Identification of misfolded proteins in body fluids for the diagnosis of prion diseases

International Journal of Cell Biology

Volumn , Issue , 2013, Pages

  Properzi, Francesca ^a   Pocchiari, Maurizio ^a  

^a ISTITUTO SUPERIORE DI SANITÀ   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; PROTEIN 14 3 3;

BLOOD ANALYSIS; BODY FLUID; BRAIN HOMOGENATE; CEREBROSPINAL FLUID ANALYSIS; FLUORESCENCE; HUMAN; IMMUNOASSAY; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BLOOD LEVEL; PROTEIN CEREBROSPINAL FLUID LEVEL; PROTEIN EXPRESSION; PROTEIN MISFOLDING; PROTEIN STRUCTURE; PROTEIN URINE LEVEL; REVIEW; SALIVA ANALYSIS; SALIVA LEVEL; SENSITIVITY AND SPECIFICITY; ULTRASOUND; URINALYSIS; VARIANT CREUTZFELDT JAKOB DISEASE; WESTERN BLOTTING;

EID: 84884250109     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2013/839329     Document Type: Review

References (77)

1. Ward H. J. T., Everington D., Cousens S. N., Smith-Bathgate B., Leitch M., Cooper S., Heath C., Knight R. S. G., Smith P. G., Will R. G., Risk factors for variant Creutzfeldt-Jakob disease: a case-control study. Annals of Neurology 2006 59 1 111 120 2-s2.0-29944439816 10.1002/ana.20708
2. Wilesmith J. W., Wells G. A., Cranwell M. P., Ryan J. B., Bovine spongiform encephalopathy: epidemiological studies. Veterinary Record 1988 123 25 638 644 2-s2.0-0024290760
3. Brown P., Brandel J. P., Sato T., Nakamura Y., MacKenzie J., Will R. G., Ladogana A., Pocchiari M., Leschek E. W., Schonberger L. B., Iatrogenic Creutzfeldt-Jakob disease, final assessment. Emerging Infectious Diseases 2012 18 6 901 907 10.3201/eid1806.120116
4. Knight R., The risk of transmitting prion disease by blood or plasma products. Transfusion and Apheresis Science 2010 43 3 387 391 2-s2.0-78649477663 10.1016/j.transci.2010.09.003
5. Ladogana A., Puopolo M., Tiple D., Graziano S., Pocchiari M., Creutzfeldt-Jakob disease: the public health perception. European Journal of Neurodegenerative Diseases 2012 1 1 101 113
6. The National CJD Research and Surveillance Unit,. http://www.cjd.ed.ac. uk/documents/figs.pdf
7. Advisory Committee on Dangerous Pathogens,. Annual Report for 2012, ACDP/100/P7a, 2013, http://www.hse.gov.uk/aboutus/meetings/committees/acdp/ ar2012.pdf
8. Brown P., Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy. Vox Sanguinis 2005 89 2 63 70 2-s2.0-23844471279 10.1111/j.1423-0410.2005.00683.x
9. Campisi E., Cardone F., Graziano S., Galeno R., Pocchiari M., Role of proteomics in understanding prion infection. Expert Reviews in Proteomics 2012 9 6 649 666 10.1586/epr.12.58
10. Safar J., Wille H., Itri V., Groth D., Serban H., Torchia M., Cohen F. E., Prusiner S. B., Eight prion strains have PrP(Sc) molecules with different conformations. Nature Medicine 1998 4 10 1157 1165 2-s2.0-0031720905 10.1038/2654
11. Brown P., Cervenáková L., McShane L. M., Barber P., Rubenstein R., Drohan W. N., Further studies of blood infectivity in an experimental model of transmissible spongiform encephalopathy, with an explanation of why blood components do not transmit Creutzfeldt-Jakob disease in humans. Transfusion 1999 39 11-12 1169 1178 2-s2.0-0032757723 10.1046/j.1537-2995.1999.39111169.x
12. Piccardo P., Manson J. C., King D., Ghetti B., Barron R. M., Accumulation of prion protein in the brain that is not associated with transmissible disease. Proceedings of the National Academy of Sciences of the United States of America 2007 104 11 4712 4717 2-s2.0-34248396416 10.1073/pnas.0609241104
