Virulence Plasmids of Spore-Forming Bacteria

Julian I. Rood

doi:10.1128/9781555817732.ch19

Chapter 19 : Virulence Plasmids of Spore-Forming Bacteria

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Affiliations: 1: Australian Bacterial Pathogenesis Program, Department of Microbiology, Monash University 3800, Australia

Content Type: Monograph

Publication Year: 2004

Category: Microbial Genetics and Molecular Biology

Book DOI: 10.1128/9781555817732

Chapter DOI: 10.1128/9781555817732.ch19

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Abstract:

Spore-forming bacteria are the causative agents of some of the most dramatic life-threatening human and animal infections and toxemias, including diseases such as tetanus, botulism, gas gangrene, pseudomembranous colitis, and anthrax. This chapter reviews the current state of knowledge of virulence plasmids of the Clostridia and the bacilli. Although other pathogens are mentioned, the focus is on the major human pathogens, Clostridium perfringens and Bacillus anthracis, primarily because most is known about virulence plasmids in these species. The major toxins involved in C. perfringens type A-mediated gas gangrene, the α-toxin and perfringolysin O, together with other extracellular toxins such as collagenase and hyaluronidase, are chromosomally encoded. Along with tetanus, botulism, and gas gangrene, anthrax is one of the four classical diseases that are caused by spore-forming bacteria. Expression of the plasmid-determined toxin genes in Bacillus thuringiensis is coordinately regulated with the sporulation process and therefore clearly involves chromosomal regulatory genes. Toxin-producing strains often carry multiple cry genes and large amounts of the δ-endotoxins are produced in stationary phase, to the extent that the crystalline inclusion may account for more than 20% of the cell's dry weight.

Citation: Rood J. 2004. Virulence Plasmids of Spore-Forming Bacteria, p 413-422. In Funnell B, Phillips G (ed), Plasmid Biology. ASM Press, Washington, DC. doi: 10.1128/9781555817732.ch19

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Virulence Plasmids of Spore-Forming Bacteria

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Citation: Rood J. 2004. Virulence Plasmids of Spore-Forming Bacteria, p 413-422. In Funnell B, Phillips G (ed), Plasmid Biology. ASM Press, Washington, DC. doi: 10.1128/9781555817732.ch19

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Figure 1

Genetic organization of the botulinum toxin region. Based on Fig. 1 of reference 36 .

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Figure 1

Genetic organization of the botulinum toxin region. Based on Fig. 1 of reference 36 .

Citation: Rood J. 2004. Virulence Plasmids of Spore-Forming Bacteria, p 413-422. In Funnell B, Phillips G (ed), Plasmid Biology. ASM Press, Washington, DC. doi: 10.1128/9781555817732.ch19

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Figure 2

Regulation of anthrax toxin production and capsule biosynthesis in B. anthracis. Only relevant genes on pXO1 and pXO2 are shown. Neither the plasmids nor the genes are drawn to scale. The arrows indicate transcriptional activation, the bars indicate transcriptional repression.

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10.1128/9781555817732/fig19-2.gif

Figure 2

Citation: Rood J. 2004. Virulence Plasmids of Spore-Forming Bacteria, p 413-422. In Funnell B, Phillips G (ed), Plasmid Biology. ASM Press, Washington, DC. doi: 10.1128/9781555817732.ch19

References

/content/book/10.1128/9781555817732.chap19

1. Andrup, L.,, L. Smidt,, K. Andersen,, and L. Boc. 1998. Kinetics of conjugative transfer: a study of the plasmid pXO16 from Bacillus thuringiensis subsp. israelensis. Plasmid 40: 30– 43.

2. Ariel, N.,, A. Zvi,, H. Grosfeld,, O. Gat,, Y. Inbar,, B. Velan,, S. Cohen,, and A. Shafferman. 2002. Search for potential vaccine candidate open reading frames in the Bacillus anthracis virulence plasmid pXO1: in silico and in vitro screening. Infect. Immun. 70: 6817– 6827.

