Chapter 22 : Prions and Prion Diseases

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Preview this chapter:
Zoom in

Prions and Prion Diseases, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555815936/9781555814595_Chap22-1.gif /docserver/preview/fulltext/10.1128/9781555815936/9781555814595_Chap22-2.gif


Prions are generally regarded as the most reliable markers of so-called prion diseases. With the advent of the protein-only concept of the transmission of prion diseases, which is predicated on the idea that prions are the infectious agents causing prion disease, and with the 1997 Nobel Prize for Medicine awarded for the prion protein concept, prions have firmly asserted their inclusion in the club of infectious agents, along with bacteria, viruses, fungi, and parasites, the club's traditional members. The essence of the protein-only theory is that the abnormal prion enters the organism and converts the host’s normal prions into abnormal prions. The efficiency of the conversion is influenced by the degree of amino acid sequence homology between the two PrPs involved, so that the greater the degree of homology, the greater the rate of conversion. Several studies suggest that white blood cells may be involved in the process. It was observed that gut-associated macrophages initially remove transmissible spongiform encephalopathy (TSE) infectivity, but once their ability to remove the infectivity completely is overcome, macrophages may facilitate the spread of infectivity. Regulatory measures introduced to prevent the spread of TSEs to humans and other animal species are likely to stay. It is possible, however, that more research and better tests will more adequately characterize risk, which in turn may lead to a gradual loosening of some of the currently existing restrictions following a carefully performed risk assessment.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
Highlighted Text: Show | Hide
Loading full text...

Full text loading...


Image of Figure 1.
Figure 1.

Common approaches to detecting TSEs.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 2.
Figure 2.

Worldwide confirmed cases of BSE as of May 2007. Adapted from http:/www.oie.int./eng/info/en_esbmonde.htm.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint
Image of Figure 3.
Figure 3.

Schematic of migration patterns of abnormal prion protein reported in cases of typical BSE (T), atypical BSE (A or light and A or heavy) and scrapie. A has been reported in Japan, Italy, and Belgium, and A in France, the United Kingdom, and the United States.

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22
Permissions and Reprints Request Permissions
Download as Powerpoint


1. Andreoletti, O.,, N. Morel,, C. Lacroux,, V. Rouillon,, C. Barc,, G. Tabouret,, P. Sarradin,, P. Berthon,, P. Bernardet,, J. Mathey,, S. Lugan,, P. Costes,, F. Corbiere,, J. C. Espinosa,, J. M. Torres,, J. Grassi,, F. Schelcher, and, F. Lantier. 2006. Bovine spongiform encephalopathy agent in spleen from an ARR/ARR orally exposed sheep. J. Gen. Virol. 87: 10431046.
2. Andreoletti, O.,, S. Simon,, C. Lacroux,, N. Morel,, G. Tabouret,, A. Chabert,, S. Lugan,, F. Corbiere,, P. Ferre,, G. Foucras,, H. Laude,, F. Eychenne,, J. Grassi, and, F. Schelcher. 2004. PrP Sc accumulation in myocytes from sheep incubating natural scrapie. Nat. Med. 10: 591593.
3. Angers, R. C.,, S. R. Browning,, T. S. Seward,, C. J. Sigurdson,, M. W. Miller,, E. A. Hoover, and, G. C. Telling. 2006. Prions in skeletal muscles of deer with chronic wasting disease. Science 311: 1117.
4. Arnold, M. E.,, and J. W. Wilesmith. 2004. Estimation of the age-dependent risk of infection to BSE of dairy cattle in Great Britain. Prev. Vet. Med. 66: 3547.
5. Baron, G. S.,, and B. Caughey. 2003. Effect of glycosylphosphatidylinositol anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform. J. Biol. Chem. 278: 1488314892.
6. Baron, T. G. M.,, A. G. Biacabe,, A. Bencsik, and, J. P. M. Langeveld. 2006. Transmission of new bovine prion to mice. Emerg. Infect. Dis. 12: 11251128.
7. Bartz, J. C.,, A. E. Kincaid, and, R. A. Bessen. 2003. Rapid prion neuroinvasion following tongue infection. J. Virol. 77: 583591.