13. Lasmézas C. I., Deslys J., Robain O., Jaegly A., Beringue V., Peyrin J., Fournier J., Hauw J., Rossier J., Dormont D., Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 1997 275 5298 402 405 2-s2.0-0344030333 10.1126/science.275.5298.402
14. Gambetti P., Cali I., Notari S., Kong Q., Zou W., Surewicz W. K., Molecular biology and pathology of prion strains in sporadic human prion diseases. Acta Neuropathologica 2011 121 1 79 90 2-s2.0-78651240044 10.1007/s00401-010-0761-3
15. Saborio G. P., Permanne B., Soto C., Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001 411 6839 810 813 2-s2.0-0035859102 10.1038/35081095
16. Soto C., Anderes L., Suardi S., Cardone F., Castilla J., Frossard M., Peano S., Saa P., Limido L., Carbonatto M., Ironside J., Torres J., Pocchiari M., Tagliavini F., Pre-symptomatic detection of prions by cyclic amplification of protein misfolding. FEBS Letters 2005 579 3 638 642 2-s2.0-19944430413 10.1016/j.febslet.2004.12.035
17. Murayama Y., Yoshioka M., Horii H., Takata M., Yokoyama T., Sudo T., Sato K., Shinagawa M., Mohri S., Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation. Biochemical and Biophysical Research Communications 2006 348 2 758 762 2-s2.0-33746914310 10.1016/j.bbrc.2006.07.130
18. Kurt T. D., Perrott M. R., Wilusz C. J., Wilusz J., Supattapone S., Telling G. C., Zabel M. D., Hoover E. A., Efficient in vitro amplification of chronic wasting disease PrPRES. Journal of Virology 2007 81 17 9605 9608 2-s2.0-34548175394 10.1128/JVI.00635-07
19. Meyerett C., Michel B., Pulford B., Spraker T. R., Nichols T. A., Johnson T., Kurt T., Hoover E. A., Telling G. C., Zabel M. D., In vitro strain adaptation of CWD prions by serial protein misfolding cyclic amplification. Virology 2008 382 2 267 276 2-s2.0-56349149507 10.1016/j.virol.2008.09.023
20. Thorne L., Terry L. A., In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie. The Journal of General Virology 2008 89 12 3177 3184 2-s2.0-58149380989 10.1099/vir.0.2008/004226-0
21. Haley N. J., Seelig D. M., Zabel M. D., Telling G. C., Hoover E. A., Detection of CWD prions in urine and saliva of deer by transgenic mouse bioassay. PLoS ONE 2009 4 3 2-s2.0-62849123278 10.1371/journal.pone.0004848 e4848
22. Cosseddu G. M., Nonno R., Vaccari G., Bucalossi C., Fernandez-Borges N., Bari M. A., Castilla J., Agrimi U., Ultra-efficient PrPSc amplification highlights potentialities and pitfalls of PMCA technology. PLoS Pathogens 2011 7 11 2-s2.0-81755187224 10.1371/journal.ppat.1002370 e1002370
23. Haley N. J., Mathiason C. K., Carver S., Telling G. C., Zabel M. D., Hoover E. A., Sensitivity of protein misfolding cyclic amplification versus immunohistochemistry in ante-mortem detection of chronic wasting disease. The Journal of General Virology 2012 93 5 1141 1150 2-s2.0-84859872977 10.1099/vir.0.039073-0
24. Jones M., Peden A. H., Prowse C. V., Gröner A., Manson J. C., Turner M. L., Ironside J. W., MacGregor I. R., Head M. W., In vitro amplification and detection of variant Creutzfeldt-Jakob disease PrPSc. Journal of Pathology 2007 213 1 21 26 2-s2.0-34548394607 10.1002/path.2204
25. Jones M., Peden A. H., Wight D., Prowse C., MacGregor I., Manson J., Turner M., Ironside J. W., Head M. W., Effects of human PrPSc type and PRNP genotype in an in-vitro conversion assay. NeuroReport 2008 19 18 1783 1786 2-s2.0-57149144250 10.1097/WNR.0b013e328318edfa
26. Jones M., Peden A. H., Yull H., Wight D., Bishop M. T., Prowse C. V., Turner M. L., Ironside J. W., MacGregor I. R., Head M. W., Human platelets as a substrate source for the in vitro amplification of the abnormal prion protein (PrPSc) associated with variant Creutzfeldt-Jakob disease. Transfusion 2009 49 2 376 384 2-s2.0-58849146750 10.1111/j.1537-2995.2008.01954.x
