The nature of the scrapie agent: The virus theory

Proceedings of the Society for Experimental Biology and Medicine

Volumn 212, Issue 3, 1996, Pages 208-224

  Narang, Harash ^a  

^a Ken Bell International   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MARKER; COAT PROTEIN; PROTEINASE; SINGLE STRANDED DNA;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; BRAIN INFECTION; BRAIN SPONGIOSIS; CELL ULTRASTRUCTURE; CREUTZFELDT JAKOB DISEASE; HAMSTER; KURU; MOUSE; NONHUMAN; POINT MUTATION; PROTEIN MODIFICATION; SCRAPIE AGENT; SHEEP DISEASE; SHORT SURVEY; SLOW VIRUS DISEASE;

ANIMALIA; CRICETINAE; OVIS ARIES; SCRAPIE PRION;

EID: 0029999761     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: 10.3181/00379727-212-44009     Document Type: Short Survey

References (139)

1. Chandler RL. Encephalopathy in mice produced by inoculation with scrapie-brain material. Lancet 1:1378-1379, 1961.
2. Hadlow WJ. Scrapie and kuru. Lancet 2:289-290, 1959.
3. Narang HK. Origin and implications of bovine spongiform encephalopathy. Proc Soc Exp Biol Med 211:306-322, 1996.
4. Sigurdsson B. Rida, a chronic encephalitis of sheep. With general remarks on infections which develop slowly and some of their special characteristics. Brit Vet J 110:341-354, 1954.
5. Brown P, Goldfarb L, Gajdusek DC. The new biology of spongiform encephalopathy infectious amyloidoses with genetic twist. Lancet 337:1019-1022, 1991.
6. Gajdusek DC. Unconventional viruses causing subacute spongiform encephalopathies. In: Field BN, Melnick L, Chanock R, Shope RF, Roizman B, Eds. Human Viral Infections. New York: Raven, pp1519-1557, 1985.
7. Narang HK. Scrapie, an unconventional virus: The current views. Proc Soc Exp Biol Med 184:375-388, 1987.
8. Taylor DM. Deactivation of BSE and scrapie agents: Rendering and other UK studies. In: Bradley R, Marchant B, Eds. EEC Meeting 1993. Brussels, Proc Consultation BSE Scientific Vet Committee Commision European Communities. pp205-224, 1994.
9. Field EJ. Slow virus infection of the nervous system. In: Richter GW, Epstein MA, Eds. International Rev of Expt Path. New York: Academic Press, pp129-239, 1969.
10. Narang HK. The molecular pathogenesis of the tubulofilamentous particles: Evidence of a homologous single-stranded DNA in scrapie, Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. In: Bradley R, Marchant B, Eds. EEC Meeting 1993. Brussels, Proc Consultation BSE Scientific Vet Committee Commision European Communities. pp385-419, 1994.
11. Porter DD, Porter HG, Cox NA. Failure to demonstrate a humoral immune response to scrapie in mice. J Immunol 111: 1407-1410, 1973.
12. Gibson RA, Hunter GD. Nature of the scrapie agent. Nature 215:1041-1043, 1967.
13. Cho HJ. Requirement of a protein component for scrapie infectivity. Intervirology 14:213-216, 1980.
14. Merz PA, Somerville RA, Wisniewski HM, Iqbal K. Abnormal fibril from scrapie infected brains. Acta Neuropathol 54:63-74, 1981.
15. Merz PA, Rohwer RG, Kascsak R, Wisniewski HM, Somerville RA, Gibbs CJ Jr., Gajdusek DC. Infectious-specific particles from the unconventional slow virus diseases. Science 225:437-440, 1984.
16. Somerville RA. Ultrastructural links between scrapie and Alzheimers disease. Lancet 2:504-506, 1985.
17. Narang HK, Perry RH. Diagnosis of Creutzfeldt-Jakob disease by electron microscopy. Lancet 335:663-664, 1990.
18. Narang HK. Scrapie-associated tubulofilamentous particles in human Creutzfeldt-Jakob disease. Res Virol 143:387-395, 1992.
