Abstract
Among the ca. 325 protein toxins produced by gram-positive and gram-negative bacteria so far identified (Alouf 2000), at least 115 (35%) belong to the group of the so-called membrane-damaging toxins (MDTs). The most characteristic feature of these effectors is to damage or disrupt the cytoplasmic phospholipid bilayer membrane (7–9nm) of appropriate human and (or) animal cells. The impairment of membrane integrity causes osmotic imbalance, reflected by cell swelling due to water influx and dissipation of electrochemical gradients, which may lead to cell lysis and death (Bernheimer 1970; Alouf 1977; Arbuthnott 1982).
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References
Abrami L, Fivaz M, Glauser P-E, Parton RG, van der Goot FG (1998) A pore-forming toxin interact with a GPI-anchored protein and causes vacuolation of the endoplasmic reticulum. J Cell Biol 140:525–540
Alouf JE (1977) Cell membranes and cytolytic toxins. In: Cuatrecasas P (ed) The specificity and action of animal, bacterial and plant toxins. Chapman and Hall, London, pp 210–270
Alouf JE (1980) Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol Ther 11:661–717
Alouf JE (1999) Introduction to the family of the structurally related cholesterol-binding cytolysins (sulfhydryl-activated toxines. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial proteins toxins. Academic, London, pp 443–56
Alouf JE (2000) Bacterial protein toxins: an overview. In: Hoist O (ed) Bacterial toxins. Methods and protocols. Humana, Totowa, NJ, pp 1–26
Alouf JE, Freer JH (1999) The comprehensive sourcebook of bacterial protein toxines. Academic, London
Alouf JE, Palmer M (1999) Streptolysin O. In: Alouf JE, Freer JH (eds) The comprehensive source book of bacterial protein toxins Academic, London, pp 459–473
Alouf JE, Georffroy C, Pattus F, Verger R (1984) Surface properties of bacterial sulfhydryl-activated cytolytic toxins. Interaction with monomolecular films of phosphatidylcholine and various sterols. Eur J Biochem 141:205–210
Alouf JE, Dufourcq J, Siffert O, Thiaudiere E, Georffroy C (1989) Interaction of staphylococcal deltatoxin and synthetic analogues with erythrocytes and phospholipid vesicles. Biological and physical properties of the amphipathic peptides. Eur J Biochem 183:381–390
Arbuthnott JP (1982) Bacterial cytolysins (membranes damaging toxins) In: Cohen L, van Heynigen S (eds) Molecular action of toxins and viruses. Elsevier, New York, pp 107–109
Arvand M, Bhakdi S, Dahlback B, Preissner KT (1990) Staphylococcus aureus alphα-toxin attack on human platelets promotes assembly of the prothrombinase complex. J Biol Chem 265:14377–14381
Balfanz J, Rautenberg P, Ullmann U (1996) Molecular mechanisms of action of bacterial exotoxins. Zbl Bakt 284:170–206
Bayley H (1997) Toxin structure: part of a hole? Curr Biol 7:R763–R767
Bernheimer AW (1970) Cytolytic toxins of bacteria, vol 1. In: Ajl S, Kadis S, Montie TC (eds) Microbial toxins. Academic, New York, pp 183–212
Bernheimer AW, Rudy B (1986) Interactions between membranes and cytolytic peptides. Biochim Biophys Acta 864:123–141
Bhakdi S, Tranum-Jensen J (1984) Mechanism of complement cytolysis and the concept of channelforming proteins. Philos Trans R Soc London Ser B 306:311–324
Bhakdi S, Tranum-Jensen J (1988) Damage to cell membranes by pore-forming bacterial cytolysins. Prog Allergy 40:1–43
Bhakdi S, Tranum-Jensen J (1991) Alphα-toxin of Staphylococcus aureus. Microbiol Rev 55:733–751
Bhakdi S, Muhly M, Korom S, Hugo F (1989) Release of interleukin-1 beta associated with potent cytocidal action of staphylococcal alphα-toxin on human monocytes. Infect Immun 57:3512–3519
