1887

Chapter 19 :

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/10.1128/9781555815912/9781555814076_Chap19-1.gif /docserver/preview/fulltext/10.1128/9781555815912/9781555814076_Chap19-2.gif

Abstract:

was initially recognized as an important cause of foodborne disease in the 1940s and 50s. It later became apparent that causes two quite different human foodborne diseases, i.e., type A food poisoning and necrotic enteritis. Since foodborne necrotic enteritis is rare in industrialized societies, this chapter focuses mainly on type A food poisoning. Compared to most other anaerobes, requires only relatively modest reductions in oxidation-reduction potential (E) for growth. A distinct toxin type is associated with each of the two foodborne diseases caused by . Necrotic enteritis, a life-threatening illness, is usually caused by type C isolates, with ß-toxin being considered the primary virulence factor responsible for this illness. enterotoxin (CPE) is classified as an enterotoxin because it induces fluid and electrolyte losses from the gastrointestinal (GI) tract of many mammalian species. The cytotoxic action of CPE is responsible for the tissue damage that initiates CPE-induced intestinal fluid and electrolyte alterations. Interestingly, both CPE-induced apoptosis and oncosis involve the cytoplasmic proteins calmodulin and calpain. Effective immunity against type A food poisoning may require a secretory immunoglobulin A response in the intestinal lumen.

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19

Key Concept Ranking

Pulsed-Field Gel Electrophoresis
0.4499615
Sodium Dodecyl Sulfate
0.44562295
Enzyme-Linked Immunosorbent Assay
0.44562295
DNA Restriction Enzymes
0.4346718
0.4499615
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of Figure 19.1
Figure 19.1

Electron micrograph of thin sections of a sporulating cell of . Magnification, ×40,000. Bar, 0.5 μm. Arrows indicate the endospore and a CPE-containing inclusion body in the cytoplasm of the mother cell. Reproduced with permission from ( ).

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.2
Figure 19.2

Pulsed-field gel electrophoresis Southern blots distinguish type A isolates carrying a chromosomal gene from those with a plasmid gene. Because of its large size, -containing DNA is unable to enter pulsed-field gels when present on the chromosome unless that DNA is digested with a restriction enzyme. However, due to the smaller size of plasmid DNA, some -containing DNA does enter pulsed-field gels when an isolate carries its gene on a plasmid. Furthermore, the restriction enzyme I-CeuI cuts chromosomal DNA but not plasmid DNA. Therefore, a change in migration of -containing DNA after I-CeuI treatment is indicative of a chromosomal gene. Shown are pulsed-field gel Southern blot results, using an internal probe, for three food poisoning isolates carrying a chromosomal gene (NCTC10239, 537-5, and 538-1) and three nonfoodborne human GI disease isolates carrying a plasmid gene (F4969, W30554, and T34058). C or UC indicates the sample was or was not, respectively, digested with I-CeuI prior to electrophoresis and Southern blotting. Reproduced with permission from reference .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.3
Figure 19.3

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. Used with permission from reference .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.4
Figure 19.4

The pathogenesis of type A food poisoning. Vegetative cells multiply rapidly in contaminated food (usually a meat or poultry product) and, after ingestion, sporulate in the small intestine. Sporulating cells produce an enterotoxin (CPE) that causes morphologic damage to the small intestine, resulting in diarrhea and abdominal cramps. Reproduced with permission from reference .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.5
Figure 19.5

Fulfilling molecular Koch’s postulates demonstrates that CPE is important for the GI virulence of type A food poisoning isolates. Tissue specimens shown were collected from rabbit ileal loops 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 treated with concentrated FTG lysates of SM101 (or its derivatives), which do not contain CPE, were indistinguishable from control ileal loop specimens and (ii) fluid accumulation was observed only in loops treated with MDS culture lysates of SM101 or MRS(pJRC 200), both of which were shown to contain CPE. Reprinted with permission from reference .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.6
Figure 19.6