8. Basler, K.,, B. Oesch,, M. Scott,, D. Westaway,, M. Walchli,, D. F. Groth,, M. P. McKinley,, S. B. Prusiner, and, C. Weissmann. 1986. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46: 417428.
9. Belay, E. D.,, R. A. Maddox,, E. S. Williams,, M. W. Miller,, P. Gambetti, and, L. B. Schonberger. 2004. Chronic wasting disease and potential transmission to humans. Emerg. Infect. Dis. 10: 977984.
10. Bellworthy, S. J.,, G. Dexter,, M. Stack,, M. Chaplin,, S. A. C. Hawkins,, M. M. Simmons,, M. Jeffrey,, S. Martin,, L. Gonzales, and, P. Hill. 2005. Natural transmission of BSE between sheep within an experimental flock. Vet. Rec. 157: 206.
11. Benczik, A.,, and T. Baron. 2007. Bovine spongiform encephalopathy agent in a prion protein (PrP) ARR/ARR genotype sheep after peripheral challenge: complete immunohistochemical analysis of disease-associated PrP and transmission studies to ovine-transgenic mice. J. Infect. Dis. 195: 989996.
12. Biacabe, A. G.,, J. L. Laplanche,, S. Ryder, and, T. Baron. 2004. Distinct molecular phenotypes in bovine prion diseases. EMBO Rep. 5: 110114.
13. Brown, P. 2001. Bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease. Br. Med. J. 322: 841844.
14. Brown, P.,, E. H. Rau,, B. K. Johnson,, A. E. Bacote,, C. J. Gibbs, and, D. C. Gajdusek. 2000. New studies on the heat resistance of hamster adapted scrapie agent: threshold survival after ashing at 600°C suggests an inorganic template of replication. Proc. Nat. Acad. Sci. USA 97: 34183421.
15. Brown, P.,, E. H. Rau,, P. Lemieux,, B. K. Johnson,, A. E. Bacote, and, D. C. Gajdusek. 2004. Infectivity studies of both ash and air emissions from simulated incineration of scrapie-contaminated tissues. Environ. Sci. Technol. 38: 61556160.
16. Brown, P.,, L. M. McShane,, G. Zanusso, and, L. Detwiler. 2006. On the question of sporadic or atypical bovine spongiform encephalopathy and Creuzfeldt-Jakob disease. Emerg. Infect. Dis. 12: 18161821.
17. Brown, P.,, R. Meyer,, F. Cardone, and, M. Pocchiari. 2003. Ultra-high-pressure inactivation of prion infectivity in processed meat: a practical method to prevent human infection. Proc. Natl. Acad. Sci. USA 100: 60936097.
18. Bueler, H.,, A. Aguzzi,, A. Sailer,, R. A. Greiner,, P. Autenried,, M. Aguet, and, C. Weissmann. 1993. Mice devoid of PrP are resistant to scrapie. Cell 73: 13391347.
19. Buschmann, A.,, and M. H. Groschup. 2005. Highly bovine spongiform encephalopathy-sensitive transgenic mice confirm the essential restriction of infectivity to the nervous system in clinically diseased cattle. J. Infect. Dis. 192: 934942.
20. Buschmann, A.,, A. Gretzschel,, A. G. Biacabe,, K. Schiebel,, C. Corona,, C. Hoffmann,, M. Eiden,, T. Baron,, C. Casalone, and, M. H. Groschup. 2006. Atypical BSE in Germany—proof of transmissibility and biochemical characterization. Vet. Microbiol. 117: 103116.
21. Capobianco, R.,, C. Casalone,, S. Suardi,, M. Mangieri,, C. Miccolo,, L. Limido,, M. Catania,, G. Rossi,, G. D. Fede,, G. Giaccone,, M. G. Bruzzone,, L. Minati,, C. Corona,, P. Acutis,, D. Gelmetti,, G. Lombardi,, M. H. Groschup,, A. Buschmann,, G. Zanusso,, S. Monaco,, M. Caramelli, and, F. Tagliavini. 2007. Conversion of the BASE prion strain into the BSE strain: the origin of BSE? PLoS Pathog. 3: e31. [Epub ahead of print.]