27. Castilla J., Saá P., Soto C., Detection of prions in blood. Nature Medicine 2005 11 9 982 985 2-s2.0-24744446203 10.1038/nm1286
28. Saá P., Castilla J., Soto C., Presymptomatic detection of prions in blood. Science 2006 313 5783 92 94 2-s2.0-33745879463 10.1126/science.1129051
29. Murayama Y., Yoshioka M., Yokoyama T., Iwamaru Y., Imamura M., Masujin K., Yoshiba S., Mohri S., Efficient in vitro amplification of a mouse-adapted scrapie prion protein. Neuroscience Letters 2007 413 3 270 273 2-s2.0-33846809450 10.1016/j.neulet.2006.11.056
30. Gonzalez-Romero D., Barria M. A., Leon P., Morales R., Soto C., Detection of infectious prions in urine. FEBS Letters 2008 582 21-22 3161 3166 2-s2.0-51249083007 10.1016/j.febslet.2008.08.003
31. Chen B., Morales R., Barria M. A., Soto C., Estimating prion concentration in fluids and tissues by quantitative PMCA. Nature Methods 2010 7 7 519 520 2-s2.0-77954705622 10.1038/nmeth.1465
32. Atarashi R., Moore R. A., Sim V. L., Hughson A. G., Dorward D. W., Onwubiko H. A., Priola S. A., Caughey B., Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nature Methods 2007 4 8 645 650 2-s2.0-34547638271 10.1038/nmeth1066
33. Lacroux C., Vilette D., Fernández-Borges N., Litaise C., Lugan S., Morel N., Corbière F., Simon S., Simmons H., Costes P., Weisbecker J., Lantier I., Lantier F., Schelcher F., Grassi J., Castilla J., Andréoletti O., Prionemia and leukocyte-platelet-associated infectivity in sheep transmissible spongiform encephalopathy models. Journal of Virology 2012 86 4 2056 2066 2-s2.0-84857072621 10.1128/JVI.06532-11
34. Rubenstein R., Chang B., Gray P., Piltch M., Bulgin M. S., Sorensen-Melson S., Miller M. W., A novel method for preclinical detection of PrPSc in blood. The Journal of General Virology 2010 91 7 1883 1892 2-s2.0-77954146990 10.1099/vir.0.020164-0
35. Rubenstein R., Chang B., Gray P., Piltch M., Bulgin M. S., Sorensen-Melson S., Miller M. W., Prion disease detection, PMCA kinetics, and IgG in urine from sheep naturally/experimentally infected with scrapie and deer with preclinical/clinical chronic wasting disease. Journal of Virology 2011 85 17 9031 9038 2-s2.0-80052275775 10.1128/JVI.05111-11
36. Maddison B. C., Raes H. C., Baker C. A., Taema M., Bellworthy S. J., Thorne L., Terry L. A., Gough K. C., Prions are secreted into the oral cavity in sheep with preclinical scrapie. Journal of Infectious Diseases 2010 201 11 1672 1676 2-s2.0-77951904692 10.1086/652457
37. Murayama Y., Yoshioka M., Masujin K., Okada H., Iwamaru Y., Imamura M., Matsuura Y., Fukuda S., Onoe S., Yokoyama T., Mohri S., Sulfated dextrans enhance in vitro amplification of bovine spongiform encephalopathy PrPSc and enable ultrasensitive detection of bovine PrPSc. PLoS ONE 2010 5 10 2-s2.0-78049253978 10.1371/journal.pone.0013152 e13152
38. Nichols T. A., Spraker T. R., Gidlewski T., Powers J. G., Telling G. C., VerCauteren K. C., Zabel M. D., Detection of prion protein in the cerebrospinal fluid of elk (Cervus canadensis nelsoni) with chronic wasting disease using protein misfolding cyclic amplification. Journal of Veterinary Diagnostic Investigation 2012 24 4 746 749 10.1177/1040638712448060
39. Orrú C. D., Wilham J. M., Raymond L. D., Kuhn F., Schroeder B., Raeber A. J., Caughey B., Prion disease blood test using immunoprecipitation and improved quaking-induced conversion. mBio 2011 2 3 e00078 e00011 2-s2.0-79960163849 10.1128/mBio.00078-11