Comparison of locus arrangement in various isolates. (I) Arrangement of the chromosomal locus in food poisoning isolate NCTC8239. The chromosomal locus appears to be similarly arranged in most other food poisoning isolates. (II and III) Arrangement of the plasmid locus in type A human nonfoodborne GI disease isolates F4969 and F5603, respectively. Note that the plasmid of F5603, like other type A isolates with a similar locus, also encodes beta2 toxin. (IV) Arrangement of the silent locus in type E isolate NCIB10748. Many other type E isolates appear to carry a similar silent locus; note the presence of function iota toxin genes ( and ) immediately upstream of the silent locus in type E isolates. Compiled from references , and .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.7
Figure 19.7

Model for the cellular action of CPE. (A) CPE binds to receptors, forming a small complex. At 37°C, the small complex interacts with other proteins to form an ∼155-kDa large complex. The ∼155-kDa complex is a pore (or portion of a pore) that triggers membrane permeability alterations, including Ca influx. With high CPE doses, a massive Ca influx occurs, which triggers oncosis; with low CPE doses, there is more moderate Ca influx, which triggers apoptosis. Activation of either cell death pathway causes morphologic damage that allows CPE access to receptors on the basolateral surface of the intoxicated cell and adjacent cells. This results in the additional formation of the ∼155-kDa large complex and promotes the formation of an ∼200-kDa complex containing occludin. Formation of those two large CPE complexes triggers internalization of TJ proteins, which causes damage to the TJ and leads to paracellular permeability alterations that contribute to CPE-induced diarrhea. Reproduced with permission from reference .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.8
Figure 19.8

Kinetics of formation of CPE-containing large complexes in CaCo-2 cells. CPE was added to a suspension of CaCo-2 cells for the indicated times at 37°C. After removal of unbound enterotoxin, the cells were lysed with SDS, and cell lysates were analyzed by SDS-polyacrylamide gel electrophoresis (no sample boiling) using 4% acrylamide gels, followed by Western blotting with either CPE antibodies or occludin antibodies, as indicated. The time (in minutes) of CPE treatment is shown above the gel, whereas the migrations of myosin (212 kDa) and β-galactosidase (122 kDa) markers are indicated in the center space between these two blots. The double, open, and closed arrows indicate the location of the ∼200-kDa large complex, the ∼155-kDa large complex, and an ∼135-kDa intermediate complex, respectively. Note that the formation of the ∼200 kDa complex develops much more slowly than shown in this figure if CaCo-2 cell monolayers are CPE treated. Reproduced with permission from reference .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 19.9
Figure 19.9

Linear map of CPE functional regions. CPE regions involved in large complex formation and cytotoxicity are shown in black, with residues D48 and I51 (asterisks) being required for both those events to occur. The C-terminal region of CPE, which also reacts with MAb 3C9, is depicted in dark gray. The extreme N-terminal sequences of CPE (light gray) are unnecessary for cytotoxicity, and some of these sequences may be removed during disease by intestinal proteases (see the text). Compiled from references , and .

