The role of PrP in pathogenesis of experimental scrapie

Cold Spring Harbor Symposia on Quantitative Biology

Volumn 61, Issue , 1996, Pages 511-522

  Weissmann, C ^a   Fischer, M ^a   Raeber, A ^a   Bueler H ^a   Sailer, A ^a,b   Shmerling, D ^a   Rulicke T ^c   Brandner, S ^c   Aguzzi, A ^c  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^c UNIVERSITY HOSPITAL ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

BOVINE SPONGIFORM ENCEPHALOPATHY; CONFERENCE PAPER; CREUTZFELDT JAKOB DISEASE; KURU; NONHUMAN; PATHOGENESIS; PRION; PRIORITY JOURNAL; SCRAPIE; VIRUS TRANSMISSION; ARTICLE; BIOSYNTHESIS; GENE CONVERSION; GENE EXPRESSION; GENETIC LINKAGE; GENETIC STRAIN; GENETIC SUSCEPTIBILITY; HUMAN; HYPOTHESIS; INCUBATION TIME; KNOCKOUT MOUSE; LINKAGE ANALYSIS; MOLECULAR PATHOLOGY; MOUSE; NEUROPATHOLOGY; PROTEIN CONTENT; PROTEIN SYNTHESIS; REVERSE GENETICS; SCRAPIE AGENT; TRANSGENE;

ANIMALIA; BOVINAE; CRICETINAE; MESOCRICETUS AURATUS; MURINAE; SCRAPIE PRION;

EID: 0030439807     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.1996.061.01.051     Document Type: Conference Paper

References (77)

