Advertisement

The Early History of the Protein-only Hypothesis: Scientific Change and Multidisciplinary Research

Chapter
  • 36 Downloads
Part of the Science, Technology and Medicine in Modern History book series (STMMH)

Abstract

In 1997, the American neurologist and biochemist Stanley B. Prusiner received the Nobel Prize in medicine for his discovery of ‘prions’ - a new biological principle of infection. Preceding this discovery lies a complicated history of the research on a number of neurodegenerative diseases, including the sheep disease scrapie. During the 1960s, research on scrapie revealed that the infectious agent had very unusual characteristics, and a variety of hypotheses regarding the principle of scrapie infection were advanced. However, not until the 1980s did a single hypothesis, Prusiner’s prion hypothesis — which is basically a protein-only hypothesis1 — succeed in attracting the attention of the majority of the scientific community. Interestingly, protein-only hypotheses had been advanced as early as the mid-1960s but without receiving any notable support from other scientists than those who had advanced them.

Keywords

Infectious Agent Prion Protein Prion Disease Bovine Spongiform Encephalopathy Central Dogma 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adams, D. H. and E. A. Caspary (1967) ‘Nature of the Scrapie Virus’, British Medical Journal 3: 173.CrossRefGoogle Scholar
  2. Adams, D. H. and E. J. Field (1968) ‘The Infective Process in Scrapie’, Lancet 2: 714–16.CrossRefGoogle Scholar
  3. Alper, T. et al. (1966) ‘The Exceptionally Small Size of the Scrapie Agent’, Biochemical and Biophysical Research Communications 22: 278–84.Google Scholar
  4. Alper, T. et al. (1967) ‘Does the Agent of Scrapie Replicate without Nucleic Acid?’, Nature 214: 764–6.CrossRefGoogle Scholar
  5. Alper, T. et al. (1978) ‘The Scrapie Agent: Evidence against its Dependence for Replication on Intrinsic Nucleic Acid’, Journal of General Virology 41: 503–16.CrossRefGoogle Scholar
  6. Andersen, H. (1996) ‘Categorization, Anomalies, and the Discovery of Nuclear Fission’, Studies in the History and Philosophy of Modem Physics 27: 463–92.CrossRefGoogle Scholar
  7. Baltimore, D. (1970) ‘Viral RNA-dependent DNA Polymerase’, Nature 226: 1209–11.CrossRefGoogle Scholar
  8. Barker, P. et al. (2002) ‘Kuhn on Concepts and Categorization’, in T. Nickles (ed.) Thomas Kuhn. Cambridge: Cambridge University Press: 212–45.CrossRefGoogle Scholar
  9. Barry, R. A. et al. (1986) ‘Scrapie and Cellular Prion Proteins Share Polypeptide Epitopes’, Journal of Infectious Diseases 153: 848–54.CrossRefGoogle Scholar
  10. Basler, K. et al. (1986) ‘Scrapie and Cellular Prp Isoforms Are Encoded by the Same Chromosomal Gene’, Cell 46: 417–28.CrossRefGoogle Scholar
  11. Bastian, F. O. (1979) ‘Spiroplasma-like Inclusions in Creutzfeldt-Jakob Disease’, Archives of Pathology and Laboratory Medicine 103: 665–9.Google Scholar
  12. Bellinger-Kawahara, C. et al. (1987a) ‘Purified Scrapie Prions Resist Inactivation by Uv Irradiation’, Journal of Virology 61: 159–66.Google Scholar
  13. Bellinger-Kawahara, C. et al. (1987b) ‘Purified Scrapie Prions Resist Inactivation by Procedures That Hydrolyze, Modify, or Shear Nucleic Acids’, Virology 160: 271–4.CrossRefGoogle Scholar
