1887

Chapter 8 :

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Preview this chapter:
Zoom in
Zoomout

, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555818388/9781555810535_Chap08-1.gif /docserver/preview/fulltext/10.1128/9781555818388/9781555810535_Chap08-2.gif

Abstract:

, the causative agent of anthrax, is the only member of the genus that is capable of causing epidemic disease in humans and other mammals. The capsule is one of the virulence factors of . Evidence that bicarbonate is involved in the regulation of capsule synthesis is presented in the discussion of the capsule plasmid pX02. For several years, it was believed that the anthrax toxin was made up of only two components, but it was later established that the toxin actually consists of three proteins. It has been demonstrated that lethal factor (LF) in combination with protective antigen (PA) lysed mouse peritoneal macrophages, as evidenced by loss of lactic dehydrogenase activity. This in vitro system for studying anthrax lethal toxin activity should expedite one's understanding of the toxic reaction. Gene exchange systems performed by transduction, transformation (transfer of plasmids by mating) and transposon mutagenesis are discussed. One of the most active reactions was that between D-phenylalanine and pyruvate, forming alanine and phenylpyruvate. The vaccine commonly used to immunize livestock against anthrax vaccines consists of live spores of a toxigenic, noncapsulated strain, i.e., a strain that has been cured of the capsule plasmid, pXO2, but still carries the toxin plasmid, pXO1. The principal antigen in the vaccine is PA. Several doses of PA vaccines have to be given initially, and frequent booster doses are necessary to sustain antibody titers.

Citation: Thorne C. 1993. , p 113-124. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch8
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of Figure 1
Figure 1

and restriction maps of toxin-encoding region of pXO 1. A 77-kb region of pXO 1 encompassing the toxin structural genes is shown. (A) pXOl from Sterne (USAMRIID). (B) pXOl from Weybridge A. The maps suggest that an inversion has occurred, as depicted in the diagram. The inverted region represents approximately 40 kb. Arrows indicate the approximate locations and directions of transcription of the and genes as shown on the restriction map of pXOl reported by Robertson et al. ( ).

Citation: Thorne C. 1993. , p 113-124. In Sonenshein A, Hoch J, Losick R (ed), and Other Gram-Positive Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555818388.ch8
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555818388.chap8
1. Ash, C.,, J. A. E. 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.
2. Avakyan, A. A.,, L. N. Katz,, K. N. Levina,, and I. B. Pavlova. 1965. Structure and composition of the Bacillus anthracis capsule. J. Bacteriol. 90: 1082 1095.
3. Bartkus, J. M.,, and S. H. Leppla. 1989. Transcriptional regulation of the protective antigen gene of Bacillus anthracis. Infect. Immun. 57: 2295 2300.
4. Battisti, L.,, B. D. Green,, and C. B. Thorne. 1985. Mating system for transfer of plasmids among Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis. J. Bacteriol. 162: 543 550.
5. Beall, F. A.,, M. J. Taylor,, and C. B. Thorne. 1962. Rapid lethal effect in rats of a third component found upon fractionating the toxin of Bacillus anthracis. J. Bacteriol. 83: 1274 1280.
6. Belton, F. C.,, and R. E. Strange. 1954. Studies on a protective antigen produced in vitro from Bacillus anthracis: medium and methods of production. Br. J. Exp. Pathol. 35: 144 152.
7. Bernhard, K.,, H. Schrempf,, and W. Goebel. 1978. Bacteriocin and antibiotic resistance plasmids in Bacillus cereus and Bacillus subtilis. J. Bacteriol. 133: 897 903.
8. Bhatnagar, R.,, Y. Singh,, S. H. Leppla,, and A. M. Friedlander. 1989. Calcium is required for the expression of anthrax lethal toxin activity in the macrophage-like cell line J774A.1. Infect. Immun. 57: 2107 2114.