19. Diringer H, Gelderblom H, Hilmert H, Ozel M, Edelbluth D, Kimberlin RH. Scrapie infectivity, fibrils and low molecular weight protein. Nature 306:476-478, 1983.
20. Bode L, Pocchiari M, Gelderblom H, Diringer H. Characterisation of antisera against scrapie-associated fibrils (SAF) from affected hamster and cross-reactivity with SAF from scrapie affected mice and from patients with Creutzfeldt-Jakob disease. J Gen Vir 66:2471-2478, 1985.
21. Diringer H, Hilmert H, Simon D, Werner E, Ehlers B. Toward purification of the scrapie agent. Eur J Biochem 134:555-560, 1983.
22. Carp RI, Merz PA, Kascsak RJ, Merz G, Wisniewski HM. Biological properties of scrapie, an unconventional slow virus. Gen Virol 53:596-606, 1985.
23. Somerville RA, Merz PA, Carp RI. Partial copurification of scrapie-associated fibrils and scrapie infectivity. Intervirology 25:48-55, 1986.
24. Somerville RA, Carp RI. Altered scrapie infectivity estimates by titration and incubation period in the presence of detergents. J Gen Virology 64:2045-2050, 1983.
25. Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science 218:1309-1311, 1982.
26. Oesch B, Westaway D, Walchli M, McKinley MP, Kent SBH, Aebersold R, Barry RA, Tenpst P, Teplow DB, Hood LE, Prusiner SB, Weissmann C. A cellular gene encodes scrapie PrP 27-30 protein. Cell 40:735-746, 1985.
27. Prusiner SB, Bolton DC, Groth DF, Bowman KA, Cochran SP, McKinley MP. Further identification and characterisation of scrapie prions. Biochemistry 21:6942-6950, 1982.
28. Bendheim PE, Berry RA, DeArmond SJ, Stites DP, Prusiner SB. Antibodies to a scrapie prion protein. Nature 310:418-421, 1984.
29. DeArmond SJ, McKinley MP, Barry RA, Braunfeld MB, McColloch JR, Prusiner SB. Identification of prion amyloid filaments in scrapie-infected brains. Cell 41:221-235, 1985.
30. Diringer H, Rahn HC, Bode L. Antibodies to protein of scrapie-associated fibrils. Lancet 2:661-662, 1985.
31. Prusiner SB. Prions. Sci Am 251:50-59, 1984.
32. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144, 1982.
33. Basler K, Oesch B, Scott M, Westaway D, Walchli M, Groth DF, McKinley MP, Prusiner SB, Weissmann C. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46:417-428, 1986.
34. Prusiner SB, McKinley M, Bowman KA, Bolton DC, Bendheim PE, Groth DF, Glenner GG. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358, 1983.
35. Narang HK, Asher DM, Gajdusek DC. Tubulofilaments in negatively stained scrapie-infected brains: Relationship to scrapie-associated fibrils. Proc Natl Acad Sci USA 84:7730-7734, 1987.
36. Narang HK, Asher DM, Gajdusek DC. Evidence that DNA is present in abnormal tubulofilamentous structures found in scrapie. Proc Natl Acad Sci U S A 85:3575-3579, 1988.
37. Narang HK. Evidence of ssDNA in tubulofilamentous particles: Their relationship to scrapie-associated fibrils. Intervirology 32:185-192, 1991.
38. Narang HK. Scrapie-associated tubulofilamentous particles in scrapie hamsters. Intervirology 34:105-111, 1992.
39. Narang HK. Relationship of protease-resistant protein, scrapie-associated fibrils and tubulofilamentous particles to the agent of spongiform encephalopathies. Res Virol 143:381-386, 1992.
40. Roberts GW, Lofthouse R, Allsop D, Landon M, Kidd M, Prusiner SB, Crow JT. CNS amyloid proteins in neurodegenerative diseases. Neurology 38:1534-1540, 1988.
