A 116-year story of bacterial protein toxins (1888-2004): From "diphtheritic poison" to molecular toxinology

The Comprehensive Sourcebook of Bacterial Protein Toxins

Volumn , Issue , 2006, Pages 3-21

  Alouf, Joseph E ^a  

^a INSTITUT PASTEUR   (France)

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EID: 84882889982     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012088445-2/50006-8     Document Type: Chapter

References (218)

1. Abe J., Takeda T., Watanabe H., Nakao H., Kobayashi N., Leung D.Y.M., Kohsaka T. Evidence for superantigen production by Yersinia pseudotuberculosis. J. Immunol. 1993, 151:4183-4188.
2. Achalme P. Examen bactériologique d'un cas de rhumatisme articulaire aigu mort de rhumatisme cérébral C. R. Soc. Biol. 1891, 3:651-658.
3. Ahrens P., Andresen L.O. Cloning and sequence analysis of genes encoding Staphylococcus hyicus exfoliative toxin types A, B, C, and D. J. Bacteriol. 2004, 186:1833-1837.
4. Aktories K. Glucolysating and deamidating bacterial protein toxins. Bacterial Proteins Toxins 2003, 229-243. ASM Press. D. Burrs, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
5. Aktories K., Barth H. Clostridium botulinum C2 toxin-New insights into the cellular up-take of the actin-ADP ribosylating toxin. Int. J. Med. Microbiol. 2004, 293:557-564.
6. Alouf J.E. Streptococcal toxins (streptolysin Ostreptolysin S, erythrogenic toxin). Pharmacol. Ther. 1980, 11:211-270.
7. Alouf J.E. Pore-forming bacterial protein toxins. Curr. Topics Microbiol. Immunol. 2000, 257:1-11.
8. Alouf J.E. Cholesterol-binding cytolytic protein toxins. Int. J. Med. Microbiol. 2001, 290:351-356.
9. Alouf J.E. Molecular features of the cytolytic pore-forming bacterial protein toxins. Folia Microbiol (Prague) 2003, 48:5-16.
10. Alouf J.E., Raynaud M. Suppression du pouvoir inhibiteur du fer sur la toxinogénèse diphtérique par la levure. Ann. Inst. Pasteur. 1960, 99:708-722.
11. Alouf J.E., Jolivet-Reynaud C. Purification and characterization of Clostridium perfringens delta-toxin. Infect. Immun. 1981, 31:536-546.
12. Alouf J.E., Müller-Alouf H. Staphylococcal and streptococcal superantigens: molecular, biological, and clinical aspects. Int. J. Med. Microbiol. 2003, 292:429-440.
13. Arbuthnott J.P. Staphylococcal α-toxin. Microbial Toxins 1970, 189-236. Academic Press, Washington, D.C. S.E. Ajl, S. Kadis, T.C. Montie (Eds.).
14. Barbieri J.T., Burns D.T. Bacterial toxins that covalently modify eukaryotic proteins by ADP-ribosylation. Bacterial Proteins Toxins 2003, 215-228. ASM Press, New York. D. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
15. Barbieri L., Battelli M.G., Stirpe F. Ribosomes inactivating proteins from plants. Biochim. Biophys. Acta 1993, 1154:237-282.
16. Barksdale L., Arden S.B. Persisting bacteriophage infections, lysogeny and phage conversion. Ann. Rev. Microbiol. 1974, 28:265-299.
17. Barth H., Aktories K., Popoff M.R., Stiles B.G. Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol. Mol. Biol. Rev. 2004, 68:373-402.
18. Beall F.A., Taylor M.J., Thorne C.B. Rapid lethal effects in rats of a third component upon fractionating the toxin of Bacillus anthracis. J. Bacteriol. 1962, 83:1274-1280.
19. Behring E., Kitasato S. Ueber das Zustandekommen der Diphtherie-Immunität und der Tetanus-Immunität bei Thieren. Deutsch. Med. Wochenschr. 1890, 16:1113-1114.
20. Behring E. Die Blutserumtherapie bei Diphtherie und Tetanus. Z. Hyg. Infectionskrankh. 1882, 12:1-9.
21. Bergdoll M.S., Crass B.A., Reiser R.F., Robbins R.N., Davis J.P. A new staphylococcal enterotoxin, enterotoxin F associated with toxic-shock syndrome Staphylococcus aureus isolates. Lancet 1981, i:1017-1021.
22. Bernheimer A.W. Parallelism in the lethal and hemolytic activity of the toxin of Cl. septicum. J. Exp. Med. 1944, 80:309-320.
23. Bernheimer A.W., Rudy B. Interactions between membranes and cytolytic peptides. Biochim. Biophys. Acta 1986, 864:123-141.
24. Billington S.J., Jost B.H., Songer J.G. Thiol-activated cytolysins: structure, function, and role in pathogenesis. FEMS Microbiol; Lett. 2000, 182:197-205.