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555815912.ch19
1. Bartholomew, B. A.,, M. F. Stringer,, G. N. Watson, and, R. J. Gilbert. 1985. Development and application of an enzyme-linked immunosorbent assay for Clostridium perfringens type A enterotoxin. J. Clin. Pathol. 38:222228.
2. Billington, S. J.,, E. U. Wieckowski,, M. R. Sarker,, D. Bueschel,, J. G. Songer, and, B. A. McClane. 1998. Clostridium perfringens type E animal enteritis isolates with highly conserved, silent enterotoxin sequences. Infect. Immun. 66:45314536.
3. Birkhead, G.,, R. L. Vogt,, E. M. Heun,, J. T. Snyder, and, B. A. McClane. 1988. Characterization of an outbreak of Clostridium perfringens food poisoning by quantitative fecal culture and fecal enterotoxin measurement. J. Clin. Microbiol. 26:471474.
4. Bos, J.,, L. Smithee,, B. A. McClane,, R. F. Distefano,, F. Uzal,, J. G. Songer,, S. Mallonee, and, J. M. Crutcher. 2005. Fatal necrotizing enteritis following a foodborne outbreak of enterotoxigenic Clostridium perfringens type A infection. Clin. Infect. Dis. 15:e78e83.
5. Brynestad, S., and, P. E. Granum. 1999. Evidence that Tn5565, which includes the enterotoxin gene in Clostridium perfringens, can have a circular form which may be a transposition intermediate. FEMS Microbiol. Lett. 170:281286.
6. Brynestad, S.,, M. R. Sarker,, B. A. McClane,, P. E. Granum, and, J. I. Rood. 2001. The enterotoxin (CPE) plasmid from Clostridium perfringens is conjugative. Infect. Immun. 69:34833487.
7. Brynestad, S.,, B. Synstad, and, P. E. Granum. 1997. The Clostridium perfringens enterotoxin gene is on a transposable element in type A human food poisoning strains. Microbiology 143:21092115.
8. Chakrabarti, G., and, B. A. McClane. 2005. The importance of calcium influx, calpain, and calmodulin for the activation of CaCo-2 cell death pathways by Clostridium perfringens enterotoxin. Cell. Microbiol. 7:129146.
9. Chakrabartys activated in CaCo-2 cells by Clostridium perfringens enterotoxin. Infect. Immun. 71:42604270.
10. Collie, R. E.,, J. F. Kokai-Ki,, G., X. Zhou, and, B. A. McClane. 2003. Death pathwaun, and B. A. McClane. 1998. Phenotypic characterization of enterotoxigenic Clostridium perfringens isolates from non-foodborne human gastrointestinal diseases. Anaerobe 4:6979.
11. Collie, R. E., and, B. A. McClane. 1998. Evidence that the enterotoxin gene can be episomal in Clostridium perfringens isolates associated with nonfoodborne human gastrointestinal diseases. J. Clin. Microbiol. 36:3036.
12. Cornillot, E.,, B. Saint-Joanis,, G. Daube,, S. Katayama,, P. E. Granum,, B. Carnard, and, S. T. Cole. 1995. The enterotoxin gene (cpe) of Clostridium perfringens can be chromosomal or plasmid-borne. Mol. Microbiol. 15:639647.
13. Czeczulin, J. R.,, R. E. Collie, and, B. A. McClane. 1996. Regulated expression of Clostridium perfringens enterotoxin in naturally cpe-negative type A, B, and C isolates of C. perfringens. Infect. Immun. 64:33013309.
14. Czeczulin, J. R.,, P. C. Hanna, and, B. A. McClane. 1993. Cloning, nucleotide sequencing, and expression of the Clostridium perfringens enterotoxin gene in Escherichia coli. Infect. Immun. 61:34293439.
15. Daube, G.,, P. Simon,, B. Limbourg,, C. Manteca,, J. Mainil, and, A. Kaeckenbeeck. 1996. Hybridization of 2,659 Clostridium perfringens isolates with gene probes for seven toxins (α, β, ɛ, ι, θ, μ and enterotoxin) and for sialidase. Am. J. Vet. Res. 57:496501.
16. Fernandez-Miyakawa, M. E.,, V. Pistone-Creydt,, F. Uzal,, B. A. McClane, and, C. Ibarra. 2005. Clostridium perfringens enterotoxin damages the human intestine in vitro. Infect.Immun. 73:84078410.
17. Fisher, D. J.,, K. Miyamoto,, B. Harrision,, S. Akimoto,, M. R. Sarker, and, B. A. McClane. 2005. Association of beta2 toxin production with Clostridium perfringens type A human gastrointestinal disease isolates carrying a plasmid enterotoxin gene. Mol. Microbiol. 56:747762.