Bhakdi S, Muhly M, Korom S, Schmidt G (1990) Effects of Escherichia coli hemolysin on human monocytes. Cytocidal action and stimulation of interleukin 1 release. J Clin Invest 85:1746–1753
Bhakdi S, Bayley H, Valeva A, Walev I, Walker B, Kehoe M, Palmer M (1996) Staphylococcal alphatoxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch Microbiol 165:73–79
Billington SJ, Jost BH, Songer JG (2000) Thiol-activated cytolysins: structure, function and role in pathogenesis. FEMS Microbiol Lett 182:197–205
Braun V, Focareta T (1991) Pore-forming bacterial protein hemolysins (cytolysins). Crit Rev Microbiol 18:115–158
Braun V, Hertle R (1999) The family of serration and proteins cytolysins. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 349–361
Braun JS, Novak R, Gao G, Murray PJ, Shenep JL (1999) Pneumolysin, a protein toxin of Streptococcus pneumoniae, induces nitric oxide production from macrophages. Infect Immun 67:3750–3756
Bryant AE, Stevens DL (1996) Phospholipase C and perfringolysin O from Clostridium perfringens upregulate endothelial cell-leukocyte adherence molecule 1 and intercellular leukocyte adherence molecule 1 expression and induce interleukin-8 synthesis in cultured human umbilical vein endothelial cells. Infect Immun 64:358–362
Buckley AT (1999) The channel-forming toxin aerolysin. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 362–372
Coote J (1996) The RTX toxins of gram-negative bacterial pathogens modulators of the host immune response. Rev Med Microbiol 7:53–62
Czajkowsky DM, Sheng S, Shao Z (1998) Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers. J Mol Biol 276:325–330
Derewenda ZS, Martin TW (1998) Structure of the gangrene alphα-toxin: the beauty in the beast. Nat Struct Biol 5:659–662
Dobereiner A, Schmid A, Ludwig A, Goebel W, Benz R (1996) The effects of calcium and other polyvalent cations on channel formation by Escherichia coli alpha-hemolysin in red blood cells and lipid bilayer membranes. Eur J Biochem 240:454–460
Dobrindt U, Hacker J (1999) Plasmids, phages and pathologicity islands: lesson on the evolution of bacterial toxins. In: Alouf JE, Free JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 3–23
Dourmashkin RR, Rosse WF (1966) Morphologic changes in the membranes of red blood cells undergoing hemolysis. Am J Med 41:699–710
Dufourcq J, Castano S, Talbot JC (1999) Deltα-toxin related haemolytic toxins and peptidic analogues. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 386–401
Ellemor DM, Baird RN, Awad MM, Boyd RL, Rood JI, Emmins JJ (1999) Use of genetically manipulated strains of Clostridium perfringens reveals that both alphα-toxin and thetα-toxin are required for vascular leukocytosis to occur in experimental gas gangrene. Infect Immun 67:4902–4907
Finlay BB, Falkow S (1997) Common themes in microbial pathogenicity revisited. Microbiol Mol Biol Rev 61:136–169
Freer JH, Birkbeck TH (1982) Possible conformation of delta-lysin, a membrane-damaging peptide of Staphylococcus aureus. J Theor Biol 94:535–540
Freer JH, Arbuthnott JP (1983) Toxins of Staphylococcus aureus. Pharmacol. Ther 19:55–106
Frey J (1995) Virulence in Actinobacillus pleuropneumoniae and RTX toxins. Trends Microbiol 3:257–261
Gaillard JL, Berche P, Sansdnetti P (1986) Transposon mutagenesis as a tool to study the role of hemolysin in the virulence of Listeria monocytogenes. Infect Immun 52:50–55
Gilbert RJ, Rossjohn J, Parker MW, Tweten RK, Morgan PJ, Mitchell TJ, Errington N, Rowe AJ, Andrew PW, Byron O (1998) Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae. J Mol Biol 284:1223–1237
Gilbert RJ, Jimenez JL, Chen S, Tickle IJ, Rossjohn J, Parker M, Andrew PW, Saibil HR (1999) Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Cell 97:647–655
