Molecular diagnostic tools in Creutzfeldt-Jakob disease and other prion disorders

Expert Review of Molecular Diagnostics

Volumn 4, Issue 3, 2004, Pages 351-359

  Van Everbroeck, Bart ^a,b   Boons, Jef ^b   De Leenheir, Evelyn ^b   Lübke, Ursula ^b   Cras, Patrick ^b  

^a UNIVERSITY OF ANTWERP   (Belgium)

^b UNIVERSITY OF ANTWERP   (Belgium)

Author keywords

Blood; Brain; Cerebrospinal fluid; Genetic polymorphisms; Infectious disorder; Pathogenesis; Susceptibility

Indexed keywords

PRION PROTEIN;

AUTOPSY; CREUTZFELDT JAKOB DISEASE; DISEASE MARKER; GENETIC MARKER; GENETIC POLYMORPHISM; HUMAN; PATHOPHYSIOLOGY; PREDICTION; PRION DISEASE; PROTEIN DETERMINATION; REVIEW;

ANIMALS; BIOLOGICAL MARKERS; CREUTZFELDT-JAKOB SYNDROME; HUMANS; MOLECULAR DIAGNOSTIC TECHNIQUES; PRION DISEASES; PRPSC PROTEINS; REAGENT KITS, DIAGNOSTIC; SENSITIVITY AND SPECIFICITY;

EID: 2542451817     PISSN: 14737159     EISSN: None     Source Type: Journal    
DOI: 10.1586/14737159.4.3.351     Document Type: Review

References (90)

1. Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519-550 (2001). Excellent paper reviewing the known molecular pathogenesis of both animal and human prion diseases.
2. Collie DA, Sellar RJ, Zeidler M et al. MRI of Creutzfeldt-Jakob disease: imaging features and recommended MRI protocol. Clin. Radiol. 56(9), 726-739 (2001).
3. Will RG, Zeidler M, Stewart GE et al. Diagnosis of new variant Creutzfeldt-Jakob disease. Ann. Neurol. 47(5), 575-582 (2000). Clear description of the signs and symptoms related to variant Creutzfeldt-Jakob disease (vCJD) and a true aid in the clinical differential diagnosis of CJD and vCJD.
4. Will RG, Alperovitch A, Poser S et al. Descriptive epidemiology of Creutzfeldt-Jakob disease in six European countries, 1993-1995. Ann. Neurol. 43(6), 763-767 (1998).
5. Wadsworth JDF, Joiner S, Hill AF et al. Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet 358(9277), 171-180 (2001).
6. Weissmann C. Spongiform encephalopathies. The prion's progress. Nature 349(6310), 569-571 (1991). Older review paper discussing the first decade of prion protein and prion pathogenesis research.
7. Meyer RK, McKinley MP, Bowman KA et al. Separation and properties of cellular and scrapie prion proteins. Proc. Natl Acad. Sci. USA 83(8), 2310-2314 (1986).
8. Zanusso G, Righetti PG, Ferrari S et al. Two-dimensional mapping of three phenotype-associated isoforms of the prion protein in sporadic Creutzfeldt-Jakob disease. Electrophoresis 23(2), 347-355 (2002).
9. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 216(4542), 136-144 (1982). Nobel price lecture given by Prof Prusiner covering his discovery and all his major contributions to prion protein research.
10. Griffith J. Self-replication and scrapie. Nature 215, 1043-1044 (1967).
11. Ckesebro B. Prion diseases: BSE and prions: uncertainties about the agent. Science 279(5347), 42-43 (1998).
12. Mabbott NA, Bruce ME. The immunobiology of TSE diseases. J. Gen. Virol 10, 2307-2318 (2001).
13. Baldauf E, Beekes M, Diringer H. Evidence for an alternative direct route of access for the scrapie agent to the brain bypassing the spinal cord. J. Gen. Virol. 78(Pt 5), 1187-1197 (1997).
14. McBride PA, Schulz Schaeffer WJ, Donaldson M et al. Early spread of scrapie from the gastrointestinal tract to the central nervous system involves autonomic fibers of the splanchnic and vagus nerves. J. Virol. 75(19), 9320-9327 (2001).
15. Doi S, Ito M, Shinagawa M et al. Western blot detection of scrapie-associated fibril protein in tissues outside the central nervous system from preclinical scrapie-infected mice. J. Gen. Virol. 69(Pt 4), 955-960 (1988).
16. Schreuder BEC, vanKeulen LJM, Vromans MEW, Langeveld JPM, Smits MA. Tonsillar biopsy and PrPSc detection in the preclinical diagnosis of scrapie. Vet. Rec. 142(21), 564-568 (1998).
17. Hill AF, Zeidler M, Ironside J, Collinge J. Diagnosis of new variant Creutzfeldt-Jakob disease by tonsil biopsy. Lancet 349(9045), 99-100 (1997).
18. Hill AF, Butterworth RJ, Joiner S et al. Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples. Lancet 353(9148), 183-189 (1999).
19. Brown P, Rohwer RG, Dunstan BC et al. The distribution of infectivity in blood components and plasma derivatives in experimental models of transmissible spongiform encephalopathy, Transfusion 38(9), 810-816 (1998).
20. Brown P, Cervenakova L, Diringer H. Blood infectivity and the prospects for a diagnostic screening test in Creutzfeldt-Jakob disease. J. Lab. Clin. Med. 137(1), 5-13 (2001).
21. Houston EF, Gravenor MB. Clinical signs in sheep experimentally infected with scrapie and BSE. Vet. Rec. 152(11), 333-334 (2003).
22. Hunter N, Foster J, Chong A et al. Transmission of prion diseases by blood transfusion. J. Gen. Virol. 83(Pt 11), 2897-2905 (2002). First paper to show actual transmission of the bovine spongiform encephalopathy (BSE) prion agent strain through blood transfusion having major public heath-related consequences.
23. Llewelyn CA, Hewitt PE, Knight RS et al. Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 363(9407), 417-421 (2004). Subsequent to [22], reported the first possible transmission of vCJD trough blood transfusion.
24. Bruce M, Chree A, McConnell I et al. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 343(1306), 405-411 (1994). First paper to confirm that BSE and vCJD were caused by the same prion protein agent through transmission experiments.
25. Bessen RA, Marsh RF. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J. Virol. 66(4), 2096-2101 (1992).
26. Bessen RA, Marsh RF. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68(12), 7859-7868 (1994).
27. Parchi P, Castellani R, Capellari S et al. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 39(6), 767-778 (1996). First indiction that multiple prion protein strains were also present in humans causing different clinical and pathological phenotypes.
28. Collinge J, Sidle KC, Meads J, Ironside J, Hill AF. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383(6602), 685-690 (1996).
29. Telling GC, Parchi P, DeArmond SJ et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274(5295), 2079-2082 (1996).
