Free access
Review
Issue
Vet. Res.
Volume 39, Number 4, July-August 2008
Prion diseases in animals
Number of page(s) 12
DOI http://dx.doi.org/10.1051/vetres:2008009
Published online 15 February 2008
How to cite this article Vet. Res. (2008) 39:33
References of Vet. Res. 39 (2008) 331-12
  1. Aksamit A.J. Jr., Preissner C.M., Homburger H.A., Quantitation of 14-3-3 and neuron-specific enolase proteins in CSF in Creutzfeldt-Jakob disease, Neurology (2001) 57:728–730.
  2. Andréoletti O., Berthon P., Marc D., Sarradin P., Grosclaude J., van Keulen L., et al., Early accumulation of PrP(Sc) in gut-associated lymphoid and nervous tissues of susceptible sheep from a Romanov flock with natural scrapie, J. Gen. Virol. (2000) 81:3115–3126.
  3. Arnold M.E., Ryan J.B., Konold T., Simmons M.M., Spencer Y.I., Wear A., et al., Estimating the temporal relationship between PrPSc detection and incubation period in experimental bovine spongiform encephalopathy of cattle, J. Gen. Virol. (2007) 88:3198–3208.
  4. Atarashi R., Moore R.A., Sim V.L., Hughson A.G., Dorward D.W., Onwubiko H.A., et al., Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein, Nat. Methods. (2007) 4:645–650.
  5. Beekes M., Otto M., Wiltfang J., Bahn E., Poser S., Baier M., Late increase of serum S100 beta protein levels in hamsters after oral or intraperitoneal infection with scrapie, J. Infect. Dis. (1999) 180:518–520.
  6. Bendheim P.E., Bolton D.C., A 54-kDa normal cellular protein may be the precursor of the scrapie agent protease-resistant protein, Proc. Natl. Acad. Sci. USA (1986) 83:2214–2218.
  7. Benestad S.L., Sarradin P., Thu B., Schonheit J., Tranulis M.A., Bratberg B., Cases of scrapie with unusual features in Norway and designation of a new type, Nor98, Vet. Rec. (2003) 153:202–208.
  8. Brown P., Blood infectivity, processing and screening tests in transmissible spongiform encephalopathy, Vox Sang. (2005) 89:63–70.
  9. Brown P., Cervenakova L., Diringer H., Blood infectivity and the prospects for a diagnostic screening test in Creutzfeldt-Jakob disease, J. Lab. Clin. Med. (2001) 137:5–13.
  10. Brown P., Will R.G., Bradley R., Asher D.M., Detwiler L., Bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease: background, evolution, and current concerns, Emerging Infect. Dis. (2001) 7:6–16.
  11. Bruce M.E., Will R.G., Ironside J.W., McConnell I., Drummond D., Suttie A., et al., Transmissions to mice indicate that “new variant” CJD is caused by the BSE agent, Nature (1997) 389:498–501.
  12. Calavas D., Ducrot C., Baron T., Morignat E., Vinard J.L., Biacabe A.G., et al., Prevalence of BSE in western France by screening cattle at risk: preliminary results of a pilot study, Vet. Rec. (2001) 149:55–56.
  13. Carmona P., Monleon E., Monzon M., Badiola J.J., Monreal J., Raman analysis of prion protein in blood cell membranes from naturally affected scrapie sheep, Chem. Biol. (2004) 11:759–764.
  14. Castilla J., Saa P., Hetz C., Soto C., In vitro generation of infectious scrapie prions, Cell (2005) 121:195–206.
  15. Castilla J., Saa P., Soto C., Detection of prions in blood, Nat. Med. (2005) 11:982–985.
  16. Chang B., Cheng X., Yin S., Pan T., Zhang H., Wong P., et al., Test for detection of disease-associated prion aggregate in the blood of infected but asymptomatic animals, Clin. Vaccine Immunol. (2007) 14:36–43.