18. Fujita, K.,, J. Katahira,, Y. Horiguchi,, N. Sonoda,, M. Furuse, and, S. Tsukita. 2000. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction membrane protein. FEBS Lett. 476:258261.
19. Garcia-Alvarado, J. S.,, R. G. Labbe, and, M. A. Rodriguez. 1992. Sporulation and enterotoxin production by Clostridium perfringens type A at 37 and 43 degrees C. Appl. Environ. Microbiol. 58:14111414.
20. Granum, P. E., and, M. Richardson. 1991. Chymotrypsin treatment increases the activity of Clostridium perfringens enterotoxin. Toxicon 29:445453.
21. Granum, P. E.,, J. R. Whitaker, and, R. Skjelkvale. 1981. Trypsin activation of enterotoxin from Clostridium perfringens type A. Biochim. Biophys. Acta 668:325332.
22. Hanna, P. C.,, E. U. Wieckowski,, T. A. Mietzner, and, B. A. McClane. 1992. Mapping functional regions of Clostridium perfringens type A enterotoxin. Infect. Immun. 60:21102114.
23. Hardy, S. P.,, M. Denmead,, N. Parekh, and, P. E. Granum. 1999. Cationic currents induced by Clostridium perfringens type A enterotoxin in human intestinal CaCo-2 cells. J. Med. Microbiol. 48:235243.
24. Hardy, S. P.,, C. Ritchie,, M. C. Allen,, R. H. Ashley, and, P. E. Granum. 2001. Clostridium perfringens type A enterotoxin forms mepacrine-sensitive pores in pure phospholipid bilayers in the absence of putative receptor proteins. Biochim. Biophys. Acta 1515:3843.
25. Hauschild, A. H.,, L. Niilo, and, W. J. Dorward. 1971. The role of enterotoxin in Clostridium perfringens type A enteritis. Can. J. Microbiol. 17:987991.
26. Huang, I. H.,, M. Waters,, R. R. Grau, and, M. R. Sarker. 2004. Disruption of the gene (spo0A) encoding sporulation transcription factor blocks endospore formation and enterotoxin production in enterotoxigenic Clostridium perfringens type A. FEMS Microbiol. Lett. 233:233240.
27. Katahira, J.,, N. Inoue,, Y. Horiguchi,, M. Matsuda, and, N. Sugimoto. 1997. Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin. J. Cell Biol. 136:12391247.
28. Katahira, J.,, H. Sugiyama,, N. Inoue,, Y. Horiguchi,, M. Matsuda, and, N. Sugimoto. 1997. Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo. J. Biol. Chem. 272:2665226658.
29. Kokai-Kun, J. F.,, K. Benton,, E. U. Wieckowski, and, B. A. McClane. 1999. Identification of a Clostridium perfringens enterotoxin region required for large complex formation and cytotoxicity by random mutagenesis. Infect. Immun. 67:65346541.
30. Kokai-Kun, J. F., and, B. A. McClane. 1997. Deletion analysis of the Clostridium perfringens enterotoxin. Infect. Immun. 65:10141022.
31. Kokai-Kun, J. F., and, B. A. McClane. 1996. Evidence that region(s) of the Clostridium perfringens enterotoxin molecule remain exposed on the external surface of the mammalian plasma membrane when the toxin is sequestered in small or large complex. Infect. Immun. 64:10201025.
32. Kokai-Kun, J. F.,, J. G. Songer,, J. R. Czeczulin,, F. Chen, and, B. A. McClane. 1994. Comparison of Western immuno-blots and gene detection assays for identification of potentially enterotoxigenic isolates of Clostridium perfringens. J. Clin. Microbiol. 32:25332539.
33. Krakauer, T.,, B. Fleischer,, D. L. Stevens,, B. A. McClane, and, B. G. Stiles. 1997. Clostridium perfringens enterotoxin lacks superantigenic activity but induces an interleukin-6 response from human peripheral blood mononuclear cells. Infect. Immun. 65:34853488.
34. Labbe, R. G. 1989. Clostridium perfringens, p. 192234. In M. P. Doyle (ed.), Foodborne Bacterial Pathogens. Marcel Decker, New York, N.Y.
35. Labbe, R. G., and, C. L. Duncan. 1977. Evidence for stable messenger ribonucleic acid during sporulation and enterotoxin synthesis by Clostridium perfringens type A. J. Bacteriol. 129:843849.
36. Lawrence, G. W. 1997. The pathogenesis of enteritis necroticans, p. 198207. In J. I. Rood,, B. A. McClane,, J. G. Songer, and, R. W. Titball (ed.), The Clostridia: Molecular Genetics and Pathogenesis. Academic Press, London, United Kingdom.
