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Chapter 11 : Bacterial Toxins in Disease Production

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Abstract:

Our current understanding of the mechanism of action of bacterial toxins includes details of their genetic, physical, and enzymatic properties and insight into their translocation across the eukaryotic cell membrane to gain access to intracellular targets. This chapter outlines the molecular aspects of bacterial toxins. Bacterial toxins are classified into several families including exotoxins, pore-forming toxins, membrane-acting toxins, and type-III secreted cytotoxins. The translocated, nascent polypeptide folds into its native conformation and the leader sequence is cleaved by a periplasmic leader peptidase to yield a mature exotoxin. While some bacterial toxins such as the heat-labile enterotoxin of remain localized to the periplasmic space, other bacterial exotoxins, such as cholera toxin and pertussis toxin, are assembled in the periplasm and subsequently transported across the bacterial outer membrane and into the external environment. Relative to bacterial exotoxins, the type-III-secreted cytotoxins are a recently recognized family of bacterial toxins. Bacteria utilize several strategies to modulate eukaryotic cell physiology at the eukaryotic cell membrane. There are several families of membrane-acting toxins, including the pore-forming toxins, the heat-stable enterotoxins, and the superantigens. Considerable progress has been made toward defining the mechanism of action of bacterial toxins and their role in bacterial pathogenesis.

Citation: Barbieri J, Pederson K. 2000. Bacterial Toxins in Disease Production, p 163-174. In Brogden K, Roth J, Stanton T, Bolin C, Minion F, Wannemuehler M (ed), Virulence Mechanisms of Bacterial Pathogens, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555818111.ch11

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Bacterial Proteins
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Bacterial Pathogenesis
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Bacterial Toxins
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Figures

Image of FIGURE 1
FIGURE 1

AB organization of bacterial exotoxins. Indicated are the schematized representations of the three recognized organizations of bacterial exotoxins. The shaded area represents the catalytic domain, A, while the clear areas represent the translocation and binding domains, B.

Citation: Barbieri J, Pederson K. 2000. Bacterial Toxins in Disease Production, p 163-174. In Brogden K, Roth J, Stanton T, Bolin C, Minion F, Wannemuehler M (ed), Virulence Mechanisms of Bacterial Pathogens, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555818111.ch11
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Image of FIGURE 2
FIGURE 2

Entry of bacterial exotoxins into sensitive eukaryotic cells. Bacterial exotoxins associate with specific receptors on the cell surface or utilize more nonspecific interactions to gain access into the eukaryotic cell by receptor-mediated endocytosis. Some exotoxins (diphtheria toxin and anthrax toxin) gain access into the intracellular environment at the level of the early endosome, while other exotoxins (cholera toxin, heat-labile enterotoxin, exotoxin A of , and shiga toxin) utilize the retrograde transport system of the eukaryotic cell to traffic to the Golgi and/or endoplasmic reticulum, where the translocation process is believed to occur.

Citation: Barbieri J, Pederson K. 2000. Bacterial Toxins in Disease Production, p 163-174. In Brogden K, Roth J, Stanton T, Bolin C, Minion F, Wannemuehler M (ed), Virulence Mechanisms of Bacterial Pathogens, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555818111.ch11
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Image of FIGURE 3
FIGURE 3

Entry of type III translocation of cytotoxins and membrane-acting toxins into sensitive eukaryotic cells. During type III translocation of cytotoxins into sensitive cells, bacteria bind to the surface of eukaryotic cells and utilize the type III secretion apparatus to translocate cytotoxins from the bacterial cytosol into the intracellular compartment of the eukaryotic cell. The membrane-active toxins bind directly to the cell surface and disrupt membrane function via the formation of a pore (aerolysin), stimulation of host guanylate cyclase (GC) through a signal transduction mechanism (heat-stable enterotoxin), or direct insertion of the catalytic domain into the eukaryotic cell cytosol (adenylate cyclase).

Citation: Barbieri J, Pederson K. 2000. Bacterial Toxins in Disease Production, p 163-174. In Brogden K, Roth J, Stanton T, Bolin C, Minion F, Wannemuehler M (ed), Virulence Mechanisms of Bacterial Pathogens, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555818111.ch11
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