22. Casalone, C.,, G. Zanusso,, P. Acutis,, S. Ferrari,, L. Capucci,, F. Tagliavini,, S. Monaco, and, M. Caramelli. 2004. Identification of a second bovine amyloidotic spongiform encephalopathy: molecular similarities with sporadic Creutzfeldt-Jakob disease. Proc. Natl. Acad. Sci. USA 101: 30653070.
23. Chesebro, B. 2004. A fresh look at BSE. Science 305: 19181921.
24. Colchester, A. C.,, and N. T. H. Colchester. 2005. The origin of bovine spongiform encephalopathy the human prion disease hypothesis. Lancet 366: 856861.
25. Comer, P. J.,, and P. J. Huntly. 2004. Exposure of the human population to BSE infectivity over the course of the BSE epidemic in Great Britain and the impact of changes to the Over Thirty Month Rule. J. Risk Res. 7: 523543.
26. Crozet, C.,, S. Lezmi,, F. Flamant,, J. Samarut,, T. Baron, and, A. Benczik. 2007. Peripheral circulation of the prion infectious agent in transgenic mice expressing the ovine prion protein gene in neurons only. J. Infect. Dis. 195: 9971006.
27. De Bosschere, H.,, S. Roels, and, E. Vanopdenbosch. 2004. Atypical case of bovine spongiform encephalopathy in an East-Flemish cow in Belgium. Int. J. Appl. Res. Vet. Med. 2: 5254.
28. DEFRA. 2007. 2005 case of H-type BSE in a cow, Information Bulletin, 71/07. Department for Environment, Food and Rural Affairs, London, United Kingdom. http://www.defra.gov.uk/news/2007/070309b.htm.
29. Deleault, N. R.,, R. W. Lucassen, and, S. Supattapone. 2003. RNA molecules stimulate prion protein conversion. Nature 425: 717720.
30. Doherr, M. G. 2006. Brief review on the epidemiology of transmissible spongiform encephalopathies. Vaccine [Epub ahead of print.] doi:10.1016/j.vaccine.2006.10.059.
31. EC. 2000. Council decision of 4 December 2000 concerning certain protection measures with regard to transmissible spongiform encephalopathies and the feeding of animal protein. Off. J. Euro. Comm. 306: 3233.
32. EC. 2001. Effective feed ban; guidance note for the third countries. European Commission, Brussels, Belgium. http://ec.europa.eu/food/fs/bse/bse30_en.pdf.
33. EFSA. 2006a. Evaluation of a rapid ante mortem BSE test. EFSA J. 95: 114.
34. EFSA. 2007. Quantitative risk assessment on the residual BSE risk in sheep meat and meat products. EFSA J. 442: 144.
35. EFSA. 2004. Scientific Report of the European Food Safety Authority on the Design of a Field Trial Protocol for the Evaluation of BSE Tests for Live Cattle. European Food Safety Authority, Parma, Italy. http://www.efsa.europa.eu/en/science/tse_assessments/bse_tse/612.html.
36. EFSA. 2005. Annex to the Opinion. Report of the Working Group on the assessment of the age limit in cattle for the removal of certain specified risk materials (SRM). EFSA J. 220: 121.
37. EFSA. 2006b. Scientific Report of the European Food Safety Authority on Transmissible Spongiform Encephalopathy (TSE) on a request from the European Commission on the evaluation of a rapid ante mortem BSE test. EFSA J. 95: 114.
38. Eloit, M.,, K. Adjou,, M. Coulpier,, J. J. Fontaine,, R. Hamel,, T. Lilin,, S. Messiaen,, O. Andreoletti,, T. Baron,, A. Bencsik,, A. G. Biacabe,, V. Beringue,, H. Laude,, A. Le Dur,, J. L. Vilotte,, E. Comoy,, J. P. Deslys,, J. Grassi,, S. Simon,, F. Lantier, and, P. Sarradin. 2005. BSE agent signatures in a goat. Vet. Rec. 156: 523524.
39. Everest, S. J.,, L. T. Thorne,, J. A. Hawthorn,, R. Jenkins,, C. Hammersley,, A. M. Ramsay,, S. A. Hawkins,, L. Venables,, L. Flynn,, R. Sayers,, J. Kilpatrick,, A. Sach,, J. Hope, and, R. Jackman. 2006. No abnormal prion protein detected in the milk of cattle infected with the bovine spongiform encephalopathy agent. J. Gen. Virol. 87: 24332441.
