Prion Diseases



Prion diseases are invariably fatal neurodegenerative diseases of humans and animals that attracted worldwide attention after detection of a bovine spongiform encephalopathy outbreak and its transmission to humans causing variant Creutzfeldt-Jakob disease. Prion diseases are unique among infectious diseases because of the unconventional characteristics of the etiologic agent and the biochemical mechanism for its propagation and because of the sporadic, genetic, and transmissible nature of some of these diseases. The agent causing prion diseases, termed prion, is an abnormal conformer of a host-encoded cellular protein known as the prion protein. The seminal event in the occurrence of prion diseases appears to be conversion of the cellular prion protein to the pathogenic prion by a poorly understood posttranslational process. Transmission of prion diseases within the same species has been extensively documented in sheep, cows, cervids, and humans. The modes of such transmissions include consumption of contaminated feed, accidental inoculation via medical or veterinary interventions, close animal-to-animal contact, and transmission via environmental contamination. Depending on the host species, these transmissions result from exposures to secretions or tissues known to harbor the infectious agent, including the brain, spinal cord, lymphatic tissues, saliva, and blood. Although cross-species spread of animal prion diseases has long been suspected, strong evidence for such spread is only available for the transmission of bovine spongiform encephalopathy to humans, domestic cats, and zoo animals.


Prion Disease Bovine Spongiform Encephalopathy Chronic Wasting Disease Fatal Familial Insomnia Atypical Scrapie 
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  1. 1.
    Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science. 1982;216:136–44.PubMedGoogle Scholar
  2. 2.
    Belay ED. Transmissible spongiform encephalopathies in humans. Annu Rev Microbiol. 1999;53:283–314.PubMedGoogle Scholar
  3. 3.
    Bell JE, Gentleman SM, Ironside JW, et al. Prion protein immunocytochemistry–UK five centre consensus report. Neuropathol Appl Neurobiol. 1997;23:26–35.PubMedGoogle Scholar
  4. 4.
    Kovacs GG, Head MW, Hegyi I, et al. Immunohistochemistry for the prion protein: comparison of different monoclonal antibodies in human prion disease subtypes. Brain Pathol. 2002;12:1–11.PubMedGoogle Scholar
  5. 5.
    Piccardo P, Safar J, Ceroni M, Gajdusek DC, Gibbs Jr CJ. Immunohistochemical localization of prion protein in spongiform encephalopathies and normal brain tissue. Neurology. 1990;40:518–22.PubMedGoogle Scholar
  6. 6.
    Privat N, Sazdovitch V, Seilhean D, LaPlanche JL, Hauw JJ. PrP immunohistochemistry: different protocols, including a procedure for long formalin fixation, and a proposed schematic classification for deposits in sporadic Creutzfeldt-Jakob disease. Microsc Res Tech. 2000;50:26–31.PubMedGoogle Scholar
  7. 7.
    Zaborowski A, Kordek R, Botts GT, Liberski PP. Immunohistochemical investigations of the prion protein accumulation in human spongiform encephalopathies. Special report II. Pol J Pathol. 2003;54:39–47.PubMedGoogle Scholar
  8. 8.
    Boelle PY, Valleron AJ. Incubation period of human prion disease. Lancet. 2006;368:914.PubMedGoogle Scholar
  9. 9.
    Collinge J, Whitfield J, McKintosh E, et al. Kuru in the 21st century–an acquired human prion disease with very long incubation periods. Lancet. 2006;367:2068–74.PubMedGoogle Scholar
  10. 10.
    Klitzman RL. Incubation period of human prion disease. Lancet. 2006;368:913.PubMedGoogle Scholar
  11. 11.
    Johnson RT. Prion diseases. Lancet Neurol. 2005;4:635–42.PubMedGoogle Scholar
  12. 12.
    Gajdusek DC, Zigas V. Degenerative disease of the central nervous system in New Guinea; the endemic occurrence of kuru in the native population. N Engl J Med. 1957;257:974–8.PubMedGoogle Scholar
  13. 13.
    Gajdusek DC. Kuru. Trans R Soc Trop Med Hyg. 1963;57:151–69.PubMedGoogle Scholar
  14. 14.
    Zigas V, Gajdusek DC. Kuru: clinical study of a new syndrome resembling paralysis agitans in natives of the Eastern Highlands of Australian New Guinea. Med J Aust. 1957;44:745–54.PubMedGoogle Scholar
  15. 15.
    Gajdusek DC, Zigas V. Kuru; clinical, pathological and epidemiological study of an acute progressive degenerative disease of the central nervous system among natives of the Eastern Highlands of New Guinea. Am J Med. 1959;26:442–69.PubMedGoogle Scholar
  16. 16.
    Hadlow WJ. Neuropathology and the scrapie-kuru connection. Brain Pathol. 1995;5:27–31.PubMedGoogle Scholar
  17. 17.
    Hadlow WJ. Scrapie and kuru. Lancet. 1959;2:289–90.Google Scholar
  18. 18.
    Gajdusek DC, Gibbs CJ. Attempts to demonstrate a transmissible agent in kuru, amyotrophic lateral sclerosis, and other sub-acute and chronic nervous system degenerations of man. Nature. 1964;204:257–9.PubMedGoogle Scholar
  19. 19.
    Gajdusek DC, Rogers NG, Basnight M, Gibbs Jr CJ, Alpers M. Transmission experiments with kuru in chimpanzees and the isolation of latent viruses from the explanted tissues of affected animals. Ann N Y Acad Sci. 1969;162:529–50.PubMedGoogle Scholar
  20. 20.
    Gajdusek DC, Gibbs Jr CJ, Asher DM, David E. Transmission of experimental kuru to the spider monkey (Ateles geoffreyi). Science. 1968;162:693–4.PubMedGoogle Scholar
  21. 21.
    Gajdusek DC, Gibbs Jr CJ, Alpers M. Transmission and passage of experimental “kuru” to chimpanzees. Science. 1967;155:212–4.PubMedGoogle Scholar
  22. 22.
    Beck E, Daniel PM, Alpers M, Gajdusek DC, Gibbs Jr CJ. Experimental “kuru” in chimpanzees. A pathological report. Lancet. 1966;2:1056–9.PubMedGoogle Scholar
  23. 23.
    Gajdusek DC, Gibbs CJ, Alpers M. Experimental transmission of a Kuru-like syndrome to chimpanzees. Nature. 1966;209:794–6.PubMedGoogle Scholar
  24. 24.
    Liberski PP. Kuru and D. Carleton Gajdusek: a close encounter. Folia Neuropathol. 2009;47:114–37.PubMedGoogle Scholar
  25. 25.
    Lindenbaum S. Cannibalism, kuru and anthropology. Folia Neuropathol. 2009;47:138–44.PubMedGoogle Scholar
  26. 26.
    Liberski PP, Sikorska B, Lindenbaum S, et al. Kuru: genes, cannibals and neuropathology. J Neuropathol Exp Neurol. 2012;71:92–103.PubMedGoogle Scholar
  27. 27.
    Sejvar JJ, Schonberger LB, Belay ED. Transmissible spongiform encephalopathies. J Am Vet Med Assoc. 2008;233:1705–12.PubMedGoogle Scholar
  28. 28.
    Sigurdson CJ, Miller MW. Other animal prion diseases. Br Med Bull. 2003;66:199–212.PubMedGoogle Scholar
  29. 29.
    Gajdusek DC. Unconventional viruses and the origin and disappearance of kuru. Science. 1977;197:943–60.PubMedGoogle Scholar
  30. 30.
    Alper T, Haig DA, Clarke MC. The exceptionally small size of the scrapie agent. Biochem Biophys Res Commun. 1966;22:278–84.PubMedGoogle Scholar
  31. 31.
    Scott MR, Supattapone S, Nguyen HOB, DeArmond SJ, Prusiner SB. Transgenic models of prion disease. Arch Virol. 2000;16(Suppl):113–24.Google Scholar
  32. 32.
    Weissmann C, Flechsig E. PrP knock-out and PrP transgenic mice in prion research. Br Med Bull. 2003;66:43–60.PubMedGoogle Scholar
  33. 33.
    Pattison IH, Jones KM. The possible nature of the transmissible agent of scrapie. Vet Rec. 1967;80:2–9.PubMedGoogle Scholar
  34. 34.
    Griffith JS. Self-replication and scrapie. Nature. 1967;215:1043–4.PubMedGoogle Scholar
  35. 35.
    Prusiner SB, Bolton DC, Groth DF, Bowman KA, Cochran SP, McKinley MP. Further purification and characterization of scrapie prions. Biochemistry. 1982;21:6942–50.PubMedGoogle Scholar
  36. 36.
    Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science. 1982;218:1309–11.PubMedGoogle Scholar
  37. 37.
    Manuelidis L. A 25 nm virion is the likely cause of transmissible spongiform encephalopathies. J Cell Biochem. 2007;100:897–915.PubMedGoogle Scholar
  38. 38.
    Manuelidis L, Liu Y, Mullins B. Strain-specific viral properties of variant Creutzfeldt-Jakob disease (vCJD) are encoded by the agent and not by host prion protein. J Cell Biochem. 2009;106:220–31.PubMedPubMedCentralGoogle Scholar
  39. 39.
    Miyazawa K, Emmerling K, Manuelidis L. High CJD infectivity remains after prion protein is destroyed. J Cell Biochem. 2011;112:3630–7.PubMedPubMedCentralGoogle Scholar
  40. 40.
