The In Vitro Bioassay Systems for the Amplification and Detection of Abnormal Prion PrPSc in Blood and Tissues

Transfusion Medicine Reviews

Volumn 22, Issue 3, 2008, Pages 234-242

  Zhang, Wandong ^a,b   Wu, Jun ^a,b   Li, Yan ^a,b   Carke, Robert C ^a,b   Wong, Tom ^a,b  

^a Faculty of Medicine   (Canada)

^b PUBLIC HEALTH AGENCY OF CANADA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

ARTICLE; BLOOD TRANSFUSION; CELL LINE; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; IMMUNOASSAY; IN VITRO STUDY; INFECTION; NONHUMAN; PRION; PRION DISEASE; PROTEIN EXPRESSION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

ANIMALS; BIOLOGICAL ASSAY; BLOOD TRANSFUSION; CREUTZFELDT-JAKOB SYNDROME; DONOR SELECTION; HUMANS; LIVING DONORS; PRPSC PROTEINS;

EID: 45249108663     PISSN: 08877963     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tmrv.2008.02.004     Document Type: Article

References (62)

1. Farrugia A., Ironside J.W., and Giangrande P. Variant Creutzfeldt-Jakob disease transmission by plasma products: Assessing and communicating risk in an era of scientific uncertainty. Vox Sang 89 (2005) 186-192
2. Weissmann C., and Aguzzi A. Approaches to therapy of prion diseases. Annu Rev Med 56 (2005) 321-344
3. Hewitt P.E., Llewelyn C.A., Mackenzie J., et al. Creutzfeldt-Jakob disease and blood transfusion: Results of the UK Transfusion Medicine Epidemiological Review study. Vox Sang 91 (2006) 221-230
4. Mushahwar I.K. Verses, viruses, and the vulnerability of the blood supply in industrialized countries. J Med Virol 79 (2007) 1229-1237
5. Castilla J., Saa P., and Soto C. Detection of prions in blood. Nat Med 11 (2005) 982-985
6. Supattapone S., Geoghegan J.C., and Rees J.R. On the horizon: A blood test for prions. Trends Microbiol 14 (2006) 149-151
7. Saa P., Castilla J., and Soto C. Presymptomatic detection of prions in blood. Science 313 (2006) 92-94
8. Jones M., Peden A., Prowse C., et al. In vitro amplification and detection of variant Creutzfeldt-Jakob disease PrP(Sc). J Pathol 213 (2007) 21-26
9. Chang B., Cheng X., Yin S., et al. Test for detection of disease-associated prion aggregate in the blood of infected but asymptomatic animals. Clin Vaccine Immunol 14 (2007) 36-43
10. Carp R.I., Callahan S.M., Patrick B.A., et al. Interaction of scrapie agent and cells of the lymphoreticular system. Arch Virol 136 (1994) 255-268
11. Bosque P.J., and Prusiner S.B. Cultured cell sublines highly susceptible to prion infection. J Virol 74 (2000) 4377-4386
12. Aguzzi A., Heppner F.L., Heikenwalder M., et al. Immune system and peripheral nerves in propagation of prions to CNS. Br Med Bull 66 (2003) 141-159
13. Archer F., Bachelin C., Andreoletti O., et al. Cultured peripheral neuroglial cells are highly permissive to sheep prion infection. J Virol 78 (2004) 482-490
14. de Almeida C.J., Chiarini L.B., da Silva J.P., et al. The cellular prion protein modulates phagocytosis and inflammatory response. J Leukoc Biol 77 (2005) 238-246
15. Glatzel M., Abela E., Maissen M., et al. Extraneural pathologic prion protein in sporadic Creutzfeldt-Jakob disease. N Engl J Med 349 (2004) 1812-1820
16. Saa P., Castilla J., and Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem 281 (2006) 35245-35252
17. Soto C., Saborio G.P., and Anderes L. Cyclic amplification of protein misfolding: Application to prion-related disorders and beyond. Trends Neurosci 25 (2002) 390-394
18. Minor P., Newham J., Jones N., et al. Standards for the assay of Creutzfeldt-Jakob disease specimens. J Gen Virol 85 (2004) 1777-1784 (Pt 6)
19. Health Protection Agency. 4th case of variant CJD infection associated with blood transfusion. http://www.hpa.org.uk/hpa/news/articles/press_releases/2007/070118_vCJD.htm.
20. Llewelyn C.A., Hewitt P.E., Knight R.S., et al. Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 63 (2004) 417-421
21. Sakudo A., Nakamura I., Ikuta K., et al. Recent developments in prion disease research: Diagnostic tools and in vitro cell culture models. J Vet Med Sci 69 (2007) 329-337
22. Lehto M.T., Peery H.E., and Cashman N.R. Current and future molecular diagnostics for prion diseases. Expert Rev Mol Diagn 6 (2006) 597-611
23. Castilla J., Saa P., Morales R., et al. Protein misfolding cyclic amplification for diagnosis and prion propagation studies. Methods Enzymol 412 (2006) 3-21
24. Solassol J., Crozet C., Perrier V., et al. Cationic phosphorus-containing dendrimers reduce prion replication both in cell culture and in mice infected with scrapie. J Gen Virol 85 (2004) 1791-1799 (Pt 6)
25. Ladogana A., Liu Q., Xi Y.-G., et al. Proteinase-resistant protein in human neuroblastoma cells infected with brain material from Creutzfeld-Jakob patient. Lancet 345 (1995) 594-595
26. Arjona A., Simarro L., Islinger F., et al. Two Creutzfeldt-Jakob disease agents reproduce prion protein-independent identities in cell cultures. Proc Natl Acad Sci U S A 101 (2004) 8768-8773
27. Klohn P.C., Stoltze L., Flechsig E., et al. A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions. Proc Natl Acad Sci U S A 100 (2003) 11666-11671
