.6
  • 22
    • 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 (1987) Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane-damaging thiol-activated toxins. Infect Immun 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
  • 24
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • Menestrina G (1986) Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations. J Membr Biol 90:177-190
    • (1986) J Membr Biol , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 25
    • 0025685253 scopus 로고
    • Attenuated mutants of the intracellular bacterium Listeria monocytagenes obtained by single amino acid substitutions in listeriolysin O
    • Michel E, Reich KA, Favier R, Berche P, Cossart P (1990) Attenuated mutants of the intracellular bacterium Listeria monocytagenes obtained by single amino acid substitutions in listeriolysin O. Mol Microbiol 4:2167-2178
    • (1990) Mol Microbiol , vol.4 , pp. 2167-2178
    • Michel, E.1    Reich, K.A.2    Favier, R.3    Berche, P.4    Cossart, P.5
  • 26
    • 0023783454 scopus 로고
    • Protease nicked θ-toxin of Clostridium perfringens, a new membrane probe with no catalytic effect reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes
    • Ohno-Iwashita Y, Ywamoto M, Mitsui K, Ando S, Nagai K (1988) Protease nicked θ-toxin of Clostridium perfringens, a new membrane probe with no catalytic effect reveals two classes of cholesterol as toxin-binding sites on sheep erythrocytes. Eur J Biochem 176:95-101
    • (1988) Eur J Biochem , vol.176 , pp. 95-101
    • Ohno-Iwashita, Y.1    Ywamoto, M.2    Mitsui, K.3    Ando, S.4    Nagai, K.5
  • 27
    • 0028001461 scopus 로고
    • A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae
    • Owen HG, Boulnois GJ, Andrew PW, Mitchell TJ (1994) A role in cell-binding for the C-terminus of pneumolysin, the thiol-activated toxin of Streptococcus pneumoniae. FEMS Microbiol Lett 121:217-322
    • (1994) FEMS Microbiol Lett , vol.121 , pp. 217-322
    • Owen, H.G.1    Boulnois, G.J.2    Andrew, P.W.3    Mitchell, T.J.4
  • 29
    • 0027241025 scopus 로고
    • Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin
    • Palmer M, Weller U, Meßner M, Bhakdi S (1993b) Altered pore-forming properties of proteolytically nicked staphylococcal alpha-toxin. J Biol Chem 268:11963-11967
    • (1993) J Biol Chem , vol.268 , pp. 11963-11967
    • Palmer, M.1    Weller, U.2    Meßner, M.3    Bhakdi, S.4
  • 31
    • 0024720325 scopus 로고
    • The thiol-activated toxin streptolysin O does not require a thiol group for activity
    • Pinkney M, Beachey E, Kehoe M (1989) The thiol-activated toxin streptolysin O does not require a thiol group for activity. Infect Immun 57:2553-2558
    • (1989) Infect Immun , vol.57 , pp. 2553-2558
    • Pinkney, M.1    Beachey, E.2    Kehoe, M.3
  • 32
    • 0026587933 scopus 로고
    • Molecular determinants of Listeria monocytogenes pathogenesis
    • Portnoy DA, Chakraborty T, Goebel W, Cossart P (1992) Molecular determinants of Listeria monocytogenes pathogenesis. Infect Immun 60:1263-1267
    • (1992) Infect Immun , vol.60 , pp. 1263-1267
    • Portnoy, D.A.1    Chakraborty, T.2    Goebel, W.3    Cossart, P.4
  • 33
    • 0028567924 scopus 로고
    • Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin
    • Stanley P, Packman LC, Koronakis V, Hughes C (1994) Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin. Science 266:1992-1996
    • (1994) Science , vol.266 , pp. 1992-1996
    • Stanley, P.1    Packman, L.C.2    Koronakis, V.3    Hughes, C.4
  • 34
    • 0021844629 scopus 로고
    • Secondary structure and assembly mechanism of an oligomeric channel protein
