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Possible Implications of the Cellular Component of the Immune System in the Pathogenesis of Unconventional Slow Virus Infections

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Trends in Neuroimmunology

Abstract

A group of infectious degenerative disorders of the CNS naturally occurring in animals and man is referred as unconventional slow virus diseases although the etiological agent has yet to be definitively identified. The transmissibility of these disorders, their long latency period, the atypical properties of the infectious agent such as its resistance to nucleases,101 its inactivation only with high doses of UV59, or ionizing radiations2 and its peculiar structure devoid of a detectable nucleic acid, account for the definition given of unconventional slow virus diseases.48

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References

  1. A. L. Abbamondi, G. Di Trapani, M. Pocchiari, A. Sbriccoli, G. Macchi, Problemes de pathologie experimentale dans la maladie de Creutzfeldt-Jakob, in: ‘Virus non Conventionnels et Affections du Systeme Nerveux Central’, L.A. Court, ed., Masson, Paris, pp.309–316 (1983).

    Google Scholar 

  2. T. Alper, D.A. Haig, M.C. Clarke, The exceptionally small size of the scrapie agent, Bioch.Biophys.Res. Commun., 22:278–284 (1966).

    Article  Google Scholar 

  3. T. Aoki, C.J. Gibbs, Jr., J.Sotelo, D.C. Gajdusek, Heterogeneic autoantibody against neurofilament protein in the sera of animals with experimental kuru and Creutzfeldt-Jakob disease and natural scrapie infection, Infect.Immun., 38:316–324 (1982).

    Google Scholar 

  4. S. Bahmanyar, M.C. Moreau-Dubois, P. Brown, F. Cathala, D.C. Gajdusek, Serum antibodies to neurofilament antigens in patients with neurological and other diseases and in healthy controls, J.Neuroimmunol., 5:191–196 (1983).

    Article  Google Scholar 

  5. H. Baron, A Baron-Van Evercooren, J.M. Brucher, Anti-serum to scrapie-associated fibril protein reacts with amyloid plaques in familial transmissible dementia, J.Neuropathol.Exp.Neurol., 47:158–165 (1988).

    Article  Google Scholar 

  6. K. Basler, B.Oesch, M. Scott, D. Westaway, M. Walchli, D.F. Groth, M.P. McKinley, S. B. Prusiner, C. Weissmann, Scrapie and cellular Prp isoforms are encoded by the same chromosomal gene, Cell, 46:417–428 (1986).

    Article  Google Scholar 

  7. P. E. Bendheim, R.A. Barry, S.J. DeArmond, D.P. Stites, S.B. Prusiner, Antibodies to a scrapie prion protein, Nature, 310:418–421 (1984).

    Article  Google Scholar 

  8. P. E. Bendheim, J.M. Bookman, M.P. McKinley, D.T. Kingsbury, S. B. Prusiner, Scrapie and Creutzfeldt-Jakob disease prion proteins share physical properties and antigenic determinants, Proc.NatlAcad.Sci.USA, 82:997–1001 (1985).

    Article  Google Scholar 

  9. N. Bloksma, M.J. de Reuver, J.M.N. Willers, Influence on macrophage functions as a possible basis of immuno-modification by polyanions, Ann. Immunol. (Inst.Pasteur), 131 D: 255–265 (1980)

    Google Scholar 

  10. L. Bode, M. Pocchiari, H. Gelderblom, H. Diringer, Characterization 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.Virol., 66:2471–2478 (1985).

    Article  Google Scholar 

  11. D. C. Bolton, M.P. McKinley, S.B. Prusiner, Identification of a protein that purifies with the scrapie prion,Science, 218:1309–1311 (1982).

    Article  Google Scholar 

  12. D. C. Bolton, R.K. Meyer, S.B. Prusiner, Scrapie PrP27–30 is a sialoglyco-protein, J.Virol., 53:596–606 (1985).

    Google Scholar 

  13. P. Brown, Biological and chemotherapeutic forays into the field of unconventional viruses, in: Targets for the design of antiviral agents, E.De Clerq, R.T. Walker, eds., Plenum Press, New York, pp. 131–137 (1984).