9. Bohm, R.,, and G. Spath,. 1990. The taxonomy of Bacillus anthracis according to DNA-DNA hybridization and G+C content, p. 29 31. In P. C. Turnbull (ed.), Proceedings of the International Wortehop on Anthrax, Winchester, England. Salisbury medical bulletin, no. 68, special supplement. Salisbury Medical Society, Salisbury, England.
10. 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.
11. Brewer, C. R.,, W. G. McCullough,, R. C. Mills,, W. G. Roessler,, E. J. Herbst,, and A. F. Howe. 1946. Studies on the nutritional requirements of Bacillus anthracis. Arch. Biochem. 10: 65 75.
12. Bricas, E.,, and C. Fromageot. 1953. Naturally occurring peptides. Adv. Protein Chem. 8: 1 125.
13. Bruckner, V.,, M. Kajtar,, J. Kovacs,, H. Nagy,, and J. Wein. 1958. Synthese des immunspezifischen, polypep-tid-artigen Haptens der anthrax-subtilis Bacillen-Gruppe. Ein synthetischer Beweis der Konstitution der naturlichen Poly-glutaminsauren. Tetrahedron 2: 211 240.
14. Bruckner, V.,, J. Kovacs,, and G. Denes. 1953. Structure of poly-D-glutamic acid isolated from capsulated strains of B. anthracis. Nature (London) 172: 508.
15. Burdon, K. L.,, and R. D. Wende. 1960. On the differentiation of anthrax bacilli from Bacillus cereus. J. Infect. Dis. 107: 224 234.
16. Cataldi, A.,, E. Labruyere,, and M. Mock. 1990. Construction and characterization of a protective antigen-deficient Bacillus anthracis strain. Mol. Microbiol. 4: 1111 1117.
17. Cole, H. B.,, J. W. Ezzell,, K. F. Keller,, and R. J. Doyle. 1984. Differentiation of Bacillus anthracis and other Bacillus species by lectins. J. Clin. Microbiol. 19: 48 53.
18. Cromartie, W. J.,, W. L. Bloom,, and D. W. Watson. 1947. Studies on infection with Bacillus anthracis. I. A histo-pathological study of skin lesions produced by B. anthracis in susceptible and resistant animal species. J. Infect. Dis. 80: 1 13.
19. Cromartie, W. J.,, D. W. Watson,, W. L. Bloom,, and R. J. Heckly. 1947. Studies on infection with Bacillus anthracis. II. The immunological and tissue damaging properties of extracts prepared from lesions of B. anthracis infections. J. Infect. Dis. 80: 14 27.
20. Dunny, G. M.,, L. N. Lee,, and D. J. LeBlanc. 1991. Improved electroporation and cloning vector system for gram-positive bacteria. Appi. Environ. Microbiol. 57: 1194 1201.
21. Eastin, J. D.,, and C. B. Thorne. 1963. Carbon dioxide fixation in Bacillus anthracis. J. Bacteriol. 85: 410 417.
22. Escuyer, V.,, and R. J. Collier. 1991. Anthrax protective antigen interacts with a specific receptor on the surface of CHO-K1 cells. Infect. Immun. 59: 3381 3386.
23. Fish, D. C.,, B. G. Mahlandt,, J. P. Dobbs,, and R. E. Lincoln. 1968. Purification and properties of in vitroproduced anthrax toxin components. J. Bacteriol. 95: 907 918.
24. Franke, A. E.,, and D. B. Clewell. 1981. Evidence for a chromosome-borne resistance transposon (Tn 916) in Streptococcus faecalis that is capable of "conjugal" transfer in the absence of a conjugative plasmid. J. Bacteriol. 145: 494 502.
25. Friedlander, A. M. 1986. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261: 7123 7126.
26. Gardner, J. M.,, and F. A. Troy. 1979. Chemistry and biosynthesis of the poly(y-d-glutamyl) capsule in Bacillus licheniformis. Activation, racemization, and polymerization of glutamic acid by a membranous polyglu-tamyl synthetase complex. J. Biol. Chem. 254: 6262 6269.