3. Aronson, A. 2002. Sporulation and delta-endotoxin synthesis by Bacillus thuringiensis. Cell Mol. Life Sci. 59: 417– 425.

4. Ben-Dov, E.,, G. Nissan,, N. Pelleg,, R. Manasherob,, S. Boussiba,, and A. Zaritsky. 1999. Refined, circular restriction map of the Bacillus thuringiensis subsp. israelensis plasmid carrying the mosquito larvicidal genes. Plasmid 42: 186– 191.

5. Bentancor, A. B.,, M. R. Fermepi'n,, L. D. Bentancor,, and R. A. de Torres. 1999. Detection of the etx gene (ϵ-toxin inducer) in plasmids of high molecular weight in Clostridium perfringens type D. FEMS Immunol. Med. Microbiol. 24: 373– 377.

6. Berry, C.,, S. O'Neil,, E. Ben-Dov,, A. F. Jones,, L. Murphy,, M. A. Quail,, M. T. Holden,, D. Harris,, A. Zaritsky,, and J. Parkhill. 2002. Complete sequence and organization of pBtoxis, the toxin-coding plasmid of Bacillus thuringiensis subsp. israelensis. Appl. Environ. Microbiol. 68: 5082– 5095.

7. Billington, S. J.,, E. U. Wieckowski,, M. R. Sarker,, D. Bueschel,, J. G. Songer,, and B. A. McClane. 1998. Clostridium perfringens type E animal enteritis isolates with highly conserved, silent enterotoxin gene sequences. Infect. Immun. 66: 4531– 4536.

8. Brüggemann, H.,, S. Bäumer,, W. F. Fricke,, A. Wiezer,, H. Liesegang,, I. Decker,, C. Herzberg,, R. Martinez-Arias,, R. Merkl,, A. Henne,, and G. Gottschalk. 2003. The genome sequence of Clostridium tetani, the causative agent of tetanus disease. Proc. Natl. Acad. Sci. USA 100: 1316– 1321.

9. Brynestad, S.,, and P. E. Granum. 1999. Evidence that Tn 5565, which includes the enterotoxin gene in Clostridium perfringens, can have a circular form which may be a transposition intermediate. FEMS Microbiol. Lett. 170: 281– 286.

10. Brynestad, S.,, M. R. Sarker,, B. A. McClane,, P. E. Granum,, and J. I. Rood. 2001. Enterotoxin plasmid from Clostridium perfringens is conjugative. Infect. Immun. 69: 3483– 3487.

11. Brynestad, S.,, B. Synstad,, and P. E. Granum. 1997. The Clostridium perfringens enterotoxin gene is on a transposable genetic element in type A human food poisoning strains. Microbiology 143: 2109– 2115.

12. 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.

13. Collie, R. E.,, and B. A. McClane. 1998. Evidence that the enterotoxin gene can be episomal in Clostridium perfringens isolates associated with nonfoodborne human gastrointestinal disease. J. Clin. Microbiol. 36: 30– 36.

14. Cornillot, E.,, B. Saint-Joanis,, G. Daube,, S.-I. 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.

15. 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.

16. Daube, G.,, P. Simon,, and A. Kaeckenbeeck. 1993. IS 1151, an IS-like element of Clostridium perfringens. Nucleic Acids Res. 21: 352.

17. Dupuy, B.,, G. Daube,, M. R. Popoff,, and S. T. Cole. 1997. Clostridium perfringens urease genes are plasmid borne. Infect. Immun. 65: 2313– 2320.

18. Dupuy, B.,, and A. Sonenshein. 1999. Regulated transcription of Clostridium difficile toxin genes. Mol. Microbiol. 27: 107– 120.

19. Eisel, U.,, W. Jarausch,, K. Goretzki,, A. Henschen,, J. Engels,, U. Weller,, M. Hudel,, E. Habermann,, and H. Niemann. 1986. Tetanus toxin: primary structure, expression in E. coli. EMBO J. 5: 2495– 2502.

20. 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.

