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This chapter focuses on (i) species that induce human diseases, (ii) species that are able to produce toxins, and (iii) the association of appropriate virulence factors with possible mobile elements. With reference to bacilli, the chapter discusses mainly Bacillus anthracis and B. cereus. A section on clostridia focuses on Clostridium perfringens, neurotoxin-producing clostridia, and species capable of producing large clostridial cytotoxins (LCTs). The chapter talks about the contribution of the genetic mobility of virulence genes to the evolution of pathogenic bacilli and clostridia. B. anthracis strains produce a tripartite protein toxin, comprising PA (protective antigen), EF (edema factor) and LF (lethal factor). The main scientific interest is focused on the toxin plasmid (pXO1) and the capsule plasmid (pXO2), since they were recognized at an early stage as carrying the major virulence factors of B. anthracis. Under laboratory conditions, gene transfer has been achieved by transduction, conjugation, or conduction and has been reported to occur between B. anthracis, B. cereus, and B. thuringiensis strains. With virulence factors that are known to be mobile, the significance of the association of mobile genetic elements with virulence genes for the evolution of the pathogenic clostridia and bacilli becomes clear. The extreme flexibility of the bacteria toward the loss and acquisition of virulence factors could help pathogenic bacteria adapt to the excessive pressure of selection to which they are subjected during the complex interactions between pathogens and their hosts.
Genetic organization of the chromosomal enterotoxin gene (cpe). ORFs are shown as arrows, and IS elements are indicated by solid boxes. uapC encodes the putative purine permease; nadC encodes the putative quinolinate phosphoribosyltransferase. The figure is based on data from references 20 and 21 .
Gene arrangement of the toxin locus of selected C. botulinum strains. The figure is based on data summarized by Kubota et al. ( 108 ).
Model for the regulation of the toxin expression in C. difficile. The model is based on work in our laboratory ( 16 , 84 ) and a reporter gene analysis by Moncrief et al. ( 141 ). The antagonistic functions of the two putative regulatory molecules, TcdC and TcdD, for the expression of the C. difficile toxins are indicated. The model is described in detail by Braun ( 16 ).
Genetic organization of the pathogenicity locus of C. difficile, C. sordellii (partial), and C. novyi (partial). The figure is based on data from references 16 , 17 , 66 , and 82 .
1. Agata, N.,, M. Ohta,, Y. Arakawa,, and M. Mori. 1995. The bceT gene of Bacillus cereus encodes an enterotoxic protein. Microbiology 141: 983– 988.
2. Andersen, G. L.,, J. M. Simchock,, and K. H. Wilson. 1996. Identification of a region of genetic variability among Bacillus anthracis strains and related species. J. Bacteriol. 178: 377– 384.
3. Ash, C.,, and M. D. Collins. 1992. Comparative analysis of 23S ribosomal RNA gene sequences of Bacillus anthracis and emetic Bacillus cereus determined by PCR-direct sequencing. FEMS Microbiol. Lett. 73: 75– 80.
4. Ash, C.,, J. A. Farrow,, M. Dorsch,, E. Stackebrandt,, and M. D. Collins. 1991. Comparative analysis of Bacillus anthracis, Bacillus cereus,and related species on the basis of reverse transcriptase sequencing of 16S rRNA. Int. J. Syst. Bacteriol. 41: 343– 346.
5. Aureli, P.,, L. Fenicia,, B. Pasolini,, M. Gianfranceschi,, L. M. McCroskey,, and C. L. Hatheway. 1986. Two cases of type E infant botulism caused by neurotoxigenic Clostridium butyricum in Italy. J. Infect. Dis. 154: 207– 211.
6. Barroso, L. A.,, S. Z. Wang,, C. J. Phelps,, J. L. Johnson,, and T. D. Wilkins. 1990. Nucleotide sequence of Clostridium difficile toxin B gene. Nucleic Acids Res. 18: 4004.
7. Bartkus, J. M.,, and S. H. Leppla. 1989. Transcriptional regulation of the protective antigen gene of Bacillus anthracis. Infect. Immun. 57: 2295– 2300.
8. Battisti, L.,, B. D. Green,, and C. B. Thome. 1985. Mating system for transfer of plasmids among Bacillus anthracis, Bacillus cereus,and Bacillus thuringiensis. J. Bacteriol. 162: 543– 550.
9. Beecher, D. J.,, and A. C. Wong. 1994. Improved purification and characterization of hemolysin BL, a hemolytic dermonecrotic vascular permeability factor from Bacillus cereus. Infect. Immun. 62: 980– 986.
10. Belyi, Y. F.,, I. S. Tartakovskii,, Y. V. Vertiev,, and S. V. Prosorovskii. 1991. Partial purification and characterization of ADP-ribosyltransferase produced by Legionella pneumophila. Biomed. Set. 2: 169– 174.
11. Binz, T.,, H. Kurazono,, M. Wille,, J. Frevert,, K. Wernars,, and H. Niemann. 1990. The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J. Biol. Chem. 265: 9153– 9158.
12. Blasi, J.,, E. R. Chapman,, E. Link,, T. Binz,, S. Yamasaki,, P. De Camilli,, T. C. Sudhof,, H. Niemann,, and R. Jahn. 1993. Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25. Nature 365: 160– 163.
13. Blasi, J.,, E. R. Chapman,, S. Yamasaki,, T. Binz,, H. Niemann,, and R. Jahn. 1993. Botulinum neurotoxin CI blocks neurotransmitter release by means of cleaving HPC-l/syntaxin. EMBO J. 12: 4821– 4828.
14. Bourgouin, C.,, A. Delecluse,, J. Ribier,, A. Klier,, and G. RapoporL 1988. A Bacillus thuringiensis subsp. israelensis gene encoding a 125-kilodalton larvicidal polypeptide is associated with inverted repeat sequences. J. Bacteriol. 170: 3575– 3583.
15. Bragg, T. S.,, and D. L. Robertson. 1989. Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis. Gene 81: 45– 54.
16. Braun, V. 1997. Ph.D. thesis. Johannes Gutenberg-Universität, Mainz, Germany.
17. Braun, V.,, T. Hundsberger,, P. Leukel,, M. Sauerborn,, and C. von Eichel-Streiber. 1996. Definition of the single integration site of the pathogenicity locus in Clostridium difficile. Gene 181: 29– 38.
18. Bravo, A. 1997. Phylogenetic relationships of Bacillus thuringiensis delta-endotoxin family proteins and their functional domains. J. Bacteriol. 179: 2793– 2801.
19. Brown, E. R.,, and W. B. Cherry. 1955. Specific identification of Bacillus anthracis by means of a variant bacteriophage. J. Infect. Dis. 96: 34– 39.