  17. Curin S., V, Bresjanac M., Popovic M., Pretnar H.K., Galvani V., Rupreht R., et al., Monoclonal antibody against a peptide of human prion protein discriminates between Creutzfeldt-Jacob's disease-affected and normal brain tissue, J. Biol. Chem. (2004) 279:3694–3698.
  18. Deleault N.R., Harris B.T., Rees J.R., Supattapone S., From the cover: formation of native prions from minimal components in vitro, Proc. Natl. Acad. Sci. USA (2007) 104:9741–9746.
  19. Deleault N.R., Lucassen R.W., Supattapone S., RNA molecules stimulate prion protein conversion, Nature (2003) 425:717–720.
  20. Deslys J.P., Comoy E., Hawkins S., Simon S., Schimmel H., Wells G., et al., Screening slaughtered cattle for BSE, Nature (2001) 409:476–478.
  21. Eloit M., Adjou K., Coulpier M., Fontaine J.J., Hamel R., Lilin T., et al., BSE agent signatures in a goat, Vet. Rec. (2005) 156:523–524.
  22. Everest D.J., Waterhouse S., Kelly T., Velo-Rego E., Sauer M.J., Effectiveness of capillary electrophoresis fluoroimmunoassay of blood PrpSc for evaluation of scrapie pathogenesis in sheep, J. Vet. Diagn. Invest. (2007) 19:552–557.
  23. Fraser H., The pathology of a natural and experimental scrapie, Front. Biol. (1976) 44:267–305.
  24. Gavier-Widen D., Stack M.J., Baron T., Balachandran A., Simmons M., Diagnosis of transmissible spongiform encephalopathies in animals: a review, J. Vet. Diagn. Invest. (2005) 17:509–527.
  25. Glock B., Winter M., Rennhofer S.O., Brunholzl E., Troscher D., Reisacher R.B., Mayr W.R., Transcript level of erythroid differentiation-related factor, a candidate surrogate marker for transmissible spongiform encephalopathy diseases in blood, shows a broad range of variation in healthy individuals, Transfusion (2003) 43:1706–1710.
  26. Grassi J., Comoy E., Simon S., Creminon C., Frobert Y., Trapmann S., et al., Rapid test for the preclinical postmortem diagnosis of BSE in central nervous system tissue, Vet. Rec. (2001) 149:577–582.
  27. Grassi J., Creminon C., Frobert Y., Fretier P., Turbica I., Rezaei H., et al., Specific determination of the proteinase K-resistant form of the prion protein using two-site immunometric assays. Application to the post-mortem diagnosis of BSE, Arch. Virol. Suppl. (2000) 16:197–205.
  28. Green A.J., Cerebrospinal fluid brain-derived proteins in the diagnosis of Alzheimer's disease and Creutzfeldt-Jakob disease, Neuropathol. Appl. Neurobiol. (2002) 28:427–440.
  29. Green A.J., Jackman R., Marshall T.A., Thompson E.J., Increased S-100b in the cerebrospinal fluid of some cattle with bovine spongiform encephalopathy, Vet. Rec. (1999) 145:107–109.
  30. 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) 26:2193–2200.
  31. Hibler C.P., Wilson K.L., Spraker T.R., Miller M.W., Zink R.R., DeBuse L.L., et al., Field validation and assessment of an enzyme-linked immunosorbent assay for detecting chronic wasting disease in mule deer (Odocoileus hemionus), white-tailed deer (Odocoileus virginianus), and Rocky Mountain elk (Cervus elaphus nelsoni), J. Vet. Diagn. Invest. (2003) 15:311–319.
  32. Hilton D.A., Ghani A.C., Conyers L., Edwards P., McCardle L., Penney M., et al., Accumulation of prion protein in tonsil and appendix: review of tissue samples, BMJ (2002) 325:633–634.
  33. Hilton D.A., Ghani A.C., Conyers L., Edwards P., McCardle L., Ritchie D., et al., Prevalence of lymphoreticular prion protein accumulation in UK tissue samples, J. Pathol. (2004) 203:733–739.