40. Wilham J. M., Orrú C. D., Bessen R. A., Atarashi R., Sano K., Race B., Meade-White K. D., Taubner L. M., Timmes A., Caughey B., Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathogens 2010 6 12 2-s2.0-78651249792 10.1371/journal.ppat.1001217 e1001217
41. Orrú C. D., Wilham J. M., Hughson A. G., Raymond L. D., McNally K. L., Bossers A., Ligios C., Caughey B., Human variant Creutzfeldt-Jakob disease and sheep scrapie PrPres detection using seeded conversion of recombinant prion protein. Protein Engineering, Design and Selection 2009 22 8 515 521 2-s2.0-70349211719 10.1093/protein/gzp031
42. Atarashi R., Satoh K., Sano K., Fuse T., Yamaguchi N., Ishibashi D., Matsubara T., Nakagaki T., Yamanaka H., Shirabe S., Yamada M., Mizusawa H., Kitamoto T., Klug G., McGlade A., Collins S. J., Nishida N., Ultrasensitive human prion detection in cerebrospinal fluid by real-time quaking-induced conversion. Nature Medicine 2011 17 2 175 178 2-s2.0-79751535822 10.1038/nm.2294
43. McGuire L. I., Peden A. H., Orrú C. D., Wilham J. M., Appleford N. E., Mallinson G., Andrews M., Head M. W., Caughey B., Will R. G., Knight R. S., Green A. J., Real time quaking-induced conversion analysis of cerebrospinal fluid in sporadic Creutzfeldt-Jakob disease. Annals of Neurology 2012 72 2 278 285 10.1002/ana.23589
44. Sano K., Satoh K., Atarashi R., Takashima H., Iwasaki Y., Yoshida M., Sanjo N., Murai H., Mizusawa H., Schmitz M., Zerr I., Kim Y. S., Nishida N., Early detection of abnormal prion protein in genetic human prion diseases now possible using real-time QUIC assay. PLoS ONE 2013 8 1 e54915
45. Lourenco P. C., Schmerr M. J., MacGregor I., Will R. G., Ironside J. W., Head M. W., Application of an immunocapillary electrophoresis assay to the detection of abnormal prion protein in brain, spleen and blood speciemens from patients with variant Creuzfeldt-Jakob disease. The Journal of General Virology 2006 87 10 3119 3124 2-s2.0-33749066765 10.1099/vir.0.81935-0
46. Bannach O., Birkmann E., Reinartz E., Jaeger K., Langeveld J. P. M., Rohwer R. G., Gregori L., Terry L. A., Willbold D., Riesner D., Detection of prion protein particles in blood plasma of scrapie infected sheep. PLoS ONE 2012 7 5 2-s2.0-84860456864 10.1371/journal.pone.0036620 e36620
47. Birkmann E., Henke F., Weinmann N., Dumpitak C., Groschup M., Funke A., Willbold D., Riesner D., Counting of single prion particles bound to a capture-antibody surface (surface-FIDA). Veterinary Microbiology 2007 123 4 294 304 2-s2.0-34547138925 10.1016/j.vetmic.2007.04.001
48. Terry L. A., Howells L., Hawthorn J., Edwards J. C., Moore S. J., Bellworthy S. J., Simmons H., Lizano S., Estey L., Leathers V., Everest S. J., Detection of PrPsc in blood from sheep infected with the scrapie and bovine spongiform encephalopathy agents. Journal of Virology 2009 83 23 12552 12558 2-s2.0-70450189368 10.1128/JVI.00311-09
49. Edgeworth J. A., Farmer M., Sicilia A., Tavares P., Beck J., Campbell T., Lowe J., Mead S., Rudge P., Collinge J., Jackson G. S., Detection of prion infection in variant Creutzfeldt-Jakob disease: a blood-based assay. The Lancet 2011 377 9764 487 493 2-s2.0-79551681376 10.1016/S0140-6736(10)62308-2
50. Amorfix Life Sciences, Press Release, Amorfix vCJD assay achieves 100% sensitivity and 100% specificity on 1,000 fresh samples from uk blood donors. 2008, http://www.amorfix.com/pdf-press/pr-2008/2008-10-17-AMF-vCJD-NIBSC-Fresh- Results.pdf
51. Guntz P., Walter C., Schosseler P., Morel P., Coste J., Cazenave J., Feasibility study of a screening assay that identifies the abnormal prion protein PrPTSE in plasma: Initial results with 20,000 samples. Transfusion 2010 50 5 989 995 2-s2.0-77951693561 10.1111/j.1537-2995.2009.02569.x