40. FDA. 1997. Substances prohibited from use in animal food or feed: animal proteins prohibited in ruminant feed. Fed. Reg. 62: 3093630978.
41. FDA. 2003. Use of material from deer and elk in animal feed, guidance for industry no. 158. Food and Drug Administration, Rockville, MD. http://www.fda.gov/cvm/Documents/guide158.pdf.
42. Fevrier, B.,, D. Vilette,, F. Archer,, D. Loew,, W. Faigle,, M. Vidal,, H. Laude, and, G. Raposo. 2004. Cells release prions in association with exosomes. Proc. Natl. Acad. Sci. USA 101: 96839688.
43. Foster, J. D.,, J. Hope, and, H. Fraser. 1993. Transmission of bovine spongiform encephalopathy to sheep and goats. Vet. Rec. 133: 339341.
44. Gizzi, G.,, L. W. D. van Raamsdonk,, V. Beaten,, I. Murray,, G. Berben,, G. Brambilla, and, C. von Holst. 2003. An overview of tests for animal tissues in feeds applied in response to public health concerns regarding bovine spongiform encephalopathy. Rev. Sci. Techn. Off. Int. Epiz. 22: 311331.
45. Glatzel, M.,, O. Giger,, N. Braun, and, A. Aguzzi. 2004. The peripheral nervous system and the pathogenesis of prion diseases. Curr. Mol. Med. 4: 355359.
46. Hartsough, G. R.,, and D. Burger. 1965. Encephalopathy of mink. I. Epizootiologic and clinical observations. J. Infect. Dis. 115: 387392.
47. Heikenwalder, M.,, N. Zeller,, H. Seeger,, M. Prinz,, P. C. Klohn,, P. Schwarts,, N. H. Ruddle,, C. Weissmann, and, A. Aguzzi. 2005. Chronic lymphocytic inflammation specifies the organ tropism of prions. Science 307: 11071110.
48. Heppner, F. L.,, A. D. Christ,, M. A. Klein,, M. Prinz,, M. Fried,, J. P. Kraehenbuhl, and, A. Aguzzi. 2001. Transepithelial prion transport by M cells. Nat. Med. 7: 976977.
49. Hoffmann, C.,, U. Ziegler,, A. Buschmann,, A. Weber,, L. Kupfer,, A. Oelschlegel,, B. Hammerschmidt, and, M. H. Groschup. 2007. Prions spread via the autonomic nervous system from the gut to the central nervous system in cattle incubating bovine spongiform encephalopathy. J. Gen. Virol. 88: 10481055.
50. Jackson, G. S.,, E. McKintosh,, E. Flechsig,, K. Prodromidou,, P. Hirsch,, J. Linehan,, S. Brandner,, A. R. Clarke,, C. Weissmann, and, J. Collinge. 2005. An enzyme-detergent method for effective prion decontamination of surgical steel. J. Gen. Virol. 86: 869878.
51. James, T. L.,, H. Liu,, N. B. Ulyanov,, S. Farr-Jones,, H. Zhang,, D. G. Donne,, K. Kaneko,, D. Groth,, I. Mehlhorn,, S. B. Prusiner, and, F. E. Cohen. 1997. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94: 1008610091.
52. Jeffrey, M.,, L. Gonzales,, A. Espenes,, C. M. Press,, S. Martin,, M. Chaplin,, L. Davis,, T. Landsverk,, C. MacAldowie,, S. Eaton, and, G. McGovern. 2006. Transportation of prion protein across the intestinal mucosa of scrapie-susceptible and scrapie-resistant sheep. J. Pathol. 209: 414.
53. Kasermann, F.,, and C. Kempf. 2003. Sodium hydroxide renders the prion protein PrP Sc sensitive to proteinase K. J. Gen. Virol. 84: 31733176.
54. Kim, T. Y.,, H. J. Shon,, Y. S. Joo,, U. K. Mun,, K. S. Kang, and, Y. S. Lee. 2005. Additional cases of chronic wasting disease in imported deer in Korea. J. Vet. Med. Sci. 67: 753759.