  34. Jackman R., Everest D.J., Schmerr M.J., Khawaja M., Keep P., Docherty J., Evaluation of a preclinical blood test for scrapie in sheep using immunocapillary electrophoresis, J. AOAC Int. (2006) 89:720–727.
  35. Jackman R., Schmerr M.J., Analysis of the performance of antibody capture methods using fluorescent peptides with capillary zone electrophoresis with laser-induced fluorescence, Electrophoresis (2003) 24:892–896.
  36. Jones M., Peden A., Prowse C., Groner A., Manson J., Turner M., et al., In vitro amplification and detection of variant Creutzfeldt-Jakob disease PrP(Sc), J. Pathol. (2007) 213:21–26.
  37. Korth C., Stierli B., Streit P., Moser M., Schaller O., Fischer R., et al., Prion (PrPSc)-specific epitope defined by a monoclonal antibody, Nature (1997) 390:74–77.
  38. Kurt T.D., Perrott M.R., Wilusz C.J., Wilusz J., Supattapone S., Telling G.C., et al., Efficient in vitro amplification of chronic wasting disease PrPres, J. Virol. (2007) 81:9605–9608.
  39. Lasch P., Beekes M., Schmitt J., Naumann D., Detection of preclinical scrapie from serum by infrared spectroscopy and chemometrics, Anal. Bioanal. Chem. (2007) 387:1791–1800.
  40. Lasch P., Schmitt J., Beekes M., Udelhoven T., Eiden M., Fabian H., et al., Antemortem identification of bovine spongiform encephalopathy from serum using infrared spectroscopy, Anal. Chem. (2003) 75:6673–6678.
  41. Llewelyn C.A., Hewitt P.E., Knight R.S., Amar K., Cousens S., Mackenzie J., Will R.G., Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion, Lancet (2004) 363:417–421.
  42. 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 specimens from patients with variant Creutzfeldt-Jakob disease, J. Gen. Virol. (2006) 87:3119–3124.
  43. Miele G., Manson J., Clinton M., A novel erythroid-specific marker of transmissible spongiform encephalopathies, Nat. Med. (2001) 7:361–364.
  44. Missler U., Wiesmann M., Wittmann G., Magerkurth O., Hagenstrom H., Measurement of glial fibrillary acidic protein in human blood: analytical method and preliminary clinical results, Clin. Chem. (1999) 45:138–141.
  45. Moussa A., Coleman A.W., Bencsik A., Leclere E., Perret F., Martin A., Perron H., Use of streptomycin for precipitation and detection of proteinase K resistant prion protein (PrPsc) in biological samples, Chem. Commun. (Camb.) (2006) 9:973–975.
  46. Moynagh J., Schimmel H., Tests for BSE evaluated. Bovine spongiform encephalopathy, Nature (1999) 400:105.
  47. Murayama Y., Yoshioka M., Horii H., Takata M., Yokoyama T., Sudo T., et al., Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation, Biochem. Biophys. Res. Commun. (2006) 348:758–762.
  48. Nazor K.E., Kuhn F., Seward T., Green M., Zwald D., Purro M., et al., Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice, EMBO J. (2005) 24:2472–2480.
  49. Oesch B., Doherr M., Heim D., Fischer K., Egli S., Bolliger S., et al., Application of prionics Western blotting procedure to screen for BSE in cattle regularly slaughtered at Swiss abattoirs, Arch. Virol. Suppl. (2000) 16:189–195.
  50. Otto M., Wiltfang J., Differential diagnosis of neurodegenerative diseases with special emphasis on Creutzfeldt-Jakob disease, Restor. Neurol. Neurosci. (2003) 21:191–209.
  51. Otto M., Wiltfang J., Cepek L., Neumann M., Mollenhauer B., Steinacker P., et al., Tau protein and 14-3-3 protein in the differential diagnosis of Creutzfeldt-Jakob disease, Neurology (2002) 58:192–197.
