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Abstract:

This chapter focuses on type A food poisoning. is a gram-positive, rod-shaped, encapsulated, nonmotile anaerobe that causes a spectrum of human and veterinary diseases. The virulence of this bacterium largely results from its prolific toxin-producing ability, including several toxins (e.g., enterotoxin [CPE] and β-toxin) with activity on the human gastrointestinal (GI) tract. growth in food is affected by a variety of environmental factors, including temperature, E, pH, and water activity (a). Current knowledge of the reservoir(s) for type A food poisoning isolates remains deficient, which is unfortunate because it impairs efforts to rationally control/reduce outbreaks of type A food poisoning. Epidemiologic studies provided strong initial evidence that CPE plays a pivotal role in type A foodborne illness. Everyone is susceptible to type A food poisoning; however, this illness tends to be more serious in elderly, debilitated, or medicated individuals. Additional studies may also lead to the development of agents capable of blocking CPE expression or activity. Finally, continued research on the mechanism of CPE activity may lead to the development of potent new anticancer agents or to better delivery of therapeutic agents.

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Image of Figure 18.1
Figure 18.1

Pathogenesis of type A food poisoning. Vegetative cells of an enterotoxin (CPE)-producing strain multiply rapidly in contaminated food (usually a meat or poultry product) and, after ingestion, sporulate in the small intestine. Sporulating cells then produce CPE, which is released at the completion of sporulation, when the mother cell lyses to release its endospore. CPE then causes morphologic damage to the small intestine, resulting in diarrhea and abdominal cramps. Modified and reproduced from , 1992, 12:237–252, by permission of John Wiley and Sons. doi:10.1128/9781555818463.ch18f1

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Image of Figure 18.2
Figure 18.2

Fulfilling molecular Koch's postulates demonstrates that CPE is important for the gastrointestinal virulence of type A food poisoning isolates. Tissue specimens shown were collected from rabbit ileal loops that had been treated with either concentrated vegetative (FTG) or sporulating (DS) culture lysates of strain SM101, an electroporatable derivative of food poisoning strain NCTC 8798; MRS101, which is a knockout mutant of SM101; or MRS101(pJRC 200), which is the MRS101 mutant complemented with a shuttle plasmid carrying the cloned, wild-type gene. Note that (i) tissue specimens from loops treated with a concentrated FTG lysate of SM101, which does not contain CPE, were indistinguishable from control ileal loop tissue specimens, while (ii) tissue damage (and fluid accumulation) was observed only in loops treated with DS culture lysates of SM101 or MRS101(pJRC200), both of which contain CPE. Reprinted with permission of John Wiley and Sons from reference . doi:10.1128/9781555818463.ch18f2

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Image of Figure 18.3
Figure 18.3

Variations in locus arrangements. (A) Comparison of locus arrangement in different isolates. The top and middle region maps show the arrangement of the plasmid locus in type A human nonfoodborne GI disease isolates F4969 and F4013, respectively. Note that the plasmid of F4013 and other type A isolates with a similar locus also encode β2 toxin. The map on the bottom shows the arrangement of the chromosomal locus in food poisoning isolate NCTC8239. The chromosomal locus is similarly arranged in most other food poisoning isolates. (B) Multiplex PCR subtyping assay. Representative results obtained with this assay are shown for culture lysates from type A isolates known to carry a chromosomal gene (lanes 2 to 6 from the left), a plasmid gene with an associated IS-like sequence (lanes 7 to 11 from the left), or a plasmid gene with an associated IS sequence (lanes 12 to 15 from the left). The migration positions of molecular size markers are shown on the left. The sizes of expected PCR products are shown on the right. Compiled from references , and . doi:10.1128/9781555818463.ch18f3

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Figure 18.4

Regulation of sporulation and CPE expression by alternative sigma factors. When induced by stress, a regulatory cascade is induced and results in production of SigF, an alternative sigma factor. Production of SigF then controls expression of three other alternative sigma factors (SigE, SigK, and SigG) that are necessary for sporulation. In addition, SigE and SigK mediate CPE expression from SigE- and SigK-dependent promoters for the gene. Based upon data presented in references and . doi:10.1128/9781555818463.ch18f4