55. Kimberlin, R. H.,, and C. A. Walker. 1989. Pathogenesis of scrapie in mice after intragastric infection. Virus Res. 12: 213220
56. King, C. Y.,, and R. Diaz-Avalos. 2004. Protein-only transmission of three yeast prion strains. Nature 428: 319323.
57. Kreeger, T. J.,, D. L. Montgomery,, J. E. Jewell,, W. Schultz, and, E. S. Williams. 2006. Oral transmission of chronic wasting disease in captive Shira’s moose. J. Wildl. Dis. 42: 640645.
58. Lasmezas, C. I.,, E. Comay,, S. Hawkins,, C. Herzog,, F. Mouthon,, T. Konold,, F. Auvre,, E. Correia,, N. Lescoutra-Etchegaray,, N. Sales,, G. Wells,, P. Brown, and, J.-P. Deslys. 2005. Risk of oral infection with bovine spongiform encephalopathy agent in primates. Lancet 365: 781783.
59. Ligios, C.,, C. J. Sigurdson,, C. Santucciu,, G. Carcassola,, G. Manco,, M. Basagni,, C. Maestrale,, M. G. Cancedda,, L. Madau, and, A. Aguzzi. 2005. PrP Sc in mammary glands of sheep affected by scrapie and mastitis. Nat. Med. 11: 11371138.
60. Ma, J.,, and S. Lindquist. 2002. Conversion of PrP to a self-perpetuating PrP Sc-like conformation in the cytosol. Science 298: 17851788.
61. Ma, J.,, R. Wollmann, and, S. Lindquist. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298: 17811785.
62. Maignien, T.,, M. Shakweh,, P. Calvo,, D. Marce,, N. Sales,, E. Fattal,, J. P. Deslys,, P. Couvreur, and, C. I. Lasmezas. 2005. Role of gut macrophages in mice orally contaminated with scrapie or BSE. Int. J. Pharm. 298: 293304.
63. Marsh, R. F.,, A. E. Kincaid,, R. A. Bessen, and, J. C. Bartz. 2005. Interspecies transmission of chronic wasting disease prions to squirrel monkeys (Saimiri sciureus). J. Virol. 79: 1379413796.
64. Mathiason, C. K.,, J. G. Powers,, S. J. Dahmes,, D. A. Osborn,, K. V. Miller,, R. J. Warren,, G. L. Mason,, S. A. Hays,, J. Hayes-Klug,, D. M. Seelig,, M. A. Wild,, L. L. Wolfe,, T. R. Spraker,, M. W. Miller,, C. J. Sigurdson,, G. C. Telling, and, E. A. Hoover. 2006. Infectious prions in the saliva and blood of deer with chronic wasting disease. Science 314: 131136.
65. Miller, M. W.,, and E. S. Williams. 2003. Horizontal prion transmission in mule deer. Nature 425: 3536.
66. Miller, M. W. 2006. Chronic wasting disease in Colorado, 2005–2007. Colorado Division of Wildlife, Denver, CO. http://wildlife.state.co.us/NR/rdonlyres/763F5731-F895-4D52-9F27-2-B8D5BE91175/0/CWDReport2005_2006.pdf.
67. Miller, M. W.,, E. S. Williams,, N. Thompson-Hobbs, and, L. L. Wolfe. 2004. Environmental sources of prion transmission in mule deer. Emerg. Infect. Dis. 10: 10031006.
68. Momcilovic, D.,, and A. Rasooly. 2000. Detection and analysis of animal materials in food and feed. J. Food Prot. 63: 16021609.
69. Morel, E.,, S. Fouquet,, D. Chateau,, L. Yvernault,, Y. Frobert,, M. Pincon-Raymond,, J. Chambaz,, T. Pillot, and, M. Rousset. 2004. The cellular prion protein PrPc is expressed in human enterocytes in cell-cell junctional domains. J. Biol. Chem. 279: 14991505.
70. Nobel Assembly. 1976. Press release of 14 October 1976. Nobel Foundation, Stockholm, Sweden. http://nobelprize.org/nobel_prizes/medicine/laureates/1976/press.html.
71. Nobel Assembly. 1997. Press release of 6 October 1997. Karolinska, Institutet, Stockholm, Sweden. http://www.csb.ki.se/kisv/nobel.97.