  14. Bellinger-Kawahara, C. G. et al. (1988) ‘Scrapie Prion Liposomes and Rods Exhibit Target Sizes of 55,000 Da’, Virology 164: 537–41.CrossRefGoogle Scholar
  15. Bolton, D. C. and P. E. Bendheim (1988) ‘A Modified Host Protein Model of Scrapie’, Ciba Foundation Symposium 135: 164–81.Google Scholar
  16. Bolton, D. C. et al. (1982) ‘Identification of a Protein That Purifies with the Scrapie Prion’, Science 218: 1309–11.CrossRefGoogle Scholar
  17. Cantor, G. N. (1975) ‘The Edinburgh Phrenology Debate’, Ann. Sci. 32: 195–218.CrossRefGoogle Scholar
  18. Chandler, R. L. (1959) ‘Attempts to Demonstrate Antibodies in Scrapie Disease’, Veterinary Record 71: 58–9.Google Scholar
  19. Chandler, R. L. (1961) ‘Encephalopathy in Mice Produced by Inoculation with Scrapie Brain Material’, Lancet 1: 1378–9.CrossRefGoogle Scholar
  20. Chesebro, B. et al. (1985) ‘Identification of Scrapie Prion Protein-Specific Messenger-RNA in Scrapie-Infected and Uninfected Brain’, Nature 315: 331–3.CrossRefGoogle Scholar
  21. Cuillé, J. and P. L. Chelle (1936) ‘La Maladie Dite Tremblante du Mouton. Est-elle Inoculable?’, Comptes Rendus Heb. des Séances de lAcadémie des Sciences 203: 1552–4.Google Scholar
  22. Cuillé, J. and P. L. Chelle (1939) ‘Transmission Expérimentale de la Tremblante à La Chèvre’, Comptes Rendus Heb. des Séances de lAcadémie des Sciences 208: 1058–60.Google Scholar
  23. Darden, L. (1992) ‘Strategies for Anomaly Resolution’, in R. Giere (ed.) Cognitive Models of Science. Minnesota Studies in the Philosophy of Science Vol. XV, Minneapolis: University of Minnesota Press: 251–73.Google Scholar
  24. Darden, L. (1998) ‘Exemplars, Abstractions, and Anomalies: Representation and Theory Change in Mendelian and Molecular Genetics’, in G. Wolters, J. G. Lennox and P. McLaughlin (eds) Concepts, Theories and Rationality in the Biological Sciences: the Second Pittsburgh-Konstanz Colloquium in the Philosophy of Science. Konstanz/Pittsburgh: Universitätsverlag Konstanz/University of Pittsburgh Press: 137–58.Google Scholar
  25. Diener, T. O. (1972) ‘Is the Scrapie Agent a Viroid?’, Nature - New Biology 235: 218–19.CrossRefGoogle Scholar
  26. Diener, T. O. (1973) ‘Similarities between the Scrapie Agent and the Agent of the Potato Spindle Tuber Disease’, Annals of Clinical Research 5: 268–78.Google Scholar
  27. Eklund, C. M. et al. (1967) ‘Pathogenesis of Scrapie Virus Infection in the Mouse’, Journal of Infectious Diseases 117: 15–22.CrossRefGoogle Scholar
  28. Feyerabend, P. K. (1970) ‘Consolations for the Specialist’, in I. Lakatos and A. Musgrave (eds) Criticism and the Growth of Knowledge. Cambridge: Cambridge University Press: 197–230.Google Scholar
  29. Field, E. J. (1966) ‘Transmission Experiments with Multiple Sclerosis: an Interim Report’, British Medical Journal 2: 564–5.CrossRefGoogle Scholar
  30. Gajdusek, D. C. and C. J. Gibbs (1968) ‘Infections of the Nervous System’, Research Publications Association for Research in Nervous and Mental Disease 44: 259.Google Scholar
  31. Gajdusek, D. C. et al. (1966) ‘Experimental Transmission of a Kuru-like Syndrome to Chimpanzees’, Nature 209: 794–6.CrossRefGoogle Scholar
  32. Gibbons, R. A. and G. D. Hunter (1967) ‘Nature of the Scrapie Agent’, Nature 215: 1041–3.CrossRefGoogle Scholar