20. Brynestad, S.,, L. A. Iwanejko,, G. S. Stewart,, and P. E. Granum. 1994. A complex array of Hpr consensus DNA recognition sequences proximal to the enterotoxin gene in Clostridium perfringens type A. Microbiology 140: 97– 104.
21. Brynestad, S.,, B. Synstad,, and P. E. Granum. 1997. The Clostridium perfringens enterotoxin gene is on a transposable element in type A human food poisoning strains. Microbiology 143: 2109– 2115.
22. Buck, C. A.,, R. L. Anacker,, F. S. Newman,, and A. Eisentark. 1963. Phage isolated from lysogenic Bacillus anthracis. J. Bacteriol. 85: 1423– 1430.
23. Bullen, J. J.,, and R. Scarisbrick. 1957. Enterotoxaemia of sheep: experimental reproduction of the disease. J. Pathol. Bacteriol. 73: 494– 509.
24. Canard, B.,, and S. T. Cole. 1989. Genome organization of the anaerobic pathogen Clostridium perfringens. Proc. Natl. Acad. Sci. USA 86: 6676– 6680.
25. Canard, B.,, B. Saint Joanis,, and S. T. Cole. 1992. Genomic diversity and organization of virulence genes in the pathogenic anaerobe Clostridium perfringens. Mol. Microbiol. 6: 1421– 1429.
26. Carlson, C. R.,, T. Johansen,, and A. B. Kolsto. 1996. The chromosome map of Bacillus thuringiensis subsp. canadensis HD224 is highly similar to that of the Bacillus cereus type strain ATCC 14579. FEMS Microbiol. Lett. 141: 163– 167.
27. Carlson, C. R.,, and A. B. Kolsto. 1994. A small (2.4 Mb) Bacillus cereus chromosome corresponds to a conserved region of a larger (5.3 Mb) Bacillus cereus chromosome. Mol. Microbiol. 13: 161– 169.
28. Chardin, P.,, P. Boquet,, P. Madaule,, M. R. Popoff,, E. J. Rubin,, and D. M. Gill. 1989. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8: 1087– 1092.
29. Collie, R. E.,, and B. A. McClane. 1998. Evidence that the enterotoxin gene can be episomal in Clostridium perfringens isolates associated with non-food-borne human gastrointestinal diseases. J. Clin. Microbiol. 36: 30– 36.
30. Cornillot, E.,, B. Saint Joanis,, G. Daube,, S. Katayama,, P. E. Granum,, B. Canard,, and S. T. Cole. 1995. The enterotoxin gene ( cpe) of Clostridium perfringens can be chromosomal or plasmid-borne. Mol. Microbiol. 15: 639– 647.
31. Cowles, P. B. 1931. A bacteriophage for Bacillus anthracis. J. Bacteriol. 21: 161– 166.
32. Dai, Z.,, and T. M. Koehler. 1997. Regulation of anthrax toxin activator gene ( atxA) expression in Bacillus anthracis: temperature, not CO 2/bicarbonate, affects AtxA synthesis. Infect. Immun. 65: 2576– 2582.
33. Dai, Z.,, J. C. Sirard,, M. Mock,, and T. M. Koehler. 1995. The atxA gene product activates transcription of the anthrax toxin genes and is essential for virulence. Mol. Microbiol. 16: 1171– 1181.
34. Das, P. K.,, and D. D. Amalraj. 1997. Biological control of malaria vectors. Indian J. Med. Res. 106: 174– 197.
35. Daube, G.,, B. China,, P. Simon,, K. Hvala,, and J. Mainil. 1994. Typing of Clostridium perfringens by in vitro amplification of toxin genes. J. Appl. Bacteriol. 77: 650– 655.
36. Daube, G.,, P. Simon,, and A. Kaeckenbeeck. 1993. IS 1151, an IS-like element of Clostridium perfringens. Nucleic Acids Res. 21: 352.
37. Daube, G.,, P. Simon,, B. Limbourg,, C. Manteca,, J. Mainil,, and A. Kaeckenbeeck. 1996. Hybridization of 2,659 Clostridium perfringens isolates with gene probes for seven toxins (alpha, beta, epsilon, iota, theta, mu, and enterotoxin) and for sialidase. Am. J. Vet. Res. 57: 496– 501.
38. Dove, C. H.,, S. Z. Wang,, S. B. Price,, C. J. Phelps,, D. M. Lyerly,, T. D. Wilkins,, and J. L. Johnson. 1990. Molecular characterization of the Clostridium difficile toxin A gene. Infect. Immun. 58: 480– 488.
39. Drobniewski, F. A. 1993. Bacillus cereus and related species. Clin. Microbiol. Rev. 6: 324– 338.
40. Duesbery, N. S.,, C. P. Webb,, S. H. Leppla,, V. M. Gordon,, K. R. Klimpel,, T. D. Copeland,, N. G. Ahn,, M. K. Oskarsson,, K. Fukasawa,, K. D. Paul),, and G. F. Vande Woude. 1998. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280: 734– 737.
41. East, A. K.,, M. Bhandari,, J. M. Stacey,, K. D. Campbell,, and M. D. Collins. 1996. Organization and phylogenetic interrelationships of genes encoding components of the botulinum toxin complex in proteolytic Clostridium botulinum types A, B, and F: evidence of chimeric sequences in the gene encoding the nontoxic nonhemagglutinin component. Int. J. Syst. Bacteriol. 46: 1105– 1112.
42. East, A. K.,, and M. D. Collins. 1994. Conserved structure of genes encoding components of botulinum neurotoxin complex M and the sequence of the gene coding for the nontoxic component in nonproteolytic Clostridium botulinum type F. Curr. Microbiol. 29: 69– 77.
43. East, A. K.,, P. T. Richardson,, D. Allaway,, M. D. Collins,, T. A. Roberts,, and D. E. Thompson. 1992. Sequence of the gene encoding type F neurotoxin of Clostridium botulinum. FEMS Microbiol. Lett. 75: 225– 230.
44. Eklund, M. W., 1993. The role of bacteriophages and plasmids in the production of toxins and other biologically active substances by Clostridium botulinum and Clostridium novyi, p. 179– 194. In M. Sebald (ed.), Genetics and Molecular Biology of Anaerobic Bacteria. Springer-Verlag, Heidelberg, Germany.
45. Eklund, M. W.,, F. T. Poysky,, J. A. Meyers,, and G. A. Pelroy. 1974. Interspecies conversion of Clostridium botulinum type C to Clostridium novyi type A by bacteriophage. Science 186: 456– 458.