72. Oesch, B.,, D. Westaway,, M. Walchli,, M. P. McKinley,, S. B. H. Kent,, R. Aebersold,, R. A. Barry,, P. Tempst,, D. B. Teplow,, L. E. Hood,, S. B. Prusiner, and, C. Weissmann. 1985. A cellular gene encodes scrapie PrP 27–30 protein. Cell 40: 735746.
73. OIE. 2007. World animal health situation. World Organization for Animal Health, Paris, France. http://www.oie.int/eng/info/en_esbmonde.htm.
74. O’Rourke, K. I.,, D. Zhuang,, A. Lyda,, G. Gomez,, E. S. Williams,, W. Tuo, and, M. W. Miller. 2003. Abundant PrP CWD in tonsil from mule deer with preclinical chronic wasting disease. J. Vet. Diagn. Invest. 15: 320323.
75. Pan, K.-M.,, M. Baldwin,, J. Nguyen,, M. Gasset,, A. Serban,, D. Groth,, I. Mehlhorn,, Z. Huang,, R. J. Fletterick,, F. E. Cohen, and, S. B. Prusiner. 1993. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion protein. Proc. Natl. Acad. Sci. USA 90: 1096210966.
76. Pearson, G. R.,, J. M. Wyatt,, T. J. Gruffydd-Jones,, J. Hope,, A. Chong,, R. J. Higgins,, A. C. Scott, and, G. A. Wells. 1992. Feline spongiform encephalopathy: fibril and PrP studies. Vet. Rec. 131: 307310.
77. Polak, M. P.,, W. Rozek,, J. Rola, and, J. F. Zmudzinski. 2004. Prion protein glycoforms from BSE cases in Poland. Bull. Vet. Inst. Pulawy 48: 201205.
78. Prusiner, S. B. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216: 136144.
79. Prusiner, S. B. 1997. Prion diseases and the BSE crisis. Science 278: 245251.
80. Prusiner, S. B. 1998. Prions. Proc. Natl. Acad. Sci. USA 95: 1336313383.
81. Race, R.,, A. Jenny, and, D. Sutton. 1998. Scrapie infectivity and proteinase K-resistant prion protein in sheep placenta, brain, spleen, and lymph node: implications for transmission and ante-mortem diagnosis. J. Infect. Dis. 178: 949953.
82. Raymond, G. J.,, A. Bossers,, L. D. Raymond,, K. I. O’Rourke,, L. E. McHolland,, P. K. Bryant III,, M. W. Miller,, E. S. Williams,, M. Smits, and, B. Caughey. 2000. Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease. EMBO J. 19: 44254430.
83. Richt, J. A.,, R. A. Kunkle,, D. Alt,, E. M. Nicholson,, A. N. Hamir,, S. Czub,, J. Kluge,, A. J. Davis, and, S. Mark Hall. 2007. Identification and characterization of two bovine spongiform encephalopathy cases diagnosed in the United States. J. Vet. Diagn. Invest. 19: 142154.
84. Rustom, A.,, R. Saffrich,, I. Markovic,, P. Walther, and, H. H. Gerdes. 2004. Nanotubular highways for intercellular organelle transport. Science 303: 10071010.
85. Safar, J. G.,, K. Kellings,, A. Serban,, D. Groth,, J. E. Cleaver,, S. B. Prusiner, and, D. Riesner. 2005. Search for a prion-specific nucleic acid. J. Virol. 79: 1079610806.
86. Schreuder, B. E. C. 1993. General aspects of transmissible spongiform encephalopathies and hypotheses about the agents. Vet. Q. 15: 167174.
87. SEAC. 2006. Chronic wasting disease in UK deer update. Spongiform Encephalopathy Advisory Committee, London, United Kingdom. http://www.seac.gov.uk/papers/93-2.pdf.
88. Seeger, H.,, M. Heikenwalder,, N. Zeller,, J. Kranich,, P. Schwarz,, A. Gaspert,, B. Seifert,, G. Miele, and, A. Aguzzi. 2005. Coincident scrapie infection and nephritis lead to urinary prion excretion. Science 310: 324326.