  33. Gibbs, C. J. and D. C. Gajdusek (1969) ‘Infection as the Etiology of Spongiform Encephalopathy (Creutzfeldt-Jakob Disease)’, Science 165: 1023–5.CrossRefGoogle Scholar
  34. Gibbs, C. J. et al. (1968) ‘Creutzfeldt-Jakob Disease (Spongiform Encephalopathy): Transmission to the Chimpanzee’, Science 161: 388–9.CrossRefGoogle Scholar
  35. Gordon, W. S. (1946) ‘Advances in Veterinary Research’, Veterinary Record 58: 516–20.Google Scholar
  36. Greig, J. Russell (1950) ‘Scrapie in Sheep’, Journal of Comparative Pathology 60: 263–6.CrossRefGoogle Scholar
  37. Griffith, J. S. (1967) ‘Self-replication and Scrapie’, Nature 215: 1043–4.CrossRefGoogle Scholar
  38. Griffith, J. S. (1968a) ‘Mathematics of Cellular Control Processes. I. Negative Feedback to One Gene’, Journal of Theoretical Biology 20: 202–8.CrossRefGoogle Scholar
  39. Griffith, J. S. (1968b) ‘Mathematics of Cellular Control Processes. II. Positive Feedback to One Gene’, Journal of Theoretical Biology 20: 209–16.CrossRefGoogle Scholar
  40. Hadlow, W. J. (1959) ‘Scrapie and Kuru’, Lancet 2: 289–90.CrossRefGoogle Scholar
  41. Haig, D. A. et al. (1969) ‘Further Studies on the Inactivation of the Scrapie Agent by Ultraviolet Light’, Journal of General Virology 5: 455–7.CrossRefGoogle Scholar
  42. Hay, B. et al. (1987) ‘Evidence for a Secretory Form of the Cellular Prion Protein’, Biochemistry 26: 8110–15.CrossRefGoogle Scholar
  43. Hsiao, K. et al. (1989) ‘Linkage of a Prion Protein Missense Variant to Gerstmann-Straussler Syndrome’, Nature 338: 342–5.CrossRefGoogle Scholar
  44. Hull, D. et al. (1978) ‘Planck’s Principle. Do Younger Scientists Accept New Scientific Ideas with Greater Alacrity than Older Scientists?’, Science 202: 717–23.CrossRefGoogle Scholar
  45. Hunter, G. D. (1969) ‘The Size and Intracellular Location of the Scrapie Agent’, Biochemical Journal 114: 22P–23P.CrossRefGoogle Scholar
  46. Hunter, G. D. (1992) ‘The Search for the Scrapie Agent: 1961–1981’, in S. B. Prusiner et al. (eds) Prion Diseases of Humans and Animals. New York: Ellis Horwood: 23–9.Google Scholar
  47. Hunter, G. D. and G. C. Millson (1964) ‘Studies on the Heat Stability and Chromatographic Behaviour of the Scrapie Agent’, Journal of General Microbiology 37: 251–8.CrossRefGoogle Scholar
  48. Keyes, M. E. (1999a) ‘The Prion Challenge to the “Central Dogma” of Molecular Biology, 1965–1991. Part I: Prelude to Prions’, Studies in the History and Philosophy of Biological and Biomedical Sciences 30: 1–20.CrossRefGoogle Scholar
  49. Keyes, M. E. (1999b) ‘The Prion Challenge to the “Central Dogma” of Molecular Biology, 1965–1991. Part II: The Problem with Prions’, Studies in the History and Philosophy of Biological and Biomedical Sciences 30: 181–218.CrossRefGoogle Scholar
  50. Klatzo, I. et al. (1959) ‘Pathology of Kuru’, Laboratory Investigation 8: 799–847.Google Scholar
  51. Kuhn, T. S. (1962) The Structure of Scientific Revolutions, 2nd edn 1970. Chicago: University of Chicago Press.Google Scholar
  52. Lakatos, I. (1970) ‘Falsification and the Methodology of Research Programmes’, in I. Lakatos and A. Musgrave (eds) Criticism and the Growth of Knowledge. Cambridge: Cambridge University Press: 91–196.Google Scholar
  53. Laudan, L. (1977) Progress and Its Problems. Berkeley: University of California Press.Google Scholar
