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Molecular Pathology of the Prions pp 85–110Cite as

Differential Targeting of Neurons by Prion Strains

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Part of the book series: Methods in Molecular Medicine™ ((MIMM,volume 59))

Abstract

A basic principle of microbiology that applies to all conventional infectious pathogens is that the disease phenotype is a function of both the infecting agent and the host’s response to it. All evidence indicates that this principle is also true for diseases acquired by infection with prions, given that inoculation of different scrapie prion strains into inbred mouse strains shows that reproducible differences in the disease phenotype are determined by both the strain of scrapie prion and a host gene or genes (1-6). The disease parameters used to characterize and define each prion strain, then and now, include: the relative or complete failure of transmission of a prion strain from one animal species to another, designated the “host species barrier”; incubation time, defined as the time from inoculation of a prion strain to the onset of clinical signs; the neuroanatomic distribution of spongiform degeneration, also designated the “lesion profile”; and whether or not PrP amyloid plaques are formed in the brain. Of these parameters, least is known about how each prion strain targets a different population of neurons for degeneration to create the strain-specific lesion profile. The goal of this report is to review the evidence, which argues that PrPSc is the main and perhaps sole prion factor determining the disease phenotype, and that PrPC expressed by the host animal is the predominant host factor determining the disease phenotype, including differential targeting of neurons.

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References

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

    Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

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

    Article  PubMed  CAS  Google Scholar 

  4. Fraser, H. and Dickinson, A. G. (1973) Scrapie in mice. Agent-strain differences in the distribution and intensity of grey matter vacuolation. J. Comp. Pathol. 83, 29–40.

    Article  PubMed  CAS  Google Scholar 

  5. Fraser, H. (1979) Neuropathology of scrapie: the precision of the lesions and their diversity, in Slow Transmissible Diseases of the Nervous System, vol. 1 (Prusiner, S. B. and Hadlow, W. J. Academic, eds.), New York, pp. 387–406.

    Google Scholar 

  6. Bruce, M. E., McConnell, I., Fraser, H., and Dickinson, A. G. (1991) Disease characteristics of different strains of scrapie in Sinc congenic mouse lines: implications for the nature of the agent and host control of pathogenesis. J. Gen. Virol. 72, 595–603.

    Article  PubMed  CAS  Google Scholar 

  7. Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136–144.

    Article  PubMed  CAS  Google Scholar 

  8. Oesch, B., Westaway, D., Wälchli, M., McKinley, M. P., Kent, S. B. H., Aebersold, R., et al. (1985) A cellular gene encodes scrapie PrP 27-30 protein. Cell 40, 735–746.

    Article  PubMed  CAS  Google Scholar 

  9. Chesebro, B., Race, R., Wehrly, K., Nishio, J., Bloom, M., Lechner, D., et al. (1985) Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain. Nature 315, 331–333.

    Article  PubMed  CAS  Google Scholar 

  10. Basler, K., Oesch, B., Scott, M., Westaway, D., et al. (1986) Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46, 417–428.

    Article  PubMed  CAS  Google Scholar 

  11. Prusiner, S. B. (1997) Prion diseases and the BSE crisis. Science 278, 245–251.

    Article  PubMed  CAS  Google Scholar 

  12. Prusiner, S. B. (1998) Prions. Les Prix Nobel, The Nobel Prizes, 1997. Edited by Frängsmyr T. Stockholm, Norstedts Tryckeri AB, pp. 268–323.

    Google Scholar 

  13. Prusiner, S. B., Scott, M. R., DeArmond, S. J., and Cohen, F. E. (1998) Prion protein biology. Cell 93, 337–348.

    Article  PubMed  CAS  Google Scholar 

  14. Pan, K.-M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., et al. (1993) Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90, 10,962–10,966.

    Article  PubMed  CAS  Google Scholar 

  15. Safar. J., Roller, P. P., Gajdusek, D. C., and Gibbs, C.J., Jr. (1993) Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268, 20,276–20,284.

    PubMed  CAS  Google Scholar 

  16. Taraboulos, A., Raeber, A. J., Borchelt, D. R., Serban, D., and Prusiner, S. B. (1992) Synthesis and trafficking of prion proteins in cultured cells. Mol. Biol. Cell 3, 851–86

    PubMed  CAS  Google Scholar 

  17. Caughey, J. and So B., Raymond, G. J. (1991) The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-and phospholipase-sensitive. J. Biol. Chem. 266, 18,217–18,223.