Gilmore MS, Callegan MC, Jett BD (1999) Enterococcus faecalis cytolysin and Bacillus cereus bi-and tricomponent haemolysins. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 419–432
Goebel W, Kreft J (1997) Cytolysins and the intracellular life of bacteria. Trends Microbiol 5:86–88
Gouaux E (1997) Channel-forming toxins: tales of transformation. Curr Opin Struct Biol 7:566–573
Gouaux E (1998) Alpha-hemolysin from Staphylococcus aureus: an archetype of beta-barrel, channelforming toxins. J Struct Biol 121:110–122
Gouaux E, Hobaugh M, Song L (1997) Alpha-hemolysin, gamma-hemolysin, and leukocidin from Staphylococcus aureus: distant in sequence but similar in structure. Protein Sci 6:2631–2635
Grimminger F, Sibelius U, Bhakdi S, Suttorp N, Seeger W (1991) Escherichia coli hemolysin is a potent inductor of phosphoinositide hydrolysis and related metabolic responses in human neutrophils. J Clin Invest 88:1531–1539
Hackett SP, Stevens DL (1992) Streptococcal toxic shock syndrome: synthesis of tumor necrosis factor and interleukin-1 by monocytes stimulated with pyrogenic exotoxin A and streptolysin O. J Infect Dis 165:879–885
Harshman S, Boquet P, Duflot E, Alouf JE, Montecucco C, Papini E (1989) Staphylococcal alphα-toxin: a study of membrane penetration and pore formation. J Biol Chem 14978–14984
Henderson B, Poole S, Wilson M (1996) Bacterial modulins: a novel class of virulence factors which cause host tissue pathology by inducing cytokine synthesis. Microbiol Rev 60:316–341
Henderson B, Wilson M, Wren B (1997) Are bacterial exotoxins cytokine network regulators? Trends Microbiol 5:454–458
Houldsworth S, Andrew PW, Mitchell TJ (1994) Pneumolysin stimulates production of tumor necrosis factor alpha and interleukin-1 beta by human mononuclear phagocytes. Infect Immun 62:1501–1503
Jacobs T, Darji A, Weiss S, Chakraborty T (1999) Listeriolysin the thiol-activated haemolysin of Listeria monocytogenes. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 511–521
Jost BH, Songer JG, Billington SJ (1999) An Arcanobacterium (Actinomyces) pyogenes mutant deficient in production of the pore-forming cytolysin pyolysin has reduced virulence. Infect Immun 67:1723–1728
Kaper J, Hacker J (2000) Pathogenicity islands and other mobile virulence elements. ASM, Washington D.C.
Kayal S, Lilienbaum A, Poyart C, Memet S, Israel A, Berche P (1999) Listeriolysin O-dependent activation of endothelial cells during infection with Listeria monocytogenes: activation of NF-kappa B and upregulation of adhesion molecules and chemokines. Mol Microbiol 31:1709–1722
Köller M, Hensler T, König B, Prévost G, Alouf J, König W (1993) Induction of heat-shock proteins by bacterial toxins, lipid mediators and cytokines in human leukocytes. Zentralbl Bakteriol 278:365–376
König B, König W (1994) Effect of growth factors on Escherichia coli alpha-hemolysin-induced mediator release from human inflammatory cells: involvement of the signal transduction pathway. Infect Immun 62:2085–2093
König B, Köller M, Prévost G, Piémont Y, Alouf JE, Schreiner A, König W (1994a) Activation of human effector cells by different bacterial toxins (leukocidin, alveolysin, and erythrogenic toxin A): generation of interleukin-8. Infect Immun 62:4831–837
König B, Ludwig A, Goebel W, König W (1994b) Pore formation by the Escherichia coli alphahemolysin: role for mediator release from human inflammatory cells. Infect Immun 62:4611–4617
König B, Vasil ML, König W (1997) Role of hemolytic and nonhemolytic phospholipase C from Pseudomonas aeruginosa for inflammatory mediator release from human granulocytes. Int Arch Allergy Immunol 112:115–124
König B, Drynda A, Ambrosch A, König W (1999) Toxin-induced modulation of inflammatory processes. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 637–656