25. Bingel K.F. Neue Untersuchungen zur Scharlachätiologie. Deutsch. Med. Wochenschr. 1949, 127:703-706.
26. Bisno A.L., Brito M.O., Collins C.M. Molecular basis of group A streptococcal virulence. The Lancet 2003, 3:191-199.
27. Braun V., Hertle R. The family of Serratia and Proteus cytolysins. The Comprehensive Sourcebook of Bacterial Protein Toxins 1999, 349-361. Academic Press, Washington, D.C. J.E. Alouf, J.H. Freer (Eds.).
28. Bruschettini A. Sulla diffusione del veleno del tetano nell'organismo. Riforma Medica 1892, 8:256-259.
29. Bull C.G., Pritchett I.W. Toxin and antitoxin of and protective inoculation against Bacillus welchii. J. Exp. Med. 1917, 26:119.
30. Carle A., Rattone G. Studio sull'oziologia del tetano. Giorn. Accad. Med. Torino. 1884, 32:174-179.
31. Carnoy C., Müller-Alouf H., Desreumaux P., Mullet C., Grangette C., Simonet M. The superantigenic toxin of Yersinia pseudotuberculosis: a novel virulence factor?. Int. J. Med. Microbiol. 2000, 290:477-482.
32. Carnoy C., Floquet S., Marceau M., Sebbane F., Haentjens-Herwegh S., Devalckenaere A., Simonet M. The superantigen gene ypm is located in an unstable chromosomal locus of Yersinia pseudotuberculosis. J Bacteriol. 2002, 184:4489-4499.
33. Carpusca I., Schirmer J., Aktories K. Two-site autoinhibition of the ADP-ribosylating mosquitocidal toxin (MTX) from Bacillus sphaericus by its 70-kDa ricin-like binding domain. Bichemistry 2004, 43:12009-12019.
34. Chaudry G.J., Moayeri M., Liu S., Leppla S.H. Quickening the pace of anthrax research: three advances point towards possible therapies. Trends Microbiol. 2001, 10:58-62.
35. Cole A.R., Gibert M., Popoff M., Moss D.S., Titball R.W., Basak A.K. Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin. Nature Struct. Mol. Biol. 2000, 1:797-798.
36. Collier R.J. Diphtheria toxin: mode of action and structure. Bacteriol. Rev. 1975, 39:54-85.
37. Collier R.J. Inhibition of protein synthesis by exotoxins from Corynebacterium diphtheriae and Pseudomonas aeruginosa. The Specificity and Action of Animal, Bacterial, and Plant Toxins 1977, 67-98. Chapman and Hall, London. P. Cuatrecasas (Ed.).
38. Confer D.L., Eaton J.W. Phagocyte impotence caused by an invasive adenylate cyclase. Science 1982, 217:948-950.
39. Cotter P.A., Jones A.M. Phosphorylated control of virulence gene expression in Bordetella. Trends Microbiol. 2003, 11:367-373.
40. Coye L.H., Collins C.M. Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes. Mol. Microbiol. 2004, 54:89-98.
41. Cunningham M.W. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 2000, 13:470-511.
42. Davaine C. Recherche sur les infusoires du sang dans la maladie connue sous le nom de sang de rate. C. R. Acad. Sci. 1862, 57:220-223.
43. De S.N. Enterotoxicity of bacteria-free culture filtrate of Vibrio cholerac. Nature 1959, 183:1533-1534.
44. De Christmas M.J. Recherche expérimentale sur la suppuration. Ann Inst. Pasteur. 1888, 2:469-478.
45. Derewenda Z.S., Martin T.W. Structure of the α-toxin: the beauty in the beast. Nature Structur. Biol. 1998, 5:659-662.
46. Dick G.F., Dick G.H. The etiology of scarlet fever. JAMA 1924, 82:301-302.
47. Dick G.F., Dick G.H. A skin test for susceptibility to scarlet fever. JAMA 1924, 82:265-266.
48. Dreyfus L.A. Cytolethal distending toxins. Bacterial Protein Toxins 2003, 257-270. ASM Press, London. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
49. Dutta N.K., Panse M.W., Kulkakarni D.R. Role of cholera toxin in experimental cholera. J. Bacteriol. 1959, 78:594-595.
50. Endo Y., Tsurgi K., Yutsudo T., Takeda Y., Igasawara T., Igarashi E. Site of action of a verotoxin (VT2) from Escherichia coli O157:H7 and of shiga toxin on eukaryotic ribosomes. Eur. J. Biochem 1988, 171:45-50.
51. Eisenberg P. Sur la toxine du bacille du charbon symptomatique. C. R. Soc. Biol. (Paris) 1907, 613-615.
52. Faber K. Die Pathogenie des Tetanos. Berl. Klin. Wochensch. 1890, 27:717-720.
53. Finkelstein R.A., LoSpalluto J.J. Pathogenesis of experimental cholera: preparation and isolation of choleragen and choleragenoid. J. Exp. Med. 1969, 130:185-202.
54. Fivaz M., Abrami L., Tsitrin Y., van der Goot F.G. Curr. Top. Microbiol. Immunol. 2001, 257:35-52.
55. Fivaz M., Abrami L., Tsitrin Y., van der Goot F.G. Curr. Top. Microbiol. Immunol. 2001, 257:85-111.
56. Flateau G., Lemichez E., Gauthier M., Chardin P., Paris S., Fiorentini C., Boquet P. Toxin-induced activation of the G protein Rho by deamidation of glutamine. Nature 1997, 389:758-762.