    PubMed  CAS  Google Scholar 

  18. Büeler, H., Fischer, M., Lang, Y., Bluethmann, H., Lipp, H-P., DeArmond, S. J., et al. (1992) Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577–582.

    Article  PubMed  Google Scholar 

  19. Büeler, H., Aguzzi, A., Sailer, A., Greiner, R.-A., Autenried, P., Aguet, M., and Weissmann, C. (1993) Mice devoid of PrP are resistant to scrapie. Cell 73, 1339–1347.

    Article  PubMed  Google Scholar 

  20. Prusiner, S. B., Groth, D., Serban, A., Koehler, R., Foster, D., Torchia, M., et al. (1993) Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. USA 90, 10,608–10,612.

    Article  PubMed  CAS  Google Scholar 

  21. Brandner, S., Isenmann, S., Raeber, A., Fischer, M., Sailer, A., Kobayashi, Y., et al. (1996) Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 379, 339–343.

    Article  PubMed  CAS  Google Scholar 

  22. Scott, M., Foster, D., Mirenda, C., Serban, D., Coufal, F., Wälchli, M., et al. (1989) Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59, 847–857.

    Article  PubMed  CAS  Google Scholar 

  23. Scott, M., Groth, D., Foster, D., Torchia, M., Yang, S-L., DeArmond, S. J., and Prusiner S. B. (1993) Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 73, 979–988.

    Article  PubMed  CAS  Google Scholar 

  24. Telling, G. C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F. E., DeArmond, S. J, and Prusiner, S. B. (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79–90.

    Article  PubMed  CAS  Google Scholar 

  25. Kaneko, K., Zulianello, L., Scott, M., Cooper, C. M., Wallace, A. C., James, T. L., Cohen, F. E., and Prusiner, S. B. (1997) Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94, 10,069–10,074.

    Article  PubMed  CAS  Google Scholar 

  26. Cohen, F. E., Pan, K-M., Huang, Z., Baldwin, M., Fletterick, R. J., and Prusiner, S. B. (1994) Structural clues to prion replication. Science 264, 530–531.

    Article  PubMed  CAS  Google Scholar 

  27. Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., et al. (1996) Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274, 2079–2082.

    Article  PubMed  CAS  Google Scholar 

  28. Vey, M., Pilkuhn, S., Wille, H., Nixon, R., DeArmond, S. J., Smart, E. J., et al. (1996) Subcellular colocalization of cellular and scrapie prion proteins in caveolaelike membranous domains. Proc. Natl. Acad. Sci. USA 93, 14,945–14,949.

    Article  PubMed  CAS  Google Scholar 

  29. Monari, L., Chen, S. G., Brown, P., Parchi, P., Petersen, R. B., Mikol, J., et al. (1994) Fatal familial insomnia and familial Creutzfeldt-Jakob disease: different prion proteins determined by a DNA polymorphism. Proc. Natl. Acad. Sci. USA 91, 2839–2842.

    Article  PubMed  CAS  Google Scholar 

  30. Mastrianni, J. A., Nixon, R., Layzer, R., Telling, G. C., Han, D., DeArmond, S. J., and Prusiner, S. B. (1999) Prion protein conformation in a patient with sporadic fatal insomnia. N. Eng. J. Med. 340, 1630–1638.

    Article  CAS  Google Scholar 

  31. Kellings, K., Prusiner, S. B., and Riesner, D. (1994) Nucleic acids in prion preparations: unspecific background or essential component? Phil. Trans. R. Soc. Lond. B 343, 425–430.

    Article  CAS  Google Scholar 

  32. Kellings, K., Meyer, N., Mirenda, C., Prusiner, S. B., and Riesner, D. (1992) Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE). J. Gen. Virol. 73, 1025–1029.

    Article  PubMed  CAS  Google Scholar 

  33. Prusiner, S. B., Scott, M., Foster, D., Pan, K-M., Groth, D., Mirenda, C., et al. (1990) Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63, 673–686.