  52. Pan T., Chang B., Wong P., Li C., Li R., Kang S.C., et al., An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimers and PrP(Sc) aggregates, J. Virol. (2005) 79:12355–12364.
  53. 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) 47:1418–1425.
  54. Paramithiotis E., Pinard M., Lawton T., LaBoissiere S., Leathers V.L., Zou W.Q., et al., A prion protein epitope selective for the pathologically misfolded conformation, Nat. Med. (2003) 9:893–899.
  55. Parveen I., Moorby J., Allison G., Jackman R., The use of non-prion biomarkers for the diagnosis of transmissible spongiform encephalopathies in the live animal, Vet. Res. (2005) 36:665–683.
  56. Peden A.H., Head M.W., Ritchie D.L., Bell J.E., Ironside J.W., Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient, Lancet (2004) 364:527–529.
  57. Prusiner S.B., Prions, Proc. Natl. Acad. Sci. USA (1998) 95:13363–13383.
  58. Prusiner S.B., Scott M.R., DeArmond S.J., Cohen F.E., Prion protein biology, Cell (1998) 93:337–348.
  59. Ruth L., The quest for new prion tests, Anal. Chem. (2003) 75:32A–36A.
  60. Saa P., Castilla J., Soto C., Presymptomatic detection of prions in blood, Science (2006) 313:92–94.
  61. Saa P., Castilla J., Soto C., Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification, J. Biol. Chem. (2006) 281:35245–35252.
  62. Saborio G.P., Permanne B., Soto C., Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding, Nature (2001) 411:810–813.
  63. Safar J., Wille H., Itri V., Groth D., Serban H., Torchia M., et al., Eight prion strains have PrP(Sc) molecules with different conformations, Nat. Med. (1998) 4:1157–1165.
  64. Safar J.G., Scott M., Monaghan J., Deering C., Didorenko S., Vergara J., et al., Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice, Nat. Biotechnol. (2002) 20:1147–1150.
  65. Schaller O., Fatzer R., Stack M., Clark J., Cooley W., Biffiger K., et al., Validation of a western immunoblotting procedure for bovine PrP(Sc) detection and its use as a rapid surveillance method for the diagnosis of bovine spongiform encephalopathy (BSE), Acta Neuropathol. (1999) 98:437–443.
  66. Schmerr M.J., Cutlip R.C., Jenny A., Capillary isoelectric focusing of the scrapie prion protein, J. Chromatogr. A (1998) 802:135–141.
  67. Schmerr M.J., Goodwin K.R., Cutlip R.C., Jenny A.L., Improvements in a competition assay to detect scrapie prion protein by capillary electrophoresis, J. Chromatogr. B, Biomed. Appl. (1996) 681:29–35.
  68. 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, J. Chromatogr. A (1999) 853:207–214.
  69. Schmitt J., Beekes M., Brauer A., Udelhoven T., Lasch P., Naumann D., Identification of scrapie infection from blood serum by Fourier transform infrared spectroscopy, Anal. Chem. (2002) 74:3865–3868.
  70. Schutz E., Urnovitz H.B., Iakoubov L., Schulz-Schaeffer W., Wemheuer W., Brenig B., Bov-tA short interspersed nucleotide element sequences in circulating nucleic acids from sera of cattle with bovine spongiform encephalopathy (BSE) and sera of cattle exposed to BSE, Clin. Diagn. Lab Immunol. (2005) 12:814–820.
  71. Simmons M.M, Spiropoulos J., Hawkins S.A.C., Bellworthy S.J., Tongue S.C., Approaches to investigating transmission of spongiform encephalopathies in domestic animals using BSE as an exemple, Vet. Res. (2008) 39:34.
  72. Soto C., Anderes L., Suardi S., Cardone F., Castilla J., Frossard M.J., et al., Pre-symptomatic detection of prions by cyclic amplification of protein misfolding, FEBS Lett. (2005) 579:638–642.