    Google Scholar 

  14. P. Brown, M. Coker-Vann, K. Pomeroy, M. Franko, D.M. Asher, C.J. Gibbs, Jr., D.C. Gajdusek, Diagnosis of Creutzfeldt-Jakob disease by Western blot identification of marker protein in human brain tissue, N.Engl.J.Med., 314:547–551 (1986).

    Article  Google Scholar 

  15. M. E. Bruce, A.G. Dickinson, Genetic control of amyloid plaque production and incubation period in scrapie-infected mice, J.Neuropathol. Exp.Neurol., 44:285–294 (1985).

    Article  Google Scholar 

  16. M. E. Bruce, A.G. Dickinson, H.Fraser, Cerebral amyloidosis in scrapie in the mouse, effect of agent strain and mouse genotype, Neuropathol. Appl. Neurobiol., 2:471–478 (1976).

    Article  Google Scholar 

  17. M. Brunori, M.C. Silvestrini, M. Pocchiari, The scrapie agent and the prion hypothesis. Trends Biochem.Sci., 13:309–313 (1988).

    Article  Google Scholar 

  18. G. A. Carlson, D.T. Kingsbury, P. Goodman, S. Coleman, S.T. Marshall, S.J. DeArmond, D. Westway, S.B. Prusiner, Prion protein and scrapie incubation time genes are linked, Cell 46:503–511 (1986).

    Article  Google Scholar 

  19. R. I. Carp, S.M. Callahan, In vitro interaction of scrapie agent and mouse peritoneal macrophages, Intervirology, 16:8–13 (1981).

    Article  Google Scholar 

  20. R. I. Carp, S.M. Callahan, Effect of mouse peritoneal macrophages on scrapie infectivity during extended in vitro incubation, Intervirology, 17:201–207 (1982).

    Article  Google Scholar 

  21. R. I. Carp, S.M; Callahan, Scrapie incubation periods and end-point titers in mouse strains differing at the H-2D locus, Intervirology, 26:85–92 (1986).

    Article  Google Scholar 

  22. R. L. Chandler, Encephalopathy in mice produced by inoculation with scrapie brain material, Lancet, i:1378–1379 (1961).

    Article  Google Scholar 

  23. R. L. Chandler, J.Fisher, Experimental transmission of scrapie to rats, Lancet ii:1165 (1963).

    Article  Google Scholar 

  24. R. L. Chandler, B.A. Turfrey, Inoculation of voles, chinese hamsters, gerbils, and guinea pigs with scrapie brain material, Res.Vet. Sci., 13:219–224 (1972).

    Google Scholar 

  25. B. Chesebro, R. Race, K. Wehrly, J. Nishio, M. Bloom, D. Lechner, S. Bergstrom, K. Robbins, L. Mayer, J.M. Keith, C. Garon, A. Haase, Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain, Nature, 315:331–333 (1985).

    Article  Google Scholar 

  26. M. C. Clarke, The antibody response of scrapie-affected mice to immunisation with sheep red blood cells, Res.Vet.Sci., 9:595–597 (1968).

    Google Scholar 

  27. M. C. Clarke, D.A. Haig, Multiplication of scrapie agent in mouse spleen, Res.Vet.Sci., 12:195–197 (1971).

    Google Scholar 

  28. S. C. Collis, R.H. Kimberlin, Further studies on changes in immunoglobulin G in the sera and CSF of Herdwiek sheep with natural and experimental scrapie, J.Comp.Path., 93:331–338 (1983).

    Article  Google Scholar 

  29. S. C. Collis, R.H. Kimberlin, G.C. Millson, Immunoglobulin G concentrations in the sera of Herdwick sheep with natural scrapie, J.Comp.Path., 89:389–396 (1979).

    Article  Google Scholar 

  30. J. Cuille, P.L. Chelle, Pathologie animale, la maladie dite tremblant du mouton est-elle inoculable? C.R.Acad.Sci.(Paris), 203:1552–1554 (1936).

    Google Scholar 

  31. M. Czub, H.R. Braig, H. Diringer, Pathogenesis of scrapie, study of the temporal development of clinical symptons, of infectivity titres and scrapie-associated fibrils in brains of hamsters infected intraperitoneally, J.Gen.Virol., 67:2005–2009 (1986).