    Miyazawa K, Emmerling K, Manuelidis L. Replication and spread of CJD, kuru and scrapie agents in vivo and in cell culture. Virulence. 2011;2:188–99.PubMedPubMedCentralGoogle Scholar
  41. 41.
    Eiden M, Buschmann A, Kupfer L, Groschup MH. Synthetic prions. J Vet Med B Infect Dis Vet Public Health. 2006;53:251–6.PubMedGoogle Scholar
  42. 42.
    Legname G, Nguyen HOB, Baskakov IV, Cohen FE, DeArmond SJ, Prusiner SB. Strain-specified characteristics of mouse synthetic prions. Proc Natl Acad Sci U S A. 2005;102:2168–73.PubMedPubMedCentralGoogle Scholar
  43. 43.
    Oesch B, Westaway D, Walchli M, et al. A cellular gene encodes scrapie PrP 27–30 protein. Cell. 1985;40:735–46.PubMedGoogle Scholar
  44. 44.
    Basler K, Oesch B, Scott M, et al. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell. 1986;46:417–28.PubMedGoogle Scholar
  45. 45.
    Pan KM, Stahl N, Prusiner SB. Purification and properties of the cellular prion protein from syrian-hamster brain. Protein Sci. 1992;1:1343–52.PubMedPubMedCentralGoogle Scholar
  46. 46.
    Viles JH, Cohen FE, Prusiner SB, Goodin DB, Wright PE, Dyson HJ. Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc Natl Acad Sci U S A. 1999;96:2042–7.PubMedPubMedCentralGoogle Scholar
  47. 47.
    Collinge J, Clarke AR. A general model of prion strains and their pathogenicity. Science. 2007;318:930–6.PubMedGoogle Scholar
  48. 48.
    DeArmond SJ, Prusiner SB. Perspectives on prion biology, prion disease pathogenesis, and pharmacologic approaches to treatment. Clin Lab Med. 2003;23:1–41.PubMedGoogle Scholar
  49. 49.
    Jansen K, Schafer O, Birkmann E, et al. Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form. Biol Chem. 2001;382:683–91.PubMedGoogle Scholar
  50. 50.
    Milhavet O, Casanova D, Chevallier N, McKay RD, Lehmann S. Neural stem cell model for prion propagation. Stem Cells. 2006;24:2284–91.PubMedGoogle Scholar
  51. 51.
    Wickner RB, Edskes HK, Shewmaker F, Kryndushkin D, Nemecek J. Prion variants, species barriers, generation and propagation. J Biol. 2009;8:47.PubMedPubMedCentralGoogle Scholar
  52. 52.
    Prusiner SB. Prions. Proc Natl Acad Sci U S A. 1998;95:13363–83.PubMedPubMedCentralGoogle Scholar
  53. 53.
    Bueler H, Aguzzi A, Sailer A, et al. Mice devoid of prp are resistant to scrapie. Cell. 1993;73:1339–47.PubMedGoogle Scholar
  54. 54.
    Baskakov IV, Legname G, Prusiner SB, Cohen FE. Folding of prion protein to its native alpha-helical conformation is under kinetic control. J Biol Chem. 2001;276:19687–90.PubMedGoogle Scholar
  55. 55.
    Principe S, Maras B, Schinina ME, Pocchiari M, Cardone F. Unraveling the details of prion (con)formation(s): recent advances by mass spectrometry. Curr Opin Drug Discov Devel. 2008;11:697–707.PubMedGoogle Scholar
  56. 56.
    Richardson EP, Masters CL. The nosology of Creutzfeldt-Jakob disease and conditions related to the accumulation of PrPCJD in the nervous system. Brain Pathol. 1995;5:33–41.PubMedGoogle Scholar
  57. 57.
    Brown P, Cathala F, Castaigne P, Gajdusek DC. Creutzfeldt-Jakob disease – clinical analysis of a consecutive series of 230 neuropathologically verified cases. Ann Neurol. 1986;20:597–602.PubMedGoogle Scholar
  58. 58.
    Brown P, Cathala F, Sadowsky D, Gajdusek DC. Creutzfeldt-Jakob disease in France: II. Clinical characteristics of 124 consecutive verified cases during the decade 1968–1977. Ann Neurol. 1979;6:430–7.PubMedGoogle Scholar
  59. 59.
    Gibbs Jr CJ, Joy A, Heffner R, et al. Clinical and pathological features and laboratory confirmation of Creutzfeldt-Jakob disease in a recipient of pituitary-derived human growth hormone. N Engl J Med. 1985;313:734–8.PubMedGoogle Scholar
  60. 60.
    Brown P, Cathala F, Gajdusek DC. Creutzfeldt-Jakob disease in France: III. Epidemiological study of 170 patients dying during the decade 1968–1977. Ann Neurol. 1979;6:438–46.PubMedGoogle Scholar
  61. 61.
    Zerr I, Poser S. Clinical diagnosis and differential diagnosis of CJD and vCJD with special emphasis on laboratory tests. APMIS. 2002;110:88–98.PubMedGoogle Scholar
  62. 62.
    Krasnianski A, Meissner B, Heinemann U, Zerr I. Clinical findings and diagnostic tests in Creutzfeldt-Jakob disease and variant Creutzfeldt-Jakob disease. Folia Neuropathol. 2004;42(Suppl B):24–38.PubMedGoogle Scholar
  63. 63.
    Brown P. EEG findings in Creutzfeldt-Jakob disease. JAMA. 1993;269:3168.PubMedGoogle Scholar
  64. 64.
    Cambier DM, Kantarci K, Worrell GA, Westmoreland BF, Aksamit AJ. Lateralized and focal clinical, EEG, and FLAIR MRI abnormalities in Creutzfeldt-Jakob disease. Clin Neurophysiol. 2003;114:1724–8.PubMedGoogle Scholar
  65. 65.
    Sakuishi K, Hanajima R, Kanazawa I, Ugawa Y. Periodic motor cortical excitability changes associated with PSDs of EEG in Creutzfeldt-Jakob disease (CJD). Clin Neurophysiol. 2005;116:1222–6.PubMedGoogle Scholar
  66. 66.
    Cuadrado-Corrales N, Jimenez-Huete A, Albo C, et al. Impact of the clinical context on the 14-3-3 test for the diagnosis of sporadic CJD. BMC Neurol. 2006;6:25.PubMedPubMedCentralGoogle Scholar
  67. 67.
    Huang N, Marie SK, Livramento JA, Chammas R, Nitrini R. 14-3-3 protein in the CSF of patients with rapidly progressive dementia. Neurology. 2003;61:354–7.PubMedGoogle Scholar
  68. 68.
    Peoc’h K, Delasnerie-Laupretre N, Beaudry P, Laplanche JL. Diagnostic value of CSF 14-3-3 detection in sporadic CJD diagnosis according to the age of the patient. Eur J Neurol. 2006;13:427–8.PubMedGoogle Scholar
  69. 69.
    Saiz A, Nos C, Yague J, Dominguez A, Graus F, Munoz P. The impact of the introduction of the 14-3-3 protein assay in the surveillance of sporadic Creutzfeldt-Jakob disease in Catalonia. J Neurol. 2001;248:592–4.PubMedGoogle Scholar
  70. 70.
    Shiga Y, Wakabayashi H, Miyazawa K, Kido H, Itoyama Y. 14-3-3 protein levels and isoform patterns in the cerebrospinal fluid of Creutzfeldt-Jakob disease patients in the progressive and terminal stages. J Clin Neurosci. 2006;13:661–5.PubMedGoogle Scholar
  71. 71.
    Sanchez-Juan P, Green A, Ladogana A, et al. CSF tests in the differential diagnosis of Creutzfeldt-Jakob disease. Neurology. 2006;67:637–43.PubMedGoogle Scholar
  72. 72.
    Cohen OS, Hoffmann C, Lee H, Chapman J, Fulbright RK, Prohovnik I. MRI detection of the cerebellar syndrome in Creutzfeldt-Jakob disease. Cerebellum. 2009;8:373–81.PubMedGoogle Scholar
  73. 73.
    Geschwind MD, Potter CA, Sattavat M, et al. Correlating DWI MRI with pathologic and other features of Jakob-Creutzfeldt disease. Alzheimer Dis Assoc Disord. 2009;23:82–7.PubMedPubMedCentralGoogle Scholar
  74. 74.
    Kong A, Kleinig T, Van der Vliet A, et al. MRI of sporadic Creutzfeldt-Jakob disease. J Med Imaging Radiat Oncol. 2008;52:318–24.PubMedGoogle Scholar
  75. 75.
    Lou X, Ma L, An NY, Cai YQ, Liang Y, Guo XG. Diffusion-weighted magnetic resonance imaging in diagnosis of Creutzfeldt-Jakob disease. Chin Med J (Engl). 2006;119:1242–7.Google Scholar
  76. 76.
    Poon MA, Stuckey S, Storey E. MRI evidence of cerebellar and hippocampal involvement in Creutzfeldt-Jakob disease. Neuroradiology. 2001;43:746–9.PubMedGoogle Scholar
  77. 77.
    Zanusso G. Should MRI, signs be included in the diagnostic criteria for sporadic Creutzfeldt-Jakob disease? Nat Clin Pract Neurol. 2006;2:68–9.PubMedGoogle Scholar
  78. 78.