21. Finn, Jr.,, C.,, R. Silver,, W. Habig,, M. Hardegrec,, G. Zon,, and C. Garon. 1984. The structural gene for tetanus neurotoxin is on a plasmid. Science 224: 881– 884.

22. Fischetti, V. A.,, R. P. Novick,, J. J. Ferretti,, D. A. Portnoy,, and J. I. Rood (ed.). 2000. Gram-Positive Pathogens. ASM Press, Washington, D.C..

23. Garmory, H. S.,, N. Chanter,, N. P. French,, D. Bueschel,, J. G. Songer,, and R. W. Titball. 2000. Occurrence of Clostridium perfringens beta2-toxin amongst animals, determined using genotyping and subtyping PCR assays. Epidemiol. Infect. 124: 61– 67.

24. Gibert, M.,, C. Jolivet-Renaud,, and M. R. Popoff, 1997. Beta2 toxin, a novel toxin produced by Clostridium perfringens. Gene 203: 65– 73.

25. Gibert, M.,, S. Perelle,, G. Daube,, and M. Popoff. 1997. Clostridium spiroforme toxin genes are related to C. perfringens iota toxin genes but have a different genomic localization. Syst. Appl. Microbiol. 20: 337– 347.

26. Green, B. D.,, L. Battisti,, and C. B. Thorne. 1989. Involvement of Tn 4430 in transfer of Bacillus anthracis plasmids mediated by Bacillus thuringiensis plasmid pXO12. J. Bacteriol. 171: 104– 113.

27. Guidi-Rontani, C.,, Y. Pereira,, S. Ruffie,, J. C. Sirard,, M. Weber-Levy,, and M. Mock. 1999. Identification and characterization of a germination operon on the virulence plasmid pXO1 of Bacillus anthracis. Mol. Microbiol. 33: 407– 414.

28. Guidi-Rontani, C.,, M. Weber-Levy,, E. Labruyere,, and M. Mock. 1999. Germination of Bacillus anthracis spores with alveolar macrophages. Mol. Microbiol. 31: 9– 17.

29. 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– 7.

30. Han, S.,, J. A. Craig,, C. D. Putnam,, N. B. Carozzi,, and J. A. Tainer. 1999. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nature Struct. Biol. 6: 932– 936.

31. 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. 99: 251– 256.

32. Helgason, E.,, O. A. Okstad,, D. A. Caugant,, H. A. Johansen,, A. Fouet,, M. Mock,, I. Hegna,, and A.-B. Kolsto. 2000. Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis—one species on the basis of genetic evidence. Appl. Environ. Microbiol. 66: 2627– 2630.

33. Herholz, C.,, R. Miserez,, J. Nicolet,, J. Frey,, M. Popoff,, M. Gibert,, H. Gerber,, and R. Straub. 1999. Prevalence of β-toxigenic Clostridium perfringens in horses with intestinal disorders. J. Clin. Microbiol. 37: 358– 361.

34. Hoffmaster, A. R.,, and T. M. Koehler. 1999. Autogenous regulation of the Bacillus anthracis pag operon. J. Bacteriol. 181: 4485– 4492.

35. Hoffmaster, A. R.,, and T. M. Koehler. 1999. Control of virulence gene expression in Bacillus anthracis. J. Appl. Bacteriol. 87: 279– 281.

36. Johnson, E. A.,, and M. Bradshaw, 2001. Clostridium botulinum and its neurotoxins: a metabolic and cellular perspective. Toxicon 39: 1703– 1722.

37. 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.

38. Klaasen, H. L.,, M. J. Molkenboer,, J. Bakker,, R. Miserez,, H. Hani,, J. Frey,, M. R. Popoff,, and J. F. van den Bosch. 1999. Detection of the beta2 toxin gene of Clostridium perfringens in diarrhoeic piglets in The Netherlands and Switzerland. FEMS Immunol. Med. Microbiol. 24: 325– 332.