    Article  Google Scholar 

  32. M. Czub, H.R. Braig, H.Diringer, Replication of the scrapie agent in hamsters infected intracerebrally confirms the pathogenesis of amyloid-inducing virosis, J.Gen.Virol., 69:1753–1756 (1988).

    Article  Google Scholar 

  33. S. J. DeArmond, M.P. McKinley, R.A. Barry, M.B. Braunfeld, J.R. McColloch, S.B. Prusiner, Identification of prion amyloid filaments in scrapie-infected brain, Cell, 41:221–235 (1985).

    Article  Google Scholar 

  34. A. G. Dickinson, H.Fraser, Scrapie, effect of Dh gene on the incubation period of extraneurally injected agent, Heredity, 29:91–93 (1972).

    Article  Google Scholar 

  35. A. G. Dickinson, V.M.H. Meikle, Host genotype and agent effects in scrapie incubation, change in allelic interaction with different strains of agent, Mol.Gen.Genet., 112:73–79 (1971).

    Article  Google Scholar 

  36. A. G. Dickinson, V.M.H. Meikle, H.Fraser, Identification of a gene which controls the incubation period of some strains of scrapie in mice, J.Comp.Pathol., 78:293–299 (1968).

    Article  Google Scholar 

  37. A. G. Dickinson, D.M. Taylor, H. Fraser, Depression of polymorph counts by various scrapie agents, Nature, 248:510–511 (1974).

    Article  Google Scholar 

  38. J. Diedrich, S. Wietgrefe, M. Zupancic, K. Staskus, E. Retzel, A.T. Haase, R. Race, The molecular pathogenesis in scrapie and Alzheimer’s disease, Microb.Pathog., 2:435–442 (1987).

    Article  Google Scholar 

  39. H. Diringer, H. Gelderblom, H. Hilmert, M. Ozel, C. Edelbluth, R.H. Kimberlin, Scrapie infectivity, fibrils and low molecular weight protein, Nature, 306:471–478 (1983).

    Article  Google Scholar 

  40. H. Diringer, H. Hilmert, D. Simon, E. Werner, B. Ehlers, Toward purification of the scrapie agent, Eur.J.Biochem., 134:555–560 (1983).

    Article  Google Scholar 

  41. H. Diringer, H.C. Rahn, L. Bode, Antibodies to protein of scrapie-associated fibtilis, Lancet ii:345 (1984)

    Article  Google Scholar 

  42. B. Ehlers, H.Diringer, Dextrane sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen, J.Gen.Virol., 65:1325–1330 (1984).

    Article  Google Scholar 

  43. C. G. Farquhar, A.G. Dickinson, Prolongation of scrapie incubation period by an injection of dextrane sulphate 500 within the month before or after infection, J.Gen.Virol., 67:463–473 (1986).

    Article  Google Scholar 

  44. H. Fraser, The pathology of natural and experimental scrapie, in: ‘Slow Virus Diseases of Animals and Man,’ RH, Kimberlin, ed., North Holland, Amsterdam, pp.267–305 (1976).

    Google Scholar 

  45. H. Fraser, A.G. Dickinson, The sequential development of the brain lesions of scrapie in three strains of mice, J.Comp.Pathol., 78:301–311 (1968).

    Article  Google Scholar 

  46. H. Fraser, A.G. Dickinson, Pathogenesis of scrapie in the mouse, the role of the spleen, Nature, 226:462–463 (1970).

    Article  Google Scholar 

  47. H. Fraser, A.G. Dickinson, Studies of the lymphoreticular system in the pathogenesis of scrapie, the role of spleen and thymus, J.Comp.Pathol., 88:563–573 (1978).

    Article  Google Scholar 

  48. D. C. Gajdusek, Unconventional viruses and the origin and disappearance of kuru, Science, 197:943–960 (1977).

    Article  Google Scholar 

  49. D. C. Gajdusek, Hypothesis: interference with axonal transport of neurofilament as a common pathogenetic mechanism in certain diseases of the central nervous system, N.Engl.J.Med., 312:711–719 (1985).