46. Eklund, M. W.,, F. T. Poysky,, L. M. Mseitif,, and M. S. Strom. 1988. Evidence for plasmid-mediated toxin and bacteriocin production in Clostridium botulinum type G. Appl. Environ. Microbiol. 54: 1405– 1408.
47. Eklund, M. W.,, F. T. Poysky,, M. E. Peterson,, and J. A. Meyers. 1976. Relationship of bacteriophages to alpha toxin production in Clostridium novyi types A and B. Infect. Immun. 14: 793– 803.
48. EtieShe Toumelin, I.,, J. C. Sirard,, E. Duflot,, M. Mock,, and A. Fouet. 1995. Characterization of the Bacillus anthracis S-layer: cloning and sequencing of the structural gene. J. Bacteriol. 177: 614– 620.
49. Ezzell, J. W.,, B. E. Ivins,, and S. H. Leppla. 1984. Immunoelectrophoretic analysis, toxicity, and kinetics of in vitro production of the protective antigen and lethal factor components of Bacillus anthracis toxin. Infect. Immun. 45: 761– 767.
50. Fairweather, N. F.,, and V. A. Lyness. 1986. The complete nucleotide sequence of tetanus toxin. Nucleic Acids Res. 14: 7809– 7812.
51. Finn, C. W. Jr.,, R. P. Silver,, W. H. Habig,, M. C. Hardegree,, G. Zon,, and C. F. Garon. 1984. The structural gene for tetanus neurotoxin is on a plasmid. Science 224: 881– 884.
52. Fouet, A.,, and M. Mock. 1996. Differential influence of the two Bacillus anthracis plasmids on regulation of virulence gene expression. Infect. Immun. 64: 4928– 4932.
53. Franciosa, G.,, J. L. Ferreira,, and C. L. Hatheway. 1994. Detection of type A, B, and E botulism neurotoxin genes in Clostridium botulinum and other Clostridium species by PCR: evidence of unexpressed type B toxin genes in type A toxigenic organisms. J. Clin. Microbiol. 32: 1911– 1917.
54. Friedlander, A. M. 1986. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261: 7123– 7126.
55. Fujii, N.,, K. Kimura,, N. Yokosawa,, K. Oguma,, T. Yashiki,, K. Takeshi,, T. Ohyama,, E. Isogai,, and H. Isogai. 1993. Similarity in nucleotide sequence of the gene encoding nontoxic component of botulinum toxin produced by toxigenic Clostridium butyricum strain BL6340 and Clostridium botulinum type E strain Mashike. Microbiol. Immunol. 37: 395– 398.
56. Fujii, N.,, K. Kimura,, N. Yokosawa,, T. Yashiki,, K. Tsuzuki,, and K. Oguma. 1993. The complete nucleotide sequence of the gene encoding the nontoxic component of Clostridium botulinum type E progenitor toxin. J. Gen. Microbiol. 139: 79– 86.
57. Fujinaga, Y.,, K. Inoue,, S. Shimazaki,, K. Tomochika,, K. Tsuzuki,, N. Fujii,, T. Watanabe,, T. Ohyama,, K. Takeshi,, and K. Inoue. 1994. Molecular construction of Clostridium botulinum type C progenitor toxin and its gene organization. Biochem. Biophys. Res. Commun. 205: 1291– 1298.
58. Genth, H.,, F. Hofmann,, J. Selzer,, G. Rex,, K. Aktories,, and I. Just. 1996. Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii. Biochem. Biophys. Res. Commun. 229: 370– 374.
59. Gonzalez, J. M. Jr.,, B. J. Brown,, and B. C. Carlton. 1982. Transfer of Bacillus thuringiensis plasmids coding for delta-endotoxin among strains of B. thuringiensis and B. cereus. Proc. Natl. Acad. Sci. USA 79: 6951– 6955.
60. Gonzalez, J. M. Jr.,, H. T. Dulmage,, and B. C. Carlton. 1981. Correlation between specific plasmids and delta-endotoxin production in Bacillus thuringiensis. Plasmid 5: 352– 365.
61. Gordon, V. M.,, S. H. Leppla,, and E. L. Hewlett. 1988. Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin. Infect. Immun. 56: 1066– 1069.
62. Granum, P. E. 1994. Bacillus cereus and its toxins. Soc. Appl. Bacteriol. Symp. Ser. 23: 61s– 66s.
63. Granum, P. E.,, and T. Lund. 1997. Bacillus cereus and its food poisoning toxins. FEMS Microbiol. Lett. 157: 223– 228.
64. Green, B. D.,, L. Battisti,, T. M. Koehler,, C. B. Thorne,, and B. E. Ivins. 1985. Demonstration of a capsule plasmid in Bacillus anthracis. Infect. Immun. 49: 291– 297.
65. Green, B. D.,, L. Battisti,, and C. B. Thorne. 1989. Involvement of 1n4430 in transfer of Bacillus anthracis plasmids mediated by Bacillus thuringiensis plasmid pX012. J. Bacteriol. 171: 104– 113.
66. Green, G. A.,, V. Schue,, and H. Monteil. 1995. Cloning and characterization of the cytotoxin L-encoding gene of Clostridium sordellii: homology with Clostridium difficile cytotoxin B. Gene 161: 57– 61.
67. Guignot, J.,, M. Mock,, and A. Fouet 1997. AtxA activates the transcription of genes harbored by both Bacillus anthracis virulence plasmids. FEMS Microbiol. Lett. 147: 203– 207.
68. Hacker, J.,, G. Blum Oehler,, I. Muhldorfer,, and H. Tschape. 1997. Pathogenicity islands of virulent bacteria: structure, function and impact on microbial evolution. Mol. Microbiol. 23: 1089– 1097.
69. Hall, J. D.,, L. M. McCroskey,, B. J. Pincomb,, and C. L. Hatheway. 1985. Isolation of an organism resembling Clostridium barati which produces type F botulinal toxin from an infant with botulism. J. Clin. Microbiol. 21: 654– 655.
70. Hambleton, P. 1992. Clostridium botulinum toxins: a general review of involvement in disease, structure, mode of action and preparation for clinical use. J. Neurol. 239: 16– 20.
71. Hambleton, P.,, J. A. Carman,, and J. Melling. 1984. Anthrax: the disease in relation to vaccines. Vaccine 2: 125– 132.
72. Hammond, G. A.,, and J. L. Johnson. 1995. The toxigenic element of Clostridium difficile strain VPI 10463. Microb. Pathog. 19: 203– 213.