    Zerr I, Kallenberg K, Summers DM, et al. Updated clinical diagnostic criteria for sporadic Creutzfeldt-Jakob disease. Brain. 2009;132:2659–68.PubMedPubMedCentralGoogle Scholar
  79. 79.
    Meissner B, Kallenberg K, Sanchez-Juan P, et al. MRI lesion profiles in sporadic Creutzfeldt-Jakob disease. Neurology. 2009;72:1994–2001.PubMedGoogle Scholar
  80. 80.
    Belay ED, Holman RC, Schonberger LB. Creutzfeldt-Jakob disease surveillance and diagnosis. Clin Infect Dis. 2005;41:834–6.PubMedGoogle Scholar
  81. 81.
    Gibbons RV, Holman RC, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States: 1979–1998. JAMA. 2000;284:2322–3.PubMedGoogle Scholar
  82. 82.
    Holman RC, Belay ED, Christensen KY, et al. Human prion diseases in the United States. PLoS One. 2010;5:e8521.PubMedPubMedCentralGoogle Scholar
  83. 83.
    Holman RC, Khan AS, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States, 1979–1994: using national mortality data to assess the possible occurrence of variant cases. Emerg Infect Dis. 1996;2:333–7.PubMedPubMedCentralGoogle Scholar
  84. 84.
    Holman RC, Khan AS, Kent J, Strine TW, Schonberger LB. Epidemiology of Creutzfeldt-Jakob disease in the United States, 1979–1990: analysis of national mortality data. Neuroepidemiology. 1995;14:174–81.PubMedGoogle Scholar
  85. 85.
    Peden AH, McGuire LI, Appleford NEJ, et al. Sensitive and specific detection of sporadic Creutzfeldt-Jakob disease brain prion protein using real-time quaking-induced conversion. J Gen Virol. 2012;93:438–49.PubMedPubMedCentralGoogle Scholar
  86. 86.
    Zanusso G. Detection of the pathological prion protein in the olfactory epithelium of Subjects with Sporadic Creutzfeldt-Jakob Disease. Chemical Senses 2008;33:S12. Fifteenth International Symposium on Olfaction and Taste, July 21–26, 2008, San Francisco, California.Google Scholar
  87. 87.
    Smith-Bathgate B. Creutzfeldt-Jakob disease: diagnosis and nursing care issues. Nurs Times. 2005;101:52–3.PubMedGoogle Scholar
  88. 88.
    Parry A, Baker I, Stacey R, Wimalaratna S. Long term survival in a patient with variant Creutzfeldt-Jakob disease treated with intraventricular pentosan polysulphate. J Neurol Neurosurg Psychiatry. 2007;78:733–4.PubMedPubMedCentralGoogle Scholar
  89. 89.
    Spilman P, Lessard P, Sattavat M, et al. A gamma-secretase inhibitor and quinacrine reduce prions and prevent dendritic degeneration in murine brains. Proc Natl Acad Sci U S A. 2008;105:10595–600.PubMedPubMedCentralGoogle Scholar
  90. 90.
    Collinge J, Gorham M, Hudson F, et al. Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient-preference trial. Lancet Neurol. 2009;8:334–44.PubMedPubMedCentralGoogle Scholar
  91. 91.
    Iuvone T, Esposito G, De Filippis D, Scuderi C, Steardo L. Cannabidiol: a promising drug for neurodegenerative disorders? CNS Neurosci Ther. 2009;15:65–75.PubMedGoogle Scholar
  92. 92.
    Ludewigs H, Zuber C, Vana K, Nikles D, Zerr I, Weiss S. Therapeutic approaches for prion disorders. Expert Rev Anti Infect Ther. 2007;5:613–30.PubMedGoogle Scholar
  93. 93.
    Rainov NG, Tsuboi Y, Krolak-Salmon P, Vighetto A, Doh-Ura K. Experimental treatments for human transmissible spongiform encephalopathies: is there a role for pentosan polysulfate? Expert Opin Biol Ther. 2007;7:713–26.PubMedGoogle Scholar
  94. 94.
    Stewart LA, Rydzewska LH, Keogh GF, Knight RS. Systematic review of therapeutic interventions in human prion disease. Neurology. 2008;70:1272–81.PubMedGoogle Scholar
  95. 95.
    Tremblay P, Meiner Z, Galou M, et al. Doxycycline control of prion protein transgene expression modulates prion disease in mice. Proc Natl Acad Sci U S A. 1998;95:12580–5.PubMedPubMedCentralGoogle Scholar
  96. 96.
    Gallardo-Godoy A, Gever J, Fife KL, Silber BM, Prusiner SB, Renslo AR. 2-Aminothiazoles as therapeutic leads for prion diseases. J Med Chem. 2011;54:1010–21.PubMedPubMedCentralGoogle Scholar
  97. 97.
    Mallucci G, Collinge J. Rational targeting for prion therapeutics. Nat Rev Neurosci. 2005;6:23–34.PubMedGoogle Scholar
  98. 98.
    Ward HJ, Knight RS. Surgery and risk of sporadic Creutzfeldt-Jakob disease. Neuroepidemiology. 2008;31:241–2.PubMedGoogle Scholar
  99. 99.
    Ruegger J, Stoeck K, Amsler L, et al. A case-control study of sporadic Creutzfeldt-Jakob disease in Switzerland: analysis of potential risk factors with regard to an increased CJD incidence in the years 2001–2004. BMC Public Health. 2009;9:18.PubMedPubMedCentralGoogle Scholar
  100. 100.
    van Duijn CM, Delasnerie-Laupretre N, Masullo C, et al. Case-control study of risk factors of Creutzfeldt-Jakob disease in Europe during 1993–95. European Union (EU) Collaborative Study Group of Creutzfeldt-Jakob disease (CJD). Lancet. 1998;351:1081–5.PubMedGoogle Scholar
  101. 101.
    Ward HJ, Everington D, Croes EA, et al. Sporadic Creutzfeldt-Jakob disease and surgery: a case-control study using community controls. Neurology. 2002;59:543–8.PubMedGoogle Scholar
  102. 102.
    Mahillo-Fernandez I, de Pedro-Cuesta J, Bleda MJ, et al. Surgery and risk of sporadic Creutzfeldt-Jakob disease in Denmark and Sweden: registry-based case-control studies. Neuroepidemiology. 2008;31:229–40.PubMedPubMedCentralGoogle Scholar
  103. 103.
    Bobowick AR, Brody JA, Matthews MR, Roos R, Gajdusek DC. Creutzfeldt-Jakob disease: a case-control study. Am J Epidemiol. 1973;98:381–94.PubMedGoogle Scholar
  104. 104.
    Davanipour Z, Alter M, Sobel E, Asher D, Gajdusek D. A case-control study of Creutzfeldt-Jakob disease. Am J Epidemiol. 1984;120:472.Google Scholar
  105. 105.
    Davanipour Z, Alter M, Sobel E, Asher D, Gajdusek DC. Creutzfeldt-Jakob disease – possible medical risk-factors. Neurology. 1985;35:1483–6.PubMedGoogle Scholar
  106. 106.
    Davanipour Z, Alter M, Sobel E, Asher DM, Gajdusek DC. A case-control study of Creutzfeldt-Jakob disease – dietary risk-factors. Am J Epidemiol. 1985;122:443–51.PubMedGoogle Scholar
  107. 107.
    Wientjens D, Davanipour Z, Hofman A, et al. Risk factors for Creutzfeldt-Jakob disease: a reanalysis of case-control studies. Neurology. 1996;46:1287–91.PubMedGoogle Scholar
  108. 108.
    Kondo K, Kuroiwa Y. A case control study of Creutzfeldt-Jakob disease – association with physical injuries. Ann Neurol. 1982;11:377–81.PubMedGoogle Scholar
  109. 109.
    de Pedro CJ, Ruiz Tovar M, Ward H, et al. Sensitivity to biases of case-control studies on medical procedures, particularly surgery and blood transfusion, and risk of Creutzfeldt-Jakob disease. Neuroepidemiology. 2012;39:1–18.Google Scholar
  110. 110.
    Collins S, Law MG, Fletcher A, Boyd A, Kaldor J, Masters CL. Surgical treatment and risk of sporadic Creutzfeldt-Jakob disease: a case-control study. Lancet. 1999;353:693–7.PubMedGoogle Scholar
  111. 111.
    Hamaguchi T, Noguchi-Shinohara M, Nozaki I, et al. Medical procedures and risk for sporadic Creutzfeldt-Jakob disease, Japan, 1999–2008. Emerg Infect Dis. 2009;15:265–71.PubMedPubMedCentralGoogle Scholar
  112. 112.
    Alcalde-Cabero E, Almazan-Isla J, Brandel JP, et al. Health professions and risk of sporadic Creutzfeldt-Jakob disease, 1965 to 2010. Euro Surveill. 2012;17:13–22.Google Scholar
  113. 113.
    Gambetti P, Kong QZ, Zou WQ, Parchi P, Chen SG. Sporadic and familial CJD: classification and characterisation. Br Med Bull. 2003;66:213–39.PubMedGoogle Scholar
  114. 114.
    Parchi P, Giese A, Capellari S, et al. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol. 1999;46:224–33.PubMedGoogle Scholar
  115. 115.