41. Kitamoto T, Tateishi J, Sato Y. Immunohistochemical verification of senile and kuru plaques in Creutzfeldt-Jakob disease and the allied disease. Ann Neurol 24:537-542, 1988.
42. Snow AD, Kisilevsky R, Willmer J, Prusiner SB, DeArmond SJ. Sulpated glycosaminoglycans in amyloid plaques of prion diseases. Acta Neuropathol 77:337-343, 1989.
43. Goldgaber D, Lerman MI, McBride OW, Saffiotti U, Gajdusek DC. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 235:877-880, 1987.
44. Lovett M, Goldgaber D, Ashley P, Cox DR, Gajdusek DC, Epstein J. The mouse homology of human amyloid β protein (AD-AP) gene is located on the distal end of mouse chromosome 16: Further extension of homology between human chromosome 21 and mouse chromosome 16. Biochem Biophys Res Commun 144:1069-1075, 1987.
45. Robakis NK, Sawh PR, Wolfe GC, Rubenstein R. Isolation of cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues. Proc Natl Acad Sci U S A 83:6377-6381, 1986.
46. Liao KJ, Lebo RV, Clawson GA, Smuckler EA. Human prion protein cDNA: Molecular cloning, chromosomal mapping and biological implications. Science 233:364-367, 1986.
47. Sparkes RS, Simon M, Cohn VH, Rournier REK. Assignment of the human and mouse prion protein gene to homologous chromosomes Proc Natl Acad Sci U S A 83:7358-7362, 1986.
48. Hay B, Barry RA, Lieberburg I, Prusiner SB, Lingappa VR. Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein. Mol Cell Biol 7:914-920, 1987.
49. Goldmann W, Hunter N, Martin T, Dawson M, Hope J. Different forms of the bovine PrP gene have five or six copies of a short g-c-rich element with the protein-coding exon. J Gen Virol 72:2411-2417, 1991.
50. Kretzschmar HA, Stowring LE, Westaway D, Stubblebine WH, Prusiner SB, DeArmond SJ. Molecular cloning of a human prion protein cDNA. DNA 5:315-324, 1986.
51. Blalock JE, Smith EM. Hydropathic anti-complementary of amino acids based on the genetic code. Biochem Biophys Res Commun 121:203-207, 1984.
52. Brown P. The molecular biology of the transmissible spongiform encephalopathies (scrapie, kuru and Creutzfeldt-Jakob disease). Discussions in Neurosciences 5:57-69, 1988.
53. Hsiao KK, Baker HF, Crow TJ, Poulter M, Owen F, Terwilliger JD, Westaway D, Ott J, Prusiner SB. Linkage of prion protein missense variant to Gerstmann-Straussler syndrome. Nature 338:342-345, 1989.
54. Owen F, Lofthouse R, Crow TJ, Baker HF, Poulter M, Collinge J, Risby D, Ridley RM, Hsiao K, Prusiner SB. Insertion in prion protein gene in familial Creutzfeldt-Jakob disease. Lancet i:51-52, 1989.
55. Goldfarb LG, Brown P, Cervenakova L, Gajdusek CD. Molecular genetic studies of Creutzfeldt-Jakob disease. Mol Neurobiol 8:89-97, 1994.
56. Brown P. The "Brave New world" of transmissible spongiform encephalopathy (Infectious cerebral amyloidosis) Mol Neurobiol 8:79-87, 1994.
57. Baker HF, Poulter M, Crow TJ, Frith CD, Lofthouse R, Ridley RM, Collinge J. Aminoacid polymorphism in human prion protein and age at death in inherited prion disease. Lancet 337: 1286, 1991.
58. Owen F, Poulter M, Shah T, Collinge J, Lofthouse R, Baker H, Ridley RM, McVey J, Crow TS. An in-frame insertion in the prion protein gene in familial Creutzfeldt-Jakob disease. Brain Res Mol Brain Res 7:273-276, 1990.