30. Somerville RA. Host and transmissible spongiform encephalopathy agent strain control glycosylation of PrP. J. Gen. Virol 7, 1865-1872 (1999).
31. DeArmond SJ, Sanchez H, Yehiely F et al. Selective neuronal targeting in prion disease. Neuron 19(6), 1337-1348 (1997).
32. Hill AF, Joiner S, Wadsworth JDF et al. Molecular classification of sporadic Creutzfeldt-Jakob disease. Brain 6, 1333-1346 (2003).
33. Hope J, Wood S, Birkett CR et al. Molecular analysis of ovine prion protein identifies similarities between BSE and an experimental isolate of natural scrapie, CH1641. J. Gen. Virol. 1, 1-4 (1999).
34. Hill AF, Sidle KCL, Joiner S et al. Molecular screening of sheep for bovine spongiform encephalopathy. Neurosci. Lett. 255(3), 159-162 (1998).
35. Safar J, Wille H, Itrri V et al. Eight prion strains have PrPSc molecules with different conformations. Nat. Med. 4(10), 1157-1165 (1998).
36. Wickner RB, Masison DC. Evidence for two prions in yeast: [URE3] and [PSI]. Curr. Top. Microbiol. Immunol. 207, 147-160 (1996).
37. Wickner RB. A new prion controls fungal cell fusion incompatibility. Proc. Natl Acad. Sci. USA 94(19), 10012-10014 (1997).
38. Prusiner SB. Prions. Proc. Natl Acad. Sci. USA 95(23), 13363-13383 (1998). Review discussing all types of prion diseases in humans and animals and also giving the present pathogenetic information.
39. Beekes M, Baldauf E, Diringer H. Sequential appearance and accumulation of pathognomonic markers in the central nervous system of hamsters orally infected with scrapie. J. Gen. Virol. 77(Pt 8), 1925-1934 (1996).
40. Lasmezas CI, Deslys JP, Robain O et al. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 275(5298), 402-405 (1997).
41. Fischer MB, Roeckl C, Parizek P, Schwarz HP, Aguzzi A. Binding of disease-associated prion protein to plasminogen. Nature 408(6811), 479-483 (2000).
42. Saborio GP, Permanne B, Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411(6839), 810-813 (2001).
43. Shaked GM, Shaked Y, Kariv Inbal Z et al. A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J. Biol. Chem. 276(34), 31479-31482 (2001).
44. Bosque PJ, Ryou C, Telling G et al. Prions in skeletal muscle. Proc. Natl Acad. Sci. USA 99(6), 3812-3817 (2002).
45. Zanusso G, Ferrari S, Cardone F et al. Detection of pathologic prion protein in the olfactory epithelium in sporadic Creutzfeldt-Jakob disease. New Engl. J. Med. 348(8), 711-719 (2003).
46. Paramithiotis E, Pinard M, Lawton T et al. A prion protein epitope selective for the pathologically misfolded conformation. Nat. Med. 9(7), 893-899 (2003).
47. Korth C, Stierli B, Streit P et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 390(6655), 74-77 (1997).
48. Kuczius T, Groschup MH. Differences in proteinase it resistance and neuronal deposition of abnormal prion proteins characterize bovine spongiform encephalopathy (BSE) and scrapie strains. Mol. Med. 5(6), 406-418 (1999).
49. Deslys JP, Comoy E, Hawkins S et al. Public health: screening slaughtered cattle for BSE. Nature 409(6819), 476-478 (2001).
50. Biffiger K, Zwald D, Kaufmann L et al. Validation of a luminescence immunoassay for the detection of PrPSc in brain homogenate. J. Virol. Methods 101(1-2), 79-84 (2002).
51. Grassi J, Comoy E, Simon S et al. Rapid test for the preclinical postmortem diagnosis of BSE in central nervous system tissue. Vet. Rec. 149(19), 577-582 (2001).
52. MacGregor I, Drummond O. Immunoassay of human plasma cellular prion protein. Transfusion 41 (11), 1453-1454 (2001).
53. Volkel D, Zimmermann K, Zerr I et al. Immunochemical determination of cellular prion protein in plasma from healthy subjects and patients with sporadic CJD or other neurologic diseases. Transfusion 41(4), 441-448 (2001).
54. Schmerr MJ, Jenny AL, Bulgin MS et al. Use of capillary electrophoresis and fluorescent labeled peptides to detect the abnormal prion protein in the blood of animals that are infected with a transmissible spongiform encephalopathy. J. Chromatogr. A. 853(1-2), 207-214 (1999).
55. Cervenakova L, Brown P, Soukharev S et al. Failure of immunocompetitive capillary electrophoresis assay to detect disease-specific prion protein in buffy coat from humans and chimpanzees with Creutzfeldt-Jakob disease. Electrophoresis 24(5), 853-859 (2003).
56. Rubenstein R, Gray PC, Wehlburg CM, Wagner JS, Tisone GC. Detection and discrimination of PrPSc by multi-spectral ultraviolet fluorescence. Biochem. Biophys. Res. Commun. 246(1), 100-106 (1998).
57. Giese A, Bieschke J, Eigen M, Kretzschmar HA. Putting prions into focus: application of single molecule detection to the diagnosis of prion diseases. Arch. Virol. 16, 161-171 (2000).
58. Bieschke J, Giese A, Schulz-Schaeffer W et al. Ultrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targets. Proc. Natl Acad. Sci. USA 97(10), 5468-5473 (2000).
59. Harrington MG, Merril CR, Asher DM, Gajdusek DC. Abnormal proteins in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. N. Engl. J. Med. 315(5), 279-283 (1986).
60. Zerr I, Bodemer M, Otto M et al. Diagnosis of Creutzfeldt-Jakob disease by 2D gel electrophoresis of cerebrospinal fluid. Lancet 348(9031), 846-849 (1996).
61. Hsich G, Kenney K, Gibbs CJ, Lee KH, Harrington MG. The 14-3-3 brain protein in cerebrospinal fluid as a marker for transmissible spongiform encephalopathies. N. Engl. J. Med. 335(13), 924-930 (1996).