    Parchi P, Saverioni D. Molecular pathology, classification, and diagnosis of sporadic human prion disease variants. Folia Neuropathol. 2012;50:20–45.PubMedGoogle Scholar
  116. 116.
    Parchi P, Strammiello R, Giese A, Kretzschmar H. Phenotypic variability of sporadic human prion disease and its molecular basis: past, present, and future. Acta Neuropathol. 2011;121:91–112.PubMedGoogle Scholar
  117. 117.
    Parchi P, Strammiello R, Notari S, et al. Incidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with mixed phenotype and co-occurrence of PrPSc types: an updated classification. Acta Neuropathol. 2009;118:659–71.PubMedPubMedCentralGoogle Scholar
  118. 118.
    Parchi P, Castellani R, Capellari S, et al. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann Neurol. 1996;39:767–78.PubMedGoogle Scholar
  119. 119.
    Cali I, Castellani R, Alshekhlee A, et al. Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics. Brain. 2009;132:2643–58.PubMedPubMedCentralGoogle Scholar
  120. 120.
    Zou W-Q, Puoti G, Xiao X, et al. Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein. Ann Neurol. 2010;68:162–72.PubMedPubMedCentralGoogle Scholar
  121. 121.
    Brown P, Brandel J-P, Sato T, et al. Latrogenic Creutzfeldt-Jakob disease, final assessment. Emerg Infect Dis. 2012;18:901–7.PubMedPubMedCentralGoogle Scholar
  122. 122.
    Duffy P, Wolf J, Collins G, DeVoe AG, Streeten B, Cowen D. Letter: possible person-to-person transmission of Creutzfeldt-Jakob disease. N Engl J Med. 1974;290:692–3.PubMedGoogle Scholar
  123. 123.
    Hogan RN, Brown P, Heck E, Cavanagh HD. Risk of prion disease transmission from ocular donor tissue transplantation. Cornea. 1999;18:2–11.PubMedGoogle Scholar
  124. 124.
    Maddox RA, Belay ED, Curns AT, et al. Creutzfeldt-Jakob disease in recipients of corneal transplants. Cornea. 2008;27:851–4.PubMedGoogle Scholar
  125. 125.
    Bernoulli C, Siegfried J, Baumgartner G, et al. Danger of accidental person-to-person transmission of Creutzfeldt-Jakob disease by surgery. Lancet. 1977;1:478–9.PubMedGoogle Scholar
  126. 126.
    Gibbs CJ, Asher DM, Kobrine A, Amyx HL, Sulima MP, Gajdusek DC. Transmission of Creutzfeldt-Jakob-disease to a chimpanzee by electrodes contaminated during neurosurgery. J Neurol Neurosurg Psychiatry. 1994;57:757–8.PubMedPubMedCentralGoogle Scholar
  127. 127.
    Koch TK, Berg BO, De Armond SJ, Gravina RF. Creutzfeldt-Jakob disease in a young adult with idiopathic hypopituitarism. Possible relation to the administration of cadaveric human growth hormone. N Engl J Med. 1985;313:731–3.PubMedGoogle Scholar
  128. 128.
    Preece MA. Creutzfeldt-Jakob disease: implications for growth hormone deficient children. Neuropathol Appl Neurobiol. 1986;12:509–15.PubMedGoogle Scholar
  129. 129.
    Centers for Disease Control. Fatal degenerative neurologic disease in patients who received pituitary-derived human growth hormone. Morb Mortal Wkly Rep. 1985;34:359.Google Scholar
  130. 130.
    Centers for Disease Control and Prevention. Update: Creutzfeldt-Jakob disease in a patient receiving a cadaveric dura mater graft. Morb Mortal Wkly Rep. 1987;36:324–5.Google Scholar
  131. 131.
    Centers for Disease Control (CDC). Rapidly progressive dementia in a patient who received a cadaveric dura mater graft. Morb Mortal Wkly Rep. 1987;36:49–50, 5.Google Scholar
  132. 132.
    Thadani V, Penar PL, Partington J, et al. Creutzfeldt-Jakob disease probably acquired from a cadaveric dura mater graft – case-report. J Neurosurg. 1988;69:766–9.PubMedGoogle Scholar
  133. 133.
    Belay ED, Schonberger LB. The public health impact of prion diseases. Annu Rev Public Health. 2005;26:191–212.PubMedGoogle Scholar
  134. 134.
    Blossom DB, Maddox RA, Beavers SF, et al. A case of Creutzfeldt-Jakob disease associated with a dura mater graft in the United States. Infect Control Hosp Epidemiol. 2007;28:1396–7.PubMedGoogle Scholar
  135. 135.
    Centers for Disease Control and Prevention. Creutzfeldt-Jakob disease in patients who received a cadaveric dura mater graft – Spain, 1985–1992. Morb Mortal Wkly Rep. 1993;42:560–3.Google Scholar
  136. 136.
    Dobbins JG, Belay ED, Malecki J, et al. Creutzfeldt-Jakob disease in a recipient of a dura mater graft processed in the US: cause or coincidence? Neuroepidemiology. 2000;19:62–6.PubMedGoogle Scholar
  137. 137.
    Hannah EL, Belay ED, Gambetti P, et al. Creutzfeldt-Jakob disease after receipt of a previously unimplicated brand of dura mater graft. Neurology. 2001;56:1080–3.PubMedGoogle Scholar
  138. 138.
    Centers for Disease Control (CDC). Update: Creutzfeldt-Jakob disease in a second patient who received a cadaveric dura mater graft. Morb Mortal Wkly Rep. 1989;38:37–8, 43.Google Scholar
  139. 139.
    Centers for Disease Control and Prevention (CDC). Creutzfeldt-Jakob disease in patients who received a cadaveric dura mater graft–Spain, 1985–1992. Morb Mortal Wkly Rep. 1993;42:560–3.Google Scholar
  140. 140.
    Centers for Disease Control and Prevention (CDC). Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts – Japan, January 1979-May 1996. Morb Mortal Wkly Rep. 1997;46:1066–9.Google Scholar
  141. 141.
    Centers for Disease Control and Prevention (CDC). Update: Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts – Japan, 1979–2003. Morb Mortal Wkly Rep. 2003;52:1179–81.Google Scholar
  142. 142.
    Centers for Disease Control and Prevention (CDC). Update: Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts – Japan, 1978–2008. Morb Mortal Wkly Rep. 2008;57:1152–4.Google Scholar
  143. 143.
    Brown P, Preece M, Brandel JP, et al. Iatrogenic Creutzfeldt-Jakob disease at the millennium. Neurology. 2000;55:1075–81.PubMedGoogle Scholar
  144. 144.
    Esmonde T, Lueck CJ, Symon L, Duchen LW, Will RG. Creutzfeldt-Jakob-disease and lyophilized dura-mater grafts – report of 2 cases. J Neurol Neurosurg Psychiatry. 1993;56:999–1000.PubMedPubMedCentralGoogle Scholar
  145. 145.
    Iwasaki Y, Mimuro M, Yoshida M, Hashizume Y, Kitamoto T, Sobue G. Clinicopathologic characteristics of five autopsied cases of dura mater-associated Creutzfeldt-Jakob disease. Neuropathology. 2008;28:51–61.PubMedGoogle Scholar
  146. 146.
    Kim HL, Do JY, Cho HJ, et al. Dura mater graft-associated creutzfeldt-jakob disease: the first case in Korea. J Korean Med Sci. 2011;26:1515–7.PubMedPubMedCentralGoogle Scholar
  147. 147.
    Toovey S, Britz M, Hewlett RH. A case of dura mater graft-associated Creutzfeldt-Jakob disease in South Africa. S Afr Med J. 2006;96:592–3.PubMedGoogle Scholar
  148. 148.
    Brown P, Gajdusek DC, Gibbs Jr CJ, Asher DM. Potential epidemic of Creutzfeldt-Jakob disease from human growth hormone therapy. N Engl J Med. 1985;313:728–31.PubMedGoogle Scholar
  149. 149.
    Dixit K, Kreitschmann-Andermahr I, Basu A, et al. Human growth hormone-related iatrogenic Creutzfeldt-Jakob disease–being aware of diagnostic features 25 years later. J Clin Endocrinol Metab. 2009;94:2684–5.PubMedGoogle Scholar
  150. 150.
    Furtner M, Gelpi E, Kiechl S, et al. Iatrogenic Creutzfeldt-Jakob disease 22 years after human growth hormone therapy: clinical and radiological features. J Neurol Neurosurg Psychiatry. 2008;79:229–31.PubMedGoogle Scholar
  151. 151.
    Rappaport EB, Graham DJ. Pituitary growth hormone from human cadavers: neurologic disease in ten recipients. Neurology. 1987;37:1211–3.PubMedGoogle Scholar
  152. 152.
    Abrams JY, Schonberger LB, Belay ED, et al. Lower risk of Creutzfeldt-Jakob disease in pituitary growth hormone recipients initiating treatment after 1977. J Clin Endocrinol Metab. 2011;96:E1666–9.PubMedGoogle Scholar
  153. 153.
    Centers for Disease Control and Prevention. Update: Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts – Japan, 1979–2003. Morb Mortal Wkly Rep. 2003;52:1179–81.Google Scholar
  154. 154.
    Centers for Disease Control and Prevention. Update: Creutzfeldt-Jakob disease associated with cadaveric dura mater grafts – Japan, 1978–2008. Morb Mortal Wkly Rep. 2008;57:1152–4.Google Scholar
  155. 155.