52. Amorfix Life Sciences, Press Release, Amorfix announces third quarter, 2010 results. 2010, http://www.amorfix.com/pdf-press/pr-2010/2009-02-08-amf-q3- results-2010.pdf
53. Amorfix Life Sciences, Press Release, Corporate update on vCJD test development. 2010, http://www.amorfix.com/pdf-press/pr-2010/2010-05-31- corporate-update-on-vCJD.pdf
54. Cooper J. K., Ladhani K., Minor P., Comparison of candidate vCJD in vitro diagnostic assays using identical sample sets. Vox Sanguinis 2012 102 2 100 109 2-s2.0-84856008271 10.1111/j.1423-0410.2011.01525.x
55. Choi E. M., Geschwind M. D., Deering C., Pomeroy K., Kuo A., Miller B. L., Safar J. G., Prusiner S. B., Prion proteins in subpopulations of white blood cells from patients with sporadic Creutzfeldt-Jakob disease. Laboratory Investigation 2009 89 6 624 635 2-s2.0-66549125845 10.1038/labinvest.2009.30
56. Pan T., Sethi J., Nelsen C., Rudolph A., Cervenakova L., Brown P., Orser C. S., Detection of misfolded prion protein in blood with conformationally sensitive peptides. Transfusion 2007 47 8 1418 1425 2-s2.0-34547100753 10.1111/j.1537-2995.2007.01284.x
57. An S. S. A., Lim K. T., Oh H. J., Lee B. S., Zukic E., Ju Y. R., Yokoyama T., Kim S. Y., Welker E., Differentiating blood samples from scrapie infected and non-infected hamsters by detecting disease-associated prion proteins using multimer detection system. Biochemical and Biophysical Research Communications 2010 392 4 505 509 2-s2.0-76749105206 10.1016/j.bbrc.2010.01.053
58. Haley N. J., Mathiason C. K., Carver S., Zabel M., Telling G. C., Hoover E. A., Detection of chronic wasting disease prions in salivary, urinary, and intestinal tissues of deer: potential mechanisms of prion shedding and transmission. Journal of Virology 2011 85 13 6309 6318 2-s2.0-80052042050
59. Castilla J., Saá P., Hetz C., Soto C., In vitro generation of infectious scrapie prions. Cell 2005 121 2 195 206 2-s2.0-17444413067 10.1016/j.cell.2005.02.011
60. Deleault N. R., Harris B. T., Rees J. R., Supattapone S., Formation of native prions from minimal components in vitro. Proceedings of the National Academy of Sciences of the United States of America 2007 104 23 9741 9746 2-s2.0-34547491652 10.1073/pnas.0702662104
61. Barria M. A., Mukherjee A., Gonzalez-Romero D., Morales R., Soto C., De novo generation of infectious prions in vitro produces a new disease phenotype. PLoS Pathogens 2009 5 5 2-s2.0-67249123069 10.1371/journal.ppat.1000421 e1000421
62. Atarashi R., Wilham J. M., Christensen L., Hughson A. G., Moore R. A., Johnson L. M., Onwubiko H. A., Priola S. A. S. A., Caughey B., Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nature Methods 2008 5 3 211 212 2-s2.0-40149090017 10.1038/nmeth0308-211
63. Colby D. W., Zhang Q., Wang S., Groth D., Legname G., Riesner D., Prusiner S. B., Prion detection by an amyloid seeding assay. Proceedings of the National Academy of Sciences of the United States of America 2007 104 52 20914 20919 2-s2.0-38049170554 10.1073/pnas.0710152105
64. Peden A. H., McGuire L. I., Appleford N. E. J., Mallinson G., Wilham J. M., Orrú C. D., Caughey B., Ironside J. W., Knight R. S., Will R. G., Green A. J. E., Head M. W., Sensitive and specific detection of sporadic Creutzfeldt-Jakob disease brain prion protein using real-time quaking-induced conversion. The Journal of General Virology 2012 93 2 438 449 2-s2.0-84855913114 10.1099/vir.0.033365-0