57. Franco A.A., Mundy L.M., Truc M., Wu S., Kaperk J.B., Sears S.L. Cloning and characterization of the Bacteriodes fragilis metalloprotease toxin gene. Infect. Immun. 1997, 65:1007-1013.
58. Freeman V.J. Studies on the virulence of bacteriophage-infected strains of Corynebacterium diphtheriae. J. Bacteriol. 1951, 61:675-688.
59. Frobisher M., Brown J.H. Transmissible toxinogenicity of streptococci. Bull. Johns Hopkins Hosp. 1927, 41:167-173.
60. Gerlach D., Reichardt W., Fleischer B., Schmidt K.H. Separation of mitogenic and pyrogenic activities from so-called erythrogenic toxin type B (Streptococcal proteinase). Zentralbl. Bakteriol. 1994, 280:507-514.
61. Gill D.M., Pappenheimer A.M., Brown R., Kurnick J.J. Studies on the mode of action of diphtheria toxin. VII. Toxinstimulated hydrolysis of nicotinamide adening dinucleotide in mammalian cell extracts. J. Exp. Med. 1969, 129:1-21.
62. Glenny A.T., Sudmersen H.J. Note on the production of immunity to diphtheria toxin. J. Hyg. (London) 1921, 20:176-220.
63. Goranson-Siekierke J., Holmes R.K. Regulation of diphtheria toxin production: characterization of the role of iron and the diphtheria toxin repressor. The Comprehensive Sourcebook of Bacterial Protein Toxins 1999, 94-103. Academic Press, London. J.E. Alouf, J.H. Freer (Eds.).
64. Groman N.B. Evidence for the induced nature of the change from non toxinogenicity in Corynaebacterium diphtheriae as a result of exposure to specific bacteriophage. J. Bacteriol. 1953, 66:134-191.
65. Hacker J., Kaper J.B. Pathogenicity islands and the evolution of microbes. Ann. Rev. Microbiol. 2000, 54:641-679.
66. Hacker J., Hochhut B., Middendorf B., Schneider G., Buchrieser C., Gottschalk G., Dobrindt U. Pathogenomics of mobile genetic elements of toxigenic bacteria. Int. J. Med. Microbiol. 2004, 293:453-461.
67. Han S., Tainer J.A. The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases. Int. J. Med. Microbiol. 2002, 291:523-529.
68. Hanakawa Y., Schechter N.M., Lin C., Nishifugi K., Amagai M., Stanley J.R. Enzymatic and molecular characteristics of the efficiency and specificity of exfoliative toxin cleavage of desmoglein 1. J. Biol. Chem. 2004, 279:5268-5277.
69. Hantke K. Iron and metal regulation in bacteria. Curr. Opin Micribiol. 2001, 4:172-177.
70. Hatheway C.L. Toxigenic clostridia. Clin. Microbiol. Rev. 1990, 3:66-98.
71. Herreros J., Lalli G., Montecucco C., Schiavo G. Pathophysiological properties of clostridial neurotoxins. The Comprehensive Sourcebook of Bacterial Protein Toxins 1999, 202-228. Academic Press. J.E. Alouf, J.H. Freer (Eds.).
72. Hewlett E.L., Gray M.C. Adenylyl cyclase toxin from Bordetella pertussis. Bacterial Protein Toxins 2000, 473-488. Springer Verlag, London. K. Aktories, I. Just (Eds.).
73. Hinnebusch J., Chrepanov P., Du Y., Rudolph A., Dixon J.D., Schwan T., Forsberg A. Murine toxine toxin of Yersinia pestis shows phospholipase D activity but is not required for virulence in mice. Int. J. Med. Microbiol. 2000, 290:483-487.
74. Honjo T., Nishizuka Y., Hayaishi O., Kato I. Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyltransferase II and inhibition of protein synthesis. J. Biol. Chem. 1968, 243:3553-3555.
75. Iglewski B.H., Liu P.W., Kabat D. Mechanism of action of Pseudomonas aeruginosa exotoxin A adenosine diphosphate-ribosylation of mammalian elongation factor 2 in vivo and in vitro. Infect. Immun. 1977, 15:138-144.
76. Iglewski B.H., Sadoff J., Bjorn M.J., Maxwell E.S. Pseudomonas aeruginosa exoenzyme S: anadenosine diphosphateribosyltransferase distinct from toxin A. Proc. Natl. Acad. Sci. USA 1978, 75:3211-3215.
77. Jepson M., Titball R. Structure and function of clostridial phospholipases. Microbes and Infection 2000, 2:1277-1284.
78. Jernigan J.A., Stephens D.S., Ashford D.A., et al. Bioterrorism-related inhalational anthrax: the first 10 cases reported in the United States. Emerg. Infect. Dis. 2001, 7:933-944.
79. Johnson L.P., Schlievert P.M. Group A streptococcal phage T 12 carries the structural gene for pyrogenic exotoxin type A. Mol. Gen. Genet. 1984, 194:52-56.
80. Johnson L.P., L'Italien J.J., Schlievert P.M. Streptococcal pyrogenic exotoxin type A (scarlet fever toxin) is related to Staphylococcus aureus enterotoxin B. Mol. Gen. Genet. 1986, 203:354-356.