    Wells GAH, Scott AC, Johnson CT, et al. A novel progressive spongiform encephalopathy in cattle. Vet Rec. 1987;121:419–20.PubMedGoogle Scholar
  156. 156.
    Collee JG. Bovine spongiform encephalopathy. Lancet. 1990;336:1300–3.PubMedGoogle Scholar
  157. 157.
    Collee JG, Bradley R. BSE: a decade on–part I. Lancet. 1997;349:636–41.PubMedGoogle Scholar
  158. 158.
    Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet. 1996;347:921–5.PubMedGoogle Scholar
  159. 159.
    Cohen CH, Valleron AJ. When did bovine spongiform encephalopathy (BSE) start? Implications on the prediction of a new variant of Creutzfeldt-Jakob disease (nvCJD) epidemic. Int J Epidemiol. 1999;28:526–31.PubMedGoogle Scholar
  160. 160.
    Belay ED, Schonberger LB. Variant Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Clin Lab Med. 2002;22:849–62, v–vi.PubMedGoogle Scholar
  161. 161.
    Haessig M, Haessig BU, Knubben-Schweizer G. Objectivity of BSE symptoms using Bayes theorem. Schweiz Arch Tierheilkd. 2011;153:565–7.Google Scholar
  162. 162.
    Brown P. Bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease. Br Med J. 2001;322:841–4.Google Scholar
  163. 163.
    Capobianco R, Casalone C, Suardi S, et al. Conversion of the BASE prion strain into the BSE strain: the origin of BSE? Plos Pathog. 2007;3:e31.PubMedPubMedCentralGoogle Scholar
  164. 164.
    Baron T, Biacabe AG. Origin of bovine spongiform encephalopathy. Lancet. 2006;367:297–8.PubMedGoogle Scholar
  165. 165.
    Torres J-M, Andreoletti O, Lacroux C, et al. Classical bovine spongiform encephalopathy by transmission of H-type prion in homologous prion protein context. Emerg Infect Dis. 2011;17:1636–44.PubMedPubMedCentralGoogle Scholar
  166. 166.
    Brown P. Afterthoughts about bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease. Emerg Infect Dis. 2001;7:598–600.PubMedPubMedCentralGoogle Scholar
  167. 167.
    Smith PG, Bradley R. Bovine spongiform encephalopathy (BSE) and its epidemiology. Br Med Bull. 2003;66:185–98.PubMedGoogle Scholar
  168. 168.
    Ghani AC, Ferguson NM, Donnelly CA, Anderson RM. Predicted vCJD mortality in Great Britain – Modelling the latest data puts a ceiling on the likely number of vCJD cases. Nature. 2000;406:583–4.PubMedGoogle Scholar
  169. 169.
    Ghani AC, Ferguson NM, Donnelly CA, Anderson RM. Factors determining the pattern of the variant Creutzfeldt-Jakob disease (vCJD) epidemic in the UK. Proc Biol Sci. 2003;270:689–98.PubMedPubMedCentralGoogle Scholar
  170. 170.
    Kelly DF, Wells GA, Haritani M, Higgins RJ, Jeffrey M. Neuropathological findings in cats with clinically suspect but histologically unconfirmed feline spongiform encephalopathy. Vet Rec. 2005;156:472–7.PubMedGoogle Scholar
  171. 171.
    Centers for Disease Control and Prevention (CDC). Bovine spongiform encephalopathy in a dairy cow – Washington state, 2003. Morb Mortal Wkly Rep. 2004;52:1280–5.Google Scholar
  172. 172.
    Centers for Disease Control and Prevention (CDC). Overview of BSE in North America. (Accessed at
  173. 173.
    Richt JA, Kunkle RA, Alt D, et al. Identification and characterization of two bovine spongiform encephalopathy cases diagnosed in the United States. J Vet Diagn Invest. 2007;19:142–54.PubMedGoogle Scholar
  174. 174.
    Richt JA, Hall SM. BSE case associated with prion protein gene mutation. PLoS Pathog. 2008;4:e1000156.PubMedPubMedCentralGoogle Scholar
  175. 175.
    Zeidler M, Stewart GE, Barraclough CR, et al. New variant Creutzfeldt-Jakob disease: neurological features and diagnostic tests. Lancet. 1997;350:903–7.PubMedGoogle Scholar
  176. 176.
    Bruce ME, Will RG, Ironside JW, et al. Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent. Nature. 1997;389:498–501.PubMedGoogle Scholar
  177. 177.
    Ironside JW. Variant Creutzfeldt-Jakob disease: an update. Folia Neuropathol. 2012;50:50–6.PubMedGoogle Scholar
  178. 178.
    Will RG, Zeidler M, Stewart GE, et al. Diagnosis of new variant Creutzfeldt-Jakob disease. Ann Neurol. 2000;47:575–82.PubMedGoogle Scholar
  179. 179.
    Collie DA, Summers DM, Sellar RJ, et al. Diagnosing variant Creutzfeldt-Jakob disease with the pulvinar sign: MR imaging findings in 86 neuropathologically confirmed cases. AJNR Am J Neuroradiol. 2003;24:1560–9.PubMedGoogle Scholar
  180. 180.
    Zeidler M, Stewart G, Cousens SN, Estibeiro K, Will RG. Codon 129 genotype and new variant CJD. Lancet. 1997;350:668.PubMedGoogle Scholar
  181. 181.
    Ironside JW, Head MW, Bell JE, McCardle L, Will RG. Laboratory diagnosis of variant Creutzfeldt-Jakob disease. Histopathology. 2000;37:1–9.PubMedGoogle Scholar
  182. 182.
    Peden AH, Head MW, Ritchie DL, Bell JE, Ironside JW. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet. 2004;364:527–9.PubMedGoogle Scholar
  183. 183.
    Peden AH, Ritchie DL, Ironside JW. Risks of transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Folia Neuropathol. 2005;43:271–8.PubMedGoogle Scholar
  184. 184.
    Zou S, Fang CT, Schonberger LB. Transfusion transmission of human prion diseases. Transfus Med Rev. 2008;22:58–69.PubMedGoogle Scholar
  185. 185.
    Llewelyn CA, Hewitt PE, Knight RS, et al. Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet. 2004;363:417–21.PubMedGoogle Scholar
  186. 186.
    Wilson K, Ricketts MN. A third episode of transfusion-derived vCJD. Lancet. 2006;368:2037–9.PubMedGoogle Scholar
  187. 187.
    Hewitt PE, Llewelyn CA, Mackenzie J, Will RG. Three reported cases of variant Creutzfeldt-Jakob disease transmission following transfusion of labile blood components. Vox Sang. 2006;91:348.PubMedGoogle Scholar
  188. 188.
    Hilton DA, Ghani AC, Conyers L, et al. Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J Pathol. 2004;203:733–9.PubMedGoogle Scholar
  189. 189.
    Casalone C, Zanusso G, Acutis P, et al. Identification of a second bovine amyloidotic spongiform encephalopathy: molecular similarities with sporadic Creutzfeldt-Jakob disease. Proc Natl Acad Sci U S A. 2004;101:3065–70.PubMedPubMedCentralGoogle Scholar
  190. 190.
    Biacabe AG, Laplanche JL, Ryder S, Baron T. Distinct molecular phenotypes in bovine prion diseases. EMBO Rep. 2004;5:110–5.PubMedPubMedCentralGoogle Scholar
  191. 191.
    Ono F, Tase N, Kurosawa A, et al. Atypical L-type bovine spongiform encephalopathy (L-BSE) transmission to cynomolgus macaques, a non-human primate. Jpn J Infect Dis. 2011;64:81–4.PubMedGoogle Scholar
  192. 192.
    Brown P, McShane LM, Zanusso G, Detwile L. On the question of sporadic or atypical bovine spongiform encephalopathy and Creutzfeldt-Jakob disease. Emerg Infect Dis. 2006;12:1816–21.PubMedPubMedCentralGoogle Scholar
  193. 193.
    Gavier-Widen D, Noremark M, Langeveld JP, et al. Bovine spongiform encephalopathy in Sweden: an H-type variant. J Vet Diagn Invest. 2008;20:2–10.PubMedGoogle Scholar
  194. 194.
    Buschmann A, Gretzschel A, Biacabe AG, et al. Atypical BSE in Germany–proof of transmissibility and biochemical characterization. Vet Microbiol. 2006;117:103–16.PubMedGoogle Scholar
  195. 195.
    Biacabe AG, Morignat E, Vulin J, Calavas D, Baron TG. Atypical bovine spongiform encephalopathies, France, 2001–2007. Emerg Infect Dis. 2008;14:298–300.PubMedPubMedCentralGoogle Scholar
  196. 196.
    Beringue V, Herzog L, Reine F, et al. Transmission of atypical bovine prions to mice transgenic for human prion protein. Emerg Infect Dis. 2008;14:1898–901.PubMedPubMedCentralGoogle Scholar
  197. 197.
    Kong Q, Zheng M, Casalone C, et al. Evaluation of the human transmission risk of an atypical bovine spongiform encephalopathy prion strain. J Virol. 2008;82:3697–701.PubMedPubMedCentralGoogle Scholar
  198. 198.
    Mestre-Frances N, Nicot S, Rouland S, et al. Oral transmission of L-type bovine spongiform encephalopathy in primate model. Emerg Infect Dis. 2012;18:142–5.PubMedPubMedCentralGoogle Scholar
  199. 199.