37. McClane, B. A. 1994. Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes. Toxicology 87:4367.
38. McClane, B. A. 1992. Clostridium perfringens enterotoxin: structure, action and detection. J. Food Safety 12:237252.
39. McClane, B. A. 1984. Osmotic stabilizers differentially inhibit permeability alterations induced in Vero cells by Clostridium perfringens enterotoxin. Biochim. Biophys. Acta 777:99106.
40. McClane, B. A.,, D. M. Lyerly,, J. S. Moncrief, and, T. D. Wilkins. 2000. Enterotoxic clostridia: Clostridium perfringens type A and Clostridium difficile, p. 551562. In V. A. Fischetti,, R. P. Novick,, J. J. Ferretti,, D. A. Portnoy, and, J. Rood (ed.), Gram-Positive Pathogens. ASM Press, Washington, D.C.
41. McClane, B. A., and, J. I. Rood. 2001. Clostridial toxins involved in human enteric and histotoxic infections, p. 169209. In H. Bahl and, P. Duerre (ed.), Clostridia: Biotechnology and Medical Applications. Wiley-VCH, Weinheim, Germany.
42. McDonel, J. L. 1986. Toxins of Clostridium perfringens types A, B, C, D, and E, p. 477517. In F. Dorner and, H. Drews (ed.), Pharmacology of Bacterial Toxins. Pergamon Press, Oxford, United Kingdom.
43. Mead, P. S.,, L. Slutsker,, V. Dietz,, L. F. McCaig,, J. S. Bresee,, C. Shapiro,, P. M. Griffen, and, R. V. Tauxe. 1999. Food-related illness and death in the United States. Emerg. Infect. Dis. 5:607625.
44. Melville, S. B.,, R. E. Collie, and, B. A. McClane. 1997. Regulation of enterotoxin production in Clostridium perfringens, p. 471487. In J. I. Rood,, B. A. McClane,, J. G. Songer, and, R. Titball (ed.), The Clostridia: Molecular Genetics and Pathogenesis. Academic Press, London, United Kingdom.
45. Melville, S. B.,, R. Labbe, and, A. L. Sonenshein. 1994. Expression from the Clostridium perfringens cpe promoter in C. perfringens and Bacillus subtilus. Infect. Immun. 62:55505558.
46. Michl, P.,, M. Buchholz,, M. Rolke,, S. Kunsch,, M. Lohr,, B. McClane,, S. Tsukita,, G. Leder,, G. Adler, and, T. M. Gress. 2001. Claudin-4: a new target for pancreatic cancer treatment using Clostridium perfringens enterotoxin. Gastroenterology 121:678684.
47. Mietzner, T. A.,, J. F. Kokai-Kun,, P. C. Hanna, and, B. A. McClane. 1992. A conjugated synthetic peptide corresponding to the C-terminal region of Clostridium perfringens type A enterotoxin elicits an enterotoxin-neutralizing antibody response in mice. Infect. Immun. 60:39473951.
48. Miyamoto, K.,, G. Chakrabarti,, Y. Morino, and, B. A. McClane. 2002. Organization of the plasmid cpe locus of Clostridium perfringens type A isolates. Infect. Immun. 70:42614272.
49. Miyamoto, K.,, Q. Wen, and, B. A. McClane. 2004. Multiplex PCR genotyping assay that distinguishes between isolates of Clostridium perfringens type A carrying a chromosomal enterotoxin gene (cpe) locus, a plasmid cpe locus with an IS1470-like sequence, or a plasmid cpe locus with an IS1151 sequence. J. Clin. Microbiol. 42:15521558.
50. Olsen, S. J.,, L. C. MacKinon,, J. S. Goulding,, N. H. Bean, and, L. Slutsker. 2000. Surveillance for foodborne-disease outbreaks—United States, 1993–97. Morb. Mortal. Wkly. Rep. 49:151.
51. Rahner, C.,, L. Mitic, and, J. Anderson. 2001. Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut. Gastroenterology 120:411422.
52. Rahner, C.,, L. L. Mitic,, B. A. McClane, and, J. M. Anderson. 1999. Clostridium perfringens enterotoxin impairs bile flow in the isolated perfused rat liver and induces fragmentation of tight junction fibrils. Hepatology 30:326A.
53. Sarker, M. R.,, R. J. Carman, and, B. A. McClane. 1999. Inactivation of the gene (cpe) encoding Clostridium perfringens enterotoxin eliminates the ability of two cpe-positive C. perfringens type A human gastrointestinal disease isolates to affect rabbit ileal loops. Mol. Microbiol. 33:946958.