81. Johnson W.M., Lior H. A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material. Microb. Pathog. 1988, 4:103-113.
82. Johnson W.M., Lior H. A new heat-labile cytolethal distending toxin (CLDT) produced by Campylobacter spp. Microb. Pathog. 1988, 4:115-126.
83. Kitasato S. Über den Tetanusbazillus. Z. Hyg. Infektkr. 1889, 7:225-230.
84. Klebs E. Beiträge zur pathologischen Anatomie der Schubwunden 1872, Vogel, Berlin.
85. Klimpel K.R., Molloy S.S., Thomas G., Leppla S.H. Anthrax toxin lethal factor contains a zinc metalloprotease consenus sequence which is required for lethal toxin activity. Mol. Microbiol. 1994, 13:1093-1100.
86. Knöll H., Shramek J., Verbova K., Gerlach D., Reichardt W., Köhler W. Scarlet fever and types of erythrogenic toxins produced by the infecting streptococcal strains. Zbl. Bakt. 1991, 276:94-106.
87. Koch R. Ueber die Cholerabakterien. Deut. Med. Wochenschr. 1884, 2:11-13.
88. Koch R. Untersuchungen über Bacterien V. Die Aetiologie der Milzbrandkrankheit, begründet auf der Entwicklungsgeschichte des Bazillus anthracis. Beitr. z. Biol. d. Pflanzen. 1876, 2:277-310.
89. Koehler T.M. Bacillus anthracis genetics and virulence gene regulation. Curr. Top. Microbiol. Immunol. 2002, 271:143-164.
90. Krakauer T., Stiles B.G. Staphylococcal enterotoxins, toxic shock toxin-1, and streptococcal pyrogenic exotoxins: Some basic biology of bacterial superantigens. Recent Res. Devel. Infection & Immunity 2003, 1:1-27.
91. Krall R., Schmidt G., Aktories K., Barbieri J.T. Pseudomonas aeruginosa ExoT is a Rho GTPase-activating protein. Infect. Immun. 2000, 68:6066-6068.
92. Kunkel S.V., Robertson D.C. Purification and chemical characterization of the heat-labile enterotoxin produced by enterotoxigenic Escherichia coli. Infect. Immun. 1979, 24:760-769.
93. Ladant D., Ullmann A. Bordetella pertussis adenylate cyclase: a toxin with multiple talents. Trends Microbiol. 1999, 7:172-176.
94. Ladhani S., Chapple D.S., Joannou C.L., Evans R.W. A novel method for rapid production and purification of the staphylococcal exfoliative toxins. FEMS Lett. 2002, 212:35-39.
95. Lalli G., Bohnert S., Deinhardt K., Varestegui C., Schiavo G. The journey of tetanus and botulinum neurotoxins in neurons. Trends Microbiol. 2003, 11:431-437.
96. Lamanna C. Overview of bacterial toxins with a non reductiorust approach to the mode of action of botulinalneurotoxin. Microbial Toxins in Food and Feeds 1990, 19-36. Plenum Press, Leipzig. A.E. Pohl (Ed.).
97. Laohachai K.N., Bahadi R., Hardo M.B., Hardo P.G., Kourie J.I. The role of bacterial and non-bacterial toxins in the induction of changes in membrane transport: implications for diarrhea. Toxicon 2003, 42:687-707.
98. Lennox E.S., Kaplan A.S. Action of diphtheria toxin on cells cultivated in vitro. Proc. Soc. Exp. Biol. Med. 1957, 95:700-702.
99. Leppla S.H. Anthrax toxin edema factor; a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. U.S.A. 1982, 79:3162-3166.
100. Leppla S.H. Production and purification of anthrax toxin. Methods in enzymology 1988, 165:103-116.
101. Leuchs L.J. Beitraege zur Kenntnis des Toxins und Antitoxins des Bacillus botulinus. Z. Hyg. Infektionskr. 1910, 65:55-84.
102. Lincoln R.E., Walker J.S., Klein F., Haines B.W. Anthrax. Adv. Vet. Sci. 1964, 9:327-368.
103. Lincoln R.E., Fish D.C. Anthrax. Microbial Toxins 1970, 361-414. Academic Press, New York. T.C. Montie, S. Kadis, S.J. Ajl (Eds.).
104. Llwelyn M., Cohen J. Superantigens: microbial agents that corrupt immunity. Lancet. Infect. Dis. 2002, 2:156-162.
105. Locke A., Main E.R. The relation of copper and iron to the production of toxin and enzyme action. J. Infect. Dis. 1931, 48:419-435.
106. Loeffler F. Untersuchungen über die Bedeutung der Mikrorganismen für die Entstehung der Diphtherie beim Menschen, bei der Taube und beim Kalbe. Mitth. a. d. Kaiserl. Gesundheitsamte. 1884, 2:421-499.
107. Lory S., Wolfgang M., Lee V., Smith R. The multi-talented bacterial adenylcyclases. Int. J. Med. Microbiol. 2004, 293:479-482.