    Balkema-Buschmann A, Fast C, Kaatz M, et al. Pathogenesis of classical and atypical BSE in cattle. Prev Vet Med. 2011;102:112–7.PubMedGoogle Scholar
  200. 200.
    Hoffmann C, Eiden M, Kaatz M, et al. BSE infectivity in jejunum, ileum and ileocaecal junction of incubating cattle. Vet Res. 2011;42:21.PubMedPubMedCentralGoogle Scholar
  201. 201.
    Suardi S, Vimercati C, Casalone C, et al. Infectivity in skeletal muscle of cattle with atypical bovine spongiform encephalopathy. PLoS One. 2012;7:e31449.PubMedPubMedCentralGoogle Scholar
  202. 202.
    Belay ED, Maddox RA, Williams ES, Miller MW, Gambetti P, Schonberger LB. Chronic wasting disease and potential transmission to humans. Emerg Infect Dis. 2004;10:977–84.PubMedPubMedCentralGoogle Scholar
  203. 203.
    Miller MW, Williams ES. Chronic wasting disease of cervids. Curr Top Microbiol Immunol. 2004;284:193–214.PubMedGoogle Scholar
  204. 204.
    Saunders SE, Bartelt-Hunt SL, Bartz JC. Occurrence, transmission, and zoonotic potential of chronic wasting disease. Emerg Infect Dis. 2012;18:369–76.PubMedPubMedCentralGoogle Scholar
  205. 205.
    Miller MW, Swanson HM, Wolfe LL, et al. Lions and prions and deer demise. PLoS One. 2008;3:e4019.PubMedPubMedCentralGoogle Scholar
  206. 206.
    White SN, Spraker TR, Reynolds JO, O’Rourke KI. Association analysis of PRNP gene region with chronic wasting disease in Rocky Mountain elk. BMC Res Notes. 2010;3:314.PubMedPubMedCentralGoogle Scholar
  207. 207.
    Wilson GA, Nakada SM, Bollinger TK, Pybus MJ, Merrill EH, Coltman DW. Polymorphisms at the PRNP gene influence susceptibility to chronic wasting disease in two species of deer (Odocoileus Spp.) in Western Canada. J Toxicol Environ Health A. 2009;72:1025–9.PubMedGoogle Scholar
  208. 208.
    Wilson R, Plinston C, Hunter N, et al. Chronic wasting disease and atypical forms of bovine spongiform encephalopathy and scrapie are not transmissible to mice expressing wild-type levels of human prion protein. J Gen Virol. 2012;93:1624–9.PubMedGoogle Scholar
  209. 209.
    Sigurdson CJ. A prion disease of cervids: chronic wasting disease. Vet Res. 2008;39:41.PubMedGoogle Scholar
  210. 210.
    Almberg ES, Cross PC, Johnson CJ, Heisey DM, Richards BJ. Modeling routes of chronic wasting disease transmission: environmental prion persistence promotes deer population decline and extinction. PLoS One. 2011;6:e19896.PubMedPubMedCentralGoogle Scholar
  211. 211.
    Wasserberg G, Osnas EE, Rolley RE, Samuel MD. Host culling as an adaptive management tool for chronic wasting disease in white-tailed deer: a modelling study. J Appl Ecol. 2009;46:457–66.PubMedPubMedCentralGoogle Scholar
  212. 212.
    Krumm CE, Conner MM, Miller MW. Relative vulnerability of chronic wasting disease infected mule deer to vehicle collisions. J Wildl Dis. 2005;41:503–11.PubMedGoogle Scholar
  213. 213.
    Gough KC, Maddison BC. Prion transmission, prion excretion and occurrence in the environment. Prion. 2010;4:275–82.PubMedPubMedCentralGoogle Scholar
  214. 214.
    Maddison BC, Baker CA, Terry LA, et al. Environmental sources of scrapie prions. J Virol. 2010;84:11560–2.PubMedPubMedCentralGoogle Scholar
  215. 215.
    Spraker TR, Zink RR, Cummings BA, Sigurdson CJ, Miller MW, O’Rourke KI. Distribution of protease-resistant prion protein and spongiform encephalopathy in free-ranging mule deer (Odocoileus hemionus) with chronic wasting disease. Vet Pathol. 2002;39:546–56.PubMedGoogle Scholar
  216. 216.
    Race B, Meade-White K, Race R, Chesebro B. Prion infectivity in fat of deer with chronic wasting disease. J Virol. 2009;83:9608–10.PubMedPubMedCentralGoogle Scholar
  217. 217.
    Denkers ND, Telling GC, Hoover EA. Minor oral lesions facilitate transmission of chronic wasting disease. J Virol. 2011;85:1396–9.PubMedPubMedCentralGoogle Scholar
  218. 218.
    Williams ES. Chronic wasting disease. Vet Pathol. 2005;42:530–49.PubMedGoogle Scholar
  219. 219.
    Saunders SE, Bartz JC, Bartelt-Hunt SL. Influence of prion strain on prion protein adsorption to soil in a competitive matrix. Environ Sci Technol. 2009;43:5242–8.PubMedPubMedCentralGoogle Scholar
  220. 220.
    Saunders SE, Bartz JC, Vercauteren KC, Bartelt-Hunt SL. Enzymatic digestion of chronic wasting disease prions bound to soil. Prion. 2010;4:209.Google Scholar
  221. 221.
    Saunders SE, Bartz JC, Vercauteren KC, Bartelt-Hunt SL. An enzymatic treatment of soil-bound prions effectively inhibits replication. Appl Environ Microbiol. 2011;77:4313–7.PubMedPubMedCentralGoogle Scholar
  222. 222.
    Saunders SE, Shikiya RA, Langenfeld K, Bartelt-Hunt SL, Bartz JC. Replication efficiency of soil-bound prions varies with soil type. J Virol. 2011;85:5476–82.PubMedPubMedCentralGoogle Scholar
  223. 223.
    Saunders SE, Yuan Q, Bartz JC, Bartelt-Hunt S. Effects of solution chemistry and aging time on prion protein adsorption and replication of soil-bound prions. PLoS One. 2011;6:e18752.PubMedPubMedCentralGoogle Scholar
  224. 224.
    Schramm PT, Johnson CJ, Mathews NE, McKenzie D, Aiken JM, Pedersen JA. Potential role of soil in the transmission of prion disease. Med Miner Geochem. 2006;64:135–52.Google Scholar
  225. 225.
    Smith CB, Booth CJ, Pedersen JA. Fate of prions in soil: a review. J Environ Qual. 2011;40:449–61.PubMedPubMedCentralGoogle Scholar
  226. 226.
    Denkers ND, Seelig DM, Telling GC, Hoover EA. Aerosol and nasal transmission of chronic wasting disease in cervidized mice. J Gen Virol. 2010;91:1651–8.PubMedPubMedCentralGoogle Scholar
  227. 227.
    Kincaid AE, Bartz JC. The nasal cavity is a route for prion infection in hamsters. J Virol. 2007;81:4482–91.PubMedPubMedCentralGoogle Scholar
  228. 228.
    Mathiason CK, Hays SA, Powers J, et al. Infectious prions in pre-clinical deer and transmission of chronic wasting disease solely by environmental exposure. PLoS One. 2009;4:e5916.PubMedPubMedCentralGoogle Scholar
  229. 229.
    Belay ED, Gambetti P, Schonberger LB, et al. Creutzfeldt-Jakob disease in unusually young patients who consumed venison. Arch Neurol. 2001;58:1673–8.PubMedGoogle Scholar
  230. 230.
    Anderson CA, Bosque P, Filley CM, et al. Colorado surveillance program for chronic wasting disease transmission to humans: lessons from 2 highly suspicious but negative cases. Arch Neurol. 2007;64:439–41.PubMedGoogle Scholar
  231. 231.
    Mawhinney S, Pape WJ, Forster JE, Anderson CA, Bosque P, Miller MW. Human prion disease and relative risk associated with chronic wasting disease. Emerg Infect Dis. 2006;12:1527–35.PubMedGoogle Scholar
  232. 232.
    Centers for Disease Control and Prevention (CDC). Fatal degenerative neurologic illnesses in men who participated in wild game feasts – Wisconsin, 2002. Morb Mortal Wkly Rep. 2003;52:125–7.Google Scholar
  233. 233.
    Barria MA, Telling GC, Gambetti P, Mastrianni JA, Soto C. Generation of a new form of human PrPSc in vitro by interspecies transmission from cervid prions. J Biol Chem. 2011;286:7490–5.PubMedPubMedCentralGoogle Scholar
  234. 234.
    Sandberg MK, Al-Doujaily H, Sigurdson CJ, et al. Chronic wasting disease prions are not transmissible to transgenic mice overexpressing human prion protein. J Gen Virol. 2010;91:2651–7.PubMedPubMedCentralGoogle Scholar
  235. 235.
    Tamguney G, Giles K, Bouzamondo-Bernstein E, et al. Transmission of elk and deer prions to transgenic mice. J Virol. 2006;80:9104–14.PubMedPubMedCentralGoogle Scholar
  236. 236.
    Race B, Meade-White KD, Miller MW, et al. Susceptibilities of nonhuman primates to chronic wasting disease. Emerg Infect Dis. 2009;15:1366–76.PubMedPubMedCentralGoogle Scholar
  237. 237.