27. Gladstone, G. P. 1939. Inter-relationships between amino acids in the nutrition of B. anthracis. Br. J. Exp. Pathol. 20: 189 200.
28. Gladstone, G. P. 1946. Immunity to anthrax: protective antigen present in cell-free culture filtrates. Br. J. Exp. Pathol. 27: 394 418.
29. 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.
30. Green, B. D.,, L. Battisti, and C. B. Thorne. 1989. Involvement of Tn4430 in transfer of Bacillus anthracis plasmids mediated by Bacillus thuringiensis plasmid pX012. J. Bacteriol. 171: 104 113.
31. Gryczan, T. J.,, S. Contente,, and D. Dubnau. 1978. Characterization of Staphylococcus aureus plasmids introduced by transformation into Bacillus subtilis. J. Bacteriol. 134: 318 329.
32. Guaracao-Ayala, A. I.,, and C. B. Thome. Unpublished data.
33. Guaracao-Ayala, A. I.,, and C. B. Thorne. 1991. Transposon mutagenesis of Bacillus anthracis capsule plasmid pX02, abstr. D-120, p. 98. Abstr. 91st Gen. Meet. Am. Soc. Microbiol. 1991.
34. Guex-Holzer, S.,, and J. Tomcsik. 1956. The isolation and chemical nature of capsular and cell-wall haptens in a Bacillus species. J. Gen. Microbiol. 14: 14 25.
35. Hanby, W. E.,, and H. N. Rydon. 1946. The capsular substance of Bacillus anthracis. Biochem. J. 40: 297 309.
36. Hara, T.,, Y. Fujio,, and S. Ueda. 1982. Polyglutamate production by Bacillus subtilis (natto). J. Appl. Biochem. 4: 112 120.
37. Harris-Smith, P. W.,, H. Smith,, and J. Keppie. 1958. Production in vitro of the toxin of Bacillus anthracis previously recognized in vivo. J. Gen. Microbiol. 19: 91 103.
38. Homung, J.,, and C. B. Thome. Unpublished data.
39. Homung, J. M.,, A. I. Guaracao-Ayala,, and C. B. Thome. 1989. Transposon mutagenesis in Bacillus anthracis, abstr. H-256, p. 212. Abstr. 89th Annu. Meet. Am. Soc. Microbiol. 1989.
40. Homung, J. M.,, and C. B. Thome. 1991. Insertion mutations affecting pXOl-associated toxin production in Bacillus anthracis, abstr. D-121, p. 98. Abstr. 91st Gen. Meet. Am. Soc. Microbiol. 1991.
41. Ivanovlcs, G.,, and V. Bruckner. 1937. Die chemische Struktur der Kapsel substanz des Milzbrandbazillus und der serologisch identischen spezifischen Substanz des Bacillus mesentericus. Z. Immunitatsforsch. 90: 304 318.
42. Ivins, B. E.,, J. W. Ezzell, Jr.,, J. Jemski,, K. W. Hedlund,, J. D. Ristroph,, and S. H. Leppla. 1986. Immunization studies with attenuated strains of Bacillus anthracis. Infect. Immun. 52: 454 458.
43. Ivins, B. E.,, and S. L. Welkos. 1986. Cloning and expression of the Bacillus anthracis protective antigen gene in Bacillus subtilis. Infect. Immun. 54: 537 542.
44. Ivins, B. E.,, S. L. Welkos,, G. B. Knudson,, and D. J. LeBlanc. 1988. Transposon Tn 916 mutagenesis in Bacillus anthracis. Infect. Immun. 56: 176 181.
45. Kaneko, T.,, R. Nozaki,, and K. Aizawa. 1978. Deoxyribonucleic acid relatedness between Bacillus anthracis, Bacillus cereus and Bacillus thuringiensis. Microbiol. Immunol. 22: 639 641.