108. Macfarlane M.G., Knight B.C.J.G. The biochemistry of bacterial toxins. 1. The lecithinase activity of Cl.welchii toxins. Biochem. J. 1941, 35:884-902.
109. Macfarlane M.G. The biochemistry of bacterial toxins: 3. The identification and immunological relations of lecithinases present in Clostridium.oedematiens and Clostridium sordellii toxins. Biochem. J. 1948, 42:590-595.
110. Macfarlane M.G. The biochemistry of bacterial toxins. 4. The lecithinase activity of Clostridium haemolyticum toxin. Biochem. J. 1950, 47:250-270.
111. MacLennan J.D. The histotoxic clostridial infections of man. Bacteriol. Rev. 1962, 26:177-276.
112. MacPherson W.G., Bowlby A.A., Wallace C., English C. Official History of the War. Volume 1. Medical Services Surgery of the War 1922, 134. HMSO, New York.
113. Maresso A.W., Baldwin M.R., Barbieri J.T. Ezrin/radixin/moesin proteins are high affinity targets for ADP-ribosylation by Pseudomonas aeruginosa Exo S. J. Biol. Chem. 2004, 279:38402-38408.
114. Marmorek A. La toxine streptococcique. Ann. Inst. Pasteur 1902, 16:169-178.
115. Marvaud C., Smith T., Hale M.L., Popoff M.R., Smith L., Stiles B.G. Clostridium perfringens iota-toxin: mapping of receptor binding and la docking domains on Ib. Infect. Immun. 2001, 69:2435-2441.
116. Masignani V., Balducci E., Serruto D., Veggi D., Arico B., Commanducci M., Pizza M., Rappuoli R. In silico identification of novel bacterial ADP-ribosyltransferases. Int. J. Med. Microbiol. 2004, 293:471-478.
117. McCormick J.K., Yarwood J.M., Schlievert P.M. Toxic shock syndrome and bacterial superantigens: an update. Annu. Rev. Microbiol. 2001, 55:77-104.
118. McDonel J.L. Clostridium perfringens toxins (types A, B, C, D, and E). Pharmacol. Ther 1980, 10:617-635.
119. McShan W.M., Tang Y.F., Ferretti J.J. Bacteriophage T12 of Streptococcus pyogenes integrates into the gene encoding a serine tRNA. Mol. Microbiol. 1997, 23:719-728.
120. Mekalanos J.J., Swartz D.J., Pearson G.D.N., Harford N., Groyne E., de Wilde M. Cholera toxin genes: nucleotide sequence, deletion analysis, and vaccine development. Nature 1983, 306:551-557.
121. Melish M.E., Glasgow L.A., Turner M.D. The staphylococcal scalded skin syndrome: isolation and partial characterization of the exfoliative toxin. Br. J. Dermatol. 1972, 125:129-140.
122. Melton-Celsa A., O'Brien A.D. Plant and bacterial toxins as RNA-N-glycosidases. Bacterial Proteins Toxins 2003, 245-253. ASM Press, London. D. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
123. Mock M, Fouet A. Anthrax. Annu. Rev. Microbiol. 2001, 55:647-671.
124. Mourez M., Lacy D.B., Cunningham K., Legman R., Sellman B.R., Mogridge J., Collier R.J. 2001 a year of major advances in anthrax research. Trends Microbiol. 2002, 10:287-293.
125. Mourez M. Anthrax toxins. Rev. Physiol. Biochem. Pharmacol. 2004, 152:135-164.
126. Murphy J.R., Michel J.L., Teng M. Evidence that the regulation of diphtheria toxin production is directed at the level of transcription. J. Bacteriol. 1978, 135:511-516.
127. Nagler F.P.O. Observations on a reaction between the lethal toxin of Clostridium welchii (type A) and human serum. Brit. J. Exp. Pathol. 1939, 20:473-485.
128. Naylor C., Eton J.T., Howells A., Justin N., Moss D.S., Titball R.W., Basak A.K. Structure of the key toxin in gas gangrene. Nature Struct. Biol. 1998, 5:738-746.
129. Neill J.B., Mallory T.B. Studies on the oxidation and reduction of immunological substances. IV. Streptolysin. J. Exp. Med. 1926, 44:241-260.
130. Nesic D., Hsu Y., Stebbins C.E. Assembly and function of a bacterial genotoxin. Nature 2004, 429:429-433.
131. Nicolaier A. Ueber infectiösen Tetanus. Dt. med. Wochenschr. 1884, 10:842-844.
132. Nida S.K., Ferretti J.J. Phage influence on the synthesis of extracellular toxins in group A streptococci. Infect. Immun. 1982, 36:745-750.
133. Ohishi I., Iwasaki M., Sakaguchi G. Purification and characterization of two components of botulinum C2 toxin. Infect. Immun. 1980, 65:1402-1407.
134. O'Loughlin E.V., Robins-Browne R.M. Effect of Shiga and Shiga-like toxins on eukaryotic cells. Microbes Infect. 2001, 3:493-507.
135. Oxhamre C., Richter-Dahlfors A. Membrane-damaging toxins: family of RTX toxins. Bacterial Protein Toxins 2003, 203-214. ASM Press, Washington, D.C. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
136. Pallen M.J., Lam A.C., Loman N.J., McBride A. An abundance of bacterial ADP-ribosyltransferases-implications for the origin of exotoxins and their human homologues. Trends Microbiol. 2001, 9:302-307.