89. Siso, S.,, L. Gonzales,, M. Jeffrey,, S. Martin,, F. Chianini, and, P. Steele. 2006. Prion protein in kidneys of scrapie-infected sheep. Vet. Rec. 159: 327328.
90. Sohn, H. J.,, J. H. Kim,, K. S. Choi,, J. J. Nah,, Y. S. Joo,, J. H. Jean,, S. W. Ahn,, O. K. Kim,, D. Y. Kim, and, A. Balachadran. 2002. A case of chronic wasting disease in an elk imported to Korea from Canada. J. Vet. Med. Sci. 64: 855858.
91. Solassol, J.,, M. Pastore,, C. Crozet,, V. Perrier, and, S. Lehmann. 2006. A novel copper-hydrogen peroxide formulation for prion decontamination. J. Infect. Dis. 194: 865869.
92. Spraker, T. R.,, R. R. Zink,, B. A. Cummings,, C. J. Sigurdson,, M. W. Miller, and, K. I. O’Rourke. 2002. Distribution of protease-resistant prion protein and spongiform encephalopathy in free-ranging mule deer (Odocoileus hemionus) with chronic wasting disease. Vet. Pathol. 39: 546556.
93. Spraker, T. R.,, T. L. Gidlewski,, A. Balachadran,, K. C. VerCauteren,, L. Creekmore, and, R. D. Munger. 2006. Detection of PrP(CWD) in postmortem rectal lymphoid tissues in Rocky Mountain elk (Cervus alaphus nelsoni) infected with chronic wasting disease. J. Vet. Diagn. Invest. 18: 553557.
94. SSC. 1999. Opinion on the Human Exposure Risk (HER) via Food with Respect to BSE. Scientific Steering Committee, European Commission, Brussels, Belgium. http://ec.europa.eu/food/fs/sc/ssc/out67_en.pdf.
95. Stack, M.,, M. Jeffrey,, S. Gubbins,, S. Grimmer,, L. Gonzalez,, S. Martin,, M. Chaplin,, P. Webb,, M. Simmons,, Y. Spencer,, P. Bellerby,, J. Hope,, J. Wilesmith, and, D. Matthews. 2006. Monitoring for bovine spongiform encephalopathy in sheep in Great Britain, 1998–2004. J. Gen. Virol. 87: 20992107.
96. Statutory Instrument. 1988. The bovine spongiform encephalopathy order 1988 (SI 1988/1039). HMSO, London, United Kingdom.
97. Supervie, V.,, and D. Costagliola. 2004. The unrecognized French BSE epidemic. Vet. Res. 35: 349362.
98. Tamguney, G.,, K. Giles,, E. Bouzamondo-Bernstein,, P. J. Bosque,, M. W. Miller,, J. Safar,, S. J. DeArmond, and, S. B. Prusiner. 2006. Transmission of elk and deer prions to transgenic mice. J. Virol. 80: 91049114.
99. Tanaka, M.,, P. Chien,, N. Naber,, R. Cooke, and, J. S. Weissman. 2004. Conformational variations in an infectious protein determine prion strain differences. Nature 428: 323328.
100. Taylor, D. M.,, K. Fernie,, I. McConnell, and, P. J. Steele. 1999. Survival of scrapie agent after exposure to sodium dodecyl sulphate and heat. Vet. Microbiol. 67: 1316.
101. Taylor, D. M.,, and S. L. Woodgate. 2003. Rendering practices and inactivation of transmissible spongiform encephalopathy agents. Rev. Sci. Tech. Off. Int. Epiz. 22: 297310.
102. Taylor, D. M.,, S. L. Woodgate,, A. J. Fleetwood, and, R. J. G. Cawthorne. 1997. The effect of rendering procedures on scrapie agent. Vet. Rec. 141: 643649.
103. Telling, G. C.,, M. Scott,, J. Mastrianni,, R. Gabizon,, M. Torchia,, F. E. Cohen,, S. J. DeArmond, and, S. B. Prusiner. 1995. Prion propagation in mice expressing human and chimeric PrP trans-genes implicates the interaction of cellular PrP with another protein. Cell 83: 7990.
104. USDA. 2007a. BSE test results. United States Department of Agriculture, Washington, DC. http://www.aphis.usda.gov/lpa/issues/bse_testing/test_results.html.