39. Koehler, T. M., 2000. Bacillus anthracis, p. 519– 528. In V. A. Fischetti,, J. J. Ferretti,, D. A. Portnoy,, R. P. Novick,, and J. I. Rood (ed.), Gram-Positive Pathogens. ASM Press, Washington, D.C..

40. Laird, W.,, W. Aaronson,, R. Silver,, W. Habig,, and M. Hardegree. 1980. Plasmid-associated toxigenicity in Clostridium tetani. J. Infect. Dis. 142: 623.

41. Mani, N.,, and B. Dupuy. 2001. Regulation of toxin synthesis in Clostridium difficile by an alternative RNA polymerase sigma factor. Proc. Natl. Acad. Sci. USA 98: 5844– 5849.

42. Manteca, C.,, G. Daube,, T. Jauniaux,, A. Linden,, V. Pirson,, J. Detilleux,, A. Ginter,, P. Coppe,, A. Kaeckenbeeck,, and J. G. Mainil. 2002. A role for the Clostridium perfringens beta2 toxin in bovine entcrotoxaemia? Vet. Microbiol. 86: 191– 202.

43. Marvaud, J.,, M. Gibert,, K. Inoue,, Y. Fujinaga,, K. Oguma,, and M, 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.

44. Marvaud, J.- C.,, U. Eisel,, T. Binz,, H. Niemann,, and M. R. Popoff. 1998. TetR is a positive regulator of the tetanus toxin gene in Clostridium tetani and is homologous to BotR. Infect. Immun. 66: 5698– 5702.

45. Marvaud, J. C.,, S. Raffestin,, M. Gibert,, and M. R. Popoff. 2000. Regulation of the toxinogenesis in Clostridium botulinum and Clostridium tetani. Biol. Cell. 92: 455– 457.

46. Marvaud, J. C.,, T. Smith,, M. L. Hale,, M. R. Popoff,, L. A. Smith,, and B. G. Stiles. 2001. Clostridium perfringens iota-toxin: mapping of receptor binding and Ia docking domains on Ib. Infect. Immun. 69: 2435– 2441.

47. Menestrina, G.,, M. D. Serra,, and G. Prevost. 2001. Mode of action of beta-barrel pore-forming toxins of the staphylococcal alpha-hemolysin family. Toxicon 39: 1661– 1672.

48. Mesnage, S.,, and A. Fouet. 2002. Plasmid-encoded autolysin in Bacillus anthracis: modular structure and catalytic properties. J. Bacteriol. 184: 331– 334.

49. Mignot, T.,, M. Mock,, and A. Fouet. 2003. A plasmid-encoded regulator couples the synthesis of toxins and surface structures in Bacillus anthracis. Mol. Microbiol. 47: 917– 927.

50. Minami, J.,, S. Katayama,, O. Matsushita,, C. Matsushita,, and A. Okabe. 1997. Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides. Microbiol. Immunol. 41: 527– 535.

51. Miyamoto, K.,, G. Chakrabarti,, Y. Morino,, and B. A. McClane. 2002. Organization of the plasmid cpe locus in Clostridium perfringens type A isolates. Infect. Immun. 70: 4261– 4272.

52. Miyata, S.,, O. Matsushita,, J. Minami,, S. Katayama,, S. Shimamoto,, and A. Okabe. 2001. Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens e-toxin in the synaptosomal membrane. J. Biol. Chem. 276: 13778– 13783.

53. Mock, M.,, and A. Fouet. 2001. Anthrax. Annu. Rev. Microbiol. 55: 647– 671.

54. Okinaka, R.,, K. Cloud,, O. Hampton,, A. Hoffmastcr,, K. Hill,, P. Keim,, T. Koehler,, G. Lamke,, S. Kumano,, D. Manter,, Y. Martinez,, D. Ricke,, R. Svensson,, and P. Jackson. 1999. Sequence, assembly and analysis of pX01 and pX02. J. Appl. Bacteriol. 87: 261– 262.