137. Pannifer A.D., Wong T.Y., Scawrzenbacher R., Renatus M., Petosa C., Bienkowska J. Crystal structure of the anthrax lethal factor. Nature 2001, 414:229-233.
138. Pappenheimer A.M., Johnson S.J. Studies in diphtheria toxin production. I. The effect of iron and copper. Br. J. Exp. Pathol. 1936, 17:335-341.
139. Pasteur L., Joubert P.A. Charbon et septicémie. Bull. Acad. Méd. 1877, 6:781.
140. Pasteur L. Nouvelles observations sur l'étiologie et la prophylaxie du charbon. C. R. Acad. Sci. 1880, 91:697-701.
141. Payne S.M. Regulation of bacterial toxin synthesis by iron. Bacterial Toxins 2003, 25-38. ASM Press, Washington, D.C. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
142. Penfold W.J., Tolhurst J.C. Formol-toxoids in the prophylaxis of gas gangrene. Med. J. Aust. 1937, 1:604.
143. Perelle S., Scalzo S., Kochi S., Mock M., Popoff M.R. Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins. FEMS Microbiol. Lett. 1997, 146:117-121.
144. Petersson K., Forsberg G., Walse B. Interplay between superantigens and immunoreceptors. Scand. J. Immunol. 2004, 59:345-355.
145. Petit L., Gibert M., Popoff M.R. Clostridium perfringens: toxinotype and genotype. Trends Microbiol. 1999, 7:104-110.
146. Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C. Crystal structure of the anthrax toxin protective antigen. Nature 1997, 385:833-838.
147. Pickett C.L., Whitehouse C.A. The cytolethal distending toxin family. Trends Microbiol. 1999, 7:292-297.
148. Placido-Sousa C., Evans D.G. The action of diphtheria toxin on tissue cultures and its neutralization by antitoxin. Br. J. Exp. Pathol. 1957, 38:644-649.
149. Polekhina G., Giddings K.S., Tweten R.K., Parker M.W. Crystallization and preliminary X-ray analysis of the human-specific toxin intermadilysin. Acta Crystallographica D Biol. Crystallgr. 2004, 60:347-349.
150. Pope C.G. The production of toxin by Corynebacterium diphtheriae. Effect produced by addition of iron and copper to the medium. Br. J. Exp. Pathol. 1932, 13:218-223.
151. Popoff M. Interactions between bacterial toxins and intestinal cells. Toxicon. 1998, 36:665-685.
152. Popoff M., Marvaud C. Structure and genomic features of clostridial neurotoxins. The Comprehensive Sourcebook of Bacterial Protein Toxins 1999, 174-201. Academic Press, Washington, D.C. J.E. Alouf, J.H. Freer (Eds.).
153. Popoff M.R., Milward F.W., Bancillon B., Boquet P. Purification of the Clostridium spiriforme binary toxin and activity of the toxin on HEP2 cells. Infect. Immun. 1989, 57:2462-2469.
154. Prevost G., Mourey L., Colin D.A., Menestrina G. Staphylococcal-pore-forming toxins. Curr. Top. Microbiol. Immunol. 2001, 257:53-83.
155. Proft T., Arcus V.L., Handley V., Baker E.N., Fraser J.D. Immunological and biochemical characterization of streoptococcal pyrogenic exotoxins I and J (Spe-I and SPE-J). J. Immunol. 2001, 166:6711-6719.
156. Raffestin S., Marvaud J.C., Cerrato R., Dupuy B., Popoff M.R. Organization and regulation of the neurotoxin genes in Clostridium botulinum and Clostridium tetani. Anaerobe 2004, 10:93-100.
157. Ramamurthy T., Yoshine K.-I., Abe J., Ikeda N., Takeda T. Purification, characterization, and cloning of a novel variant of the superantigen Yersinia pseudotuberculosis-derived mitogen. FEBS Lett. 1997, 413:174-176.
158. Ramon G. Sur le pouvoir floculant et les propriétés immunisantes d'une toxine diphtérique rendue anatoxique (anatoxine). C. R. Acad. Sci. (Paris) 1923, 177:1338-1340.
159. Ramon G., Descombey P.A. Sur l'immunisation antiténique et sur la production de l'antitoxine tétanique. C. R. Soc. Biol. (Paris) 1925, 93:508-598.
160. Rood J.I., Cole S.T. Molecular genetics and pathogenesis of Clostridium perfringens. Microb. Rev. 1991, 55:621-648.
161. Rossetto O., Seveso M., Caccin P., Schiavo G., Montecucco C. Tetanus and botulinum neurotoxins: turning bad guys into good by research. Toxicon 2001, 39:27-41.
162. Roux E., Yersin A. Contribution à l'étude de la diphtérie. Ann. Inst. Pasteur. 1888, 2:629-661.
163. Roux E., Martin L. Contribution à l'étude de la diphtérie (sérumthérapie). Ann. Inst. Pasteur 1894, 8:609-639.
164. Saelinger C.B. Receptors for bacterial toxins. Bacterial Protein Toxins 2004, 131-148. ASM Press, London. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
165. Sakagushi G. Clostridium botulinum toxins. Pharmacology of Bacterial Toxins 1986, 519-548. Pergamon Press, Washington, D.C. F. Dorner, J. Drews (Eds.).