73. Hanna, P. 1998. Anthrax pathogenesis and host response. Curr. Top. Microbiol. Immunol. 225: 13– 35.
74. Hanna, P. 1998. How anthrax kills. Science 280: 1671, 1673– 1674.
75. Hatheway, C. L. 1990. Toxigenic Clostridia. Clin. Microbiol. Rev. 3: 66– 98.
76. Hauser, D.,, M. Gibert,, P. Boquet,, and M. R. Popoff. 1992. Plasmid localization of a type E botulinal neurotoxin gene homologue in toxigenic Clostridium butyricum strains, and absence of this gene in non-toxigenic C. butyricum strains. FEMS Microbiol. Lett. 78: 251– 255.
77. Hauser, D.,, M. Gibert,, M. W. Eklund,, P. Boquet,, and M. R. Popoff. 1993. Comparative analysis of C3 and botulinal neurotoxin genes and their environment in Clostridium botulinum types C and D. J. Bacteriol. 175: 7260– 7268.
78. Hauser, D.,, M. Gibert,, J. C. Marvaud,, M. W. Eklund,, and M. R. Popoff. 1995. Botulinal neurotoxin CI complex genes, clostridial neurotoxin homology and genetic transfer in Clostridium botulinum. Toxicon 33: 515– 526.
79. Henderson, I.,, T. Davis,, M. Elmore,, and N. Minton,. 1997. The genetic basis of toxin production in Clostridium botulinum and Clostridium tetani, p. 261– 294. In J. I. Rood,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.). The Clostridia: Molecular Biology and Pathogenesis. Academic Press, Ltd., London, United Kingdom.
81. Hoffmaster, A. R.,, and T. M. Koehler. 1997. The anthrax toxin activator gene atxA is associated with CO 2-enhanced nontoxin gene expression in Bacillus anthracis. Infect. Immun. 65: 3091– 3099.
82. Hofmann, F.,, A. Herrmann,, E. Habermann,, and C. von Eichel-Streiber. 1995. Sequencing and analysis of the gene encoding the alpha-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile. Mol. Gen. Genet. 247: 670– 679.
83. Hoyer, L. L.,, A. C. Hamilton,, S. M. Steenbergen,, and E. R. Vimr. 1992. Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer. Mol. Microbiol. 6: 873– 884.
84. Hundsberger, T.,, V. Braun,, M. Weidmann,, P. Leukel,, M. Sauerborn,, and C. von Eichel-Streiber. 1997. Transcription analysis of the genes tcdA-E of the pathogenicity locus of Clostridium difficile. Eur. J. Biochem. 244: 735– 742.
85. Hunter, S. E.,, I. N. Clarke,, D. C. Kelly,, and R. W. Titball. 1992. Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coli. Infect. Immun. 60: 102– 110.
86. Hutson, R. A.,, M. D. Collins,, A. K. East,, and D. E. Thompson. 1994. Nucleotide sequence of the gene coding for non-proteolytic Clostridium botulinum type B neurotoxin: comparison with other clostridial neurotoxins. Curr. Microbiol. 28: 101– 110.
87. Hutson, R. A.,, D. E. Thompson,, and M. D. Collins. 1993. Genetic interrelationships of saccharolytic Clostridium botulinum types B, E and F and related Clostridia as revealed by small-subunit rRNA gene sequences. FEMS Microbiol. Lett. 108: 103– 110.
88. Inal, J. M.,, and K. V. Karunakaran. 1996. phi 20, a temperate bacteriophage isolated from Bacillus anthracis exists as a plasmidial prophage. Curr. Microbiol. 32: 171– 175.
89. Inoue, S.,, M. Sugai,, Y. Murooka,, S. Y. Paik,, Y. M. Hong,, H. Ohgai,, and H. Suginaka. 1991. Molecular cloning and sequencing of the epidermal cell differentiation inhibitor gene from Staphylococcus aureus. Biochem. Biophys. Res. Commun. 174: 459– 464.
90. Jackson, P. J.,, E. A. Walthers,, A. S. Kalif,, K. L. Richmond,, D. M. Adair,, K. K. Hill,, C. R. Kuske,, G. L. Andersen,, K. H. Wilson,, M. Hugh Jones,, and P. Keim. 1997. Characterization of the variable-number tandem repeats in vrrA from different Bacillus anthracis isolates. Appl. Environ. Microbiol. 63: 1400– 1405.
91. Just, I.,, C. Mohr,, G. Schallehn,, L. Menard,, J. R. Didsbury,, J. Vandekerckhove,, J. van Damme,, and K. Aktories. 1992. Purification and characterization of an ADP-ribosyltransferase produced by Clostridium limosum. J. Biol. Chem. 267: 10274– 10280.
92. Just, I.,, G. Schallehn,, and K. Aktories. 1992. ADP-ribosy lation of small GTP-binding proteins by Bacillus cereus. Biochem. Biophys. Res. Commun. 183: 931– 936.
93. Just, I.,, J. Selzer,, C. von Eichel-Streiber,, and K. Aktories. 1995. The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile. J. Clin. Investig. 95: 1026– 1031.
94. Just, I.,, J. Selzer,, M. Wilm,, C. von Eichel Streiber,, M. Mann,, and K. Aktories. 1995. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375: 500– 503.
95. Kamiya, S.,, H. Ogura,, X. Q. Meng,, and S. Nakamura. 1992. Correlation between cytotoxin production and sporulation in Clostridium difficile. J. Med. Microbiol. 37: 206– 210.
96. Kaneko, T.,, R. Nozaki,, and K. Aizawa. 1978. Deoxyribonucleic acid relatedness between Bacillus anthracis, Bacillus cereus and Bacillus thuringiensis. Microbiol. Immunol. 22: 639– 641.
97. Kaspar, R. L.,, and D. L. Robertson. 1987. Purification and physical analysis of Bacillus anthracis plasmids pXOl and pX02. Biochem. Biophys. Res. Commun. 149: 362– 368.
98. Katayama, S.,, B. Dupuy,, G. Daube,, B. China,, and S. T. Cole. 1996. Genome mapping of Clostridium perfringens strains with I-Ceul shows many virulence genes to be plasmid-borne. Mol. Gen. Genet. 251: 720– 726.
99. Katayama, S.,, B. Dupuy,, T. Gamier,, and S. T. Cole. 1995. Rapid expansion of the physical and genetic map of the chromosome of Clostridium perfringens CPN50. J. Bacteriol. 177: 5680– 5685.
100. Keim, P.,, A. Kalif,, J. Schupp,, K. Hill,, S. E. Travis,, K. Richmond,, D. M. Adair,, M. Hugh Jones,, C. R. Kuske,, and P. Jackson. 1997. Molecular evolution and diversity in Bacillus anthracis as detected by amplified fragment length polymorphism markers. J. Bacteriol. 179: 818– 824.
