Методы диагностики прионных заболеваний


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Эпидемия губкообразной энцефалопатии крупного рогатого скота в Великобритании и связанное с ней возникновение среди людей нового варианта болезни Крейтцфельда-Якоба (нвБКЯ), а также доказанные случаи заражения пациентов нвБКЯ путем переливания крови инициировали интенсивные исследования в области создания недорогого, быстрого и чувствительного метода ранней прижизненной диагностики прионных заболеваний. Это позволило бы начать своевременное лечение пациентов и предотвратить попадание контаминированных продуктов в пищевую цепь. Однако, несмотря на значительный прогресс, достигнутый в этом направлении, поставленная задача полностью не была решена. В настоящем обзоре представлены существующая на сегодняшний день информация о методах диагностики трансмиссивных губкообразных энцефалопатий, а также последние разработки в области ультрачувствительной детекции этих заболеваний, основанной на изменении конформации белка приона.

Список литературы

  1. Григорьев В. Б. Прионные болезни человека и животных // Вопр. вирусол. - 2004. - Т. 6. - С. 4-12.
  2. Григорьев В. Б. Прионные инфекции // Медицинская вирусология. Руководство / Под ред. Д. К. Львова. - М., 2008. - С. 240-245.
  3. Aksamit А. J., Preissner С. M., Homburger H. A. Quantitation of 14-3-3 and neuron - specific enolase proteins in CFS in Creutzfeldt-Jacob disease // Neurology. - 2001. - Vol. 57, № 4. - P. 728-730.
  4. Andreoletti O., Berthon P., Marc D. el al . Early accumulation of PrPsc in gut-associated lymphoid and nervous tissues of susceptible sheep from a Romanov flock with natural scrapie // J. Gen .Virol. - 2000. - Vol. 81.- P. 3115-3126.
  5. Angelo M., Bari D., Chianini F. et al. The bank vole (Myodes glareolus) as a sensitive bioassay for sheep scrapie // J. Gen. Virol. - 2008. - Vol. 89. - P. 2975-2985.
  6. Atarashi R., Moore R. A., Sim V. L. et al. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. // Nat. Met. - 2007. - Vol. 4, № 8. - P. 645-650.
  7. Barletta J. M., Edelman D. C., Highsmith W. E., Conslatine N. T. Detection of ultra-low level of pathologic prion protein in scrapie infected hamster brain homogenates using real-time immuno-PCR // J. Virol. Meth. - 2005. - Vol. 127, № 2. - P. 154-164.
  8. Baron T. Mouse models of prion disease transmission // Trends Mol. Med. - 2002. -Vol. 8, № 10. - P. 495-500.
  9. Benestad S. L., Sarradin P., Thu B. et al. Cases of scrapie with unusual features in Norway and designation of new type. Nor98 // Vet. Res. - 2003. - Vol. 153, № 7. - P. 202-208.
  10. Birkmann E., Schafer O., Weinmann N. et al. Detection of prion particles in samples of BSE and scrapie by fluorescence correlation spectroscopy without proteinase К digestion // Biol. Chem. - 2006. - Vol. 387. - P. 95-102.
  11. Brown P., Will R. G., Bradley R. et al. Bovine spongiform encephalopathy and variant Creutzfeldt-Jacob disease: background, evolution, and current concerns. // Emerging Infect. Dis. - 2001. - Vol. 7, № 1. - P. 6-16.
  12. Brown P. Blood infectivity. processing and screening test in transmissible spongiform encephalopathy // Vox Sang. - 2005. - Vol. 89, № 2. - P. 63-70.
  13. Carmona P., Monleon E., Monzon M. el al. In vivo detection of scrapie cases from blood by infrared spectroscopyf // J. Gen. Virol. - 2005. - Vol. 86. - P. 3425-3431.
  14. Casalone C., Zanusso G., Acutis P. et al. Identification of second bovine amyloidotic spongiform encephalopathies: molecular similarities with sporadic Creutzfeldt-Jacob disease // Proc. Natl. Acad. Sci. USA. - 2004. - Vol. 101, № 9. - P. 3065- 3070.
  15. Castilla J., Saa P., Hetz C., Solo C. In vitro generation of infectious scrapie prions // Cell. - 2005. - Vol. 121. - P. 195- 206.