    Article  Google Scholar 

  50. D. C. Gajdusek, C.J. Gibbs, Jr., M. Alpers, Experimental transmission of a kuru-like syndrome to chimpanzees, Nature, 209:794–796 (1966).

    Article  Google Scholar 

  51. D. C. Gajdusek, C.J. Gibbs, Jr., Subacute and chronic diseases caused by atypical infections with unconventional viruses in aberrant hosts, in: ‘Perspective in Virology, vol.8,’ M. Pollard, ed., Academic Press, New York, pp. 279–311 (1973).

    Google Scholar 

  52. D. C. Gajdusek, V. Zigas, Degenerative disease of the central nervous system in New Guinea, The endemic occurrence of ‘kuru’ in the native population, N.Engl.J.Med., 257:974–978 (1957).

    Article  Google Scholar 

  53. A. C. Gardiner, A.A. Marucci, Immunological responsiveness of scrapie infected mice, J.Comp.Path., 79:233–235 (1969).

    Article  Google Scholar 

  54. D. E. Garfin, D.P. Stites, J.D. Perlman, S.P. Cochran, S.B. Prusiner, Mitogen stimulation of splenocytes from mice infected with scrapie agent, J.Infect.Dis., 138:396–400 (1978).

    Article  Google Scholar 

  55. D. E. Garfin, D.P. Stites, L.A. Zitnik, S.B. Prusiner, Suppression of polyclonal B cell activation in scrapie infected C3H/HeJ mice, J.Immunol., 120:1986–1990 (1978).

    Google Scholar 

  56. C. J. Gibbs Jr., D.C. Gajdusek, Isolation and characterization of the subacute spongiform virus encephalopathies of man: kuru and Creutzfeldt-Jakob disease, J.Clin.Pathol., 25:84–96 (1972).

    Article  Google Scholar 

  57. C. J. Gibbs Jr., D.C. Gajdusek, Experimental subacute spongiform virus encephalopathies in primates and other laboratory animals, Science, 182:67–68 (1973).

    Article  Google Scholar 

  58. C. J. Gibbs Jr., D.C. Gajdusek, D.M. Asher, M.P. Alpers, E. Beck, P.M. Daniel, W.B. Matthews, Creutzfeldt-Jakob disease (subacute spongiform encephalopathy): transmission to the chimpanzee, Science, 161:388–389 (1968).

    Article  Google Scholar 

  59. C. J. Gibbs Jr., D.C. Gajdusek, R. Latarjet, Unusual resistance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease, and scrapie, Proc.Natl.Acad.Sci., USA, 75:6268–6270 (1978).

    Article  Google Scholar 

  60. W. S. Gordon, I.H. Pattison, The experimental production of scrapie in goats, Vet.Rec., 69:1444 (1957).

    Google Scholar 

  61. P. D. Hart, M.R. Young, Interference with normal phagosome-lysosome fusion in macrophages using ingested yeast cells and suramin, Nature, 256:47 (1975).

    Article  Google Scholar 

  62. M. S. Hirsch, Effect of antilymphocytic serum on host responses to infectious agents, Fed.Proc., 29:169–170 (1970).

    Google Scholar 

  63. J. Hope, L.J.D. Morton, F. Farquhar, G. Multhaup, K. Beyreuther, R.H. Kimberlim: The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distributions and N-terminal protein sequence has predicted for the normal brain protein (PrP). EMBRO J., 5:2591–2597 (1986).

    Google Scholar 

  64. J. Hope, G.Multhaup, L.J.D. Reekie, R.H. Kimberlin, K. Beyreuther, Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie, Eur.J.Biochem., 172:271–277 (1988).

    Article  Google Scholar 

  65. N. Hunter, J. Hope, I. McConnell, A.G. Dickinson, Linkage of the scrapie-associated fibril protein (PrP) gene and sinc using congenic mice and restriction fragment length polymorphism analysis, J.Gen.Virol., 69:2711–2716 (1987).

    Article  Google Scholar 

  66. D. Karcher, B.S. Soler Federsppiel, F.D. Lowenthal, F. Frank, A. Lowenthal, Anti-neurofilament antibodies in blood of patients with neurological disease, Acta Neuropathol. (Berl.), 72:82–85 (1986).