59. Prusiner SB. Molecular biology of prion diseases. Science 252:1515-1522, 1991.
60. Hsiao K, Meiner Z, Kahana E, Cass C, Kahana I, Avrahami D, Scarlato G, Abramsky O, Prusiner SB, Gabizon R. Mutation of the prion protein in Libyan Jews with Creutzfeldt-Jakob disease. N Engl J Med 324:1091-1097, 1991.
61. Brown P, Goldfarb LG, McCombie WR, Nieto A, Squillactoe D, Sheremata W, Little BW, Godec MS, Gibbs CJ Jr., Gajdusek DC. A typical Creutzfeldt-Jakob disease in an American family with an insert mutation in the PRNP amyloid precursor gene. Neurology 42:422-427, 1992.
62. Medori R, Montagna P, Tritschler HJ, LebBanc A, Cortelli P, Tinuper P, Lugaresi E, Gambetti P. Fatal familial insomnia: A second kindred with mutation of prion protein gene at codon 178. Neurology 42:669-670, 1992.
63. Chesebro B, Race R, Wehrly K, Nishio J, Bloom M, Lechner D, Bergstrom S, Robbins K, Maye L, Keith JM, Garon C, Haase A. Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brains Nature 315: 331-333, 1985.
64. Gajdusek DC. Subacute spongiform encephalopathies: Transmissible cerebral amyloidoses caused by unconventional viruses. In: Field BN, Knipe DM, et al., Eds. Virology (2nd ed.) New York: Raven Press, pp2289-2324, 1990.
65. Hsiao KK, Scott M, Foster D, Growth DF, DeArmond SJ, Prusiner SB. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 250:1587-1590, 1990.
66. Chesebro B. PrP and the scrapie agent. Nature 356:560, 1992.
67. Scott M, Foster D, Mirenda C, Serban D, Coufal F, Wälchli M, Torchia M, Groth D, Carlson G, DeArmond SJ, Westaway D, Prusiner SB. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59:847-857, 1989.
68. Epstein CJ, Foster DB, DeArmond SJ, Prusiner SB. Acceleration of scrapie in Trisomy 16-Diploid aggregation Chimeras. Ann Neurol 29:95-97, 1991.
69. Büeler H, Fischer M, Lang Y, Bluethmann H, Lipp HP, DeArmond SJ, Prusiner SB, Aguet M, Weissmann C. Normal development and behaviour of mice lacking the neuronal cellsurface PrP protein. Nature 356:577-582, 1992.
70. Büeler H, Aguzzi A, Sailer A, Greiner R-A, Autenried P, Aguet M, Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell 73:1339-1347, 1993.
71. Narang HK. Bovine spongiform encephalopathy (BSE). Report and Proc The Agri committee. Memorandum HMSO, House of Commons. Appendix 22, pp237-240, 1990.
72. Scott M, Groth D, Foster D, Torchia M, Yang S-L, DeArmond SJ, Prusiner SB. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP gene. Cell 73:979-988, 1993.
73. Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen F, DeArmond J, Prusiner SB. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79-90, 1995.
74. Narang HK. Evidence that Homologous ssDNA is present in scrapie, Creutzfeldt-Jakob disease, and bovine spongiform encephalopathy. Slow virus of the central nervous system. Ann N Y Acad Sci 724:314-326, 1994.
75. Carp RI, Ye X, Kascsak RJ, Rubenstein R. The nature of the scrapie agent: Biological characteristics of scrapie in different scrapie strain-host combinations. Ann N Y Acad Sci 724:221-234, 1994.
76. Bolton DC, McKinley MP, Prusiner SB. Molecular characteristics of the major scrapie prion protein. Biochem 23:5898-5905, 1984.
77. Oesch B, Groth DF, Prusiner SB, Weissmann C. Search for a nucleic acid: A progress report. In: Bock G, Marsh J, Eds. Novel Infectious Agents and the Central Nervous System, Ciba Foundation Symposium. John Wiley, Vol 135:pp209-223, 1988.
