1887

Chapter 8 :

Author: Curtis B. Thorne1
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Affiliations: 1: Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003
Content Type: Monograph
Publication Year: 1993

Category: Bacterial Pathogenesis; Microbial Genetics and Molecular Biology

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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
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Bacillus anthracis
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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
/content/10.1128/9781555818388.chap8.fig8-1
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. ( ).

10.1128/9781555818388/fig8-1_thmb.gif
10.1128/9781555818388/fig8-1.gif
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
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