    • Tobkes N, Wallace BA, Bayley H (1985) Secondary structure and assembly mechanism of an oligomeric channel protein. Biochemistry 24:1915-1920
    • (1985) Biochemistry , vol.24 , pp. 1915-1920
    • Tobkes, N.1    Wallace, B.A.2    Bayley, H.3
  • 35
    • 0027434924 scopus 로고
    • Staphylococcal alpha-toxin kills human keratinocytes by permeabilizing the plasma membrane for monovalent ions
    • Walev I, Martin E, Jonas D, Mohamadzadeh M, Müller-Klieser W, Kunz L, Bhakdi S (1993) Staphylococcal alpha-toxin kills human keratinocytes by permeabilizing the plasma membrane for monovalent ions. Infect Immun 61:4972-4979
    • (1993) Infect Immun , vol.61 , pp. 4972-4979
    • Walev, I.1    Martin, E.2    Jonas, D.3    Mohamadzadeh, M.4    Müller-Klieser, W.5    Kunz, L.6    Bhakdi, S.7
  • 37
    • 0028989337 scopus 로고
    • Potassium-inhibited processing of IL-1β in human monocytes
    • Walev I, Reske K, Palmer M, Valeva A, Bhakdi S (1995) Potassium-inhibited processing of IL-1β in human monocytes. EMBO J 14:1607-1614
    • (1995) EMBO J , vol.14 , pp. 1607-1614
    • Walev, I.1    Reske, K.2    Palmer, M.3    Valeva, A.4    Bhakdi, S.5
  • 38
    • 0028181019 scopus 로고
    • A pore-forming protein with a protease-activated trigger
    • Walker B, Bayley H (1994) A pore-forming protein with a protease-activated trigger. Protein Eng 7:91-97
    • (1994) Protein Eng , vol.7 , pp. 91-97
    • Walker, B.1    Bayley, H.2
  • 39
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore-forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • Walker B, Bayley H (1995) Key residues for membrane binding, oligomerization, and pore-forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J Biol Chem 270:23065-23071
    • (1995) J Biol Chem , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 40
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically engineered switch
    • Walker B, Braha O, Cheley S, Bayley H (1995) An intermediate in the assembly of a pore-forming protein trapped with a genetically engineered switch. Curr Biol 2:99-105
    • (1995) Curr Biol , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 41
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis
    • Walker B, Krishnasastry M, Zorn L, Bayley H (1992) Assembly of the oligomeric membrane pore formed by staphylococcal alpha-hemolysin examined by truncation mutagenesis. J Biol Chem 267:21782-21786
    • (1992) J Biol Chem , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 42
    • 0027480752 scopus 로고
    • Functional complementation of staphylococcal alpha-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop
    • Walker B, Krishnasastry M, Bayley H (1993) Functional complementation of staphylococcal alpha-hemolysin fragments. Overlaps, nicks, and gaps in the glycine-rich loop. J Biol Chem 268:5285-5292
    • (1993) J Biol Chem , vol.268 , pp. 5285-5292
    • Walker, B.1    Krishnasastry, M.2    Bayley, H.3
  • 44
    • 0028341551 scopus 로고
    • Identification of a putative membrane-inserted segment in the alpha-toxin of Staphylococcus aureus
    • Ward RJ, Palmer M, Leonard K, Bhakdi S (1994) Identification of a putative membrane-inserted segment in the alpha-toxin of Staphylococcus aureus. Biochemistry 33:7477-7484
    • (1994) Biochemistry , vol.33 , pp. 7477-7484
    • Ward, R.J.1    Palmer, M.2    Leonard, K.3    Bhakdi, S.4
  • 45
    • 0026080402 scopus 로고
    • Pore-forming cytolysins of gram-negative bacteria
    • Welch RA (1991) Pore-forming cytolysins of gram-negative bacteria. Mol Microbiol 5:521-529
    • (1991) Mol Microbiol , vol.5 , pp. 521-529
    • Welch, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.