    Jennelle CS, Samuel MD, Nolden CA, et al. Surveillance for transmissible spongiform encephalopathy in scavengers of white-tailed deer carcasses in the chronic wasting disease area of Wisconsin. J Toxicol Environ Health A. 2009;72:1018–24.PubMedGoogle Scholar
  238. 238.
    Harrington RD, Baszler TV, O’Rourke KI, et al. A species barrier limits transmission of chronic wasting disease to mink (Mustela vison). J Gen Virol. 2008;89:1086–96.PubMedPubMedCentralGoogle Scholar
  239. 239.
    Heisey DM, Mickelsen NA, Schneider JR, et al. Chronic wasting disease (CWD) susceptibility of several North American rodents that are sympatric with cervid CWD epidemics. J Virol. 2010;84:210–5.PubMedPubMedCentralGoogle Scholar
  240. 240.
    Bartz JC, McKenzie DI, Bessen RA, Marsh RF, Aiken JM. Transmissible mink encephalopathy species barrier effect between ferret and mink – PrP gene and protein-analysis. J Gen Virol. 1994;75:2947–53.PubMedGoogle Scholar
  241. 241.
    Angers RC, Kang H-E, Napier D, et al. Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science. 2010;328:1154–8.PubMedPubMedCentralGoogle Scholar
  242. 242.
    Bessen RA, Marsh RF. Identification of 2 biologically distinct strains of transmissible mink encephalopathy in hamsters. J Gen Virol. 1992;73:329–34.PubMedGoogle Scholar
  243. 243.
    Nicot S, Baron T. Strain-specific barriers against bovine prions in hamsters. J Virol. 2011;85:1906–8.PubMedPubMedCentralGoogle Scholar
  244. 244.
    Mastrianni JA. The genetics of prion diseases. Genet Med. 2010;12:187–95.PubMedGoogle Scholar
  245. 245.
    Kovacs GG, Puopolo M, Ladogana A, et al. Genetic prion disease: the EUROCJD experience. Hum Genet. 2005;118:166–74.PubMedGoogle Scholar
  246. 246.
    Brown P, Galvez S, Goldfarb LG, et al. Familial Creutzfeldt-Jakob disease in Chile is associated with the codon 200 mutation of the PRNP amyloid precursor gene on chromosome 20. J Neurol Sci. 1992;112:65–7.PubMedGoogle Scholar
  247. 247.
    Brown P, Goldfarb LG, Gibbs CJ, Gajdusek DC. The phenotypic-expression of different mutations in transmissible familial Creutzfeldt-Jakob disease. Eur J Epidemiol. 1991;7:469–76.PubMedGoogle Scholar
  248. 248.
    Galvez S, Cartier L, Monari M, Araya G. Familial Creutzfeldt-Jakob disease in Chile. J Neurol Sci. 1983;59:139–47.PubMedGoogle Scholar
  249. 249.
    Sanchez-Valle R, Nos C, Yague J, Graus F, Dominguez A, Saiz A. Clinical and genetic features of human prion diseases in Catalonia: 1993–2002. Eur J Neurol. 2004;11:649–55.PubMedGoogle Scholar
  250. 250.
    Lee HS, Sambuughin N, Cervenakova L, et al. Ancestral origins and worldwide distribution of the PRNP 200K mutation causing familial Creutzfeldt-Jakob disease. Am J Hum Genet. 1999;64:1063–70.PubMedPubMedCentralGoogle Scholar
  251. 251.
    Goldfarb LG, Brown P, Haltia M, et al. Creutzfeldt-Jakob disease cosegregates with the codon-178ASN PRNP mutation in families of European origin. Ann Neurol. 1992;31:274–81.PubMedGoogle Scholar
  252. 252.
    Goldfarb LG, Brown P, Cervenakova L, Gajdusek DC. Molecular-genetic studies of Creutzfeldt-Jakob-disease. Mol Neurobiol. 1994;8:89–97.PubMedGoogle Scholar
  253. 253.
    Monari L, Chen SG, Brown P, et al. Fatal familial insomnia and familial Creutzfeldt-Jakob-disease – different prion proteins determined by a DNA polymorphism. Proc Natl Acad Sci U S A. 1994;91:2839–42.PubMedPubMedCentralGoogle Scholar
  254. 254.
    Dohura K, Tateishi J, Sasaki H, Kitamoto T, Sakaki Y. PRO- LEU change at position-102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome. Biochem Biophys Res Commun. 1989;163:974–9.Google Scholar
  255. 255.
    Tranchant C, Dohura K, Steinmetz G, et al. Mutation of codon 117 of the prion gene in a family of Gerstmann-Straussler-Scheinker disease. Rev Neurol (Paris). 1991;147:274–8.Google Scholar
  256. 256.
    Ghetti B, Dlouhy SR, Giaccone G, et al. Gerstmann-Straussler-Scheinker disease and the Indiana kindred. Brain Pathol. 1995;5:61–75.PubMedGoogle Scholar
  257. 257.
    Giaccone G, Verga L, Bugiani O, et al. Prion protein preamyloid and amyloid deposits in Gerstmann-Straussler-Scheinker disease, Indiana Kindred. Proc Natl Acad Sci U S A. 1992;89:9349–53.PubMedPubMedCentralGoogle Scholar
  258. 258.
    Piccardo P, Seiler C, Dlouhy SR, et al. Proteinase-K-resistant prion protein isoforms in Gerstmann-Straussler-Scheinker disease (Indiana kindred). J Neuropathol Exp Neurol. 1996;55:1157–63.PubMedGoogle Scholar
  259. 259.
    Tagliavini F, Prelli F, Porro M, et al. Amyloid fibrils in Gerstmann-Straussler-Scheinker disease (Indiana and Swedish Kindreds) express only prp peptides encoded by the mutant allele. Cell. 1994;79:695–703.PubMedGoogle Scholar
  260. 260.
    Unverzagt FW, Farlow MR, Norton J, Dlouhy SR, Young K, Ghetti B. Neuropsychological function in patients with Gerstmann-Straussler-Scheinker disease from the Indiana kindred (F198S). J Int Neuropsychol Soc. 1997;3:169–78.PubMedGoogle Scholar
  261. 261.
    Dlouhy S, Farlow M, Ghetti B, et al. Preliminary linkage analysis of Gerstmann-Straussler-Scheinker (GSS) disease in the Indiana Kindred. Am J Hum Genet. 1991;49:339.Google Scholar
  262. 262.
    Dlouhy SR, Hsiao K, Farlow MR, et al. Linkage of the Indiana kindred of gerstmann-straussler-Scheinker disease to the prion protein gene. Nat Genet. 1992;1:64–7.PubMedGoogle Scholar
  263. 263.
    Ghetti B, Farlow MR, Frangione B, Giaccone G, Tagliavini F, Bugiani O. Natural-history of Gerstmann-Straussler-Scheinker disease (GSS) in the Indiana Kindred (IK). J Neuropathol Exp Neurol. 1991;50:317.Google Scholar
  264. 264.
    Lugaresi E, Medori R, Montagna P, et al. Fatal familial insomnia and dysautonomia with selective degeneration of thalamic nuclei. N Engl J Med. 1986;315:997–1003.PubMedGoogle Scholar
  265. 265.
    Lugaresi E, Medori R, Montagna P, et al. Fatal familial insomnia and dysautonomia – reply. N Engl J Med. 1987;316:1027–8.Google Scholar
  266. 266.
    Medori R, Tritschler HJ, Leblanc A, et al. Fatal familial insomnia, a prion disease with a mutation at codon-178 of the prion protein gene. N Engl J Med. 1992;326:444–9.PubMedGoogle Scholar
  267. 267.
    Gallassi R, Morreale A, Montagna P, Gambetti P, Lugaresi E. Fatal familial insomnia – neuropsychological study of a disease with thalamic degeneration. Cortex. 1992;28:175–87.PubMedGoogle Scholar
  268. 268.
    Manetto V, Medori R, Cortelli P, et al. Fatal familial insomnia – clinical and pathological-study of 5 new cases. Neurology. 1992;42:312–9.PubMedGoogle Scholar
  269. 269.
    Reder AT, Mednick AS, Brown P, et al. Clinical and genetic-studies of fatal familial insomnia. Neurology. 1995;45:1068–75.PubMedGoogle Scholar
  270. 270.
    Sforza E, Montagna P, Tinuper P, et al. Sleep-wake cycle abnormalities in fatal familial insomnia – evidence of the role of the thalamus in sleep regulation. Electroencephalogr Clin Neurophysiol. 1995;94:398–405.PubMedGoogle Scholar
  271. 271.
    Gallassi R, Morreale A, Montagna P, et al. Fatal familial insomnia: behavioral and cognitive features. Neurology. 1996;46:935–9.PubMedGoogle Scholar
  272. 272.
    Krasnianski A, Bartl M, Sanchez Juan PJ, et al. Fatal familial insomnia: clinical features and early identification. Ann Neurol. 2008;63:658–61.PubMedGoogle Scholar
  273. 273.
    Montagna P, Gambetti P, Cortelli P, Lugaresi E. Familial and sporadic fatal insomnia. Lancet Neurol. 2003;2:167–76.PubMedGoogle Scholar
  274. 274.
    Capellari S, Parchi P, Cortelli P, et al. Sporadic fatal insomnia in a fatal familial insomnia pedigree. Neurology. 2008;70:884–5.PubMedGoogle Scholar
  275. 275.