Krause KH, Fivaz M, Monod A, van der Goot FG (1998) Aerolysin induces G-protein activation and Ca2+ release from intracellular stores in human granulocytes. J Biol Chem 273:18122–18129
Ladant D, Ullmann A (1999) Bordetella pertussis adenylate cyclase: a toxin with multiple talents. Trends Microbiol 7:172–176
Lally ET, Hill RB, Kieba IR, Korostoff J (1999) The interaction between RTX toxins and target cells. Trends Microbiol 7:356–361
Launay JM, Alouf JE (1979) Biochemical and ultrastructural study of the disruption of blood platelets by streptolysin O. Biochim Biophys Acta 556:278–291
Launay JM, Georffroy C, Costa JL, Alouf JE (1984) Purified-SH-activated toxins (streptolysin O, alveolysin): new tools for determination of platelet enzyme activities. Thromb Res 33:189–196
Launay JM, Geoffroy C, Mutel V, Buckle M, Cesura A, Alouf JE, Da Prada M (1992) One-step purification of the serotonin transporter located at the human platelet plasma membrane. J Biol Chem 267:11344–11351
Lesieur C, Vecsey-Semjn B, Abrami L, Fivaz M, van der Goot FG (1997) Membrane insertion: the strategy of toxins. Mol Membr Biol 14:45–64
Ludwig A, Goebel W (1999) The family of the multigenic encoded RTX toxins. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 330–348
Mac Farlane MG, Knight BCJG (1941) The biochemistry of bacterial toxins. I. Lecithinase activity of CI. welchii toxins. Biochem J 35:884–902
May AK, Sawyer RG, Gleason T, Whitworth A, Pruett TL (1996) In vivo cytokine response to Escherichia coli alpha-hemolysin determined with genetically engineered hemolytic and nonhemolytic E. coli variants. Infect Immun 64:2167–2171
Mayer MM (1972) Mechanism of cytolysis by complement. Proc Natl Acad Sci USA 69:2954–2958
Menestrina G (2000) Use of Fourier-transformed infrared spectra copy for secondary structure determination of staphylococcal pore-forming toxins. In: Hoist O (ed) Bacterial toxins. Methods and protocols. Humana, Totowa, NJ, pp 115–132
Menestrina G, Bashford CL, Pasternak CA (1990) Pore-forming toxins: experiments with S. aureus alphα-toxin, C. perfringens thetα-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells. Toxicon 28:477–491
Menestrina G, Vécsey-Semjén B (1999) Biophysical methods and model membranes for the study of bacterial pore-forming toxins. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 287–309
Mims C, Dimmock N, Nash A, Stephen J (2000) Mims’ pathogenesis of infectious diseases. Academic, London
Mitchell TJ (1999) Pneurolysin: structure, function and role in disease. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial proteins toxins. Academic, London, pp 476–495
Morgan PJ, Hyman SC, Byron O, Andrew PW, Mitchell TJ, Rowe AJ (1994) Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J Biol Chem 269:25315–25320
Morgan PJ, Hyman SC, Rowe AJ, Mitchell TJ, Andrew PW, Saibil HR (1995) Subunit organization and symmetry of pore-forming oligomeric pneumolysin. FEBS Lett. 371:77–80
Morgan PJ, Andrew PW, Mitchell TJ (1996) Thiol-activated cytolysins. Rev Med Microbiol 7:221–229
Naylor CE, Eaton JT, Howells A, Justin N, Moss DS, Titball RW, Basak AK (1998) Structure of the key toxin in gas gangrene. Nat Struct Biol 5:738–746
Nelson KL, Brodsky RA, Buckley JT (1999) Channels formed by subnanomolar concentrations of the toxin aerolysin trigger apoptosis of T lymphomas. Cell Microbiol 1:69–74
Nishibori T, Xiong H, Kawamura I, Arakawa M, Mitsuyama M (1996) Induction of cytokine gene expression by listeriolysin O and roles of macrophages and NK cells. Infect Immun 64:3188–3195
Olson R, Nariya H, Yokota K, Kamio Y, Gouaux E (1999) Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat Struct Biol 6:134–140