101. Kimura, K.,, N. Fujii,, K. Tsuzuki,, T. Murakami,, T. Indoh,, N. Yokosawa,, K. Takeshi,, B. Syuto,, and K. Oguma. 1990. The complete nucleotide sequence of the gene coding for botulinum type CI toxin in the C-ST phage genome. Biochem. Biophys. Res. Commun. 171: 1304– 1311.
102. Klimpel, K. R.,, N. Arora,, and S. H. Leppla. 1994. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13: 1093– 1100.
103. Koehler, T. M.,, Z. Dai,, and M. Kaufman Yarbray. 1994. Regulation of the Bacillus anthracis protective antigen gene: C0 2 and a trans-acting element activate transcription from one of two promoters. J. Bacteriol. 176: 586– 595.
104. Kokai Kun, J. F.,, J. G. Songer,, J. R. Czeczulin,, F. Chen,, and B. A. McClane. 1994. Comparison of Western immunoblots and gene detection assays for identification of potentially enterotoxigenic isolates of Clostridium perfringens. J. Clin. Microbiol. 32: 2533– 2539.
105. Kramer, J. M.,, and R. J. Gilbert 1989,. Bacillus cereus and other Bacillus species, p. 21– 70. In M. P. Doyle (ed.), Foodborne Bacterial Pathogens. Marcel Dekker, New York, N.Y.
106. Kronstad, J. W.,, and H. R. Whiteley. 1984. Inverted repeat sequences flank a Bacillus thuringiensis crystal protein gene. J. Bacteriol. 160: 95– 102.
107. Kubota, T.,, S. Shirakawa,, S. Kozaki,, E. Isogai,, H. Isogai,, K. Kimura,, and N. Fujii. 1996. Mosaic type of the nontoxic-nonhemagglutinin component gene in Clostridium botulinum type A strain isolated from infant botulism in Japan. Biochem. Biophys. Res. Commun. 224: 843– 848.
108. Kubota, T.,, N. Yonekura,, Y. Hariya,, E. Isogai,, H. Isogai,, K. Amano,, and N. Fujii. 1998. Gene arrangement in the upstream region of Clostridium botulinum type E and Clostridium butyricum BL6340 progenitor toxin genes is different from that of other types. FEMS Microbiol. Lett. 158: 215– 221.
109. LaForce, F. M. 1994. Anthrax. Clin. Infect. Dis. 19: 1009– 1013.
110. Laird, W. J.,, W. Aaronson,, R. P. Silver,, W. H. Habig,, and M. C. Hardegree. 1980. Plasmid-associated toxigenicity in Clostridium tetani. J. Infect. Dis. 142: 623.
111. Lawrence, D.,, S. Heitefuss,, and H. S. Seifert 1991. Differentiation of Bacillus anthracis from Bacillus cereus by gas chromatographic whole-cell fatty acid analysis. J. Clin. Microbiol. 29: 1508– 1512.
112. Lawson, P. A.,, P. LIop Perez,, R. A. Hutson,, H. Hippe,, and M. D. Collins. 1993. Towards a phytogeny of the Clostridia based on 16S rRNA sequences. FEMS Microbiol. Lett. 113: 87– 92.
113. Lee, C. A. 1996. Pathogenicity islands and the evolution of bacterial pathogens. Infect. Agents Dis. 5: 1– 7.
114. Leimeister Wachter, M.,, E. Domann,, and T. Chakraborty. 1992. The expression of virulence genes in Listeria monocytogenes is thermoregulated. J. Bacteriol. 174: 947– 952.
115. Leppla, S. H. 1982. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. USA 79: 3162– 3166.
116. Leppla, S. H., 1995. Anthrax toxins, p. 543– 567. In J. Moss,, B. Iglewski,, M. Vaughan,, and A. T. Tu (ed.), Handbook of Natural Toxins, vol. 8. Marcel Dekker, New York, N.Y.
117. Leppla, S. H. 1984. Bacillus anthracis calmodulin-dependent adenylate cyclase: chemical and enzymatic properties and interactions with eucaryotic cells. Adv. Cyclic Nucleotide Protein Phosphorylation Res. 17: 189– 198.
118. Leppla, S. H. 1988. Production and purification of anthrax toxin. Methods Enzymol. 165: 103– 116.
119. Lereclus, D.,, J. Mahillon,, G. Menou,, and M. M. Lecadet. 1986. Identification of Tn4430, a transposon of Bacillus thuringiensis functional in Escherichia coli. Mol. Gen. Genet. 204: 52– 57.
120. Lereclus, D.,, G. Menou,, and M. M. Lecadet. 1983. Isolation of a DNA sequence related to several plasmids from Bacillus thuringiensis after a mating involving the Streptococcus faecalis plasmid pAM beta 1. Mol. Gen. Genet. 191: 307– 313.
121. Lereclus, D.,, J. Ribier,, A. Klier,, G. Menou,, and M. M. Lecadet. 1984. A transposon-like structure related to the delta-endotoxin gene of Bacillus thuringiensis. EMBO J. 3: 2561– 2567.
122. Lereclus, D.,, M. Vallade,, J. Chaufaux,, O. Arantes,, and S. Rambaud. 1992. Expansion of insecticidal host range of Bacillus thuringiensis by in vivo genetic recombination. Bio/Technology 10: 418– 421.
123. Lesieur, C.,, B. Vecsey Semjen,, L. Abrami,, M. Fivaz,, and F. Gisou van der Goot 1997. Membrane insertion: the strategies of toxins. Mol. Membr. Biol. 14: 45– 64.
124. Lund, T.,, and P. E. Granum. 1996. Characterisation of a non-haemolytic enterotoxin complex from Bacillus cereus isolated after a foodborne outbreak. FEMS Microbiol. Lett. 141: 151– 156.
125. Mahillon, J.,, and M. Chandler. 1998. Insertion sequences. Microbiol. Mol. Biol. Rev. 62: 725– 774.
126. Mahillon, J.,, R. Rezsohazy,, B. Hallet,, and J. Delcour. 1994. IS231 and other Bacillus thuringiensis transposable elements: a review. Genetica 93: 13– 26.
127. Makino, S.,, I. Uchida,, N. Terakado,, C. Sasakawa,, and M. Yoshikawa. 1989. Molecular characterization and protein analysis of the cap region, which is essential for encapsulation in Bacillus anthracis. J. Bacteriol. 171: 722– 730.
128. Marvaud, J. C.,, M. Gibert,, K. Inoue,, V. Fujinaga,, K. Oguma,, and M. R. Popoff. 1998. botR/A is a positive regulator of botulinum neurotoxin and associated non-toxin protein genes in Clostridium botulinum A. Mol. Microbiol. 29: 1009– 1018.