1. Aizawa, S.-I., F. Vonderviszt, R. Ishima, and K. Akasaka 1990. Termini of Salmonella flagellin are disordered and become organized upon polymerization into flagellar filament. J. Mol. Biol. 211: 673.
2. Alper, T., W.A. Cramp, D.A. Haig, and M.C. Clarke. 1967. Does the agent of scrapie replicate without nucleic acid? Nature 214: 764.
3. Asakura, S., G. Eguchi, and T. Iino. 1966. Salmonella flagella: In vitro reconstruction and over-all shapes of flagellar filaments. J. Mol. Biol. 16: 302.
4. Baker, H.F. and R.M. Ridley. 1992. The genetics and trans-missibility of human spongiform encephalopathy. Neurodegeneration 1: 3.
5. Basler, K., B. Oesch, M. Scott, D. Westaway, M. Wälchli, D.F. Groth, M.P. McKinley, S.B. Prusiner, and C. Weissmann. 1986. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46: 417.
6. Bendheim, P.E., H.R. Brown, R.D. Rudelli, L.J. Scala, N.L. Goller, G.Y. Wen, R.J. Kascsak, N.R. Cashman, and D.C. Bolton. 1992. Nearly ubiquitous tissue distribution of the scrapie agent precursor protein. Neurology 42: 149.
7. Bessen, R.A. and R.F. Marsh. 1992. Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J. Virol. 66: 2096.
8. Bessen, R.A., D.A. Kocisko, G.J. Raymond, S. Nandan, P.T. Lansbury, and B. Caughey. 1995. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375: 698.
9. Bolton, D.C., R.D. Rudelli, J.R. Currie, and P.E. Bendheim. 1991. Copurification of Sp33-37 and scrapie agent from hamster brain prior to detectable histopathology and clinical disease. J. Gen. Virol. 72: 2905.
10. Borchelt, D.R., A. Taraboulos, and S.B. Prusiner. 1992. Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267: 16188.
11. Borchelt, D.R., M. Scott, A. Taraboulos, N. Stahl, and S.B. Prusiner. 1990. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110: 743.
12. Brandner, S., S. Isenmann, A. Raeber, M. Fischer, A. Sailer, Y. Kobayashi, S. Marino, C. Weissmann, and A. Aguzzi. 1996. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 379: 339.
13. Brown, D.R., J. Herms, and H.A. Kretzschmar. 1994. Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. NeuroReport 5: 2057.
14. Brown, D.R., B. Schmidt, and H.A. Kretzschmar. 1996. Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380: 345.
15. Brown, P., L.G. Goldfarb, and D.C. Gajdusek. 1991. The new biology of spongiform encephalopathy: Infectious amyloidoses with a genetic twist. Lancet 337: 1019.
16. Bruce, M.E., H. Fraser, P.A. McBride, J.R. Scott, and A.G. Dickinson. 1992. The basis of strain variation in scrapie. In Prion diseases of humans and animals (ed. S.B. Prusiner et al.), p. 487. Ellis Horwood, New York.
17. Büeler, H., A. Aguzzi, A. Sailer, R.A. Greiner, P. Autenried, M. Aguet, and C. Weissmann. 1993. Mice devoid of PrP are resistant to scrapie. Cell 73: 1339.
18. Büeler, H., M. Fischer, Y. Lang, H. Bluethmann, H.P. Lipp, S.J. DeArmond, S.B. Prusiner, M. Aguet, and C. Weissmann. 1992. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356: 577.
19. Büeler, H., A. Raeber, A. Sailer, M. Fischer, A. Aguzzi, and C. Weissmann. 1994. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol. Med. 1: 19.
20. Campbell, K.H., J. McWhir, W.A. Ritchie, and I. Wilmut. 1996. Sheep cloned by nuclear transfer from a cultured cell line. Nature 380: 64.
21. Caughey, B. and G.J. Raymond. 1991. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-sensitive and phospholipase-sensitive. J. Biol. Chem. 266: 18217.
22. Caughey, B., G.J. Raymond, D. Ernst, and R.E. Race. 1991a. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 65: 6597.
23. Caughey, B.W., A. Dong, K.S. Bhat, D. Ernst, S.F. Hayes, and W.S. Caughey. 1991b. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30: 7672.
24. Chernoff, Y.O., S.L. Lindquist, B. Ono, S.G. Inge-Vechtomov, and S.W. Liebman. 1995. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268: 880.
25. Chesebro, B., R. Race, K. Wehrly, J. Nishio, M. Bloom, D. Lechner, S. Bergstrom, K. Robbins, L. Mayer, J.M. Keith, C. Garon, and A. Haase. 1985. Identification of scrapie prion protein-specific messenger RNA in scrapie-infected and uninfected brain. Nature 315: 331.
26. Cohen, F.E., K.M. Pan, Z. Huang, M. Baldwin, R.J. Fletterick, and S.B. Prusiner. 1994. Structural clues to prion replication (see comments). Science 264: 530.
27. Collinge, J., M.A. Whittington, K.C.L. Sidle, C.J. Smith, M.S. Palmer, A.R. Clarke, and J.G.R. Jefferys. 1994. Prion protein is necessary for normal synaptic function. Nature 370: 295.