    Article  Google Scholar 

  67. K. C. Kasper, K. Bowman, D.P. Stites, S.B. Prusiner, Toward development of assays for scrapie-specific antibodies, Adv.Exp.Med.Biol., 134:401–413 (1981).

    Google Scholar 

  68. K. C. Kasper, D.P. Stites, K.A. Bowman, H. Panitch, S.B. Prusiner, Immunological studies of scrapie infection, J.Neuroimmunol., 3:187–201 (1982).

    Article  Google Scholar 

  69. R. H. Kimberlin, P.G. Cunnington, Reduction of scrapie incubation time in mice and hamsters by a single injection of methanol extraction residue of BCG., FEBS Microb.Lett., 3:169–172 (1978).

    Article  Google Scholar 

  70. R. H. Kimberlin, C.A. Walker, Pathogenesis of mouse scrapie, dynamics of agent replication in spleen, spinal cord and brain after infection by different routes, J.Comp.Pathol., 89:551–562 (1979).

    Article  Google Scholar 

  71. R. H. Kimberlin, C.A. Walker, The antiviral compound HPA-23 can prevent scrapie when administered at the time of infection, Arch.Virol., 78:9–18 (1983).

    Article  Google Scholar 

  72. R. H. Kimberlin, C.A. Walker, Suppression of scrapie infection in mice by heteropolyanion 23, dextrane sulphate, and some other polyanions, Antimicrob.Agents Chemother., 30:409–413 (1986).

    Google Scholar 

  73. D. T. Kingsbury, K.C. Kasper, D.P. Stites, J.D. Watson, R.N. Hogan, S.B. Prusiner, Genetic control of scrapie and Creutzfeldt-Jakob disease in mice, J.Immunol., 131:491–496 (1983).

    Google Scholar 

  74. D. T. Kingsbury, D.A. Smeltzer, C.J. Gibbs Jr., D.C. Gajdusek, Evidence for normal cell-mediated immunity in scrapie-infected mice, Infect. Immun., 32:1176–1180 (1981).

    Google Scholar 

  75. H. A. Kretzschmar, L.E. Stowring, D. Westway, W.H. Stubblebine, S.B. Prusiner, S.J. DeArmond, Molecular cloning of a human prion protein cDNA. DNA, 5:315–324 (1986).

    Article  Google Scholar 

  76. Y. Kuroda, C.J. Gibbs Jr., H.L. Amyx, D.C. Gajdusek, Creutzfeldt-Jakob disease in mice, persistent viremia and preferential replication of virus in low-density lymphocytes, Infect.Immun., 41:154–161 (1983).

    Google Scholar 

  77. A. Ladogana, P. Casaccia, S. Schmittinger, A. Iavarone, H.Y.G. Xi, C. Masullo, M. Pocchiari, Therapeutical approach in hamsters experimentally affected with scrapie: pathogenetic implications. Ageing Brain and Dementia, Padua, 22–24 September (1988).

    Google Scholar 

  78. G. C., Lavelle, L. Sturman, W.J. Hadlow, Isolation from mouse spleen of cell populations with high specific infectivity for scrapie virus, Infect.Immun., 5:319–323 (1972).

    Google Scholar 

  79. Y. C. J. Liao, R.V. Lebo, G.A. Lawson, E.A. Smuckler, Human prion protein cDNA, molecular cloning, chromosomal mapping, and biological implications, Science, 233:364–367 (1986).

    Article  Google Scholar 

  80. P. C. Licursi, P.A. Merz, G.S. Merz, R.I. Carp, Scrapie-induced changes in the percentage of polymorphonuclear neutrophils in mouse peripheral blood, Infect.Immun., 6:370–376 (1972).

    Google Scholar 

  81. H. L. Lin, G. Medoff, G.S. Kobayashi, Effects of amphotericin B on macrophages and their precursor cells, Antimicrob.Agents Chemother., 11:154–160 (1977).

    Google Scholar 

  82. C. Locht, B. Chesebro, R. Race, J.M. Keith, Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent, Proc.Natl.Acad.Sci., USA, 83:6372–6376 (1986).