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Image of Figure 18.5
Figure 18.5

Model for the cellular action of CPE. (Left to right) CPE binds to claudin receptors, forming a small complex. At 37°C, several small complexes interact to form an ∼450-kDa CH-1 prepore. The CH-1 prepore then inserts into membranes to form an active pore. The CH-1 active pore allows a Ca influx. With high CPE doses, a massive Ca influx occurs and triggers oncosis; with low CPE doses, there is a more moderate Ca influx that triggers apoptosis. Morphologic damage caused by membrane permeability alterations allows unbound CPE access to the basolateral surface, resulting in formation of a second CPE complex, named CH-2, containing claudins and occludin. doi:10.1128/9781555818463.ch18f5

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Image of Figure 18.6
Figure 18.6

CPE interactions with claudin receptors. (A) Alignment of strong CPE-binding claudin receptors versus weak or non-CPE binding receptors. Note the presence of an Asn residue in the middle of the extracellular loop 2 (ECL-2) domain of all strong CPE-binding claudins. The equivalent ECL-2 residue is never an Asn in the weak- or non-CPE-binding claudins. TM domains 3 and 4 refer to putative transmembrane domains of claudins. (B) Evidence that the Asn residue in the middle of ECL-2 of CPE receptor claudins is important for CPE binding and cytotoxicity. The equivalent ECL-2 residues in claudin-1 and -4 (residues 150 in claudin-1 and 149 in claudin-4) were changed from D to N and from N to D, respectively. Photos show CPE sensitivity of parent fibroblasts or fibroblast transfectants expressing claudin-1, claudin-1D150N, claudin-4, or claudin-4N149D. The graph shows the cytotoxic effects of CPE on these cells. Note that as shown in both the photos and the graph, changing this key ECL-2 Asn residue profoundly affects CPE sensitivity. Reproduced with permission from , 2010, 78:505–517. doi:10.1128/9781555818463.ch18f6

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Figure 18.7

Heteromer gel shift analyses indicate that CPE is present as a hexamer in large complexes. In this experiment, two different-sized CPE variants mixed together at varying ratios are applied to Caco-2 cells. After cell lysis, the CPE large complexes are separated by electrophoresis on an SDS-containing polyacrylamide gel and visualized by Western blotting using CPE antibodies. The stoichiometry of CPE in each large complex is calculated by counting the number of CPE complex bands (which is 7) on these gels and then subtracting one (because there are two homomer complexes). Therefore, it is concluded that CPE is present as a hexamer in CH-2 (shown here). CH-1 was also determined to contain six copies of CPE (not shown). Reproduced with permission from reference . doi:10.1128/9781555818463.ch18f7

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Figure 18.8

Linear map of CPE functional regions. CPE regions involved in CH-1 oligomerization are located between residues 45 and 54 of CPE, with residues D48 and I51 being required for both those events to occur. A putative transmembrane stem domain that may mediate CPE insertion into membranes during pore formation has been localized to residues 80 to 110 of CPE. The C-terminal region of CPE, which also reacts with MAb 3C9, is depicted as located between residues 290 to 319 of CPE. The extreme N-terminal sequences of CPE (residues 1 to 44) are unnecessary for cytotoxicity, and some of these sequences may be removed during disease by intestinal proteases (see the text). Compiled from references , and . doi:10.1128/9781555818463.ch18f8

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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Figure 18.9

Structure of the C-terminal half of the CPE protein. (A) Structure of the C-terminal half of the CPE protein, showing a structure consisting of a 9-strand β-sandwich and a large loop containing Tyr residues 306, 310, and 312, which are important for CPE binding to claudins. (B) The C-terminal half of CPE has structural, but not sequence, similarity to the receptor binding domain of Cry4Ba, a toxin produced by . Reproduced with permission from reference . doi:10.1128/9781555818463.ch18f9

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
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References

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Tables

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Table 18.1

Toxinotyping of strains

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
Generic image for table
Table 18.2

Spore resistance properties against food environment stresses

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18
Generic image for table
Table 18.3

Resistance properties of strains showing importance of the SASP-4 variant with an Asp at residue 36

Citation: McClane B, Robertson S, Li J. 2013. , p 465-489. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch18

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