28. Demaimay, R., K. Adjou, C. Lasmezas, F. Lazarini, K. Cherifi, M. Seman, J.P. Deslys, and D. Dormont. 1994. Pharmacological studies of a new derivative of amphotericin B, MS-8209, in mouse and hamster scrapie. J. Gen. Virol. 75: 2499.
29. Dickinson, A.G. and V.M. Meikle. 1969. A comparison of some biological characteristics of the mouse-passaged scrapie agents, 22A and ME7. Genet. Res. 13: 213.
30. Dickinson, A.G. and G.W. Outram. 1988. Genetic aspects of unconventional virus infections: the basis of the virino hypothesis. Ciba Found. Symp. 135: 63.
31. Fischer, M., T. Rülicke, A. Raeber, A. Sailer, M. Moser, B. Oesch, S. Brandner, A. Aguzzi, and C. Weissmann. 1996. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15: 1255.
32. Gabizon, R., M.P. McKinley, D. Groth, and S.B. Prusiner. 1988. Immunoaffinity purification and neutralization of scrapie prion infectivity. Proc. Natl. Acad. Sci. 85: 6617.
33. Gajdusek, D.C. 1988. Transmissible and non-transmissible amyloidoses: Autocatalytic post-translational conversion of host precursor proteins to β-pleated configurations. J. Neuroimmunology 20: 95.
34. Gerlai, R. 1996. Gene-targeting studies of mammalian behaviour: Is it the mutation or the background genotype? Trends Neurosci. 19: 177.
35. Goldfarb, L.G., P. Brown, L. Cervenakova, and D.C. Gajdusek. 1994. Genetic analysis of Creutzfeldt-Jakob disease and related disorders. Philos. Trans. R. Soc. Lond. B Biol. Sci. 343: 379.
36. Griffith, J.S. 1967. Self-replication and scrapie. Nature 215: 1043.
37. Hecker, R., A. Taraboulos, M. Scott, K.M. Pan, S.L. Yang, M. Torchia, K. Jendroska, S.J. DeArmond, and S.B. Prusiner. 1992. Replication of distinct scrapie prion isolates is region specific in brains of transgenic mice and hamsters. Genes Dev. 6: 1213.
38. Hofrichter, J., P.D. Ross, and W.A. Eaton. 1974. Kinetics and mechanism of deoxyhemoglobin S gelation: A new approach to understanding sickle cell disease. Proc. Natl. Acad. Sci. 71: 4864.
39. Hope, J., G. Multhaup, L.J. Reekie, R.H. Kimberlin, and K. Beyreuther. 1988. Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie. Eur. J. Biochem. 172: 271.
40. Hope, J., L.J. Morton, C.F. Farquhar, G. Multhaup, K. Beyreuther, and R.H. Kimberlin. 1986. The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO J. 5: 2591.
41. Hsiao, K.K., M. Scott, D. Foster, D.F. Groth, S.J. DeArmond, and S.B. Prusiner. 1990. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 250: 1587.
42. Hsiao, K.K., D. Groth, M. Scott, S.L. Yang, H. Serban, D. Rapp, D. Foster, M. Torchia, S.J. Dearmond, and S.B. Prusiner. 1994. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc. Natl. Acad. Sci. 91: 9126.
43. Jarrett, J.T. and P.J. Lansbury. 1993. Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73: 1055.
44. Jeffrey, M., C.M. Goodsir, M.E. Bruce, P.A. McBride, N. Fowler, and J.R. Scott. 1994. Murine scrapie-infected neurons in vivo release excess prion protein into the extracellular space. Neurosci. Lett. 174: 39.
45. Kellings, K., N. Meyer, C. Mirenda, S.B. Prusiner, and D. Riesner. 1992. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis. J. Gen. Virol. 73: 1025.
46. _. 1993. Analysis of nucleic acids in purified scrapie prion preparations. Arch. Virol. (suppl.) 7: 215.
47. Kocisco, D.A., S.A. Priola, G.J. Raymond, B. Chesebro, P.T. Lansbury, Jr., and B. Caughey. 1995. Species specificity in the cell-free conversion of prion protein to protease-resistant forms: A model for the scrapie species barrier. Proc. Natl. Acad. Sci. 92: 3923.
48. Kocisko, D.A., J.H. Come, S.A. Priola, B. Chesebro, G.J. Raymond, P.T. Lansbury, and B. Caughey. 1994. Cell-free formation of protease-resistant prion protein. Nature 370: 471.
49. Lledo, P.-M., P. Tremblay, S.J. DeArmond, S.B. Prusiner, and R.A. Nicoll. 1996. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc. Natl. Acad. Sci. 93: 2403.
50. Manson, J., P. McBride, and J. Hope. 1992. Expression of the PrP gene in the brain of sine congenic mice and its relationship to the development of scrapie. Neurodegeneration 1: 45.
51. Manson, J.C., A.R. Clarke, M.L. Hooper, L. Aitchison, I. McConnell, and J. Hope. 1994. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol. Neurobiol. 8: 121.
52. Masison, D.C. and R.B. Wickner. 1995. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270: 93.