    Article  PubMed  CAS  Google Scholar 

  34. Carlson, G. A., Kingsbury, D. T., Goodman, P. A., Coleman, S., Marshall, S. T., DeArmond, S. J., Westaway, D., and Prusiner, S. B. (1986) Linkage of prion protein and scrapie incubation time genes. Cell 46, 503–511.

    Article  PubMed  CAS  Google Scholar 

  35. Westaway, D., Goodman, P. A., Mirenda, C. A., McKinley, M. P., Carlson, G.A., and Prusiner, S. B. (1987) Distinct prion proteins in short and long scrapie incubation period mice. Cell 51, 651–662.

    Article  PubMed  CAS  Google Scholar 

  36. Carlson, G. A., Ebeling, C., Yang, S-L., Telling, G., Torchia, M., Groth, D., et al. (1994) Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice. Proc. Natl. Acad. Sci. USA 91, 5690–5694.

    Article  PubMed  CAS  Google Scholar 

  37. Ghetti, B., Piccardo, P., Frangione, B., Bugiani, O., Giaccone, G., Young, K., et al. (1996) Prion protein amyloidosis. Brain Pathol. 6, 127–145.

    Article  PubMed  CAS  Google Scholar 

  38. DeArmond, S. J., Mobley, W. C., DeMott, D. L., Barry, R. A., Beckstead, J. H., and Prusiner, S. B. (1987) Changes in the localization of brain prion proteins during scrapie infection. Neurology 37, 1271–1280.

    PubMed  CAS  Google Scholar 

  39. DeArmond, S. J. and Prusiner, S. B. (1993) The neurochemistry of prion diseases. J. Neurochem. 61, 1589–1601.

    Article  PubMed  CAS  Google Scholar 

  40. Hecker, R., Taraboulos, A., Scott, M., Pan, K.-M., Torchia, M., Jendroska, K., DeArmond, S. J., and Prusiner, S. B. (1992) Replication of distinct prion isolates is region specific in brains of transgenic mice and hamsters. Genes Dev. 6, 1213–1228.

    Article  PubMed  CAS  Google Scholar 

  41. Jendroska, K., Heinzel, F. P., Torchia, M., Stowring, L., Kretzschmar, H. A., Kon, A., et al. (1991) Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity. Neurology 41, 1482–1490.

    PubMed  CAS  Google Scholar 

  42. Hsiao, K. K., Groth, D., Scott, M., Yang, S-L., Serban, H., Rapp, D., et al. (1994) Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc. Natl. Acad. Sci. USA 91, 9126–9130.

    Article  PubMed  CAS  Google Scholar 

  43. Hegde, R. S., Mastrianni, J. A., Scott, M. R., DeFea, K. A., Tremblay, P., Torchia, et al. (1998) A transmembrane form of prion protein in neurodegenerative disease. Science 279, 827–834.

    Article  PubMed  CAS  Google Scholar 

  44. Bruce, M. E., McBride, P. A., and Farquhar, C. F. (1989) Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie. Neurosci. Lett. 102, 1–6.

    Article  PubMed  CAS  Google Scholar 

  45. DeArmond, S. J., Yang, S-L., Lee, A., Bowler, R., Taraboulos, A., Groth, D., and Prusiner, S. B. (1993) Three scrapie prion isolates exhibit different accumulation patterns of the prion protein scrapie isoform. Proc. Natl. Acad. Sci. USA 90, 6449–6453.

    Article  PubMed  CAS  Google Scholar 

  46. Endo, T., Groth, D., Prusiner, S. B., and Kobata, A. (1989) Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 28, 8380–8388.

    Article  PubMed  CAS  Google Scholar 

  47. Haraguchi, T., Fisher, S., Olofsson, S., Endo, T., Groth, D., Tarantino, A., et al. (1989) Asparagine-linked glycosylation of the scrapie and cellular prion proteins. Arch. Biochem. Biophys. 274, 1–13.

    Article  PubMed  CAS  Google Scholar 

  48. O’Connor, S. E. and Imperiali, B. (1996) Modulation of protein structure and function by asparagine-linked glycosylation. Chem. and Biol. 3, 803–812.