166. Sandvig K. Transport of toxins across intracellular membranes. Bacterial Protein Toxins 2003, 157-172. ASM Press, Oxford. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
167. Schlievert P.M., Shands K.N., Schmid G.P., Dan B.B., Nishimura R.D. Identification and characterization of an exotoxin from Staphylococcus aureus assiociated with toxic-shock syndrome. J. Infect. Dis. 1981, 143:509-516.
168. Schlievert P.M., Gray E.D. Group A streptococcal pyrogenic exotoxin (scarlet fever toxin) type and blastogen A are the same protein. Infect. Immun. 1989, 57:1865-1867.
169. Schmidt G., Sehr P., Wilm M., Mann M., Just I., Aktories K. Gln 63 of Rho is deamidated by Escherichia coli necrotizing factor-1. Nature 1997, 387:725-729.
170. Sears C.L., Kaper J.B. Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion. Microbiol. Rev. 1996, 60:167-215.
171. Sears C.L. The toxins of Bacteroides fragilis. Toxicon 2001, 39:1737-1746.
172. Seiffert G. Eine Reaktion menschlicher Sera mit Perfringenstoxin. Z. Immun. Forsch. Exp. Ther. 1939, 96:515-520.
173. Selzer J., Hoffmann F., Rex J., Wilm M., Mann M., Just I., Aktories K. Clostridium novyi α-toxin-catalyzed incorporation of GlcNac into Rho subfamily proteins. J. Biol. Chem. 1996, 271:173-177.
174. Shiga K. Üeber den Dysenteriebacillus (Bacillus dysenteriae). Zentralbl Bakt. 1898, 24:817-828.
175. Shinoda S. Hemolysins of Vibrio cholerae and other Vibrio species. The Comprehensive Sourcebook of Bacterial Protein Toxins 1999, 373-385. Academic Press, Washington, D.C. J.E. Alouf, J.H. Freer (Eds.).
176. Smith H. Discovery of the anthrax toxin: the beginning of studies of virulence determinants regulated in vivo. Int. J. Med. Microbiol. 2002, 291:411-417.
177. Smith H., Tempest D.W., Stanley J.L., Harris-Smith P.W., Gallop R.C. The chemical basis of the virulence of Bacillus anthracis. VII. Two components of the anthrax toxin: their relationship to known immunizing aggressins. Brit. J. Exp. Pathol. 1956, 37:263-271.
178. Songer J.G. Clostridial enteric diseases. Clin. Microbiol. Rev. 1996, 9:216-234.
179. Songer J.G. Bacterial phospholipases and their role in virulence. Trends Microbiol. 1997, 5:156-161.
180. Stanley J.L., Smith H. Purification of fraction I and recognition of a third factor of the anthrax toxin. J. Gen. Microbiol. 1961, 26:49-66.
181. Stephen J. Anthrax toxin. Pharmacology of Bacterial Toxins 1986, 381-395. Pergamon Press, London. F. Dorner, J. Drews (Eds.).
182. Stevens D.L. The pathogenesis of clostridial myonecrosis. Int. J. Med. Microbiol. 2000, 290:497-502.
183. Stibitz S. Two-component systems. Bacterial Protein Toxins 2003, 3-23. ASM Press, Oxford. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
184. Stiles B.G., Wilkins T.D. Purification and characterization of Clostridtum perfringens iota toxin: dependence on two non-linked proteins for biological activity. Infect. Immun. 1986, 54:683-688.
185. Strathdee C.A., Lo R.Y. Cloning, nucleotide sequence, and characterization of genes encoding the secretion function of the Pasteurella hemolytica leukotoxin determinant. J. Bacteriol. 1989, 171:916-928.
186. Strauss N., Hendee E.D. The effect of diphtheria toxin on the metabolism of HeLa cells. J. Exp. Med. 1959, 109:144-163.
187. Tesh V.L., O'Brien A.D. The pathogenic mechanisms of Shiga and Shiga-like toxins. Mol. Microbiol. 1991, 5:1817-1822.
188. Thelestam M., Frisan T. Cytolethal distending toxins. Rev. Physiol. Biochem. Pharmacol. 2004, 152:111-133.
189. Titball R.W., Naylor C.E., Miller J., Moss D.S., Basak A.K. Opening of the active site of Clostridium perfringens α-toxin may be triggered by membrane binding. Int. J. Med. Microbiol. 2000, 290:357-361.
190. Tizzoni G., Cattani G. Über das Tetanus Gift. Zentralbl. Bakt. 1890, 8:69-73.
191. Todd E.W. The differentiation of two distinct serological varieties of streptolysin, streptolysin O, and streptolysin S. J. Pathol. Bacteriol. 1938, 47:423-445.
192. Turnbull P.C. Introduction: anthrax history, disease, and ecology. Curr. Top. Microbiol. Immunol. 2002, 271:1-19.
193. Tweten R.K., Parker M.W., Johnson A.E. The cholesterol-dependent cytolysins (2001). Curr. Top. Microbiol. Immunol. 2001, 257:15-33.
