Eight prion strains have PrP(Sc) molecules with different conformations

Nature Medicine

Volumn 4, Issue 10, 1998, Pages 1157-1165

  Safar, Jiri ^a   Wille, Holger ^a   Itri, Vincenza ^a   Groth, Darlene ^a   Serban, Hana ^a   Torchia, Marilyn ^a   Cohen, Fred E ^a   Prusiner, Stanley B ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

ARTICLE; IMMUNOASSAY; NONHUMAN; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRAIN DIFFERENCE; SYRIAN HAMSTER;

ANIMALS; BRAIN; BRAIN CHEMISTRY; CRICETINAE; IMMUNOASSAY; MESOCRICETUS; PEPTIDE FRAGMENTS; PHOSPHOTUNGSTIC ACID; PRECIPITATION; PRION DISEASES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PRPSC PROTEINS;

CRICETINAE; MESOCRICETUS AURATUS;

EID: 0031720905     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/2654     Document Type: Article

References (58)

1. Prusiner, S.B. Prion diseases and the BSE crisis. Science 278, 245-251 (1997).
2. Pattison, I.H. & Millson, G.C. Scrapie produced experimentally in goats with special reference to the clinical syndrome. J. Comp. Pathol. 71, 101-108 (1961).
3. Sigurdsson, B. Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics. Br. Vet. J. 110, 341-354 (1954).
4. Gajdusek, D.C. Unconventional viruses and the origin and disappearance of kuru. Science 197, 943-960 (1977).
5. Bruce, M.E. & Dickinson, A.G. Biological evidence that the scrapie agent has an independent genome. J. Gen. Virol. 68, 79-89 (1987).
6. Dickinson, A.G. & Outram, G.W. in Novel Infectious Agents and the Central Nervous System. Ciba Foundation Symposium 135 (eds. Bock, G. & Marsh, J.) 63-83 (John Wiley and Sons, Chichester, England, 1988).
7. Bruce, M.E. & Fraser, H. Scrapie strain variation and its implications. Curr. Top. Microbiol. Immunol. 172, 125-138 (1991).
8. Fraser, H. & Dickinson, A.G. The sequential development of the brain lesions of scrapie in three strains of mice. J. Comp. Pathol. 78, 301-311 (1968).
9. Bruce, M.E., McBride, P.A. & Farquhar, C.F. Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie. Neurosci. Lett. 102, 1-6 (1989).
10. Taraboulos, A. et al. Regional mapping of prion proteins in brains. Proc. Natl. Acad. Sci. USA 89, 7620-7624 (1992).
11. Scott, M.R. et al. Propagation of prion strains through specific conformers of the prion protein. J. Virol. 71, 9032-9044 (1997).
12. Prusiner, S.B. Molecular biology of prion diseases. Science 252, 1515-1522 (1991).
13. Cohen, F.E. et al. Structural clues to prion replication. Science 264, 530-531 (1994).
14. Bessen, R.A. & Marsh, R.F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68, 7859-7868 (1994).
15. Telling, G.C. et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274, 2079-2082 (1996).
16. Stahl, N. et al. Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002 (1993).
17. Serban, D., Taraboulos, A., DeArmond, S.J. & Prusiner, S.B. Rapid detection of Creutzfeldt-Jakob disease and scrapie prion proteins. Neurology 40, 110-117 (1990).
18. Peretz, D. et al. A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273, 614-622 (1997).
19. Mehlhorn, I. et al. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35, 5528-5537 (1996).
20. Kascsak, R.J. et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61, 3688-3693 (1987).
21. Hemmilä, I. & Harju, R. Time-resolved fluorometry. in Bioanalytical Applications of Labelling Technologies (eds. Hemmilä, I., Ståhlberg, T. & Mottram, P.) 113-119 (Wallac Oy, Turku, Finland, 1995).
22. Büeler, H. et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577-582 (1992).
23. Bessen, R.A. & Marsh, R.F. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J. Virol. 66, 2096-2101 (1992).
24. Prusiner, S.B., Scott, M.R., DeArmond, S.J. & Cohen, F.E. Prion protein biology. Cell 93, 337-348 (1998).
25. Safar, J., Roller, P.P., Gajdusek, D.C. & Gibbs, C.J., Jr. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268, 20276-20284 (1993).
26. Prusiner, S.B. et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349-358 (1983).
27. Prusiner, S.B. et al. Measurement of the scrapie agent using an incubation time interval assay. Ann. Neurol. 11, 353-358 (1982).
28. James, T.L. et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 10086-10091 (1997).