28. Baron G.S., Magalhaes A.C., Prado M.A., et al. Mouse-adapted scrapie infection of SN56 cells: Greater efficiency with microsome-associated versus purified PrP-res. J Virol 80 (2006) 2106-2117
29. Raymond G.J., Olsen E.A., Lee K.S., et al. Inhibition of protease-resistant prion protein formation in a transformed deer cell line infected with chronic wasting disease. J Virol 80 (2006) 596-604
30. Solassol J., Crozet C., and Lehmann S. Prion propagation in cultured cells. Br Med Bull 66 (2003) 87-97
31. Vorberg I., Raines A., Story B., et al. Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. J Infect Dis 189 (2004) 431-439
32. Butler D.A., Scott M.R., Bockman J.M., et al. Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J Virol 62 (1988) 1558-1564
33. Blochberger T.C., Cooper C., Peretz D., et al. Prion protein expression in Chinese hamster ovary cells using a glutamine synthetase selection and amplification system. Protein Eng 10 (1997) 1465-1473
34. Beranger F., Mange A., Solassol J., et al. Cell culture models of transmissible spongiform encephalopathies. Biochem Biophys Res Commun 289 (2001) 311-316
35. Nishida N., Katamine S., and Manuelidis L. Reciprocal interference between specific CJD and scrapie agents in neural cell cultures. Science 310 (2005) 493-496
36. Lehmann S., Daude N., and Harris D.A. A wild-type prion protein does not acquire properties of the scrapie isoform when coexpressed with a mutant prion protein in cultured cells. Brain Res Mol Brain Res 52 (1997) 139-145
37. Weissmann C. Birth of a prion: Spontaneous generation revisited. Cell 122 (2005) 165-168
38. C) is required for scrapie spread within the central nervous system. Proc Natl Acad Sci U S A 93 (1996) 13148-13151
39. Nishida N., Harris D.A., Vilette D., et al. Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J Virol 74 (2001) 320-325
40. Satoh J., and Yamamura T. Gene expression profile following stable expression of the cellular prion protein. Cell Mol Neurobiol 24 (2004) 793-814
41. Vilette D., Andreoletti O., Archer F., et al. Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein. Proc Natl Acad Sci U S A 98 (2001) 4055-4059
42. Laude H., Vilette D., Le Dur A., et al. New in vivo and ex vivo models for the experimental study of sheep scrapie: Development and perspectives. C R Biol 325 (2002) 49-57
43. Nunziante M., Gilch S., and Schatzl H.M. Prion diseases: From molecular biology to intervention strategies. Chembiochem 4 (2003) 1268-1284
44. Beringue V., Vilette D., Mallinson G., et al. PrPSc binding antibodies are potent inhibitors of prion replication in cell lines. J Biol Chem 279 (2004) 39671-39676
45. Perrier V., Solassol J., Crozet C., et al. Anti-PrP antibodies block PrPSc replication in prion-infected cell cultures by accelerating PrPC degradation. J Neurochem 89 (2004) 454-463
46. Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
47. Weber P., Giese A., Piening N., et al. Cell-free formation of misfolded prion protein with authentic prion infectivity. Proc Natl Acad Sci U S A 103 (2006) 15818-15823
48. Weber P., Giese A., Piening N., et al. Generation of genuine prion infectivity by serial PMCA. Vet Microbiol 123 (2007) 346-357
49. Supattapone S. Prion protein conversion in vitro. J Mol Med 82 (2004) 348-356
50. Kurt T.D., Perrott M.R., Wilusz C.J., et al. Efficient in vitro amplification of chronic wasting disease PrPres. J Virol 81 (2007) 9605-9608
51. Murayama Y., Yoshioka M., Yokoyama T., et al. Efficient in vitro amplification of a mouse-adapted scrapie prion protein. Neurosci Lett 413 (2007) 270-273
52. Murayama Y., Yoshioka M., Horii H., et al. Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation. Biochem Biophys Res Commun 348 (2006) 758-762
53. Bieschke J., Weber P., Sarafoff N., et al. Autocatalytic self-propagation of misfolded prion protein. Proc Natl Acad Sci U S A 101 (2004) 12207-12211
54. Nishina K.A., Deleault N.R., Mahal S.P., et al. The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry 45 (2006) 14129-14139
55. Deleault N.R., Harris B.T., Rees J.R., et al. From the cover: Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A 104 (2007) 9741-9746
56. Safar J., Wille H., Itri V., et al. Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 4 (1998) 1157-1165
57. Safar J.G., Scott M., Monaghan J., et al. Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nat Biotechnol 20 (2002) 1147-1150
58. Safar J.G., Geschwind M.D., Deering C., et al. Diagnosis of human prion disease. Proc Natl Acad Sci U S A 102 (2005) 3501-3506
59. Bellon A., Seyfert-Brandt W., Lang W., et al. Improved conformation-dependent immunoassay: Suitability for human prion detection with enhanced sensitivity. J Gen Virol 84 (2003) 1921-1925 (Pt 7)
60. Prusiner SB, Safar JG: Method of concentrating prion proteins in blood samples. US Patent #6166187 (2000).
61. Paramithiotis E., Pinard M., Lawton T., et al. A prion protein epitope selective for the pathologically misfolded conformation. Nat Med 9 (2003) 893-899
62. Caughey B. Probing for prions: Recognizing misfolded PrP. Nat Med 9 (2003) 819-820