  73. Spraker T.R., O'Rourke K.I., Balachandran A., Zink R.R., Cummings B.A., Miller M.W., Powers B.E., Validation of monoclonal antibody F99/97.6.1 for immunohistochemical staining of brain and tonsil in mule deer (Odocoileus hemionus) with chronic wasting disease, J. Vet. Diagn. Invest. (2002) 14:3–7.
  74. Stack M., Jeffrey M., Gubbins S., Grimmer S., Gonzalez L., Martin S., et al., Monitoring for bovine spongiform encephalopathy in sheep in Great Britain, 1998–2004, J. Gen. Virol. (2006) 87:2099–2107.
  75. Stack M., Jeffrey M., Gubbins S., Grimmer S., Gonzalez L., Martin S., et al., Monitoring for bovine spongiform encephalopathy in sheep in Great Britain, 1998–2004, J. Gen. Virol. (2006) 87:2099–2107.
  76. Stack M.J., Chaplin M.J., Clark J., Differentiation of prion protein glycoforms from naturally occurring sheep scrapie, sheep-passaged scrapie strains (CH1641 and SSBP1), bovine spongiform encephalopathy (BSE) cases and Romney and Cheviot breed sheep experimentally inoculated with BSE using two monoclonal antibodies, Acta Neuropathol. (2002) 104:279–286.
  77. Thomzig A., Spassov S., Friedrich M., Naumann D., Beekes M., Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein, J. Biol. Chem. (2004) 279:33847–33854.
  78. Tyler J.W., Lakritz J., Weaver D., Johnson G., VanMetre D., Smith K., et al., The 14-3-3 cerebrospinal fluid immunoassay lacks utility in the diagnosis of clinical scrapie, J. Vet. Diagn. Invest. (2001) 13:537–539.
  79. van Keulen L.J., Schreuder B.E., Meloen R.H., Mooij-Harkes G., Vromans M.E., Langeveld J.P., Immunohistochemical detection of prion protein in lymphoid tissues of sheep with natural scrapie, J. Clin. Microbiol. (1996) 34:1228–1231.
  80. van Keulen L.J., Schreuder B.E., Meloen R.H., Poelen-van den B.M., Mooij-Harkes G., Vromans M.E., Langeveld J.P., Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapie, Vet. Pathol. (1995) 32:299–308.
  81. Wadsworth J.D., Joiner S., Hill A.F., Campbell T.A., Desbruslais M., Luthert P.J., Collinge J., Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay, Lancet (2001) 358:171–180.
  82. Weber P., Giese A., Piening N., Mitteregger G., Thomzig A., Beekes M., Kretzschmar H.A., Generation of genuine prion infectivity by serial PMCA, Vet. Microbiol. (2007) 123:346–357.
  83. Wells G.A., Wilesmith J.W., The neuropathology and epidemiology of bovine spongiform encephalopathy, Brain Pathol. (1995) 5:91–103.
  84. Wroe S.J., Pal S., Siddique D., Hyare H., Macfarlane R., Joiner S., et al., Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: a case report, Lancet (2006) 368:2061–2067.
  85. Xiang W., Windl O., Wunsch G., Dugas M., Kohlmann A., Dierkes N., et al., Identification of differentially expressed genes in scrapie-infected mouse brains by using global gene expression technology, J. Virol. (2004) 78:11051–11060.
  86. Yang W.C., Schmerr M.J., Jackman R., Bodemer W., Yeung E.S., Capillary electrophoresis-based noncompetitive immunoassay for the prion protein using fluorescein-labeled protein A as a fluorescent probe, Anal. Chem. (2005) 77:4489–4494.
  87. Zou W.Q., Zheng J., Gray D.M., Gambetti P., Chen S.G., Antibody to DNA detects scrapie but not normal prion protein, Proc. Natl. Acad. Sci. USA (2004) 101:1380–1385.