55. Okinaka, R. T.,, K. Cloud,, O. Hampton,, A. R. Hoffmaster,, K. K. Hill,, P. Keim,, T. M. Koehler,, G. Lamke,, S. Kumano,, J. Mahillon,, D. Manter,, Y. Martinez,, D. Ricke,, R. Svensson,, and P. J. Jackson. 1999. Sequence and organization of pXO1, the large Bacillus anthracis plasmid harboring the anthrax toxin genes. J. Bacteriol. 181: 6509– 6515.

56. Pannucci, J.,, R. T. Okinaka,, R. Sabin,, and C. R. Kuske. 2002. Bacillus anthracis pXO1 plasmid sequence conservation among closely related bacterial species. J. Bacteriol. 184: 134– 141.

57. Pannucci, J.,, R. T. Okinaka,, E. Williams,, R. Sabin,, L. O. Ticknor, and C R. Kuske. 2002. DNA sequence conservation between the Bacillus anthracis pXO2 plasmid and closely related bacteria. BMC Genomics 3: 34.

58. Payne, D.,, and P. Oyston,. 1997. The Clostridium perfringens ϵ-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.

59. Perelle, S.,, S. Sealzo,, S. Kochi,, M. Mock,, and M. R. Popoff. 1997. Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins. FEMS Microbiol. Lett. 146: 117– 121.

60. Petit, L.,, M. Gibert,, and M. R. Popoff. 1999. Clostridium perfringens: toxinotype and genotype. Trends Microbiol. 7: 104– 110.

61. Petit, L.,, E. Maier,, M. Gibert,, M. R. Popoff,, and R. Benz. 2001. Clostridium perfringens epsilon toxin induces a rapid change of cell membrane permeability to ions and forms channels in artificial lipid bilayers. J. Biol. Chem. 276: 15736– 15740.

62. Reddy, A.,, L. Battisti,, and C. B. Thorne, 1987. Identification of self-transmissible plasmids in four Bacillus thuringiensis subspecies. J. Bacteriol. 169: 5263– 5270.

63. Rood, J. I.,, and B. A. McClane,. 2002. Clostridium perfringens: gastrointestinal infections, p. 1117– 1139. In M. Sussman (ed.), Molecular Medical Microbiology. Academic Press, London, United Kingdom.

64. Rood, J. I.,, B. A. McClane,, J. G. Songer,, and R. W. Titball (ed.). 1997. The Clostridia: Molecular Biology and Pathogenesis. Academic Press, London, United Kingdom.

65. Saile, E.,, and T. M. Koehler. 2002. Control of anthrax toxin gene expression by the transition state regulator abrB. J. Bacteriol. 184: 370– 380.

66. Sarker, M. R.,, R. J. Carman,, and B. A. McClane. 1999. Inactivation of the gene ( cpe) encoding Clostridium perfringens enterotoxin eliminates the ability of two cpe-positive C. perfringens type A human gastrointestinal disease isolates to affect rabbit ileal loops. Mol. Microbiol. 33: 946– 958.

67. Schiavo, G.,, and C. Montccucco,. 1997. The structure and mode of action of botulinum and tetanus toxins, 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.

68. 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.

69. Shao, Z.,, Z. Liu,, and Z. Yu. 2001. Effects of the 20-kilodalton helper protein on Cry1Ac production and spore formation in Bacillus thuringiensis. Appl. Environ. Microbiol. 67: 5362– 5369.

70. Shatursky, O.,, R, Bayles,, M. Rogers,, B. H. Jost,, J. G. Songer,, and R. K. Tweten. 2000. Clostridium perfringens beta-toxin forms potential-dependent, cation-selective channels in lipid bilayers. Infect. Immun. 68: 5546– 5551.

71. Shimizu, T., K. Ohtani,, H. Hirakawa,, K. Ohshima,, A. Yamashita,, T. Shiba,, N. Ogasawara,, M. Hattori,, S. Kuhara,, and H. Hayashi. 2002. Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc. Natl. Acad. Sci. USA 99: 996– 1001.

72. Sonenshein, A. L.,, J. A. Hoch,, and R. Losick. 2001. Bacillus subtilis and Its Closest Relatives: From Genes to Cells. ASM Press, Washington, D.C..