105. USDA. 2007b. Chronic wasting disease. United States Department of Agriculture, Washington, DC. http://www.aphis.usda.gov/vs/nahps/cwd/. Accessed 15 March 2007.
106. USDA. 2004. Prohibition of the use of specified risk materials for human food and requirements for the disposition of non-ambulatory disabled cattle. Fed. Reg. 69: 18611874.
107. Vidal, E.,, M. Marquez,, M. Ordonez,, A. J. Raeber,, T. Struckmeyer,, B. Oesch,, S. Siso, and, M. Pumarola. 2005. Comparative study of the PrPBSE distribution in brains from BSE field cases using rapid tests. J. Virol. Methods 127: 2432.
108. Weissmann, C.,, M. Enari,, P. C. Klohn,, D. Rossi, and, E. Flechsig. 2002. Transmission of prions. Proc. Nat. Acad. Sci. USA 99 (Suppl. 4): 1637816383.
109. Wells, G. A. H.,, A. C. Scott,, C. T. Johnson,, R. F. Gunning,, R. D. Hancock,, M. Jeffrey,, M. Dawson, and, M. Bradley. 1987. A novel progressive spongiform encephalopathy in cattle. Vet. Rec. 121: 419420.
110. Wells, G. A. H.,, S. A. C. Hawkins,, R. B. Green,, A. R. Austin,, I. Dexter,, Y. I. Spencer,, M. J. Chaplin,, M. J. Syack, and, M. Dawson. 1998. Preliminary observations on the pathogenesis of experimental bovine spongiform encephalopathy (BSE): an update. Vet. Rec. 142: 103106.
111. Wells, G. A. H.,, T. Konold,, M. E. Arnold,, A. R. Austin,, S. A. C. Hawkins,, M. Stack,, M. M. Simmons,, Y. H. Lee,, D. Gavier-Widen,, M. Dawson, and, J. W. Wilesmith. 2007. Bovine spongiform encephalopathy: the effect of oral exposure dose on attack rate and incubation period in cattle. J. Gen. Virol. 88: 13631373.
112. Wild, M. A.,, T. R. Spraker,, C. J. Sigurdson,, K. I. O’Rourke, and, M. W. Miller. 2002. Preclinical diagnosis of chronic wasting disease in captive mule deer (Odocoileus hemionus) and white-tailed deer (Odocoileus virginianus) using tonsillar biopsy. J. Gen. Virol. 83: 26292634.
113. Wilesmith, J. W.,, J. B. M. Ryan, and, M. J. Atkinson. 1991. Bovine spongiform encephalopathy—epidemiologic studies on the origin. Vet. Rec. 128: 199203.
114. Will, R. G.,, J. W. Ironside,, M. Zeidler,, S. N. Cousens,, K. Estibeiro,, A. Alperovitch,, S. Poser,, M. Pocchiari,, A. Hofman, and, P. G. Smith. 1996. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347: 921925.
115. Williams, E. S. 2005. Chronic wasting disease. Vet. Pathol. 42: 530549.
116. Williams, E. S.,, and S. Young. 1980. Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J. Wildl. Dis. 16: 8998.
117. World Health Organization. 2000. WHO Consultation on Public Health and Animal Transmissible Spongiform Encephalopathies: Epidemiology, Risk and Research Requirements, p. 52. World Health Organization, Geneva, Switzerland.
118. Yamakawa, Y.,, K. Hagiwara,, K. Nohtomi,, Y. Nakamura,, M. Nishijima,, Y. Higuchi,, Y. Sato,, T. Sata, and the Expert Committee for BSE Diagnosis, Ministry of Health, Labor and Welfare of Japan. 2003. Atypical proteinase K-resistant prion protein (PrPres) observed in an apparently healthy 23-month-old Holstein steer. Jpn. J. Infect. Dis. 56: 221222.


Generic image for table
Table 1.

Overview of prion protein properties

Citation: Momcilovic D. 2010. Prions and Prion Diseases, p 343-356. In Juneja V, Sofos J (ed), Pathogens and Toxins in Foods. ASM Press, Washington, DC. doi: 10.1128/9781555815936.ch22

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