129. Maurelli, A. T. 1989. Temperature regulation of virulence genes in pathogenic bacteria: a general strategy for human pathogens? Microb. Pathog. 7: 1– 10.
130. McClane, B. A. 1998. New insights into the genetics and regulation of expression of Clostridium perfringens enterotoxin. Curr. Top. Microbiol. Immunol. 225: 37– 55.
131. McCloy, E. W. 1951. Studies on a lysogenic Bacillus strain. I. A bacteriophage specific for Bacillus anthracis. J. Hyg. 49: 114– 125.
132. McCroskey, L. M.,, C. L. Hatheway,, L. Fenicia,, B. Pasolini,, and P. Aureli. 1986. Characterization of an organism that produces type E botulinal toxin but which resembles Clostridium butyricum from the feces of an infant with type E botulism. J. Clin. Microbiol. 23: 201– 202.
133. McDonel, J. L., 1986. Toxins of Clostridium perfringens types A. B, C, D and E, p. 477– 517. In F. Dorner, and H. Drews (ed.), Pharmacology of Bacterial Toxins. Pergamon, Oxford, United Kingdom.
134. McGaughey, W. H.,, F. Gould,, and W. Gelernter. 1998. Bt resistance management. Nat. Biotechnol. 16: 144– 146.
135. Meng, X.,, T. Karasawa,, K. Zou,, X. Kuang,, X. Wang,, C. Lu,, C. Wang,, K. Yamakawa,, and S. Naka-mura. 1997. Characterization of a neurotoxigenic Clostridium butyricum strain isolated from the food implicated in an outbreak of food-borne type E botulism. J. Clin. Microbiol. 35: 2160– 2162.
136. Mesnage, S.,, E. Tosi Couture,, P. Gounon,, M. Mock,, and A. Fouet. 1998. The capsule and S-layer: two independent and yet compatible macromolecular structures in Bacillus anthracis. J. Bacteriol. 180: 52– 58.
137. Mesnage, S.,, E. Tosi Couture,, M. Mock,, P. Gounon,, and A. Fouet. 1997. Molecular characterization of the Bacillus anthracis main S-layer component: evidence that it is the major cell-associated antigen. Mol. Microbiol. 23: 1147– 1155.
138. Meynell, E.,, and G. G. Meynell. 1964. The roles of serum and carbon dioxide in capsule formation by Bacillus anthracis. J. Gen. Microbiol. 34: 153– 164.
139. Mikesell, P.,, B. E. Ivins,, J. D. Ristroph,, and T. M. Dreier. 1983. Evidence for plasmid-mediated toxin production in Bacillus anthracis. Infect. Immun. 39: 371– 376.
140. Milne, J. C.,, D. Furlong,, P. C. Hanna,, J. S. Wall,, and R. J. Collier. 1994. Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269: 20607– 20612.
141. Moncrief, J. S.,, L. A. Barroso,, and T. D. Wilkins. 1997. Positive regulation of Clostridium difficile toxins. Infect. Immun. 65: 1105– 1108.
142. Moriishi, K.,, M. Koura,, N. Abe,, N. Fujii,, Y. Fujinaga,, K. Inoue,, and K. Oguma. 1996. Mosaic structures of neurotoxins produced from Clostridium botulinum types C and D organisms. Biochim. Biophys. Acta 1307: 123– 126.
143. Moriishi, K.,, M. Koura,, N. Fujii,, Y. Fujinaga,, K. Inoue,, B. Syuto,, and K. Oguma. 1996. Molecular cloning of the gene encoding the mosaic neurotoxin, composed of parts of botulinum neurotoxin types C1 and D, and PCR detection of this gene from Clostridium botulinum type C organisms. Appl. Environ. Microbiol. 62: 662– 667.
144. Miiller, H. E., 1992. Bacillaceae, p. 251– 257. In F. Burkhardt (ed.), Mikrobiologische Diagnostik. Thieme Verlag, Stuttgart, Germany.
145. Normore, W. M., 1973. Guanine-plus-cytosine composition of the DNA of bacteria, fungi, algae, and protozoa, p. 585– 740. In A. L. Laskin, and H. A. Lechavalier (ed.), Handbook of Microbiology, vol. II. The Chemical Rubber Co., Washington, D.C.
146. Ohyama, T.,, T. Watanabe,, Y. Fujinaga,, K. Inoue,, H. Sunagawa,, N. Fujii,, K. Inoue,, and K. Oguma. 1995. Characterization of nontoxic-nonhemagglutinin component of the two types of progenitor toxin (M and L) produced by Clostridium botulinum type D CB-16. Microbiol. Immunol. 39: 457– 465.
147. Onderdonk, A. B.,, and S. D. Allen,. 1995. Clostridium, p. 574– 586. In P. R. Murray,, E. J. Baron,, M. A. Pfaller,, F. C. Tenover,, and R. H. Yolken (ed.), Manual of Clinical Microbiology, 6th ed. ASM Press, Washington, D.C.
148. Payne, D.,, and P. Oyston,. 1997. The Clostridium perfringens e-toxin, p. 439– 447. In J. I. Rood,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, London, United Kingdom.
149. Perelle, S.,, M. Gibert,, P. Boquet,, and M. R. Popoff. 1993. Characterization of Clostridium perfringens iota-toxin genes and expression in Escherichia coli. Infect. Immun. 61: 5147– 5156.
150. Pezard, C.,, P. Berche,, and M. Mock. 1991. Contribution of individual toxin components to virulence of Bacillus anthracis. Infect. Immun. 59: 3472– 3477.
151. Pezard, C.,, M. Weber,, J. C. Sirard,, P. Berche,, and M. Mock. 1995. Protective immunity induced by Bacillus anthracis toxin-deficient strains. Infect. Immun. 63: 1369– 1372.
152. Popoff, M. R.,, E. Chaves Olarte,, E. Lemichez,, C. von Eichel Streiber,, M. Thelestam,, P. Chardin,, D. Cussac,, B. Antonny,, P. Chavrier,, G. Flatau,, M. Giry,, J. de Gunzburg,, and P. Boquet 1996. Ras, Rap, and Rae small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation. J. Biol. Chem. 271: 10217– 10224.
153. Popoff, M. R.,, and J. C. Marvaud,. 1999. Structural and genomic features of clostridial neurotoxins, p. 174– 201. In J. E. Alouf, and J. H. Freer (ed.), Bacterial Protein Toxins: a Comprehensive Sourcebook. Academic Press, London, United Kingdom.
154. Portnoy, D. A.,, T. Chakraborty,, W. Goebel,, and P. Cossart 1992. Molecular determinants of Listeria monocytogenes pathogenesis. Infect. Immun. 60: 1263– 1267.
