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Chapter 23 : Nefarious Uses of Bacterial Toxins

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Abstract:

Bacterial toxins represent some of the deadliest molecules known to man. Over the ages, evolution has led to precision engineering of these toxins such that only minute quantities of certain bacterial toxins are capable of eliciting lethal outcomes for humans. Many vaccines are inactivated bacterial toxins, which stimulate an immune response to protect the recipient from that toxin-producing pathogen. Regrettably, the power of bacterial toxins has also been harnessed for destructive purposes. Toxins and toxin-producing bacteria that are thought to pose major risks to the public are , which causes anthrax in humans and animals, , which is the causative agent of plague, and botulinum toxin. Continued studies on the basic molecular properties of bacterial toxins will provide insight to develop novel antitoxin therapies, such as the recent recognition that nontoxic forms of bacterial toxins can act in a dominant-negative manner to neutralize toxin action. The potential utilization of pathogenic bacteria and their toxins for criminal acts is a formidable problem that requires a concerted effort on the part of the scientific community. Scientific research has the promise of leading to the development of vaccines and therapeutics that will make biological agents useless in the hands of terrorists.

Citation: Burns D, Barbieri J. 2003. Nefarious Uses of Bacterial Toxins, p 327-334. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch23
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Figures

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Figure 1

Three-dimensional structure of the PA of anthrax toxin. (A) Three-dimensional structure of monomeric PA. The four domains of the protein are indicated. The dashed line indicated by the arrow represents a loop that is believed to form a segment of a transmembrane -barrel upon pore formation. (B) Modeled heptamer of PA depicting its predicted ring-like structure. Adapted from reference with permission. (See Color Plates following p. 256).

Citation: Burns D, Barbieri J. 2003. Nefarious Uses of Bacterial Toxins, p 327-334. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch23
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Image of Figure 2
Figure 2

Mechanism of action of anthrax toxin. Anthrax toxin is composed of three proteins, PA, LF, and EF. PA first binds to receptors on the eukaryotic cell. PA is nicked by the eukaryotic protease furin, producing a PA fragment that oligomerizes to form a heptamer and can bind EF and/or LF. The complex is internalized by endocytosis. Exposure of the complex to the acidic environment of the endosome is believed to result in formation of a pore by the PA heptamer, producing a channel through which LF and EF can translocate. Once inside the cytoplasm, LF expresses metalloprotease activity and EF is an adenylate cyclase that synthesizes the second messenger, cAMP.

Citation: Burns D, Barbieri J. 2003. Nefarious Uses of Bacterial Toxins, p 327-334. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch23
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References

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1. Christopher, G. W.,, T. J. Cieslak,, J. A. Pavlin,, and E. M. Eitzen. 1997. Biological warfare: a historical perspective. JAMA 278: 412 417.
2. Gill, D. M. 1982. Bacterial toxins: a table of lethal amounts. Microbiol. Rev. 46: 86 94.
3. Henderson, D. A. 1999. The looming threat of bioterrorism. Science 283: 1279 1282.
4. Lederberg, J. 1997. Infectious disease and biological weapons: prophylaxis and mitigation. JAMA 5: 435 436.
5. Meselson, M.,, J. Guillemin,, M. Hugh-Jones,, A. Langmuir,, I. Popova,, A. Shelokov,, and O. Yampoloskaya. 1994. The Sverdlovsk anthrax outbreak of 1979. Science 266: 1202 1208.
6. Olson, K. B. 1999. Aum Shinrikyo: once and future threat? Emerging Infect. Dis. 5: 513 516.
7. Sellman, B. R.,, M. Mourex,, and R. J. Collier. 2001. Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax. Science 292: 695 697.
8. Sellman, B. R.,, S. Nassi,, and R. J. Collier. 2001. Point mutations in anthrax protective antigen that block translocation. J. Biol. Chem. 276: 8371 8376.

Tables

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Table 1

Lethal amounts of some bacterial toxins

Citation: Burns D, Barbieri J. 2003. Nefarious Uses of Bacterial Toxins, p 327-334. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch23

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