78. Meyer N, Rosenbaum V, Schmidt B, Gilles K, Mirenda C, Groth D, Prusiner SB, Riesner D. Search for a putative scrapie genome in purified prion fractions revealed a paucity of nucleic acids. J Gen Virol 72:37-49, 1991.
79. Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis. J Gen Virol 73:1025-1029, 1992.
80. Carlson GA, Kingsbury DT, Goodman PA, Coleman S, Marshall ST, DeArmond SJ, Westaway D, Prusiner SB. Linkage of prion protein and scrapie incubation time genes. Cell 46:503-511, 1986.
81. Hunter N, Hope J, McConnell I, Dickinson AG. Linkage of the scrapie-associated fibril protein (PrP) gene and Sine using congenie mice and restriction fragment length polymorphism analysis. J Gen Virol 68:2711-2716, 1987.
82. Kimberlin RH. Scrapie agent: Prions or virinos? Nature 297: 107-108, 1982.
83. Hunter N, Goldmann W, Benson G, Foster JD, Hope J. PrP genotype studies. In: Bradley R, Marchant B, Eds. EEC Meeting 1993. Brussels, Proc Consultation BSE Scientific Vet Committee Commision European Communities. pp125-139, 1994.
84. Laplanche JL, Chatelain J, Westaway D, Thomas S, Dussaucy M, Brugere-Picoux J, Launay JM. PrP polymorphisms associated with natural scrapie discovered by denaturing gradient gel electrophoresis. Genomics 15:30-37, 1993.
85. Ryan AM, Womack JE. Somatic cell mapping of the bovine prion protein gene and restriction fragment length polymorphism studies in cattle and sheep. Anim Genet 24:23-26, 1993.
86. Dickinson AG, Fraser H. Genetic control of the concentration of ME7 scrapie agent in mouse spleen. J Comp Pathol 79:363-366, 1969.
87. Fraser H. Neuropathology of scrapie, the precision of the lesions and their diversity. In: Prusiner SB, Hadlow WJ, Eds. Slow Transmissible Disease of the Nervous System. New York: Academic Press, Vol 1:pp387-406, 1979.
88. Kim YS, Carp RI, Callahan SM, Wisniewski HM. Clinical course of three strains in mice injected stereotaxically in different brain regions. J Gen Virol 68:695-702, 1987.
89. Dickinson AG, Meikle VH, Fraser H. Identification of a gene which controls the incubation period of some strains of scrapie in mice. J Comp Pathol 78:293-299, 1968.
90. Akowitz A, Sklaviadis T, Manuelidis EE, Manuelidis L. Nuclease-resistant polyadenylated RNAs of significant size are detected by PCR in highly purified Creutzfeldt-Jakob disease preparations. Microb Pathog 9:33-45, 1990.
91. Rohwer RG. Scrapie infectious agent is virus-like in size and susceptibility to inactivation. Nature 308:658-662, 1984.
92. Latarjet R. Inactivation of the agents of scrapie, Creutzfeldt-Jakob disease, and kuru by radiations. In: Prusiner SB, Hadlow WJ, Eds. Slow Transmissible Disease of the Nervous System. New York: Academic Press, Vo1 2:pp387-407, 1979.
93. Sambrook J, Fritsch EF, Maniatis T. Molecular Cloning. A Laboratory Manual (2nd ed). New York: Cold Spring Harbor Laboratory Press, 1989.
94. Shibata D, Martin WJ, Arnheim N. Analysis of DNA sequences in forty-year-old paraffin-embedded thin tissue sections: A bridge between molecular biology and classical histology. Cancer Res 48:4564-1566, 1988.
95. Shin YA, Eichhorn GL. Interaction of metal ions with polynucleotides and related compounds. XI. The reversible unwinding and rewinding of Deoxyribonucleic acid by zinc (II) ions through temperature manipulation. Biochemistry 7:1026-1032, 1968.