    Article  Google Scholar 

  83. G. Macchi, C. Masullo, M. Pocchiari, Le demenze trasmissibili, Federazione Medica, 38:1156–1160 (1985).

    Google Scholar 

  84. E. E. Manuelidis, Transmission of Cruetzfeldt-Jacob Disease from man to the guinea pig, Science, 190:571–572, (1975).

    Article  Google Scholar 

  85. E. E. Manuelidis, Transmission of Creutzfeldt-Jakob disease with scrapie-like syndromes to mice, Nature, 271:778–779 (1978).

    Article  Google Scholar 

  86. E. E. Manuelidis, J.N. Angelo, E.J. Gorgacz, L.Manuelidis, Transmission of Creutzfeldt-Jakob disease to Syrian hamsters, Lancet, i:479, (1977).

    Google Scholar 

  87. L. Manuelidis, T. Sklaviadis, E.E. Manuelidis, Evidence suggesting that PrP is not the infectious agent in Creutzfeldt-Jakob disease, EMBO J., 6:341–347 (1987).

    Google Scholar 

  88. L. Manuelidis, S. Valley, E.E. Manuelidis, Specific proteins associated with Creutzfeldt-Jakob disease and scrapie share antigenic and carbohydrate determinants, Proc.Natl.Acad.Sci. USA, 82:4263–4267 (1985).

    Article  Google Scholar 

  89. R. F. Marsh, Effect of vaccinia-activated macrophages on scrapie infection in hamsters, in: ‘Hamster Immune Response in Infectious and Oncologic Diseases,’ J.W. Streilein, D.A. Hart, J. Stein Streilein, W.R. Duncan, R.E. Billingham, eds., Plenum Press, New York, pp. 359–363 (1981).

    Google Scholar 

  90. R. F. Marsh, R.H. Kimberlin, Comparison of scrapie and transmissible mink encephalopathy in hamsters, II. Clinical signs, pathology and pathogenesis, J.Infect.Dis., 131:104–110 (1975).

    Article  Google Scholar 

  91. R. F. Marsh, J.M. Miller, R.P. Hanson, Transmissible mink encephalopathy, studies on the peripheral lymphocyte, Infect.Immun., 7:352–355 (1973).

    Google Scholar 

  92. C. L. Masters, D.C. Gajdusek, C.J. Gibbs Jr., Creutzfeldt-Jakob disease virus isolation from the Gerstmann-Straussler syndrome, with an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies, Brain, 104:559–588 (1981).

    Article  Google Scholar 

  93. C. L. Masters, G. Multhaup, G. Simms, J. Pottgiesser, R.N. Martins, K. Beyreuther, Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer’s disease contain the same protein as the amyloid of plaque cores and blood vessels, EMBO J., 4:2757–2763 (1985).

    Google Scholar 

  94. D. E. McFarlin, M.C. Raff, E. Simpson, S.H. Nehlsen, Scrapie in immunologically deficient mice, Nature, 233:336 (1971).

    Article  Google Scholar 

  95. M. P. McKinley, D.C. Bolton, S.B. Prusiner, A protease-resistant protein is a structural component of scrapie prion, Cell, 35:57–62 (1983).

    Article  Google Scholar 

  96. M. P. McKinley, M.B. Braunfeld, C.G. Bellinger, S.B. Prusiner, Molecular characteristics of prion rods purified from scrapie-infected hamster brains, J.Infect.Dis., 154:110–120 (1986).

    Article  Google Scholar 

  97. G. S. Merz, V. Schwenk, G. Schuller-Levis, S. Gruca, H.M. Wisniewski, Isolation and characterization of macrophages from scrapie-infected mouse brain, Acta Neuropathol.(Berl.) 72:240–247 (1987).

    Article  Google Scholar 

  98. P. A. Merz, R.G. Rohwer, R. Kascsak, H.M. Wisniewski, R.A. Somerville, C.J. Gibbs Jr., D.C. Gajdusek, An infection specific particle from the unconventional slow virus diseases, Science, 225:437–440 (1984).

    Article  Google Scholar 

  99. P. A. Merz, R.A. Somerville, H.M. Wisniewski, K. Iqbal, Abnormal fibrils from scrapie infected brain, Acta Neuropathol.(Berl.) 54:63–74 (1981).