194. Uchiyama T., Miyoshi-Akiyama T., Kato H., Fujimaki W., Imanishi K., Yan X.J. Superantigenic properties of a novel mitogenic substance produced by Yersinia pseudotuberculosis from patients manifesting acute and systemic symptoms. J. Immunol. 1993, 151:4407-4413.
195. van der Goot F.G. Membrane-damaging toxins. Bacterial Protein Toxins 2003, 189-202. ASM Press, Washington D.C. D.L. Burns, J.T. Barbieri, B.H. Iglewski, R. Rappuoli (Eds.).
196. van de Velde H. Etude sur le mécanisme de la virulence du staphylocoque pyogène. Cellule 1894, 10:401-406.
197. van Ermengem E. Über einen neunen anaeroben Bacillus und seine Beziehungen zum Botulismus. Z. Hyg. Infektkrh. 1897, 26:1-56.
198. van Heyningen W.E. The biochemistry of the gas gangrene toxins. I. Estimation of the a toxin of Cl. welchii, type A. Biochem. J. 1941, 35:1246-1256.
199. van Heyningen W.E. Bacterial Toxins 1950, Blackwell Scientific Publications, Washington, D.C.
200. van Heyningen W.E. The role of toxins in pathology. Mechanisms of Microbial Pathogenicity 1955, 17-34. Cambridge University Press, Oxford.
201. van Heyningen W.E. General characteristics. Microbial Toxins 1970, 1-28. Academic Press, Cambridge. S.E. Ajl, S. Kadis, T.C. Montie (Eds.).
202. van Heynigan W.E., Mellanby J. Tetanus toxin. Microbial Toxins 1971, 69-108. Academic Press, New York. S. Kadis, T.C. Montie, S.E. Ajl (Eds.).
203. Van Tassel R.L., Lyerly D.M., Wilkins T.D. Purification and characterization of an enterotoxin from Bacteroides fragilis. Infect. Immun. 1992, 60:1343-1350.
204. Villaseca J.M., Navarro-Garcia F., Mendoza-Hernandez G., Nataro J.M., Cravioto A., Eslava C. Pet toxin from enteroaggregative Escherichia coli produces cellular damage associated with fodrin disruption. Infect. Immun. 2000, 68:5920-5927.
205. Vitale G., Bernardi, Napolitani G., Mock M., Montecucco C. Susceptibility of mitogen-activated protein kinase kinase family members in proteolysis by anthrax lethal factor. Biochem. J. 2000, 352:739-745.
206. Von Eichel-Streiber C., Boquet P., Sauerborn M., Thelestam M. Large clostridial cytotoxins-a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol. 1996, 4:375-382.
207. von Leber T. Forsch. Med. 1888, 6:460.
208. Watson D.W. Host parasite factors in group A streptococcal infections: pyrogenic and other effects on immunologic distinct exotoxins related to scarlet fever toxins. J. Exp. Med. 1960, 111:255-283.
209. Weeks C.R., Ferretti J.J. Nucleotide sequence of the type A pyrogenic exotoxin (erythrogenic toxin) gene from Streptococcus pyogenes
210. Welch W.H., Nuttal G.H.F. A gas producing bacillus (Bacillus aerogenes capsulatus, Nov. Spec.) capable of rapid development in the blood vessels after death. Bull. Johns Hopkins Hosp 1892, 3:81-91.
211. Welch R.A. RTX toxin structure and functions: a story of numerous anomalies and few analogies in toxin biology. Curr. Top. Microbiol. Immunol. 2001, 257:85-111.
212. Welkos S.L., Holmes R.K. Regulation of toxinogenesis in Corynebacterium diphtheriae. I. Mutations in bacteriophage beta that alter the effects of iron on toxin production. J. Virol. 1981, 37:936-945.
213. White A., Diung X., van der Spek J.C., Murphy J.R., Riknge D.R. Structure of the metal-iron-activated diphtheria toxin repressor/tox operator complex. Nature 1998, 394:502-506.
214. Wren B.W. Molecular characterization of Clostridium diffcile toxins A and B. Rev. Med. Microbiol. 1992, 3:21-27.
215. Yamaguchi T., Nishifuji K., Sasaki M., Fudaba Y., Aepfelbacher M., Takata T., et al. Identification of the Staphylococcus aureus etd pathogenicity island which encodes a nove exfoliative toxin ETD and EDIN-B. Infect. Immun. 2002, 70:5835-5845.
216. Yahr T.L., Vallis A.J., Hancock M.K., Barbieri J.T., Frank D.W. ExoY, an adenylate cyclase secreted by Pseudomonas aeruginosa type III system. Proc. Natl. Acad. Sci. USA 1998, 95:13899-13904.
217. Yoshihara K., Matsushita O., Minami J., Okabe A. Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collegenase and a gelatinase. J. Bacteriol. 1994, 176:6489-6496.
218. Zabriskie J.B. The role of temperate bacteriophage in the production of erythrogenic toxin by group A streptococci. J. Exp. Med. 1964, 119:761-780.