96. Butzow JJ, Eichhorn GL. Different susceptibility of DNA and RNA to cleavage by metal ions. Nature 254:358-359, 1975.
97. Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis. J Gen Virol 73:1025-1029, 1992.
98. Hanson CV, Riggs JL, Lennette EH. Photochemical inactivation of DNA and RNA viruses by psoralen derivatives. J Gen Virol 40:345-358, 1978.
99. Schuster H, Wittmann RG. The inactivating and mutagenic action of hydroxylamine on tobacco mosaic virus ribonucleic acid. Virology 19:421-430, 1963.
100. Tessman I. Mutagenic treatment of double and single-stranded DNA phage T4 and S13 with hydroxylamine. Virology 35:330-333, 1968.
101. McKinley MP, Masinrz FR, Prusiner SB. Reversible chemical modification of scrapie agent. Science 214:1259-1260, 1981.
102. Pattison IH. The relative susceptibility of sheep, goat and mice to two types of the goat scrapie agent. Res Vet Sci 7:207-212, 1966.
103. Dickinson AG, Fraser H. An assessment of the genetics of scrapie in sheep and mice. In: Prusiner SB, Hadlow WJ, Eds. Slow Transmissible Disease of the Nervous System. New York: Academic Press, Vol 1:pp367-385, 1979.
104. Bruce ME, Dickinson AG. Biological evidence that scrapie agent has an independent genome. J Gen Virol 68:79-89, 1987.
105. Kimberlin RH, Cole S, Walker CA. Temporary and permanent modifications to a single strain of mouse scrapie on transmission to rats and hamsters. J Gen Virol 68:1875-1881, 1987.
106. Gibbs CJ Jr., Gajdusek DC, Amyx H. Strain variation in the viruses of Creutzfeldt-Jakob disease and kuru. In: Prusiner SB, Hadlow WJ, Eds. Slow Transmissible Disease of the Nervous System. New York: Academic Press, Vol 1:pp87-110, 1979.
107. Weissmann C. Unified theory of prion propagation. Nature 352:679-683, 1991.
108. Sklaviadis TK, Manuelidis L, Manuelidis EE. Physical properties of the Creutzfeldt-Jakob disease agent. J Virol 63:1212-1222, 1989.
109. Meyer RK, McKinley MP, Bowman KA, Braunfeld M, Berry RA, Prusiner SB. Separation and properties of cellular and scrapie prion proteins. Proc Natl Acad Sci USA 83:2310-2314, 1986.
110. Czub M, Braig HR, Blode H, Diringer H. The major protein of SAF is absent from spleen and thus not an essential part of the scrapie agent. Arch Virol 91:383-386, 1986.
111. Xi YG, Ingrosso L, Ladogana A, Masullo C, Pocchiari M. Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation. Nature 356:598-601, 1992.
112. Hsiao KK, Scott M, Foster D, Groth DF, DeArmond SJ, Prusiner SB. Spontaneous neurodegeneration in transgenic mice with mutation. Science 250: 1587-1590, 1990.
113. Narang HK. Ruthenium red and lanthanum nitrate - A possible trancer and negative stain for scrapie particles. Acta Neuropathol 29:37-43, 1974.
114. Narang HK, Shenton B, Giorgi PP, Field EJ. Scrapie agent and neurons. Nature 24:106-107, 1972.
115. Narang HK. An electron microscopic study of natural scrapie sheep brain: further observations on virus-like particles and paramyxovirus like tubules. Acta Neuropathol 28:317-329, 1974.
116. Narang HK, Asher DM, Pomeroy KL, Gajdusek DC. Abnormal tubulovesicular particles in brains of hamsters with scrapie. Proc Soc Exp Biol Med 184:504-509, 1987.
117. Liberski PP, Yanagihara R, Gibbs CJ Jr., Gajdusek DC. Tubulovesicular structures in experimental spongiform encephalopathy Creutzfeldt-Jakob disease and scrapie. Intervirology 29:115-119, 1988.