46. Koehler, T. M. 1987. Plasmid-related differences in capsule production by Bacillus anthracis and characterization of a fertility plasmid from Bacillus subtilis (natto). Ph.D. dissertation. University of Massachusetts, Amherst.
47. Koehler, T. M.,, R. E. Ruhfel,, B. D. Green,, and C. B. Thorne. 1986. Plasmid-related differences in capsule production by Bacillus anthracis, abstr. H-178, p. 157. Abstr. 86th Annu. Meet. Am. Soc. Microbiol. 1986.
48. Koehler, T. M.,, and C. B. Thorne. 1987. Bacillus subtilis (natto) plasmid pLS20 mediates interspecies plasmid transfer. J. Bacteriol. 169: 5271 5278.
49. Larson, D. K.,, G. J. Calton,, S. F. Little,, S. H. Leppla,, and J. W. Burnett. 1988. Separation of three exotoxic factors of Bacillus anthracis by sequential immunosorbent chromatography. Toxican 26: 913 921.
50. Lawrence, D.,, S. Heitefuss,, and H. S. H. Seifert. 1991. Differentiation of Bacillus anthracis from Bacillus cereus by gas chromatography whole-cell fatty acid analysis. J. Clin. Microbiol. 29: 1508 1512.
51. Leise, J. M.,, C. H. Carter,, H. Friedlander,, and S. W. Fried. 1959. Criteria for identification of Bacillus anthracis. J. Bacteriol. 77: 655 660.
52. Leonard, C. G.,, and R. D. Housewright. 1963. Polyglu-tamic acid synthesis by cell-free extracts of Bacillus licheniformis. Biochim. Biophys. Acta 73: 530 532.
53. Leonard, C. G.,, R. D. Housewright,, and C. B. Thome. 1958. Effects of some metallic ions on glutamyl polypeptide synthesis by Bacillus subtilis. J. Bacteriol. 76: 499 503.
54. Leppla, S. H. 1982. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations in eucaryotic cells. Proc. Natl. Acad. Sci. USA 79: 3162 3166.
55. Leppla, S. H. 1984. Bacillus anthracis calmodulin-de-pendent adenylate cyclase: chemical and enzymatic properties and interactions with eucaryotic cells. Adv. Cyclic Nucleotide Protein Phosphorylation Res. 17: 189 198.
56. Leppla, S. H. 1988. Production and purification of anthrax toxin. Methods Enzymol. 165: 103 116.
57. Leppla, S. H.,, A. M. Friedlander,, and E. Cora,. 1987. Proteolytic activation of anthrax toxin bound to cellular receptors, p. 111 112. In F. Fehrenback,, J. E. Alouf,, P. Falmagne,, W. Goebel,, J. Jeljaszewicz,, D. Jurgens,, and R. Rappuoli (ed.). Bacterial Toxins. Gustav Fischer Verlag, Stuttgart, Germany.
58. Lereclus, D.,, J. Mahillon,, G. Menou,, and M.-M. Leca-det. 1986. Identification of Tn 4430, a transposon of Bacillus thuringiensis functional in Escherichia coli. Mol. Gen. Genet. 204: 52 57.
59. Lesnyak, O. T.,, and R. A. Saltykov. 1970. Comparative assessment of the immunogenicity of anthrax vaccine strains. Zh. Mikrobiol. Epidemiol. Immunobiol. 1970: 32 35.
60. Little, S. F.,, and G. B. Knudson. 1986. Comparative efficacy of Bacillus anthracis live-spore vaccine and protective-antigen vaccine against anthrax in the guinea pig. Infect. Immun. 52: 509 512.
61. Little, S. F.,, and J. R. Lowe. 1991. Location of receptor-binding region of protective antigen from Bacillus anthracis. Biochem. Biophys. Res. Commun. 180: 531 537.
62. Makino, S.,, C. Sasakawa,, I. Uchlda,, N. Terakado,, and M. Yoshlkawa. 1987. Transformation of a cloning vector, pUB11O, into Bacillus anthracis. FEMS Microbiol. Lett. 44: 45 48.