62. Zerr I, Bodemer M, Gefeller O et al. Detection of 14-3-3 protein in the cerebrospinal fluid supports the diagnosis of Creutzfeldt-Jakob disease. Ann. Neurol. 43(1), 32-40 (1998).
63. Collins S, Boyd A, Fletcher A et al. Creutzfeldt-Jakob disease: diagnostic utility of 14-3-3 protein immunodetection in cerebrospinal fluid. J. Clin. Neurosci. 7(3), 203-208 (2000).
64. Beaudry P, Cohen P, Brandel JP et al. 14-3-3 protein, neuron-specific enolase and S-100 protein in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Dement. Geriatr. Cogn. Disord. 10(1), 40-46 (1999).
65. Van Everbroeck B, Quoilin S, Boons J, Martin JJ, Cras P. A prospective study of CSF markers in 250 patients with possible Creutzfeldt-Jakob disease. J. Neurol. Neurosurg. Psychiatry 74(9), 1210-1214 (2003).
66. Zerr I, Pocchiari M, Collins S et al. Analysis of EEG and CSF 14-3-3 proteins as aids to the diagnosis of Creutzfeldt-Jakob disease. Neurology 55(6), 811-815 (2000).
67. Otto M, Stein H, Szudra A et al. S-100 protein concentration in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. J. Neurol. 244(9), 566-570 (1997).
68. Otto M, Wiltfang J, Tumani H et al. Elevated levels of tau-protein in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Neurosci. Lett. 225(3), 210-212 (1997).
69. Zerr I, Bodemer M, Racker S et al. Cerebrospinal fluid concentration of neuron-specific enolase in diagnosis of Creutzfeldt-Jakob disease. Lancet 345(8965), 1609-1610 (1995).
70. Green AJ, Thompson EJ, Stewart GE et al. Use of 14-3-3 and other brain-specific proteins in CSF in the diagnosis of variant Creutzfeldt-Jakob disease. J. Neurol Neurosurg. Psychiatry 70(6), 744-748 (2001).
71. Van Everbroeck B, Green AJ, Pals P, Martin JJ, Cras P. Decreased levels of amyloid-β 1-42 in cerebrospinal fluid of Creutzfeldt-Jakob disease patients. J. Alzheimers Dis. 1(6), 419-424 (1999).
72. Otto M, Esselmann H, Schulz-Shaeffer W et al. Decreased β-amyloid 1-42 in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Neurology 54(5), 1099-1102 (2000).
73. Otto M. Diagnosis of Creutzfeldt-Jakob disease by measurement of S100 protein in serum: prospective case-control study (vol 316, pg 577, 1998). Br. Med. J. 317(7152), 171-171 (1998).
74. Miele G, Manson J, Clinton M. A novel erythroid-specific marker of transmissible spongiform encephalopathies. Nat. Med. 7(3), 361-364 (2001).
75. D'Alessandro M, Petraroli R, Ladogana A, Pocchiari M. High incidence of Creutzfeldt-Jakob disease in rural Calabria, Italy. Lancet 352(9145), 1989-1990 (1998).
76. Pocchiari M, Salvatore M, Cutruzzola F et al. A new point mutation of the prion protein gene in Creutzfeldt-Jakob disease. Ann. Neurol. 34(6), 802-807 (1993).
77. Chapman J, Brown P, Goldfarb LG et al. Clinical heterogeneity and unusual presentations of Creutzfeldt-Jakob disease in Jewish patients with the PRNP codon 200 mutation. J. Neurol. Neurosurg. Psychiatry 56(10), 1109-1112 (1993).
78. The EuroCJD group. Genetic epidemiology of Creutzfeldt-Jakob disease in Europe. Rev. Neurol. 157(6-7), 633-637 (2001). Discussion of the genetic findings in the largest studied sporadic CJD population.
79. Will RG. Variant Creutzfeldt-Jakob disease. J. Neurol. Neurosurg. Psychiatry 72(3), 285-286 (2002).
80. Mastrangelo P, Westaway D. The prion gene complex encoding PrPC and Doppel: insights from mutational analysis. Gene 275(1), 1-18 (2001).
81. Schroder B, Franz B, Hempfling P et al. Polymorphisms within the prion-like protein gene (Prnd) and their implications in human prion diseases, Alzheimer's disease and other neurological disorders. Hum. Genet. 109(3), 319-325 (2001).
82. Mead S, Beck J, Dickinson A, Fisher EMC, Collinge J. Examination of the human prion protein-like gene Doppel for genetic susceptibility to sporadic and variant Creutzfeldt-Jakob disease. Neurosci. Lett. 290(2), 117-120 (2000).
83. Comincini S, Foti MG, Tranulis MA et al. Genomic organization, comparative analysis and genetic polymorphisms of the bovine and ovine prion Doppel genes (PRND). Mamm. Genome 12(9), 729-733 (2001).
84. Tranulis MA. Influence of the prion protein gene, PRNP, on scrapie susceptibility in sheep. APMIS 110(1), 33-43 (2002).
85. Detwiler LA, Baylis M. The epidemiology of scrapie. Rev. Sci. Tech. 22(1), 121-143 (2003).
86. Goldmann W, Hunter N, Benson G, Foster JD, Hope J. Different scrapie-associated fibril proteins (PrP) are encoded bylines of sheep selected for different alleles of the Sip gene. J. Gen. Virol. 72 (10), 2411-2417 (1991).
87. Laplanche JL, Chatelain J, Westaway D et al. PrP polymorphisms associated with natural scrapie discovered by denaturing gradient gel electrophoresis. Genomics 15(1), 30-37 (1993).
88. Hunter N, Cairns D. Scrapie-free merino and poll dorset sheep from Australia and New Zealand have normal frequencies of scrapie-susceptible PrP genotypes. J. Gen. Virol. 79(Pt 8), 2079-2082 (1998).
89. Hunter N, Cairns D, Foster JD et al. Is scrapie solely a genetic disease? Nature 386(6621), 137 (1997).
90. Hills D, Schlaepfer J, Comincini S et al. Sequence variation in the bovine and ovine PRNP genes. Animal Genet. 34(3), 183-190 (2003).