  54. Laurent, M. (1997) ‘Autocatalytic Processes in Cooperative Mechanisms of Prion Diseases’, FEBS Letters 407: 1–6.CrossRefGoogle Scholar
  55. M’Fadyean, J. (1918) ‘Scrapie’, Journal of Comparative Pathology and Therapeutics 31: 102–31.CrossRefGoogle Scholar
  56. M’Gowan, J. P. (1914) Investigation into the Disease of Sheep called ‘Scrapie’. Edinburgh: William Blackwood.Google Scholar
  57. Mckinley, M. P. et al. (1983) ‘A Protease-Resistant Protein Is a Structural Component of the Scrapie Prion’, Cell 35: 57–62.CrossRefGoogle Scholar
  58. McMullin, E. (1992) ‘Rationality and Paradigm Change in Science’, in P. Horwich (ed.) World Changes. Cambridge, Mass.: MIT Press: 55–80.Google Scholar
  59. Masiarz, F. R. et al. (1980) ‘Purification of the Scrapie Agent-Strategy and Recent Progress’, in A. Boese (ed.) Search for the Cause of Multiple Sclerosis and other Chronic Diseases of the Central Nervous System. Weinheim: Verlag Chemie: 321–32.Google Scholar
  60. Messeri, P. (1988) ‘Age Differences in the Reception of New Scientific Theories: the Case of Plate Tectonics’, Social Studies of Science 18: 91–112.CrossRefGoogle Scholar
  61. Narang, H. K. (1974) ‘Ruthenium Red and Lanthanum Nitrate a Possible Tracer and Negative Stain for Scrapie “Particles”?’, Acta Neuropathologica 29: 37–43.CrossRefGoogle Scholar
  62. Oesch, B. et al. (1985) ‘A Cellular Gene Encodes Scrapie Prp 27–30 Protein’, Cell 40: 735–46.CrossRefGoogle Scholar
  63. Oesch, B. et al. (1988) ‘Search for a Scrapie-specific Nucleic Acid: a Progress Report’, Ciba Foundation Symposium 135: 209–23.Google Scholar
  64. Parry, H. B. (1962) ‘Scrapie: a Transmissible and Hereditary Disease of Sheep’, Heredity 17: 75–105.CrossRefGoogle Scholar
  65. Pattison, I. H. (1965) ‘Resistance of the Scrapie Agent to Formalin’, Journal of Comparative Pathology 75: 159–64.CrossRefGoogle Scholar
  66. Pattison, I. H. (1966a) ‘Experiments with Scrapie with Special Reference to the Nature of the Agent and the Pathology of the Disease’, in D. C. Gajdusek et al. (eds) Slow, Latent, and Temperate Virus Infections. NINDB monograph No. 2. Public health service publication: 249–57.Google Scholar
  67. Pattison, I. H. (1966b) ‘The Relative Susceptibility of Sheep, Goats and Mice to Two Types of the Goat Scrapie Agent’, Research in Veterinary Science 7: 207–12.Google Scholar
  68. Pattison, I. H. (1970) ‘Recent Work on Scrapie’, Pathologie Biologie 18: 673–8.Google Scholar
  69. Pattison, I. H. (1988) ‘Fifty Years with Scrapie: a Personal Reminiscence’, Veterinary Record 123: 661–6.CrossRefGoogle Scholar
  70. Pattison, I. H. (1992) ‘A Sideways Look at the Scrapie Saga: 1732–1991’, in S. B. Prusiner et al. (eds) Prion Diseases of Humans and Animals. New York: Ellis Horwood: 15–22.Google Scholar
  71. Pattison, I. H. and K. M. Jones. (1967) ‘The Possible Nature of the Transmissible Agent of Scrapie’, Veterinary Record 80: 2–9.CrossRefGoogle Scholar
  72. Pattison, I. H. and G. C. Millson (1960) ‘Further Observations on the Experimental Production of Scrapie in Goats and Sheep’, fournal of Comparative Pathology and Therapeutics 70: 182–93.CrossRefGoogle Scholar
  73. Pattison, I. H. and Millson, G. C. (1961a) ‘Further Experimental Observations on Scrapie’, Journal of Comparative Pathology and Therapeutics 71: 350–9.CrossRefGoogle Scholar