  16. Castilla J., Saa P., Soto C. Detection of prion in blood // Nat. Med. - 2005. - Vol. 11, № 9. - P. 982-985.
  17. Cervenakova L, Brown P., Soukharev S. et al. Failture of immunocompetitive capillary electrophoresis assay to detect disease-specific prion protein in buffy coat from humans and chimpanzees with Creutzfeldt-Jacob disease // Electrophoresis. - 2003. - Vol. 24, № 5. - P. 853-859.
  18. Cervenakova L., Brown P. Advances in sreening test development for transmissible spongiform encephalopathies // Expert Rev. Anti. Infect. Ther. - 2004. - Vol. 2, № 6. - P. 873-880.
  19. Chang В., Cheng В., Yin S. et al. Test for detection of disease-associated prion aggregate in the blood infected but asymptomatic animals // Clin. Vaccine Immunol. - 2007. - Vol. 14, № 1. - P. 36-43.
  20. Colby D. W., Zhang Q., Wang S. et al. Prion detection by an amyloid seeding assay // Proc. Natl. Acad. Sci. USA. - 2007. - Vol. 104, № 52. - P. 20914-20919.
  21. Come J. H., Fraser P. E., Landsbury P. T. A kinetic model for amyloid formation in the prion diseases: importance of seeding // Proc. Natl. Acad. Sci. USA. - 1993. - Vol. 90, № 13. P. 5959-5963.
  22. Creminon C., Grassi J. Characterisation of anti-PrP antybodies and measurement of PrP using ELISA techniques // Methods and Tools in Biosciences and Medicine-Techniques in Prion Research / Eds. S. Lehmann, J. Grassi. Berlin. - 2004. - P. 117-131.
  23. Curin S. V., Bresjanac M., Popovic M. et al. Monoclonal antybody against a peptide of human prion protein discriminated between Creutzfeldt-Jacob disease and normal brain tissue // J. Biol. Chem. - 2004. - Vol. 279. - P. 3694-3698.
  24. DeArmond S. J., Prusiner S. B. Etiology and pathogenesis of prion diseases // Am. J. Pathol. - 1995. - Vol. 146, № 4. - P. 785-811.
  25. Deleault N. R., Harris В. Т., Rees J. R., Supattapone S. Formation of native prions from minimal components in vitro // Proc. Natl. Acad. Sci. USA. - 2007. - Vol. 104, № 23. - P. 9741- 9746.
  26. Clock В., Winter M., Rennhofer S. O. et al. Transcript level of eritroid differentiation-related factor, a candidate surrogate marker for transmissible spongiform encephalopathies diseases in blood, show a broad range of variation in healthy individuals // Trunsfusion. - 2003. - Vol. 43, № 12. - P. 1706-1710.
  27. Gonzaless- Romero D., Barria M. A., Leon P. et al Detection of infectious prion in urine // FEBS Lett. - 2008. - Vol. 582. - P. 3161-3166.
  28. Grassi J., Maillet S., Simon S., Morel N. Progress and limits of TSE diagnostic tools // Vet. Res. - 2008. - Vol. 39. - P. 1- 39.
  29. Green A. J., Jackman R., Marshal T. A., Thompson E. J. Increased S-100b in the cerebrospinal fluid of some cattle with bovine spongiform encephalopathy // Vet. Rec. - 1999. - Vol. 145, № 4. - P. 107-109.
  30. Grigoriev V. B., Escaig-Haye F., Streichenberger. N. et al. Submicroscopic immunodetection of PrP in the brain of a patient with of new-variant of Creutzfeld-Jakob disease // Neurosci. Lett. - 1999. - Vol. 263. - P. 59-63.
  31. Grosset A., Moskovotz K., Nelsen C. et al. Rapid presymptomatic detection of PrPsc via conformationally responsive palindromic PrP peptides // Peptides. - 2005. - Vol. 26, № 11. - P. 2193-2200.
  32. Hilton D. A., Ghani A. C., Conyers L. et al Accomulation of prion protein in tonsil and appendix: review of tissue samples // Brit. Med. J. - 2002. - Vol. 325, № 7365. - P. 633-634.
  33. Hilton D. A., Ghani A. C., Conyers L . et al. Prevalence of lymphoreticular prion protein accumulation in UK tissue samples // J. Pathol. - 2004. - Vol. 203, № 3. - P. 733-739.
  34. Hilton D. A. Pathogenesis and prevalence of variant Creutzfeldt-Jacob disease // J. Pathol. - 2006. - Vol. 208, № 2. - P. 134-141.
  35. Holada K., Vostal L. G. Different levels of prion protein (PrPc) expression on hamster, mouse and human blood cells // Br. J. Hematol. - 2000. - Vol. 110, № 2. - P. 472-480.