63. Maklno, S., C. Sasakawa, I. Uchida, N. Terakado, and M. Yoshikawa. 1988. Cloning and C02-dependent expression of the genetic region for encapsulation from Bacillus anthracis. Mol. Microbiol. 2: 371 376.
64. Makino, S.-I.,, 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.
65. McCloy, E. W. 1951. Studies on a lysogenic Bacillus strain. I. A bacteriophage specific for Bacillus anthracis. J. Hyg. 49: 114 125.
66. McCuen, R. W.,, and C. B. Thorne. 1971. Genetic mapping of genes concerned with glutamyl polypeptide production by Bacillus licheniformis and a study of their relationship to the development of competence for transformation. J. Bacteriol. 107: 636 645.
67. 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.
68. Meynell, E. W. 1963. Reverting and non-reverting rough variants of Bacillus anthracis. J. Gen. Microbiol. 32: 55 60.
69. Meynell, G. G.,, and E. Meynell. 1966. The biosynthesis of poly d-glutamic acid, the capsular material of Bacillus anthracis. J. Gen. Microbiol. 43: 119 138.
70. 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.
71. Mock, M.,, E. Labruyere,, P. Glaser,, A. Danchin,, and A. Ullmann. 1988. Cloning and expression of the calmodulin-sensitive Bacillus anthracis adenylate cyclase in Escherichia coli. Gene 64: 277 284.
72. Molnar, D. M.,, and R. A. Altenbern. 1963. Alterations in the biological activity of protective antigen of Bacillus anthracis toxin. Proc. Soc. Exp. Biol. Med. 114: 294 297.
73. Mongkolsuk, S.,, Y.-W. Chiang,, R. B. Reynolds,, and P. S. Lovett. 1983. Restriction fragments that exert promoter activity during postexponential growth of Bacillus subtilis. J. Bacteriol. 155: 1399 1406.
74. 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. Microbial Composition. The Chemical Rubber Co., Washington, D.C..
75. Pezard, C.,, P. Berche,, and M. Mock. 1991. Contribution of individual toxin components to virulence of Bacillus anthracis. Infect. Immun. 59: 3472 3477.
76. Puziss, M.,, and M. B. Howard. 1963. Studies on immunity in anthrax. XI. Control of cellular permeability by bicarbonate ion in relation to protective antigen elaboration. J. Bacteriol. 85: 237 243.
77. Puziss, M.,, L. C. Manning,, J. W. Lynch,, E. Barclay,, I. Abelow,, and G. G. Wright. 1963. Large-scale production of protective antigen of Bacillus anthracis in anaerobic cultures. Appl. Microbiol. 11: 330 334.
78. Quinn, C. P.,, and B. N. Dancer. 1990. Transformation of vegetative cells of Bacillus anthracis with plasmid DNA. J. Gen. Microbiol. 136: 1211 1215.
79. Quinn, C. P.,, C. C. Shone,, P. C. B. Turnbull,, and J. Melling. 1988. Purification of anthrax-toxin components by high-performance anion-exchange, gel-filtration and hydrophobic-interaction chromatography. Biochem. J. 252: 753 758.
80. Quinn, C. P.,, Y. Singh,, K. R. Klimpel,, and S. H. Leppla. 1991. Functional mapping of anthrax toxin lethal factor by in-frame insertion mutagenesis. J. Biol. Chem. 266: 20124 20130
81. Raziuddin, A.,, and A. Friedlander. 1991. Anthrax protective antigen receptor: Identification of a protective antigen binding protein by chemical cross-linking, abstr. B-301, p. 75. Abstr. 91st Gen. Meet. Am. Soc. Microbiol. 1991.
82. Reddy, A.,, L. Battisti,, and C. B. Thorne. 1987. Identification of self-transmissible plasmids in four Bacillus thuringiensis subspecies. J. Bacteriol. 169: 5263 5270.