65. Schmerr M. J., Goodwin K. R., Cutlip R. C., Capillary electrophoresis of the scrapie prion protein from sheep brain. Journal of Chromatography A 1994 680 2 447 453 2-s2.0-0027945735 10.1016/0021-9673(94)85142-5
66. Schmerr M. J., Jenny A. L., Bulgin M. S., Miller J. M., Hamir A. N., Cutlip R. C., Goodwin K. R., 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. Journal of Chromatography A 1999 853 1-2 207 214 2-s2.0-0032768236 10.1016/S0021-9673(99) 00514-2
67. Cervenakova L., Brown P., Soukharev S., Yakovleva O., Diringer H., Saenko E. L., Drohan W. N., Failure of immunocompetitive capillary electrophoresis assay to detect disease-specific prion protein in buffy coat from humans and chimpanzees with Creutzfeldt-Jakob disease. Electrophoresis 2003 24 5 853 859 2-s2.0-0037350454 10.1002/elps.200390107
68. European Food Safety Authority (EFSA), Scientific report on the evaluation of rapid post mortem TSE tests intended for small ruminants. EFSA Journal 2005 49 1 16
69. Zobeley E., Flechsig E., Cozzio A., Enari M., Weissmann C., Infectivity of scrapie prions bound to a stainless steel surface. Molecular Medicine 1999 5 4 240 243 2-s2.0-0033066555
70. Edgeworth J. A., Jackson G. S., Clarke A. R., Weissmann C., Collinge J., Highly sensitive, quantitative cell-based assay for prions adsorbed to solid surfaces. Proceedings of the National Academy of Sciences of the United States of America 2009 106 9 3479 3483 2-s2.0-62549152288 10.1073/pnas.0813342106
71. Paramithiotis E., Pinard M., Lawton T., LaBoissiere S., Leathers V. L., Zou W., Estey L. A., Lamontagne J., Lehto M. T., Kondejewski L. H., Francoeur G. P., Papadopoulos M., Haghighat A., Spatz S. J., Head M., Will R., Ironside J., O'Rourke K., Tonelli Q., Ledebur H. C., Chakrabartty A., Cashman N. R., A prion protein epitope selective for the pathologically misfolded conformation. Nature Medicine 2003 9 7 893 899 2-s2.0-0038717543 10.1038/nm883
72. Safar J. G., Geschwind M. D., Deering C., Didorenko S., Sattavat M., Sanchez H., Serban A., Vey M., Baron H., Giles K., Miller B. L., DeArmond S. J., Prusiner S. B., Diagnosis of human prion disease. Proceedings of the National Academy of Sciences of the United States of America 2005 102 9 3501 3506 2-s2.0-20044383009 10.1073/pnas.0409651102
73. Bellon A., Seyfert-Brandt W., Lang W., Baron H., Gröner A., Vey M., Improved conformation-dependent immunoassay: suitability for human prion detection with enhanced sensitivity. The Journal of General Virology 2003 84 7 1921 1925 2-s2.0-0037813125 10.1099/vir.0.18996-0
74. Grosset A., Moskowitz K., Nelsen C., Pan T., Davidson E., Orser C. S., Rapid presymptomatic detection of PrPSc via conformationally responsive palindromic PrP peptides. Peptides 2005 26 11 2193 2200 2-s2.0-23844513036 10.1016/j.peptides.2005.03.006
75. Pan T., Chang B., Wong P., Li C., Li R., Kang S., Robinson J. D., Thompsett A. R., Tein P., Yin S., Barnard G., McConnell I., Brown D. R., Wisniewski T., Sy M. S., An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrPSc aggregates. Journal of Virology 2005 79 19 12355 12364 2-s2.0-25144445814 10.1128/JVI.79.19.12355-12364.2005
76. Tattum M. H., Jones S., Pal S., Khalili-Shirazi A., Collinge J., Jackson G. S., A highly sensitive immunoassay for the detection of prion-infected material in whole human blood without the use of proteinase K. Transfusion 2010 50 12 2619 2627 2-s2.0-78649989734 10.1111/j.1537-2995.2010.02731.x
77. National Institute for Biological Standards and Control (NIBSC), Flow chart for the evaluation of potential tests for CJD for access to rare samples (such as plasma) from vCJD patients. http://www.nibsc.org/pdf/CJDtest-draft1.pdf