155. Poulet, S.,, D. Hauser,, M. Quanz,, H. Niemann,, and M. R. Popoff. 1992. Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755). Biochem. Biophys. Res. Commun. 183: 107– 113.
156. Price, S. B.,, C. J. Phelps,, T. D. Wilkins,, and J. L. Johnson. 1987. Cloning of the carbohydrate-binding portion of the toxin A gene of Clostridium difficile. Curr. Microbiol. 16: 55– 60.
157. Priest, F. G., 1993. Systematics and ecology of Bacillus, p. 3– 16. In A. U. Sonenshein,, J. Hoch,, and R. Losick (ed.), Bacillus subtilis and Other Gram-Positive Bacteria. American Society for Microbiology, Washington, D.C.
158. Ravizzola, G.,, N. Manca,, F. Dima,, C. Signorini,, E. Garrafa,, and A. Turano. 1998. Isolation of a Clostridium exotoxin producer other than Clostridium difficile from a patient with diarrhea. J. Clin. Microbiol. 36: 2396.
159. Reddy, A.,, L. Battisti,, and C. B. Thorne. 1987. Identification of self-transmissible plasmids in four Bacillus thuringiensis subspecies. J. Bacteriol. 169: 5263– 5270.
160. Robertson, D. L.,, M. T. Tippetts,, and S. H. Leppla. 1988. Nucleotide sequence of the Bacillus anthracis edema factor gene ( cya): a calmodulin-dependent adenylate cyclase. Gene 73: 363– 371.
161. Roggentin, T.,, and R. Schauer,. 1997. Clostridial sialidases, p. 423– 437. In J. I. Rood,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, London, United Kingdom.
162. Rood, J. I. 1998. Virulence genes of Clostridium perfringens. Annu. Rev. Microbiol. 52: 333– 360.
163. Rood, J. I.,, and S. T. Cole. 1991. Molecular genetics and pathogenesis of Clostridium perfringens. Microbiol. Rev. 55: 621– 648.
164. Ruhfel, R. E.,, N. J. Robillard,, and C. B. Thorne. 1984. Interspecies transduction of plasmids among Bacillus anthracis, B. cereus,and B. thuringiensis. J. Bacteriol. 157: 708– 711.
165. Ryan, P. A.,, J. D. Macmillan,, and B. A. Zilinskas. 1997. Molecular cloning and characterization of the genes encoding the LI and L2 components of hemolysin BL from Bacillus cereus. J. Bacteriol. 179: 2551– 2556.
166. Sakaguchi, G.,, I. Ohishi,, and S. Kozaki,. 1988. Botulism—structure and chemistry of botulinum, p. 191– 216. In M. C. Hardegree, and A. T. Tu (ed.), Handbook of Natural Toxins, vol. 4. Marcel Dekker, Inc., New York, N.Y.
167. Sauerborn, M.,, and C. von Eichel-Streiber. 1990. Nucleotide sequence of Clostridium difficile toxin A. Nucleic Acids Res. 18: 1629– 1630.
168. Schallehn, G.,, M. W. Eklund,, and H. Brandis. 1980. Phage conversion of Clostridium novyi type A. Zentbl. Bakteriol. Microbiol. Hyg. Ser. A. 247: 95– 100.
169. Schiavo, G.,, and C. Montecucco,. 1997. The structure and mode of action of botulinum and tetanus toxin, p. 295– 322. In J. I. Rood,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, London, United Kingdom.
170. Schiavo, G.,, C. C. Shone,, O. Rossetto,, F. C. Alexander,, and C. Montecucco. 1993. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J. Biol. Chem. 268: 11516– 11519.
171. Schnepf, E.,, N. Crickmore,, J. Van Rie,, D. Lereclus,, J. Baum,, J. Feitelson,, D. R. Zeigler,, and D. H. Dean. 1998. Bacillus thuringiensis and its pesticidal crystal proteins. Microbiol. Mol. Biol. Rev. 62: 775– 806.
172. Selzer, J.,, F. Hofmann,, G. Rex,, M. Wilm,, M. Mann,, I. Just,, and K. Aktories. 1996. Clostridium novyi alpha-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins. J. Biol. Chem. 271: 25173– 25177.
173. Sirard, J. C.,, M. Mock,, and A. Fouet. 1994. The three Bacillus anthracis toxin genes are coordinately regulated by bicarbonate and temperature. J. Bacteriol. 176: 5188– 5192.
174. Somers, E.,, and B. R. DasGupta. 1991. Clostridium botulinum types A, B, CI, and E produce proteins with or without hemagglutinating activity: do they share common amino acid sequences and genes? J Protein Chem. 10: 415– 425.
175. Songer, J. G., 1997. Clostridial diseases of animals, p. 153– 182. In J. I. Rood,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, London, United Kingdom.
176. Stepanov, A. S.,, S. V. Gavrilov,, O. B. Puzanova,, T. M. Grigor'eva,, and R. R. Azizbekian. 1989. Plasmid transduction by Bacillus anthracis bacteriophage CP54. Mol. Gen. Mikrobiol. Virusol. 1: 14– 19.
177. Strauss, E. 1998. New clue to how anthrax kills. Science 280: 676.
178. Strom, M. S.,, M. W. Eklund,, and F. T. Poysky. 1984. Plasmids in Clostridium botulinum and related Clostridium species. Appl. Environ. Microbiol. 48: 956– 963.
179. Sugai, M.,, K. Hashimoto,, A. Kikuchi,, S. Inoue,, H. Okumura,, K. Matsumoto,, Y. Goto,, H. Ohgai,, K. Moriishi,, B. Syuto, et al. 1992. Epidermal cell differentiation inhibitor ADP-ribosylates small GTP-binding proteins and induces hyperplasia of epidermis. J. Biol. Chem. 267: 2600– 2604.
180. Sugiyama, H. 1980. Clostridium botulinum neurotoxin. Microbiol. Rev. 44: 419– 448.
181. Thompson, D. E.,, J. K. Brehm,, J. D. Oultram,, T. J. Swinfield,, C. C. Shone,, T. Atkinson,, J. Meiling,, and N. P. Minton. 1990. The complete amino acid sequence of the Clostridium botulinum type A neurotoxin, deduced by nucleotide sequence analysis of the encoding gene. Eur. J. Biochem. 189: 73– 81.
182. Thompson, D. E.,, R. A. Hutson,, A. K. East,, D. Allaway,, M. D. Collins,, and P. T. Richardson. 1993. Nucleotide sequence of the gene coding for Clostridium barati type F neurotoxin: comparison with other clostridial neurotoxins. FEMS Microbiol. Lett. 108: 175– 182.