    Article  CAS  Google Scholar 

  49. DeArmond, S. J., Sanchez, H., Qiu, Y., Ninchak-Casey, A., Daggett, V., Paminiano-Camerino, A., et al. (1997) Selective neuronal targeting in prion diseases. Neuron 19, 1337–1348.

    Article  PubMed  CAS  Google Scholar 

  50. Taraboulos, A., Rogers, M., Borchelt, D. R., McKinley, M. P., Scott, M., Serban, D., and Prusiner, S.B. (1990) 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.

    Article  PubMed  CAS  Google Scholar 

  51. Taraboulos, A., Jendroska, K., Serban, D., Yang S-L., DeArmond, S. J., and Prusiner, S.B. (1992) Regional mapping of prion proteins in brains. Proc. Natl. Acad. Sci. USA 89, 7620–7624.

    Article  PubMed  CAS  Google Scholar 

  52. DeArmond, S. J., Qiu, Y., Sànchez, H., Spilman, P. R., Ninchak-Casey, A., Alonso, D., and Daggett, V. (1999) PrPC glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. J. Neuropathol. Exp. Neurol. 58, 1000–1009

    Article  PubMed  CAS  Google Scholar 

  53. Bolton, D. C., Meyer, R. K., and Prusiner, S. B. (1985) Scrapie PrP 27-30 is a sialoglycoprotein. J. Virol. 53, 596–606.

    PubMed  CAS  Google Scholar 

  54. Rademacher, T. W., Parekh, R. B., and Dwek, R. A. (1988) Glycobiology. Annu. Rev. Biochem. 57 :785–838

    Article  PubMed  CAS  Google Scholar 

  55. Kretzschmar, H. A., Prusiner, S. B., Stowring, L. E., and DeArmond, S. J. (1986) Scrapie prion proteins are synthesized in neurons. Am. J. Pathol. 122, 1–5.

    PubMed  CAS  Google Scholar 

  56. James, T. L., Liu, H., Ulyanov, N. B., Farr-Jones, S., Zhang, H., Donne, D. G., et al. (1997) Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 10,086–10,091.

    Article  PubMed  CAS  Google Scholar 

  57. Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., et al. (1997) Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. USA 94, 13,452–13,457.

    Article  PubMed  CAS  Google Scholar 

  58. Imperiali, B. and Rickert, K. W. (1995) Conformational implications of asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 92, 97–101.

    Article  PubMed  CAS  Google Scholar 

  59. Otvos, L., Thurin, J., Kollat, E., Urge, L., Mantsch, H. M., and Hollosi, M. (1991) Glycosylation of synthetic peptides breaks helices. Int. J. Pept. Protein. Res. 38, 476–482.

    Article  PubMed  CAS  Google Scholar 

  60. Wormald, M. R., and Dwek, R. A. (1991) The conformational effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem. 198, 131–139.

    Article  PubMed  CAS  Google Scholar 

  61. Rickert, K. W., and Imperiali, B. (1995) Analysis of the conserved glycosylation site in the nicotinic acetylcholine receptor: potential roles in complex assembly. Chem. Biol. 2, 751–759.

    Article  PubMed  CAS  Google Scholar 

  62. Davis, S. J., Davies, E. A., Barclay, A. N., Daenke, S., Bodian, D. L., Jones, E. Y., Stuart, D. I., Butters, T. D., Dwek, R. A., van der Merwe, P. A. (1995) Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent. J. Biol. Chem. 270, 369–75.

    Article  PubMed  Google Scholar 

  63. Jones, E. Y., Davis, S. J., Williams, A. F., Harlos, K., and Stuart, D. I. (1992) Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature 360, 232–239.

    Article  PubMed  CAS  Google Scholar 

  64. Lindstedt, R., Larson, G., Falk, P., Jodal, U., Leffler, H., and Svanborg, C. (1991) The receptor repertoire defines the host range for attaching Escherichia coli strains that recognize globo-A. Infect. Immun. 59, 1086–1092.

    PubMed  CAS  Google Scholar 

  65. Collinge, J., Sidle, K., Meads, J., Ironside, J., and Hill, A. (1996) Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 383, 685–690.

    Article  PubMed  CAS  Google Scholar 

  66. Hill, A. F., Desbruslais, M., Joiner, S., Sidle, K. C. L., Gowland, I., Collinge, J., Doey, L. J., and Lantos, P. (1997) The same prion strain causes vCJD and BSE. Nature 389, 448–450.