83. Ristroph, J. D.,, and B. E. Ivins. 1983. Elaboration of Bacillus anthracis antigens in a new defined culture medium. Infect. Immun. 39: 483 486.
84. Roberts, D. M.,, R. Crea,, M. Malecha,, G. Alvarado-Urbina,, R. H. Chiarello,, and D. M. Watterson. 1985. Chemical synthesis and expression of a calmodulin gene designated for site-specific mutagenesis. Biochemistry 24: 5090 5098.
85. Robertson, D. L.,, and T. S. Bragg,. 1990>. Nucleotide sequence of the lethal factor (lef) and edema factor (cya) genes from Bacillus anthracis: elucidation of the EF and LF functional domains, p. 59. In P. C. B. Turnbull (ed.), Proceedings of the International Workshop on Anthrax, Winchester, England. Salisbury medical bulletin, no. 68, special supplement. Salisbury Medical Society, Salisbury, England.
86. Robertson, D. L.,, T. S. Bragg,, S. Simpson,, R. Raspar,, W. Xie,, and M. T. Tippetts,. 1990. Mapping and characterization of the Bacillus anthracis plasmids pXOl and pX02, p. 55 58. In P. C. B. Turnbull (ed.), Proceedings of the International Wortehop on Anthrax, Winchester, England. Salisbury medical bulletin, no. 68, special supplement. Salisbury Medical Society, Salisbury, England.
87. Robertson, D. L.,, and S. H. Leppla. 1986. Molecular cloning and expression in Escherichia coli of the lethal factor gene of Bacillus anthracis. Gene 44: 71 78.
88. 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.
89. Robillard, N. J. 1984. Changes associated with plasmid loss in Bacillus anthracis. Ph.D. dissertation. University of Massachusetts, Amherst..
90. Robillard, N. J.,, T. M. Koehler,, R. Murray,, and C. B. Thorne. 1983. Effects of plasmid loss on the physiology of Bacillus anthracis, abstr. H-54, p. 115. Abstr. 83rd Annu. Meet. Am. Soc. Microbiol. 1983.
91. Ruhfel, R. E. 1989. Physical and genetic characterization of the Bacillus thuringiensis subsp. kurstaki HD-1 extrachromosomal temperate phage TP-21. Ph.D. dissertation. University of Massachusetts, Amherst..
92. 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.
93. Ruhfel, R. E.,, and C. B. Thorne. 1988. Physical and genetic characterization of the Bacillus thuringiensis subsp. kurstaki HD-1 extrachromosomal temperate phage TP-21, abstr. H-4, p. 145. Abstr. 88th Annu. Meet. Am. Soc. Microbiol. 1988.
94. Sadler, D. F.,, J. W. Ezzell, Jr.,, K. F. Keller,, and R. J. Doyle. 1984. Glycosidase activities oí Bacillus anthracis. J. Clin. Microbiol. 19: 594 598.
95. Singh, Y.,, V. K. Chaudhary,, and S. H. Leppla. 1989. A deleted variant of Bacillus anthracis protective antigen is non-toxic and blocks anthrax toxin action in vivo. J. Biol. Chem. 264: 19103 19107.
96. Singh, Y.,, K. R. Klimpel,, C. P. Quinn,, V. K. Chaudhary,, and S. H. Leppla. 1991. The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity. J. Biol. Chem. 266: 15493 15497.
97. Smith, H.,, J. Keppie,, and J. L. Stanley. 1955. The chemical basis of the virulence of Bacillus anthracis. V. The specific toxin produced by B. anthracis in vivo. Br. J. Exp. Pathol. 36: 460 472.
98. Smith, H.,, D. W. Tempest,, J. L. Stanley,, P. W. Harris-Smith,, and R. C. Gallop. 1956. The chemical basis of the virulence of Bacillus anthracis. VII. Two components of the anthrax toxin: their relationship to known immunizing aggressins. Br. J. Exp. Pathol. 37: 263 271.