  36. Houston F., Foster J., Chong A. et al. Transmission of BSE by blood transfusion in sheep // Lancet. - 2000. - Vol. 356, № 9234. - P. 999-1000.
  37. Ingrosso L.,Vetugno V., Cardone F., Pocchiari M. Molecular diagnostics of transmissible spongiform encephalopathies // Trend Mol. Med. - 2002. - Vol. 8, № 6. - P. 273-280.
  38. 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. USA. - 2003. - Vol. 100, № 20. - P. 11666-11671.
  39. Korth C., Stierli P., Streit P. et al. Prion (PrPsc)-specific epitope defined by a monoclonal antibody // Nature. - 1997. - Vol. 390, № 6655. - P. 74-77.
  40. Korth C., Kaneko K., Groth D. et al. Abbreviated incubation times for human prions in mice expressing a chimeric mouse-human prion protein transgen // Proc. Natl. Acad. Sci. USA - 2003. - Vol. 100, № 8. - P. 4784-4789.
  41. Lane A., Stanley C. J., Dealler S., Wilson S. M. Polymeric ligands with specificity for aggregated prion protein // Clin. Chem. - 2003. - Vol. 49, № 10. - P. 1774-1775.
  42. Lehto M., Peery H. E., Cashman N. R. Current and future molecular diagnostics for prion diseases // Expert Rev. Mol. Diagn. - 2006. - Vol. 6, № 4. - P. 597-611.
  43. Maissen M., Roeckl C., Glatzel M. et al. Plasminogen binds to disease-associated prion protein of multiple species // Lancet. - 2001. - Vol. 357, № 9273. - P. 2026-2028.
  44. MacGregor I., Drummond Q., Turner M. et al. Distribution normal prion protein in blood // Transfus. Sci. - 2000. - Vol. 22, № 1-2. - P. 51.
  45. Miele G., Manson J., Clinton M. A novel eritroid-specific marker of transmissible spongiform encephalopathies // Nat. Med. - 2001. - Vol. 19, № 3. - P. 361-364.
  46. Missler U., Wiesmann M., Wittmann G. et al. Measurment of glial fibrillary acidic protein in human blood: analytical method and preliminary clinical results // Clin. Chem. - 1999. - Vol. 45, № 1. - P. 138-141.
  47. Moronchini G., Mangierieri M., Моrbin M. et al. Pathologic prion protein is specifically recognized in situ by a novel PrP conformational antybody // Neurobiol. Dis. - 2006. - Vol. 23. - P. 717-724.
  48. Moussa A., Coleman A. W., Bencsik A. et al. Use of streptomycin for precipitation and detection of proteinase К resistant prion protein (PrPsc) in biological samples // Chem. Commun. (Camb.). - 2006. - Vol. 9. - P. 973-975.
  49. Murayama Y., Yoshioka M., Horii H. Specific detection of prion antigenic determinants retained in bovine meat and bone meal by flow microbead immunoassay // J. Appl. Microbiol. - Vol. 101, № 2. - P. 369-376.
  50. Oesch В., Westaway D., Walchli M. et al A cellular gene encodes scrapie PrP 27-30 protein // Cell. - 1985. - Vol. 40, № 4. - P. 735-746.
  51. Otto M., Wiltfang J., Сереc L. et al. Tau protein and 14-3-3 protein in differential diagnosis of Creutzfeldt-Jacob disease // Neurology. - 2002. - Vol. 58, № 2. - P. 192-197.
  52. Pan Т., Chang В., Wong P. et al. An aggregation-specific enzyme-linked immunosorbent assay: detection of conformational differences between recombinant PrP protein dimmers and PrPsc aggregates // J. Virol. - 2005. - Vol. 79. № 19. - P. 12355-12364.
  53. Pan Т., Sethi J., Nelsen C. et al. Detection of misfolded prion protein in blood with conformationally sensitive peptides // Transfusion. - 2007. - Vol. 47, № 8. - P. 1418-1425.
  54. Panza G., Stohr J., Dumpitak C. et al. Spontaneous and BSE - prion-seeded amyloid formation of full length recombinant bovine prion protein // Biochem. Biophys. Res. Commun. 2008. - Vol. 373, № 4. - P. 493-497.
  55. Paramithiotis E., Pinard M., Lawton T. et al. A prion protein epitope selective for the pathlogically misfolded conformation // Nat. Med. - 2003. - Vol. 9, № 7. - P. 893-899.