    Groschup MH, Lacroux C, Buschmann A, et al. Classic scrapie in sheep with the ARR/ARR prion genotype in Germany and France. Emerg Infect Dis. 2007;13:1201–7.PubMedPubMedCentralGoogle Scholar
  276. 276.
    Fediaevsky A, Tongue SC, Noremark M, Calavas D, Ru G, Hopp P. A descriptive study of the prevalence of atypical and classical scrapie in sheep in 20 European countries. BMC Vet Res. 2008;4:19.PubMedPubMedCentralGoogle Scholar
  277. 277.
    Sirakov I, Peshev R, Christova L. Genetic predisposition of some Bulgarian sheep breeds to the scrapie disease. Virus Genes. 2011;43:153–9.PubMedGoogle Scholar
  278. 278.
    Sawalha RM, Villanueva B, Brotherstone S, Rogers PL, Lewis RM. Prediction of prion protein genotype and association of this genotype with lamb performance traits of Suffolk sheep. J Anim Sci. 2010;88:428–34.PubMedGoogle Scholar
  279. 279.
    Hamir AN, Kunkle RA, Richt JA, Greenlee JJ, Miller JM. Serial passage of sheep scrapie inoculum in Suffolk sheep. Vet Pathol. 2009;46:39–44.PubMedGoogle Scholar
  280. 280.
    Benestad SL, Sarradin P, Thu B, Schonheit J, Tranulis MA, Bratberg B. Cases of scrapie with unusual features in Norway and designation of a new type, Nor98. Vet Rec. 2003;153:202–8.PubMedGoogle Scholar
  281. 281.
    Benestad SL, Arsac J-N, Goldmann W, Noremark M. Atypical/Nor98 scrapie: properties of the agent, genetics, and epidemiology. Vet Res. 2008;39:19.PubMedGoogle Scholar
  282. 282.
    De Bosschere H, Roels S, Benestad SL, Vanopdenbosch E. Scrapie case similar to Nor98 diagnosed in Belgium via active surveillance. Vet Rec. 2004;155:707–8.PubMedGoogle Scholar
  283. 283.
    Gavier-Widen D, Noremark M, Benestad S, et al. Recognition of the Nor98 variant of scrapie in the Swedish sheep population. J Vet Diagn Invest. 2004;16:562–7.PubMedGoogle Scholar
  284. 284.
    Onnasch H, Gunn HM, Bradshaw BJ, Benestad SL, Bassett HF. Two Irish cases of scrapie resembling Nor98. Vet Rec. 2004;155:636–7.PubMedGoogle Scholar
  285. 285.
    Arsac J-N, Andreoletti O, Bilheude J-M, Lacroux C, Benestad SL, Baron T. Similar biochemical signatures and prion protein genotypes in atypical scrapie and Nor98 cases, France and Norway. Emerg Infect Dis. 2007;13:58–65.PubMedPubMedCentralGoogle Scholar
  286. 286.
    Bruce ME, Nonno R, Foster J, et al. Nor98-like sheep scrapie in the United Kingdom in 1989. Vet Rec. 2007;160:665–6.PubMedGoogle Scholar
  287. 287.
    Seuberlich T, Botteron C, Benestad SL, et al. Atypical scrapie in a Swiss goat and implications for transmissible spongiform encephalopathy surveillance. J Vet Diagn Invest. 2007;19:2–8.PubMedGoogle Scholar
  288. 288.
    Buschmann A, Biacabe AG, Ziegler U, et al. Atypical scrapie cases in Germany and France are identified by discrepant reaction patterns in BSE rapid tests. J Virol Methods. 2004;117:27–36.PubMedGoogle Scholar
  289. 289.
    Gretzschel A, Buschmann A, Langeveld J, Groschup MH. Immunological characterization of abnormal prion protein from atypical scrapie cases in sheep using a panel of monoclonal antibodies. J Gen Virol. 2006;87:3715–22.PubMedGoogle Scholar
  290. 290.
    Moum T, Olsaker I, Hopp P, et al. Polymorphisms at codons 141 and 154 in the ovine prion protein gene are associated with scrapie Nor98 cases. J Gen Virol. 2005;86:231–5.PubMedGoogle Scholar
  291. 291.
    Saunders GC, Cawthraw S, Mountjoy SJ, Hope J, Windl O. PrP genotypes of atypical scrapie cases in Great Britain. J Gen Virol. 2006;87:3141–9.PubMedGoogle Scholar
  292. 292.
    Caspari DK, Balkema-Buschmann A, Brandt HR, Groschup MH, Erhardt G, Luehken G. Polymorphisms in genes CTSB, CTSD, CAPN2, KLK1 and TGFB1 not associated with susceptibility to atypical or classical ovine scrapie. Arch Tierz. 2010;53:457–64.Google Scholar
  293. 293.
    Luehken G, Buschmann A, Brandt H, Eiden M, Groschup MH, Erhardt G. Epidemiological and genetical differences between classical and atypical scrapie cases. Vet Res. 2007;38:65–80.Google Scholar
  294. 294.
    Fediaevsky A, Morignat E, Ducrot C, Calavas D. A case-control study on the origin of atypical scrapie in sheep, France. Emerg Infect Dis. 2009;15:710–8.PubMedPubMedCentralGoogle Scholar
  295. 295.
    Fediaevsky A, Gasqui P, Calavas D, Ducrot C. Discrepant epidemiological patterns between classical and atypical scrapie in sheep flocks under French TSE control measures. Vet J. 2010;185:338–40.PubMedGoogle Scholar
  296. 296.
    Fediaevsky A, Maurella C, Noremark M, et al. The prevalence of atypical scrapie in sheep from positive flocks is not higher than in the general sheep population in 11 European countries. BMC Vet Res. 2010;6:9.PubMedPubMedCentralGoogle Scholar
  297. 297.
    Arsac J-N, Betemps D, Morignat E, et al. Transmissibility of atypical scrapie in ovine transgenic mice: major effects of host prion protein expression and donor prion genotype. PLoS One. 2009;4:e7300.PubMedPubMedCentralGoogle Scholar
  298. 298.
    Griffiths PC, Plater JM, Jayasena D, et al. Transmission of TSEs to transgenic mice overexpressing ovine PrP(ARR). Prion. 2010;4:152.Google Scholar
  299. 299.
    Andreoletti O, Orge L, Benestad SL, et al. Atypical/Nor98 scrapie infectivity in sheep peripheral tissues. PLoS Pathog. 2011;7:e1001285.PubMedPubMedCentralGoogle Scholar
  300. 300.
    Safar JG, Prusiner SB. New generation of prion tests: Conformation-dependent immunoassay (CDI) (Abstract). Am Chem Soc. 2003;226:U102–3.Google Scholar
  301. 301.
    Safar JG, Geschwind MD, Deering C, et al. Diagnosis of human prion disease. Proc Natl Acad Sci U S A. 2005;102:3501–6.PubMedPubMedCentralGoogle Scholar
  302. 302.
    Castilla J, Morales R, Saa P, Barria M, Gambetti P, Soto C. Cell-free propagation of prion strains. EMBO J. 2008;27:2557–66.PubMedPubMedCentralGoogle Scholar
  303. 303.
    Orru CD, Caughey B. Prion seeded conversion and amplification assays. In: Tatzelt J, editor. Prion proteins. Berlin, Germany: Springer; 2011. p. 121–33.Google Scholar
  304. 304.
    Atarashi R, Moore RA, Sim VL, et al. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat Methods. 2007;4:645–50.PubMedGoogle Scholar
  305. 305.
    Morales R, Duran-Aniotz C, Diaz-Espinoza R, Camacho MV, Soto C. Protein misfolding cyclic amplification of infectious prions. Nat Protoc. 2012;7:1397–409.PubMedPubMedCentralGoogle Scholar
  306. 306.
    Castilla J, Saa P, Morales R, Abid K, Maundrell K, Soto C. Protein misfolding cyclic amplification for diagnosis and prion propagation studies. In: Kheterpal IWR, editor. Amyloid, prions, and other protein aggregates, Pt B. San Diego, California: Academic Press; 2006. p. 3–21.Google Scholar
  307. 307.
    Saa P, Castilla J, Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem. 2006;281:35245–52.PubMedGoogle Scholar
  308. 308.
    Soto C, Saborio GP, Anderes L. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond. Trends Neurosci. 2002;25:390–4.PubMedGoogle Scholar
  309. 309.
    Cramm M, Schmitz M, Zerr I. Comparison of two diagnostic approaches-detection of PrPSc via quaking-induced conversion and 14-3-3 in cerebrospinal fluid of Creutzfeldt-Jakob disease patients. Prion. 2012;6:93–4.Google Scholar

Suggested Reading

  1. Collinge J, Palmer MS. Prion diseases. Oxford/New York: Oxford University Press; 1997.Google Scholar
  2. Prusiner SB. Prion biology and diseases. 2nd ed. New York: Cold Spring Harbor Laboratory Press; 2003.Google Scholar
  3. Soto C. Prions: the new biology of proteins. New York: CRC Press, Taylor & Francis Group; 2006.Google Scholar

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Division of High-Consequence Pathogens and PathologyNCEZID, Centers for Disease Control and PreventionAtlantaUSA
  2. 2.Department of Medical Microbiology and ImmunologyCreighton UniversityOmahaUSA

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