29. Pan, K.-M. et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90, 10962-10966 (1993).
30. Pergami, P., Jaffe, H. & Safar, J. Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form. Anal. Biochem. 236, 63-73 (1996).
31. Williamson, R.A. et al. Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein. Proc. Natl. Acad. Sci. USA 93, 7279-7282 (1996).
32. Huang, Z., Prusiner, S.B. & Cohen, F.E. Scrapie prions: a three-dimensional model of an infectious fragment. Folding & Design 1, 13-19 (1995).
33. Meyer, N. et al. Search for a putative scrapie genome in purified prion fractions reveals a paucity of nucleic acids. J. Gen. Virol. 72, 37-49 (1991).
34. Kellings, K., Prusiner, S.B. & Riesner, D. Nucleic acids in prion preparations: unspecific background or essential component? Phil. Trans. R. Soc. Lond. B 343, 425-430 (1994).
35. Kellings, K., Meyer, N., Mirenda, C., Prusiner, S.B. & Riesner, D. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE). J. Gen. Virol. 73, 1025-1029 (1992).
36. Prusiner, S.B. Prions. Les Prix Nobel (in the press).
37. Anfinsen, C.B. Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
38. Kaneko, K. et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94, 10069-10074 (1997).
39. Cohen, F.E. & Prusiner, S.B. Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67, 793-819 (1998).
40. Collinge, J., Sidle, K.C.L., Meads, J., Ironside, J. & Hill, A.F. Molecular analysis of prion strain variation and the aetiology of "new variant" CJD. Nature 383, 685-690 (1996).
41. Endo, T., Groth, D., Prusiner, S.B. & Kobata, A. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 28, 8380-8388 (1989).
42. Borchelt, D.R., Scott, M., Taraboulos, A., Stahl, N. & Prusiner, S.B. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110, 743-752 (1990).
43. Caughey, B. & Raymond, G.J. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-and phospholipase-sensitive. J. Biol. Chem. 266, 18217-18223 (1991).
44. Taraboulos, A. et al. Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 87, 8262-8266 (1990).
45. DeArmond, S.J. et al. Selective neuronal targeting in prion disease. Neuron 19, 1337-1348 (1997).
46. Will, R.G. et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921-925 (1996).
47. Brown, P. in Transmissible Subacute Spongiform Encephalopathies: Prion Diseases (eds. Court, L. & Dodet, B.) 447-450 (Elsevier, Paris, 1996).
48. Prusiner, S.B. et al. Further purification and characterization of scrapie prions. Biochemistry 21, 6942-6950 (1982).
49. Telling, G.C. et al. Transmission of Creutzfeldt-Jakob disease from humans to transgenic mice expressing chimeric human-mouse prion protein. Proc. Natl. Acad. Sci. USA 91, 9936-9940 (1994).
50. Scott, M.R. et al. Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc. Natl. Acad. Sci. USA 94, 14279-14284 (1997).
51. Marsh, R.F. & Kimberlin, R.H. Comparison of scrapie and transmissible mink encephalopathy in hamsters. II. Clinical signs, pathology and pathogenesis. J. Infect. Dis. 131, 104-110 (1975).
52. Kimberlin, R. & Walker, C. Characteristics of a short incubation model of scrapie in the golden hamster. J. Gen. Virol. 34, 295-304 (1977).
53. Gibbs, C.J., Jr., Safar, J., Sulima, M.P., Bacote, A.E. & San Martin, R.A. in Bovine Spongiform Encephalopathy: The BSE Dilemma (ed. Gibbs, C.J., Jr.) 84-91 (Springer, New York, 1996).
54. Marsh, R.F., Bessen, R.A., Lehmann, S. & Hartsough, G.R. Epidemiological and experimental studies on a new incident of transmissible mink encephalopathy. J. Gen. Virol. 72, 589-594 (1991).
55. Dickinson, A.G. in Slow Virus Diseases of Animals and Man (ed. Kimberlin, R.H.) 209-241 (North-Holland Publishing, Amsterdam, 1976).
56. Kimberlin, R.H., Cole, S. & Walker, C.A. Pathogenesis of scrapie is faster when infection is intraspinal instead of intracerebral. Microb. Pathog. 2, 405-415 (1987).
57. Turk, E., Teplow, D.B., Hood, L.E. & Prusiner, S.B. Purification and properties of the cellular and scrapie hamster prion proteins. Eur. J. Biochem. 176, 21-30 (1988).
58. Safar, J., Roller, P.P., Gajdusek, D.C. & Gibbs, C.J., Jr. Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33, 8375-8383 (1994).