99. Somerville, H. J.,, and M. L. Jones. 1972. DNA competition studies within the Bacillus cereus group of bacilli. J. Gen. Microbiol. 73: 257 265.
100. Stanley, J. L.,, and H. Smith. 1961. Purification of factor I and recognition of the third factor of anthrax toxin. J. Gen. Microbiol. 26: 49 66.
101. Stepanov, A. S.,, S. V. Gavrilov,, O. B. Puzanova,, T. M. Grigoryeva,, and R. R. Azizbekyan. 1989. Transduction of plasmids in Bacillus anthracis by bacteriophage CP-54. Mol. Genet. Microbiol. Virol. 1: 14 19.
102. Stepanov, A. S.,, O. B. Puzanova,, S. Y. Dityatldn,, O. G. Loginova,, and B. N. Ilyashenko. 1990. Glycine-induced cryotransformation of plasmids into Bacillus anthracis. J. Gen. Microbiol. 136: 1217 1221.
103. Sterne, M. 1937. Variation in Bacillus anthracis. Onderstepoort J. Vet. Sci. Anim. Ind. 8: 271 349.
104. Sterne, M. 1939. The immunization of laboratory animals against anthrax. Onderstepoort J. Vet. Sci. Anim. Ind. 13: 313 317.
105. Sterne, M. 1939. The use of anthrax vaccines prepared from avirulent (uncapsulated) variants of Bacillus anthracis. Onderstepoort J. Vet. Sci. Anim. Ind. 13: 307 312.
106. Strange, R. E.,, and C. B. Thorne. 1958. Further purification studies on the protective antigen of Bacillus anthracis produced in vitro. J. Bacteriol. 76: 192 202.
107. Thorne, C. B., 1956. Capsule formation and glutamyl polypeptide synthesis by Bacillus anthracis and Bacillus subtilis, p. 68 80. In E. T. C. Spooner, and B. A. D. Stocker (ed.), Bacterial Anatomy. Cambridge University Press, Cambridge.
108. Thorne, C. B. 1960. Biochemical properties of virulent and avirulent strains of Bacillus anthracis. Ann. N.Y. Acad. Sci. 88: 1024 1033.
109. Thorne, C. B. 1968. Transduction in Bacillus cereus and Bacillus anthracis. Bacteriol. Rev. 32: 358 361.
110. Thorne, C. B. 1978. Transduction in Bacillus thuringiensis. Appl. Environ. Microbiol. 35: 1109 1115.
111. 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..
112. Thorne, C. B.,, and F. C. Belton. 1957. An agar diffusion method for titrating Bacillus anthracis immunizing antigen and its application to a study of antigen production. 7. Gen. Microbiol. 17: 505 516.
113. Thorne, C. B.,, C. G. Gomez,, and R. D. Housewright. 1955. Transamination of d-amino acids by Bacillus subtilis. J. Bacteriol. 69: 357 362.
114. Thorne, C. B.,, and C. G. Leonard. 1958. Isolation of d-and l-glutamyl polypeptides from culture filtrates of Bacillus subtilis. J. Biol. Chem. 233: 1109 1112.
115. Thorne, C. B.,, and D. M. Molnar. 1955. d-Amino acid transamination in Bacillus anthracis. J. Bacteriol. 70: 420 426.
116. Thorne, C. B.,, D. M. Molnar,, and R. E. Strange. 1960. Production of toxin in vitro by Bacillus anthracis and its separation into two components. J. Bacteriol. 79: 450 455.
117. 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.
118. Tomesik, J., 1956. Bacterial capsules and their relation to the cell wall, p. 41 67. In E. T. C. Spooner, and B. A. D. Stocker (ed.), Bacterial Anatomy. Cambridge University Press, Cambridge.
119. Torti, M. 1956. Optical isomers of glutamic acid composing bacterial glutamyl polypeptides. Med. J. Osaka Univ. 6: 1043 1046.