    Article  Google Scholar 

  100. R. K. Meyer, M.P. McKinley, K.A. Bowman, R.A. Barry, S.B. Prusiner, Separation and properties of cellular and scrapie prion proteins, Proc.Natl.Acad.Sci. USA, 83:2310–2314 (1986).

    Article  Google Scholar 

  101. G. C. Millson, G.D. Hunter, R.H. Kimberlin, The physico-chemical nature of the scrapie agent, in: ‘Slow Virus Diseases of Animals and Man,’ R.H. Kimberlin, ed., North Holland Publishing Company, Amsterdam, pp. 243–266 (1976).

    Google Scholar 

  102. S. Mohri, S. Handa, J. Tateishi, Lack of effect of thymus and spleen on the incubation period of Creutzfeldt-Jakob disease in mice, J.Gen.Virol., 68:1187–1189 (1987).

    Article  Google Scholar 

  103. G. Multhaup, H. Diringer, H. Hilmert, H. Prinz, J. Heukeshoven, K. Beyreuther, The protein component of scrapie-associated fibrils is a glycosylated low-molecular-weight protein, EMBO J., 4:1495–1501 (1985).

    Google Scholar 

  104. B. Oesch, D. Westaway, M. Walchli, M.P. McKinley, S.B.H. Kent, R. Aebersold, R.A. Barry, P. Tempst, D.B. Teplow, L.E. Hood, S.B. Prusiner, C. Weissmann, A cellular gene encodes scrapie Prp 27–30 protein, Cell, 40:735–746 (1985).

    Article  Google Scholar 

  105. H. B. Parry, Scrapie disease in sheep, D.R Oppenheimer, ed., Academic Press, London, (1983).

    Google Scholar 

  106. M. Pocchiari, P. Casaccia, A. Iavarone, A. Ladogana, P. Mariotti, C. Masullo, S. Schmittinger, G. Macchi, Le encefalopatie spongiose subacute. Quaderni di Neuropatologia, 4:1–23 (1988).

    Google Scholar 

  107. M. Pocchiari, S. Schmittinger, A. Ladogana, C. Masullo, Effect of amphotericin B in intracerebral scrapie inoculated hamsters, in: ‘Proc. II Symp. Int. sur les Virus non Conventionnels du Systeme Nerveux Central,’ L.A. Court, D. Dormont, D. Kingsbury, eds., Abbay de Melleray, Moisdon la Riviere, in press (1989).

    Google Scholar 

  108. M. Pocchiari, S. Schmittinger, C. Masullo, Amphotericin B delays the incubation period of scrapie in intracerebrally inoculated hamsters, J.Gen.Virol., 68:219–223 (1987).

    Article  Google Scholar 

  109. S. B. Prusiner, D.C. Bolton, D.F. Groth, K.A. Bowman, S.P. Cochran, M.P. McKinley, Further purification and characterization of scrapie prions, Biochemistry, 21:6942–6950 (1982).

    Article  Google Scholar 

  110. S. B. Prusiner, D.F. Groth, D.C. Bolton, S.B. Kent, L.E. Hood, Purification and structural studies of a major scrapie prion protein, Cell, 38:127–134 (1984).

    Article  Google Scholar 

  111. S. B. Prusiner, M.P. McKinley, K.A. Bowman, D.C. Bolton, P.D. Bendheim, D.F. Groth, G.C. Glenner, Scrapie prions aggregate to form amyloid-like birefringent rods, Cell, 35:349–358 (1983).

    Article  Google Scholar 

  112. N. K. Robakis, E.A. Devine-Gage, E.C. Jenkins, RJ. Kascsak, W.T. Brown, M.S. Krawczun, W.P. Silverman, Localization of a human gene homologous to the PrP gene of the p arm of chromosome 20 and detection of PrP-related antigens in normal human brain, Biochem.Biophys.Res. Commun., 140:758–765 (1986).

    Article  Google Scholar 

  113. N. K. Robakis, P.R Sawh, G.C. Wolfe, R. Rubenstein, R.I. Carp, M.A. Innis, Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various issues, Proc.Natl.Acad.Sci. USA, 83:6377–6381 (1986).