    Article  PubMed  CAS  Google Scholar 

  67. Somerville, R. A., Chong, A., Mulqueen, O. U., Birkett, C. R., Wood, S. C. E. R., and Hope, J. (1997) Biochemical typing of scrapie strains. Nature 386, 564.

    Article  PubMed  CAS  Google Scholar 

  68. Lehmann, S. and Harris, D. A. (1997) Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 34, 21,479–21,487.

    Article  Google Scholar 

  69. Kreisel, W., Volk, B. A., Buchsel, R., and Reutter, W. (1980) Different halflives of the carbohydrate and protein moieties of a 110,000-dalton glycoprotein isolated from plasma membranes of rat liver. Proc. Natl. Acad. Sci. USA 77, 1828–1831.

    Article  PubMed  CAS  Google Scholar 

  70. Tauber, R., Park, C. S., and Reutter, W. (1983) Intramolecular heterogeneity of degradation in plasma membrane glyocproteins: evidence for a general characteristic. Proc. Natl. Acad. Sci. USA 80, 4026–4029.

    Article  PubMed  CAS  Google Scholar 

  71. McKinley, M. P., Taraboulos, A., Kenaga, L., Serban, D., DeArmond, S. J., Stieber, A., and Prusiner, S. B. (1990) Ultrastructural localization of scrapie prion proteins in secondary lysosomes of infected cultured cells. J. Cell. Biol. 111, 316a.

    Google Scholar 

  72. Tauber, R., Kreisel, W., and Reutter, W. (1991) Oligosaccharide reprocessing of plasma membrane glycoproteins, in Protein Glycosylation: Cellular, Biotechnological and Analytical Aspects (Conradt. H. S., Braunschweig, eds.) Gesellschaft für Biotecnologische Forschung, Germany, pp. 21–32.

    Google Scholar 

  73. Katz, S. A., Opsahl, J. A., Abraham, P. A., and Gardner, M. J. (1994) The relationship between renin isoelectric forms and renin glycoforms. Am. J. Physiol. 267, R244–52.

    PubMed  CAS  Google Scholar 

  74. Nitrini, R., Rosemberg, S., Passos-Bueno, M. R., Teixeira, L. S., Iughetti, P., Papadopoulos, M., et al. (1997) Familial spongiform encephalopathy associated with a novel prion protein gene mutation. Ann. Neurol. 42, 138–146.

    Article  PubMed  CAS  Google Scholar 

  75. Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1996) Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380, 345–347.

    Article  PubMed  CAS  Google Scholar 

  76. Raeber, A. J., Race, R. E., Brandner, S., Priola, S. A., Sailer, A., Bessen, R. A., et al. (1997) Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie. Embo J. 16, 6057–6065.

    Article  PubMed  CAS  Google Scholar 

  77. Rogers, M., Taraboulos, A., Scott, M., Groth, D., and Prusiner, S. B. (1990) Intracellular accumulation of the cellular prion protein after mutagenesis of its Asnlinked glycosylation sites. Glycobiology 1, 101–109.

    Article  PubMed  CAS  Google Scholar 

  78. Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., et al. (1997) The cellular prion protein binds copper in vivo. Nature 390, 684–687.

    Article  PubMed  CAS  Google Scholar 

  79. Stockel, J., Safar, J., Wallace, A. C., Cohen, F. E., and Prusiner, S. B. (1998) Prion protein selectively binds copper (II) tions. Biochemistry 37, 7185–7193.

    Article  PubMed  CAS  Google Scholar 

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  1. Department of Pathology (Neuropathology), University of California, San Francisco, CA

    Stephen J. DeArmond

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  1. Department of Experimental Psychology, MRC Comparative Cognition Team, School of Clinical Veterinary Medicine, Cambridge, UK

    Harry F. Baker

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DeArmond, S.J. (2001). Differential Targeting of Neurons by Prion Strains. In: Baker, H.F. (eds) Molecular Pathology of the Prions. Methods in Molecular Medicine™, vol 59. Humana Press. https://doi.org/10.1385/1-59259-134-5:85

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  • DOI: https://doi.org/10.1385/1-59259-134-5:85

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