  56. 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. -- Vol. 36, № 5-6. - P. 665-683.
  57. Pastrana M. A., Sajnani G., Onisko B. et al. Isolation and characterization of a proteinase K-sensitive PrPsc fraction // Biochemistry. - 2006. - Vol. 45. - P. 15710-15717.
  58. Peden A. H., Head M. W., Ritchie D. L. et al. Preclinical vCDJ after blood transfusion in PRNP codon 129 heterozygous patient // Lancet. - 2004. - Vol. 364, № 9433. - P. 527-529.
  59. Rhie A., Kirby L., Sayer N. et al. Characterisation of 2-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. // J. Biol. Chem. - 2003. - Vol. 278, № 41. - P. 39697-39705.
  60. Prusiner S. B. Novel proteinaceous infectiaous particles cause scrapie // Science. 1982. - Vol. 216, № 4542. - P. 136-144.
  61. Prusiner S. Prions // Proc. Natl. Acad. Sci. USA. - 1998. - Vol. 95. - P. 13363-13383.
  62. Rubenstein R., Gray P. C., Wehlburg C. M. et al. Detection and discrimination of PrPsc by multi-spectral ultraviolet fluorescence // Biochem. Biophys. Res. Commun. - 1998. - Vol. 246, № 1. - P. 100-106.
  63. Saborio G. P., Permanne В., Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding // Nature. - 2001. - Vol. 411, № 6839. - P. 810- 813.
  64. Safar J., Wille H., Itri V. et al. Eight prion strain have PrPsc molecules with different conformation // Nat. Med. - 1998. - Vol. 4, № 10. - P. 1157-1165.
  65. Sakudo A., Nakamura I., Ikuta K., Onodera T. Recent developments in prion disease research: Tools and in vitro cell culture models. // J. Vet. Med. Sci. - 2007. - Vol. 69, № 4. - P. 329-337.
  66. Sanchez-Valle R.. Saiz A., Graus F. Cerebrospinal fluid biomarkers in the diagnosis of Creutzfeldt-Jacob disease // Neurosci. Lett. - 2002. - Vol. 320. - P. 69-72.
  67. Sigurdson C. J., Nilsson K. P., Hornemann S. et al. Prion strain discrimination using luminescent conjugated polymers // Nature Meth. - 2007. - Vol. 4, № 12. - P. 1023-1030.
  68. Simдk J., Holada K., D'Agnillo F. et al Cellular prion protein is expressed on endothelial cells and is released during apoptosis on membrane microparticles found in human plasma // Trunsfusion. - 2002. - Vol. 42. - P. 334-342.
  69. Simon S., Nugier J., Morel N. et al. Rapid typing of transmissible spongiform encephalopathies strains with differential ELISA // Emerg. Infect. Dis. - 2008. - Vol. 14, № 4. - P. 608-616.
  70. Stack M. Western immunoblotting techniques for the study of transmissible spongiform encephalopathies // Methods and tools in Biosciences and Medicine-Techniques in prion research / Eds. S. Lehmann, J. Grassi. Berlin. - 2004. - P. 97-116.
  71. Tcherkasskaya O., Davidson E. A., Schmerr M. J., Orser C. S. Conformational biosensor for diagnosis of prion disease // Biotechn. Lett. - 2005. - Vol. 27. - P. 671-675.
  72. Trieschmann L., Navarrete S. A., Kaschig K. et al. Ultra-sensitive detection of prion protein fibrils by flow cytometry in blood from cattle affected with bovine spongiform encephalopathy // BMC Biotechnology. - 2005. - Vol. 5. - P. 26.
  73. Watts J. C., Westway D. The prion protein family: Diversity, rivalry, and dysfunction // Biochim. Biophys. Acta. - 2007. - Vol. 1772, № 6. - P. 654-672.
  74. Wroe S. J., Pal S., Siddique D. et al. Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jacob disease associated with blood transfusion; a case report, // Lancet. - 2006. - Vol. 368, № 9552. - P. 2061-2067.
  75. Yang W. C., Schmerr M. J., Jackman R. et al. Capillary electrophoresis-based noncompetitive immunoassay for the prion protein using fluorescin-labeled protein as a fluorescent probe // Anal. Chem. - 2005. - Vol. 77, № 14. - P. 4489-4494.
  76. Zou W. Q., Zheng J., Gry D. M. et al. Antybody to DNA detectes scrapie but not normal prion protein // Proc. Natl. Acad. Sci. USA. - 2004. - Vol. 101, № 5. - P. 1380-1385.

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