183. Thorne, C. B., 1993. Bacillus anthracis, p. 113– 124. In A. L. Sonenshein,, J. A. Hoch,, and R. Losick (ed.), Bacillus subtilis and Other Gram-Positive Bacteria. American Society for Microbiology, Washington, D.C.
184. Thorne, C. B., 1985. Genetics of Bacillus anthracis, p. 56– 62. In L. Leive,, P. F. Bonventre,, J. A. Morello,, S. Schlesinger,, S. D. Silver,, and H. C. Wu (ed.), Microbiology—1985. American Society for Microbiology, Washington, D.C.
185. Thorne, C. B. 1968. Transduction in Bacillus cereus and Bacillus anthracis. Bacteriol. Rev. 32: 358– 361.
186. Thorne, C. B. 1978. Transduction in Bacillus thuringiensis. Appl. Environ. Microbiol. 35: 1109– 1115.
187. Tippetts, M. T.,, and D. L. Robertson. 1988. Molecular cloning and expression of the Bacillus anthracis edema factor toxin gene: a calmodulin-dependent adenylate cyclase. J. Bacteriol. 170: 2263– 2266.
188. Titball, R. W. 1993. Bacterial phospholipases C. Microbiol. Rev. 57: 347– 366.
189. Titball, R. W., 1997. Clostridial phospholipases, p. 223– 242. In J. I. Rood,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, London, United Kingdom.
190. Turnbull, P. C.,, R. A. Hutson,, M. J. Ward,, M. N. Jones,, C. P. Quinn,, N. J. Finnie,, C. J. Duggleby,, J. M. Kramer,, and J. Meiling. 1992. Bacillus anthracis but not always anthrax. J. Appl. Bacteriol. 72: 21– 28.
191. Turnbull, P. C.,, and J. M. Kramer,. 1991. Bacillus, p. 296– 303. In A. Balows,, W. J. Hausier Jr.,, K. L. Herrmann,, H. D. Isenberg,, and H. J. Shadomy (ed.), Manual of Clinical Microbiology, 5th ed. American Society for Microbiology, Washington, D.C.
192. Turnbull, P. C. B.,, and J. M. Kramer,. 1995. Bacillus, p. 349– 359. In P. R. Murray,, E. J. Baron,, M. A. Pfaller,, F. C. Tenover,, and R. H. Yolken (ed.), Manual of Clinical Microbiology, 6th ed. ASM Press, Washington, D.C.
193. Uchida, I.,, J. M. Hornung,, C. B. Thorne,, K. R. Klimpel,, and S. H. Leppla. 1993. Cloning and characterization of a gene whose product is a trans-activator of anthrax toxin synthesis. J. Bacteriol. 175: 5329– 5338.
194. Uchida, I.,, S. Makino,, C. Sasakawa,, M. Yoshikawa,, C. Sugimoto,, and N. Terakado. 1993. Identification of a novel gene, dep,associated with depolymerization of the capsular polymer in Bacillus anthracis. Mol. Microbiol. 9: 487– 496.
195. Van Damme Jongsten, M.,, J. Rodhouse,, R. J. Gilbert,, and S. Notermans. 1990. Synthetic DNA probes for detection of enterotoxigenic Clostridium perfringens strains isolated from outbreaks of food poisoning. J. Clin. Microbiol. 28: 131– 133.
196. Vietri, N. J.,, R. Marrero,, T. A. Hoover,, and S. L. Welkos. 1995. Identification and characterization of a trans-activator involved in the regulation of encapsulation by Bacillus anthracis. Gene 152: 1– 9.
196a. von Eichel-Streiber, C. Unpublished data.
197. von Eichel-Streiber, C.,, P. Boquet,, M. Sauerborn,, and M. Thelestam. 1996. Large clostridial cytotoxins—a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol. 4: 375– 382.
198. von Eichel-Streiber, C.,, D. Suckau,, M. Wachter,, and U. Hadding. 1989. Cloning and characterization of overlapping DNA fragments of the toxin A gene of Clostridium difficile. J. Gen. Microbiol. 135: 55– 64.
199. Weickert, M. J.,, G. H. Chambliss,, and H. Sugiyama. 1986. Production of toxin by Clostridium botulinum type A strains cured by plasmids. Appl. Environ. Microbiol. 51: 52– 56.
200. Welkos, S. L. 1991. Plasmid-associated virulence factors of non-toxigenic (pXOl —) Bacillus anthracis. Microb. Pathog. 10: 183– 198.
201. Welkos, S. L.,, J. R. Lowe,, F. Eden McCutchan,, M. Vodkin,, S. H. Leppla,, and J. J. Schmidt 1988. Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis. Gene 69: 287– 300.
202. Welkos, S. L.,, N. J. Vietri,, and P. H. Gibbs. 1993. Non-toxigenic derivatives of the Ames strain of Bacillus anthracis are fully virulent for mice: role of plasmid pX02 and chromosome in strain-dependent virulence. Microb. Pathog. 14: 381– 388.
203. Whelan, S. M.,, M. J. Elmore,, N. J. Bodsworth,, T. Atkinson,, and N. P. Minton. 1992. The complete amino acid sequence of the Clostridium botulinum type-E neurotoxin, derived by nucleotide-sequence analysis of the encoding gene. Eur. J. Biochem. 204: 657– 667.
204. Willems, A.,, A. K. East,, P. A. Lawson,, and M. D. Collins. 1993. Sequence of the gene coding for the neurotoxin of Clostridium botulinum type A associated with infant botulism: comparison with other clostridial neurotoxins. Res. Microbiol. 144: 547– 556.
205. Wilson, K.H. 1993. The microecology of Clostridium difficile. Clin. Infect. Dis. 16( Suppl. 4): S214– S218.
206. Yelton, D. B.,, and C. B. Thorne. 1971. Comparison of Bacillus cereus bacteriophages CP-51 and CP-53. J. Virol. 8: 242– 253.
207. Yelton, D. B.,, and C. B. Thorne. 1970. Transduction in Bacillus cereus by each of two bacteriophages. J. Bacteriol. 102: 573– 579.
208. Zhou, Y.,, H. Sugiyama,, and E. A. Johnson. 1993. Transfer of neurotoxigenicity from Clostridium butyricum to a nontoxigenic Clostridium botulinum type E-like strain. Appl. Environ. Microbiol. 59: 3825– 3831.
209. Zhou, Y.,, H. Sugiyama,, H. Nakano,, and E. A. Johnson. 1995. The genes for the Clostridium botulinum type G toxin complex are on a plasmid. Infect. Immun. 63: 2087– 2091.

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 V. 
 V. 
 V. 
 V. 
 V. 
 V. 
 V. 
 V.