120. Toril, M. 1959. Studies on the chemical structure of bacterial glutamyl polypeptides by hydrazinolysis. J. Biochem. 46: 189 200.
121. Torii, M.,, O. Kurlmura,, S. Utsumi,, H. Nozu,, and T. Amano. 1959. Decapsulation of Bacillus megaterium. Biken J. 2: 265 276.
122. Trieu-Cuot, P.,, C. Carlier,, P. Martin,, and P. Courvalin. 1987. Plasmid transfer by conjugation from Escherichia coli to Gram-positive bacteria. FEMS Microbiol. Lett. 48: 289 294.
123. Troy, F. A. 1973. Chemistry and biosynthesis of the poly(?-d-glutamyl) capsule in Bacillus licheniformis. I. Properties of the membrane-mediated biosynthetic reaction. J. Biol. Chem. 248: 305 315.
124. Troy, F. A. 1973. Chemistry and biosynthesis of the poly(γ-d-glutamyl) capsule in Bacillus licheniformis. II. Characterization and structural properties of the enzy-matically synthesized polymer. J. Biol. Chem. 248: 316 324.
125. Turnbull, P. C. B.,, M. G. Broster,, J. A. Carman,, R. J. Manchee,, and J. Melling. 1986. Development of antibodies to protective antigen and lethal factor components of anthrax toxin in humans and guinea pigs and their relevance to protective immunity. Infect. Immun. 52: 356 363.
126. Turnbull, P. C. B.,, and J. M. Kramer,. 1991. Bacillus, p. 296 303. In A. Balows,, W. J. Hausler, 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..
127. Uchida, I.,, K. Hashimoto,, S.-I. Makino,, C. Sasakawa,, M. Yoshikawa,, and N. Terakado. 1987. Restriction map of a capsule plasmid of Bacillus anthracis. Plasmid 18: 178 181.
128. Uchida, I.,, T. Seldzaki,, K. Hashimoto,, and N. Terakado. 1985. Association of the encapsulation of Bacillus anthracis with a 60-megadalton plasmid. J. Gen. Microbiol. 131: 363 367.
129. Vodkin, M. H.,, and S. H. Leppla. 1983. Cloning of the protective antigen gene of Bacillus anthracis. Cell 34: 693 697.
130. Volcani, B. E.,, and P. Margalith. 1957. A new species (Flavobacterium polyglutamicum) which hydrolyzes the γ-L-glutamyl bond in polypeptides. J. Bacteriol. 74: 646 653.
131. Waley, S. G. 1955. The structure of bacterial polyglu-tamic acid. J. Chem. Soc. 1955: 517 522.
132. Weisblum, B.,, M. Y. Graham,, T. Gryczan,, and D. Dubnau. 1979. Plasmid copy number control: isolation and characterization of high-copy-number mutants of plasmid pE194. J. Bacteriol. 137: 635 643.
133. Welkos, S. L. 1991. Plasmid-associated virulence factors of non-toxigenic (pXOl-) Bacillus anthracis. Microb.Pathog. 10: 183 198.
134. 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.
135. Yelton, D. B.,, and C. B. Thorne. 1970. Transduction in Bacillus cereus by each of two bacteriophages. J. Bacteriol. 102: 573 579.
136. Yelton, D. B.,, and C. B. Thorne. 1971. Comparison of Bacillus cereus bacteriophages CP-51 and CP-53. J. Virol. 8: 242 253.
137. Youngman, P. J.,, J. B. Perkins,, and R. Losick. 1983. Genetic transposition and insertional mutagenesis in Bacillus subtilis with Streptococcus faecalis transposon Tn917. Proc. Natl. Acad. Sci. USA 80: 2305 2309.
138. Youngman, P. J.,, J. B. Perkins,, and R. Losick. 1983. Construction of a cloning site near one end of Tn917 into which foreign DNA may be inserted without affecting transposition in Bacillus subtilis or expression of the transposon-borne erm gene. Plasmid 12: 1 9.

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error