    Article  Google Scholar 

  114. R. Rubenstein, R.J. Kascsak, P.A. Merz, M.C. Papini, R.I. Carp, N.K. Robakis, H.M. Wisniewski, Detection of scrapie-associated fibril (SAF) proteins using anti-SAF antibody in non-purified tissue preparations, J.Gen.Virol., 67:671–681 (1986).

    Article  Google Scholar 

  115. J. Sotelo, C.J. Gibbs Jr., D.C. Gajdusek, Autoantibodies against axonal neurofilaments in patients with kuru and Creutzfeldt-Jakob disease, Science, 210:190–193 (1980).

    Article  Google Scholar 

  116. J. Sotelo, C.J. Gibbs Jr., D.C. Gajdusek, B.H. Toh, M. Wurth, Method for preparing cultures of central neurons: cytochemical and immunochemical studies, Proc.Natl. Acad.Sci. USA, 77:653–657 (1980).

    Article  Google Scholar 

  117. R. S. Sparkes, M. Simon, V.H. Cohn, R.E.K. Fournier, J. Lem, I. Klisak, C. Heinzmann, C. Blatt, M. Lucero, T. Mohandas, S.J.DeArmond, D. Westway, S.B. Prusiner, L.P. Weiner, Assignment of the human and mouse prion protein genes to homologous chromosomes, Proc.Natl.Acad.Sci. USA, 83:7358–7362 (1986).

    Article  Google Scholar 

  118. D. P. Stites, D.E. Garfin, S.B. Prusiner, The immunology of scrapie, in: ‘Slow Transmissible Diseases of the Nervous System,’ Vol. 2, S.B. Prusiner, W.J. Hadlow, eds., Academic Press, New York, pp. 211–221 (1979).

    Google Scholar 

  119. G. M. Stites, D. Barta, B.M. Olcott, W.F. Brown Jr., Serum and cerebrospinal fluid concentrations of immunoglobulin G in Suffolk sheep with scrapie. Am. J.Vet.Res., 45: 1812–1813 (1984).

    Google Scholar 

  120. J. Tateishi, M.Ohta, N. Koga, Y. Sato, Y. Kuroiwa, Transmission of chronic spongiform encephalopathy with kuru plaque and leukomalacia of man to small rodents, Ann.Neurol., 5:581–584 (1979).

    Article  Google Scholar 

  121. B. H. Toh, C.J. Gibbs Jr., D.C. Gajdusek, J.Goudsmit, D. Dahl, The 200- and 150-kDa neurofilament proteins react with IgG autoantibodies from patients with kuru, Creutzfeldt-Jakob disease and other neurologic diseases, Proc.NatlAcad.Sci. USA, 82:3485–3489 (1985).

    Article  Google Scholar 

  122. B. H. Toh, C.J. Gibbs Jr., D.C. Gajdusek, D.D. Tuthill, D. Dahl, The 200–250-kDa neurofilament proteins react with IgG autoantibodies from chimpanzees with kuru or Creutzfeldt-Jakob disease; a 62-kDa neuro-filament-associated protein reacts with sera from sheep with natural scrapie, Proc.Natl.Acad.Sci. USA, 82:3894–3896 (1985).

    Article  Google Scholar 

  123. G. A. H. Wells, A.C. Scott, C.T. Johnson, R.F. Gunning, R.D. Hancock, M. Jeffrey, M. Dawson, R. Bradley, A novel progressive spongiform encephalopathy in cattle, Vet.Rec. 121:419–420 (1987).

    Article  Google Scholar 

  124. E. S. Williams, S. Young, Chronic wasting disease of captive mule deer: a spongiform encephalopathy, J.Wildlife Dis., 16:89–98 (1980).

    Google Scholar 

  125. M. Worthington, R. Clark, Lack of effect of immuno-suppression on scrapie infection, J.Gen.Virol., 13:349–351 (1971).

    Article  Google Scholar 

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Casaccia, P., Ladogana, A., Masullo, C., Macchi, G., Pocchiari, M. (1990). Possible Implications of the Cellular Component of the Immune System in the Pathogenesis of Unconventional Slow Virus Infections. In: Marrosu, M.G., Cianchetti, C., Tavolato, B. (eds) Trends in Neuroimmunology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0607-8_17

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