73. 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.

74. Sparks, S.,, R. Carman,, M. Sarker,, and B. A. McClanc. 2001. Genotyping of enterotoxigenic Clostridium perfringens fecal isolates associated with antibiotic-associated diarrhea and food poisoning in North America. J. Clin. Microbiol. 39: 883– 888.

75. Steinthórsdóttir, V.,, H. Halldórsson,, and O. S. Andrésson. 2000. Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells. Microbial Pathogen 28: 45– 50.

76. Thomas, D. J.,, J. A. Morgan,, J. M. Whipps,, and J. R. Saunders. 2001. Plasmid transfer between Bacillus thuringiensis subsp. israelensis strains in laboratory culture, river water, and dipteran larvae. Appl. Environ. Microbiol. 67: 330– 338.

77. Titball, R. W.,, and J. I. Rood,. 2002. Clostridium perfringens: wound infections, p. 1875– 1903. In M. Sussman (ed.), Molecular Medical Microbiology. Academic Press, London, United Kingdom.

78. Tweten, R, K. 2001. Clostridium perfringens beta toxin and Clostridium septicum alpha toxin: their mechanisms and possible role in pathogenesis. Vet. Microbiol. 82: 1– 9.

79. Uchida, I.,, S. Makino,, T. Sekizaki,, and N. Terakado. 1997. Cross-talk to the genes for Bacillus anthracis capsule synthesis by atxA, the gene encoding the trans-activator of anthrax toxin synthesis. Mol. Microbiol. 23: 1229– 1240.

80. Vitale, G.,, L. Bernardi,, G. Napolitani,, M. Mock,, and C. Montecucco. 2000. Susceptibility of mitogen-activatcd protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 352: 739– 745.

81. Wang, X.,, T. Maegawa,, T. Karasawa,, S. Kozaki,, K. Tsukamoto,, Y. Gyobu,, K. Yamakawa,, K. Oguma,, Y. Sakaguchi,, and S. Nakamura. 2000. Genetic analysis of type E botulinum toxin-producing Clostridium butyricum strains. Appl. Environ. Microbiol. 66: 4992– 4997.

82. Wilcks, A.,, N. Jayaswal,, D. Lereclus,, and L. Andrup. 1998. Characterization of plasmid pAW63, a second self-transmissible plasmid in Bacillus thuringiensis subsp. kurstaki HD73. Microbiology 144: 1263– 1270.

83. Wilcks, A.,, L. Smidt,, O. A. Okstad,, A. B. Kolsto,, J. Mahillon,, and L. Andrup. 1999. Replication mechanism and sequence analysis of the replicon of pAW63, a conjugative plasmid from Bacillus thuringiensis. J. Bacteriol. 181: 3193– 3200.

84. Zhou, Y.,, H. Sugiyama,, and E. A. Johnson. 1993. Transfer of neurotoxigeniciry from Clostridium butyricum to a nontoxigenic Clostridium botulinum type E-like strain. Appl. Environ. Microbiol. 59: 3825– 3831.

85. 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.

Tables

Virulence Plasmids of Spore-Forming Bacteria

Citation: Rood J. 2004. Virulence Plasmids of Spore-Forming Bacteria, p 413-422. In Funnell B, Phillips G (ed), Plasmid Biology. ASM Press, Washington, DC. doi: 10.1128/9781555817732.ch19

/content/10.1128/9781555817732.chap19.tab19-1

Table 1

Genetic location of toxins and extracellular enzymes of C. perfringens

10.1128/9781555817732/tab19-1_thmb.gif

10.1128/9781555817732/tab19-1.gif

Table 1

Genetic location of toxins and extracellular enzymes of C. perfringens

Citation: Rood J. 2004. Virulence Plasmids of Spore-Forming Bacteria, p 413-422. In Funnell B, Phillips G (ed), Plasmid Biology. ASM Press, Washington, DC. doi: 10.1128/9781555817732.ch19