118. Liberski PP, Yanagihara R, Gibbs CJ Jr., Gajdusek DC. Appearance of tubulovesicular structures in experimental Creutzfeldt-Jakob disease and scrapie proceeds the onset of clinical disease. Acta Neuropathol 79:349-354, 1990.
119. Liberski PP. Ultrastructural neuropathological features of bovine spongiform encephalopathy. J Am Vet Med Assoc 196: 1682, 1990.
120. Gibson PH, Doughty LA. An electron microscopic study of inclusion bodies in synaptic terminals of scrapie-infected animals. Acta Neuropathol 77:420-425, 1989.
121. Baringer JR, Prusiner SB, Wong JS. Scrapie associated particles in post-synaptic processes: Further ultrastructural studies. J Neuropathol Exp Neurol 40:281-288, 1981.
122. Narang HK. A chronological study of experimental scrapie in mice. Virus Res 9:293-306, 1988.
123. Come JH, Fraser PE, Lansbury PT. A kinetic model for amyloid formation in the prion diseases: Importance of seeding. Proc Natl Acad Sci U S A 90:5959-5963, 1993.
124. Narang HK, Millar NS, Asher DM, Gajdusek DC. Increased multimeric mitochondrial DNA in the brain of scrapie-infected hamsters. Intervirology 32:316-324, 1991.
125. Aiken JM, Williamson JL, Borchardt M, Marsh RF. Presence of mitochondrial D-loop DNA in scrape-infected brain preparations enriched for the prion protein. J Virol 64:1684-1694, 1990.
126. Hudson B, Vinograd J. Catenated circular DNA molecules in HeLa cell mitochondria. Nature 216:647-652, 1967.
127. Nass MMK. Reversible generation of circular dimmer and higher multiple forms of mitochondrial DNA. Nature 223: 1124-1129, 1969.
128. Smith CA, Vinograd J. Complex mitochondrial DNA in human tumors. Cancer Res 33:1065-1070, 1973.
129. Narang HK. Detection of single-stranded DNA in scrapie-infected brain by electron microscopy. J Mol Biol 216:469-473, 1990.
130. Narang HK. Molecular cloning of single-stranded DNA purified from scrapie-infected hamster brain. Res Virol 144:375-387, 1993.
131. Wietgrefe S, Zupancic M, Haase A, Chesebro B, Race R, Frey W, Rustan T, Freedman RL. Cloning of a gene whose expression is increased in scrapie and in senile plaques in human brains. Science 230:1177-1181, 1985.
132. Diedrich J, Wietgrefe S, Zupancic M, Staskus K, Retzel E, Haase AT, Race R. The molecular pathogenesis of astrogliosis in scrapie and Alzheimer's disease. Microb Pathog 2:435-442, 1987.
133. Duguid JR, Rohwer RG, Seed B. Isolation of cDNAs of scrapie-modulated RNAs by subtractive hybridisation of a cDNA library. Proc Natl Acad Sci U S A 85:5738-5742, 1988.
134. Bellinger-Kawahara C, Diener TO, McKinley MP, Groth DF, Smith DR, Prusiner SB. Purified scrapie prion resist inactivation by procedures that hydrolyze, modify, or shear nucleic acids. Virology 160:271-274, 1987.
135. Gabizon R, McKinley MP, Prusiner SB. Purified prion protein and scrapie infectivity copartition into liposomes. Proc Natl Acad Sci U S A 84:4017-4021, 1987.
136. Lewin B. Genes (3rd ed). New York: John Wiley & Sons, 1988.
137. Verweij CL, Hart M, Pannekoek H. Proteolytic cleavage of precursor of von Willebrand factor (vWF) is not essential for multimeric formation. J Biol Chem 263:7921-7924, 1988.
138. Stryer L. Control of enzymatic activity. In: Biochemistry. New York: W. H. Freeman, pp233-260, 1988.
139. Narang HK. The Structure and Transmission of BSE and CJD. In: Collinge P, Ed. The BSE Business. Birmingham: The Public Health Trust, pp30-44, 1995.