Palmer M, Saweljew P, Vulicevic I, Valeva A, Kehoe M, Bhakdi S (1996) Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis. J Biol Chem 271:26664–26667
Parker MW, Buckley JT, Postma JPM, Tucker AD, Leonard K, Pattus F, Tsernoglou D (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367:292–295
Parker MW, van der Goot FG, Buckley JT (1996) Aerolysin-the ins and outs of a channel forming toxin. Mol Microbiol 19:205–212
Paton JC (1996) The contribution of pneumolysin to the pathogenicity of Streptococcus pneumoniae. Trends Microbiol 4:103–106
Pedelacq JD, Maveyraud L, Prévost G, Baba-Moussa L, Gonzalez A, Courcelle E, Shepard W, Monteil H, Samama JP, Mourey L (1999) The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins. Structure 7:277–287
Prévost G (1999) The bi-component staphylococcal leucodidins and gamma-haemolysins (toxins). In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 402–418
Rossjohn J, Buckley JT, Hazes B, Murzin AG, Read RJ, Parker MW (1997a) Aerolysin and pertussis toxin share a common receptor-binding domain. EMBO J 16:3426–3434
Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, Parker MW (1997b) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89:685–692
Rossjohn J, Gilbert RJ, Crane D, Morgan PJ, Mitchell TJ, Rowe AJ, Andrew PW, Paton JC, Tweten RK, Parker MW (1998) The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae. J Mol Biol 284:449–461
Rossjohn J, Tweten RK, Rood JI, Parker MW (1999) Perfringolysin O. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 496–510
Roth JA, Bolin CA, Brogden KA, Minion C, Wannemuehler MJ (1995) Virulence mechanisms in bacterial pathogens. ASM, Washington D.C.
Rowe GE, Welch RA (1994) Assays of hemolytic toxins. Meth Enzymol 235:657–667
Rubins JB, Charboneau D, Fasching C, Berry AM, Paton JC, Alexander JE, Andrew PW, Mitchell TJ, Janoff EN (1996) Distinct roles for pneumolysin’s cytotoxic and complement activities in the pathogenesis of pneumococcal pneumonia. Am J Respir Crit Care Med 153:1339–1346
Ruiz N, Wang B, Pentland A, Caparon M (1998) Streptolysin O and adherence synergistically modulate proinflammatory responses of keratinocytes to group A streptococci. Mol Microbiol 27:337–346 Salyers AA, Whitt D (1994) Bacterial pathogenesis: a molecular approach. ASM, Washington D.C.
Sato N, Kurotaki H, Watanabe T, Mikami T, Matsumoto T (1998) Use of hemoglobin as an iron source by Bacillus cereus. Biol Pharm Bull 21:311–314
Schmiel DH, Miller VL (1999) Bacterial phospholipases and pathogenesis Microbes Infect 1:1103–1112
Schmitt CK, Meysick KC, O’Brien AD (1999) Bacterial toxins: friends or foes? Emerg Infect Dis 5:224–234
Sekiya K, Satoh R, Danbara H, Futaesaku Y (1993) A ring-shaped structure with a crown formed by streptolysin O on the erythrocyte membrane. J Bacteriol 175:5953–5961
Sekiya K, Satoh R, Danbara H, Futaesaku Y (1996) Electron microscopic evaluation of a two-step theory of pore formation by streptolysin O. J Bacteriol 178:6998–7002
Sellman BR, Kagan BL, Tweten RK (1997) Generation of a membrane-bound, oligomerized pre-pore complex is necessary for pore formation by Clostridium septicum alpha toxin. Mol Microbiol 23:551–558
Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for poreforming toxins. Cell 99:293–299
Shepard LA, Heuck AP, Hamman BD, Rossjohn J, Parker MW, Ryan KR, Johnson AE, Tweten RK (1998) Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37:14563–14574
Shinoda S (1999) Haemolysins of Vibrio cholerae and other Vibrio species. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 373–385 Sibelius U, Schulz EC, Rose F, Hattar K, Jacobs T, Weiss S, Chakraborty T, Seeger W, Grimminger F (1999) Role of Listeria monocytogenes exotoxins listeriolysin and phosphatidylinositol-specific phospholipase C in activation of human neutrophils. Infect Immun 67:1125–1130
Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE (1996) Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274:1859–1866 Songer JG (1997) Bacterial phospholipases and their role in virulence. Trends Microbiol 5:156–161
Staali L, Monteil H, Colin DA (1998) The staphylococcal pore-forming leukotoxins open Ca2+ channels in the membrane of human polymorphonuclear neutrophils. J Membr Biol 162:209–216
Stevens DL, Bryant AE (1999) The pathogenesis of shock and tissue injury in clostridial gas gangrene. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 628–636
Stevens DL, Tweten RK, Awad MM, Rood JI, Bryant AE (1997) Clostridial gas gangrene: evidence that alpha and theta toxins differentially modulate the immune response and induce acute tissue necrosis. J Infect Dis 176:189–195
Suttorp N, Fuhrmann M, Tannert-Otto S, Grimminger F, Bhadki S (1993) Pore-forming bacterial toxins potently induce release of nitric oxide in porcine endothelial cells. J Exp Med 178:337–341
Tanabe Y, Xiong H, Nomura T, Arakawa M, Mitsuyama M (1999) Induction of protective T cells against Listeria monocytogenes in mice by immunization with a listeriolysin O-negative avirulent strain of bacteria and liposome-encapsulated listeriolysin O. Infect Immun 67:568–575
Tang P, Rosenshine I, Cossart P, Finlay BB (1996) Listeriolysin O activates mitogen-activated protein kinase in eucaryotic cells. Infect Immun 64:2359–2361
Tatum FM, Briggs RE, Sreevatsan SS, Zehr ES, Ling Hsuan S, Whiteley LO, Ames TR, Maheswaran SK (1998) Construction of an isogenic leukotoxin deletion mutant of Pasteurella haemolytica serotype 1: characterization and virulence. Microb Pathog 24:37–46
Thelestam M, Mollby R (1979) Classification of microbial, plant and animal cytolysins based on their membrane-damaging effects of human fibroblasts. Biochim Biophys Acta 557:156–169
Tilney LG, Portnoy DA (1989) Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 109:1597–1608
Titball RW (1999) membrane-damaging and cytotoxic phospholipases. In: Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 311–329
Tweten RK (1995) Pore forming toxins in gram positive bacteria. In: Roth JA, Bolin CA, Brogden KA, Minion C, Wannemuehler MJ (eds) Virulence mechanisms of bacterial pathogens. ASM, Washington D.C, pp 207–229
Tweten RK, Sellman B (1999) Clostridium septicum pore-forming and lethal x-toxin. In Alouf JE, Freer JH (eds) The comprehensive sourcebook of bacterial protein toxins. Academic, London, pp 435–442
Valeva A, Palmer M, Bhakdi S (1997) Staphylococcal alphα-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 36:13298–13304
van der Goot FG (2000) Plasticity of the transmembrane P-barrel. Trends Microbiol 8:89–90
Vandana S, Raje M, Krishnasastry MV (1997) The role of the amino terminus in the kinetics and assembly of alpha-hemolysin of Staphylococcus aureus. J Biol Chem 272:24858–24863
Walker B, Bayley H (1995) Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal a-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J Biol Chem 270:23065–23071
Weiglein I, Goebel W, Troppmair J, Rapp UR, Demuth A, Kuhn M (1997) Listeria monocytogenes infection of HeLa cells results in listeriolysin O-mediated transient activation of the Raf-MEK-MAP kinase pathway. FEMS Microbiol Lett 148:189–195
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Alouf, J.E. (2001). Pore-Forming Bacterial Protein Toxins: An Overview. In: van der Goot, F.G. (eds) Pore-Forming Toxins. Current Topics in Microbiology and Immunology, vol 257. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56508-3_1
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