54. Sarker, M. R.,, R. P. Shivers,, S. G. Sparks,, V. K. Juneja, and, B. A. McClane. 2000. Comparative experiments to examine the effects of heating on vegetative cells and spores of Clostridium perfringens isolates carrying plasmid versus chromosomal enterotoxin genes. Appl. Environ. Microbiol. 66:32343240.
55. Sherman, S.,, E. Klein, and, B. A. McClane. 1994. Clostridium perfringens type A enterotoxin induces concurrent development of tissue damage and fluid accumulation in the rabbit ileum. J. Diarrhoeal Dis. Res. 12:200207.
56. Singh, U.,, L. L. Mitic,, E. Wieckowski,, J. M. Anderson, and, B. A. McClane. 2001. Comparative biochemical and immunochemical studies reveal differences in the effects of Clostridium perfringens enterotoxin on polarized CaCo-2 cells versus Vero cells. J. Biol. Chem. 276:3340233412.
57. Singh, U.,, C. M. Van Itallie,, L. L. Mitic,, J. M. Anderson, and, B. A. McClane. 2000. CaCo-2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin. J. Biol. Chem. 275:1840718417.
58. Smedley, J. G., III, and, B. A. McClane. 2004. Fine-mapping of the N-terminal cytotoxicity region of Clostridium perfringens enterotoxin by site-directed mutagenesis. Infect. Immun. 72:69146923.
59. Sonoda, N.,, M. Furuse,, H. Sasaki,, S. Yonemura,, J. Katahira,, Y. Horiguchi, and, S. Tsukita. 1999. Clostridium perfringens enterotoxin fragments remove specific claudins from tight junction strands: evidence for direct involvement of claudins in tight junction barrier. J. Cell Biol. 147:195204.
60. Sparks, S. G.,, R. J. Carman,, M. R. Sarker, and, B. A. McClane. 2001. Genotyping of enterotoxigenic Clostridium perfringens isolates associated with gastrointestinal disease in North America. J. Clin. Microbiol. 39:883888.
61. Strong, D. H.,, C. L. Duncan, and, G. Perna. 1971. Clostridium perfringens type A food poisoning. II. Response of the rabbit ileum as an indication of enteropathogenicity of strains of Clostridium perfringens. Infect. Immun. 3:171178.
62. Swisshelm, K.,, R. Macek, and, M. Kubbies. 2005. Role of claudins in tumorigenesis. Adv. Drug Deliv. Rev. 57:919928.
63. Todd, E. C. D. 1989. Preliminary estimates of costs of food-borne disease in the United States. J. Food Prot. 52:595601.
64. Varga, J.,, V. L. Stirewalt, and, S. B. Melville. 2004. The CcpA protein is necessary for efficient sporulation and enterotoxin gene (cpe) regulation in Clostridium perfringens. J. Bacteriol. 186:52215229.
65. Wallace, F. M.,, A. S. Mach,, A. M. Keller, and, J. A. Lindsay. 1999. Evidence for Clostridium perfringens enterotoxin inducing a mitogenic and cytokine response in vitro and a cytokine response in vivo. Curr. Microbiol. 38:96100.
66. Wen, Q., and, B. A. McClane. 2004. Detection of enterotoxigenic Clostridium perfringens type A isolates in American retail foods. Appl. Environ. Microbiol. 70:26852691.
67. Wieckowski, E.,, J. F. Kokai-Kun, and, B. A. McClane. 1998. Characterization of membrane-associated Clostridium perfringens enterotoxin following pronase treatment. Infect. Immun. 66:58975905.
68. Wieckowski, E. U.,, A. P. Wnek, and, B. A. McClane. 1994. Evidence that an ∼50kDa mammalian plasma membrane protein with receptor-like properties mediates the amphiphilicity of specifically-bound Clostridium perfringens enterotoxin. J. Biol. Chem. 269:1083810848.
69. Zhao, Y., and, S. B. Melville. 1998. Identification and characterization of sporulation-dependent promoters upstream of the enterotoxin gene (cpe) of Clostridium perfringens. J. Bacteriol. 180:136142.

Tables

Generic image for table
Table 19.1

Typing of based on toxins produced

Citation: McClane B. 2007. , p 423-444. In Doyle M, Beuchat L (ed), Food Microbiology: Fundamentals and Frontiers, Third Edition. ASM Press, Washington, DC. doi: 10.1128/9781555815912.ch19

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