53. McKinley, M.P., D C. Bokon, and S.B. Prusiner. 1983. A protease-resistant protein is a structural component of the scrapie prion. Cell 35: 57.
54. McKinley, M.P., R.K. Meyer, L. Kenaga, F. Rahbar, R. Cotter, A. Serban, and S.B. Prusiner. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65: 1340.
55. Oesch, B., D. Westaway, M. Wälchli, M.P. McKinley, S.B. Kent, R. Aebersold, R.A. Barry, P. Tempst, D.B. Teplow, L.E. Hood, S.B. Prusiner, and C. Weissmann. 1985. A cellular gene encodes scrapie PrP 27-30 protein. Cell 40: 735.
56. Pan, K.M., M. Baldwin, J. Nguyen, M. Gasset, A. Serban, D. Groth, I. Mehlhorn, Z. Huang, R.J. Fletterick, F.E. Cohen, and S.B. Prusiner. 1993. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. 90: 10962.
57. Prusiner, S.B. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216: 136.
58. _. 1989. Scrapie prions. Annu. Rev. Microbiol. 43: 345.
59. _. 1991. Molecular biology of prion diseases. Science 252: 1515.
60. _. 1993. Transgenetic investigations of prion diseases of humans and animals. Philos. Trans. R. Soc. Lond. B Biol. 339: 239.
61. Prusiner, S.B., D.C. Bolton, D.F. Groth, K.A. Bowman, S.P. Cochran, and M.P. McKinley. 1982. Further purification and characterization of scrapie prions. Biochemistry 21: 6942.
62. Prusiner, S.B., M. Scott, D. Foster, K.M. Pan, D. Groth, C. Mirenda, M. Torchia, S.L. Yang, D. Serban, G.A. Carlson, P.C. Hoppe, D. Westaway, and S.J. DeArmond. 1990. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63: 673.
63. Riek, R., S. Hornemann, G. Wider, M. Billeter, R. Glockshuber, and K. Wüthrich. 1996. NMR structure of the mouse prion protein domain PrP(121-231). Nature 382: 180.
64. Sailer, A., H. Büeler, M. Fischer, A. Aguzzi, and C. Weissmann. 1994. No propagation of prions in mice devoid of PrP. Cell 77: 967.
65. Sakaguchi, S., S. Katamine, N. Nishida, R. Moriuchi, K. Shigematsu, T. Sugimoto, A. Nakatani, Y. Kataoka, T. Houtani, S. Shirabe, H. Okada, S. Hasegawa, T. Miyamoto, and T. Noda. 1996. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 380: 528.
66. Sakaguchi, S., S. Katamine, K. Shigematsu, A. Nakatani, R. Moriuchi, N. Nishida, K. Kurokawa, R. Nakaoke, H. Sato, K. Hishage, J. Kuno, T. Noda, and T. Miyamoto. 1995. Accumulation of proteinase K-resistant prion protein (PrP) is restricted by the expression level of normal PrP in mice inoculated with a mouse-adapted strain of the Creutzfeldt-Jakob disease agent. J. Virol. 69: 7586.
67. Scott, M., D. Foster, C. Mirenda, D. Serban, F. Coufal, M. Wälchli, M. Torchia, D. Groth, G. Carlson, S.J. DeArmond, D. Westaway, and S.B. Prusiner. 1989. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59: 847.
68. Shyng, S.L., M.T. Huber, and D.A. Harris. 1993. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 268: 15922.
69. Stahl, N., D.R. Borchelt, K. Hsiao, and S.B. Prusiner. 1987. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51: 229.
70. Stahl, N., M.A. Baldwin, R. Hecker, K.M. Pan, A L. Burlingame, and S. Prusiner. 1992. Glycosylinositol phospholipid anchors of the scrapie and cellular prion proteins contain sialic acid. Biochemistry 31: 5043.
71. Stahl, N., M.A. Baldwin, D.B Teplow, L. Hood, B.W. Gibson, A.L. Burlingame, and S.B. Prusiner. 1993. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32: 1991.
72. Tobler, I., S.E. Gaus, T. Deboer, P. Achermann, M. Fischer, T. Rulicke, M. Moser, B. Oesch, P.A. McBride, and J.C. Manson. 1996. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 380: 639.
73. Weissmann, C. 1991. Spongiform encephalopathies. The prion's progress (news). Nature 349: 569.
74. Weissmann, C., H. Büeler, M. Fischer, and M. Aguet. 1993. Role of the PrP gene in transmissible spongiform encephalopathies. Intervirology 35: 164.
75. Whittington, M.A., K.C. Sidle, I. Gowland, J. Meads, A.F. Hill, M.S. Palmer, J.G. Jefferys, and J. Collinge. 1995. Rescue of neurophysiological phenotype seen in PrP null mice by transgene encoding human prion protein. Nat. Genet. 9: 197.
76. Wilesmith, J.W., J.B. Ryan, W.D. Hueston, and L.J. Hoinville. 1992. Bovine spongiform encephalopathy: Epidemiological features 1985 to 1990. Vet. Rec. 130: 90.
77. Will, R.G., J. W. Ironside, M. Zeidler, S.N. Cousens, K. Estibeiro, A. Alperovitch, S. Poser, M. Pocchiari, A. Hofman, and P.G. Smith. 1996. A new variant of Creutzfeld-Jakob disease in the UK. Lancet 347: 921.