  74. Pattison, I. H. and G. C. Millson (1961b) ‘Scrapie Produced Experimentally in Goats with Special Reference to the Clinical Syndrome’, Journal of Comparative Pathology and Therapeutics 71: 101–8.CrossRefGoogle Scholar
  75. Penrose, L. S. and R. Penrose (1957) ‘A Self-reproducing Analogue’, Nature 179: 1183.CrossRefGoogle Scholar
  76. Prusiner, S. B. (1982) ‘Novel Proteinaceous Infectious Particles Cause Scrapie’, Science 216: 136–44.CrossRefGoogle Scholar
  77. Prusiner, S. B. (1984) ‘Prions’, Scientific American 251: 48–57.CrossRefGoogle Scholar
  78. Prusiner, S. B. (1991) ‘Molecular-Biology of Prion Diseases’, Science 252: 1515–22.CrossRefGoogle Scholar
  79. Prusiner, S. B. (1995) ‘The Prion Diseases’, Scientific American 272: 30–7.CrossRefGoogle Scholar
  80. Prusiner, S. B. (1999) ‘Development of the Prion Concept’, in S. B. Prusiner (ed.) Prion Biology and Diseases. New York: Cold Spring Harbor Laboratory Press: 67–112.Google Scholar
  81. Prusiner, S. B. et al. (1981) ‘Scrapie Agent Contains a Hydrophobic Protein’, Proceedings of the National Academy of Sciences of the United States of America - Biological Sciences 78: 6675–9.CrossRefGoogle Scholar
  82. Prusiner, S. B. et al. (1982) ‘Further Purification and Characterization of Scrapie Prions’, Biochemistry 21: 6942–50.CrossRefGoogle Scholar
  83. Prusiner, S. B. et al. (1990) ‘Transgenetic Studies Implicate Interactions between Homologous PRP Isoforms in Scrapie Prion Replication’, Cell 63: 673–86.CrossRefGoogle Scholar
  84. Rappa, M. and K. Debackere (1993) ‘Youth and Scientific Innovation: the Role of Young Scientists in the Development of a New Field’, Minerva 31: 1–20.CrossRefGoogle Scholar
  85. Rohwer, R. G. and D. C. Gajdusek (1980) ‘Scrapie - Virus or Viroid. The Case for a Virus’, in A. Boese (ed.) Search for the Cause of Multiple Sclerosis and other Chronic Diseases of the Central Nervous System. Weinheim: Verlag Chemie: 333–55.Google Scholar
  86. Scott, M. et al. (1989) ‘Transgenic Mice Expressing Hamster Prion Protein Produce Species-Specific Scrapie Infectivity and Amyloid Plaques’, Cell 59: 847–57.CrossRefGoogle Scholar
  87. Sigurdsson, B. (1954) ‘Rida, a Chronic Encephalitis of Sheep’, British Veterinary Journal 110: 341–54.Google Scholar
  88. Stamp, J. T. (1962) ‘Scrapie: a Transmissible Disease of Sheep’, Veterinary Record 74: 357–62.Google Scholar
  89. Stamp, J. T. (1967) ‘Scrapie and its Wider Implications’, British Medical Bulletin 23: 133–7.Google Scholar
  90. Stockman, S. (1926) ‘Contribution to the Study of the Disease Known as Scrapie’, Journal of Comparative Pathology and Therapeutics 39: 42–71.CrossRefGoogle Scholar
  91. Temin, H. M. and S. Mizutani (1970) ‘RNA-dependent DNA-polymerase in Virions of Rous Sarcoma Virus’, Nature 226: 1211–13.CrossRefGoogle Scholar
  92. Toulmin, S. (1972) Human Understanding, Vol. 1. Princeton, NJ: Princeton University Press.Google Scholar
  93. Yost, C. S. et al. (1990) ‘Non-hydrophobic Extracytoplasmic Determinant of Stop Transfer in the Prion Protein’, Nature 343: 669–72.CrossRefGoogle Scholar

Copyright information

© Palgrave Macmillan, a division of Macmillan Publishers Limited 2004

Authors and Affiliations

There are no affiliations available

Personalised recommendations