Abstract
Prions are proteins generally characterized by the ability to exist in two different forms or more precisely two different three-dimensional structures, one of them possibly causing disease when it aggregates. The prion hypothesis, as formulated by Stanley Prusiner, states that this aggregation causes specific neurological diseases such as bovine spongiform encephalopathy (BSE). Even if both the mechanisms of this change of conformation and that of the aggregation are still enigmatic, the prion hypothesis has become a dominant model to which much heuristic power has been attributed in the 1990s. This could be a first paradox. Moreover, whereas three-dimensional structures clearly appear to be at the heart of the matter, Prusiner used mostly biochemical evidence to develop his hypothesis, without using, in the early days, any other graphic representations than that given by electron microscopy. This constitutes the second paradox at the origin of the present chapter since only computer representations of three-dimensional structures can explain and justify the prion theory as a model. Here, models are defined as theories with two distinct properties. First, models have an explanatory power more or less confirmed by experimental evidence, which distinguishes them from mere hypotheses. Second, models can be applied in domains other than those where they come from. Such application is possible due to the underlying formalism of models, or, as in the prion case, to the diffusion of a specific visualization culture.
A scientific concept that is not supported by direct visualization is always difficult to establish, whatever its origin may be.
D. Dormont
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References
Aguzzi, A. et al. (1997) ‘Neuro-immune Connection in Spread of Prions in the Body?’, The Lancet 349: 742–3.
Aigle, M. and F. Lacroute (1975) ‘Genetical aspects of [URE3], a Non-mitochon- drial, Cytoplasmically Inherited Mutation in Yeast’, Mol. Gen. Genet. 136: 327–35.
Amann, K. and K. Knorr-Cetina (1990) ‘The Fixation of (Visual) Evidence’, in M. Lynch and S. Woolgar (eds) Representation in Scientific Practice. Cambridge: MIT Press: 85–122.
Anfinsen, C. (1973) ‘Principles that Govern the Folding of Protein Chains’, Science 181: 223–30.
Appel, R. D. et al. (1994) ‘A New Generation of Information Retrieval Tools for Biologists: the Example of the ExPASy WWW Server’, Trends Biochem. Sci. 19: 258–60.
Baldwin, M. A. et al. (1998) ‘The Three-dimensional Structure of Prion Protein: Implications for Prion Disease’, Biochemical Society Transactions 26: 481–6.
Bousset, L. et al. (2001) ‘Structure of the Globular Region of the Prion Protein Ure2 from the Yeast Saccharomyces cerevisiae’, Structure (Camb.) 9(1): 39–46.
Bousset, L. et al. (2002) ‘Structure and Assembly Properties of the Yeast Prion Ure2’, C.R. Biologies 325: 3–8.
Brandner, S. et al. (1996) ‘Normal Host Prion Protein (PrPC) is Required for Scrapie Spread within the Central Nervous System’, PNAS USA 93: 13148–51.
Cambrosio, A. (2000) ‘Argumentation, représentation, intervention: les rôles de l’imagerie dans les discours scientifiques’, ASp 27/30: 95–112.
Chernoff, Y. O. et al. (1995) ‘Role of the Chaperone Protein Hspl04 in Propagation of the Yeast Prion-like Factor [psi+]’, Science 268(5212): 880–4.
Corth, C. et al. (1997) ‘Prion (PrPSc)-specific Epitope Defined by a Monoclonal Antibody’, Nature 390(6655): 74–7.
Couzin, J. (2002) ‘In Yeast, Prions’ Killer Image Doesn’t Apply’, Science 297: 758–61.
Cox, B. S. (1965) ‘PSI, a Cytoplasmic Suppressor of Super-suppressor in Yeast’, Heredity 20: 505–21.
Crick, F. (1958) ‘On Protein Synthesis’, in F. K. Sanders (ed.) The Biological Replication of Macromolecules. Cambridge: Cambridge University Press: 138–63.
Donne, D. G. et al. (1997) ‘Structure of the Recombinant Full-length Hamster Prion Protein PrP(29–231): the N Terminus is Highly Flexible’, PNAS USA 94(25): 13452–7.
Fernandez-Bellot, E. and C. Cullin (2001) ‘The Protein-only Theory and the Yeast Saccharomyces cerevisiae: the Prions and the Propagons’, Cell Mol. Life Sci. 58(12–13): 1857–78.
Ferrin, T. E. et al. (1988) ‘The MIDAS Display System’, J. Mol. Graphics 6(1): 13–27, 36–7.
Francoeur, E. (2001) ‘Molecular Models and the Articulation of Structural Constraints in Chemistry’, in U. Klein (ed.) Tools and Modes of Representation in the Laboratory Sciences. Dordrecht: Kluwer Academic Publishers: 95–115.
Francoeur, E. and J. Segal (2004) ‘From Model Kits to Interactive Computer Graphics’, in S. de Chadarevian and N. Hopwood (eds) Models: the Third Dimension of Science. Stanford: Stanford University Press.
Gasset, M. et al. (1992) ‘Predicted Alpha-helical Regions of the Prion Protein when Synthesized as Peptides Form Amyloid’, PNAS USA 89(22): 10940–4.
Glatzel, M. and A. Aguzzi (2000) ‘PrPC Expression in the Peripheral Nervous System is a Determinant of Prion Neuroinvasion’, Journal of General Virology 81: 2813–21.
Glockshuber, R. et al. (1997) ‘Three-dimensional NMR Structure of a Self-folding Domain of the Prion Protein PrP(121–231)’, Trends in Biochemical Sciences 22(7): 241–2.
Griesemer, J. R. (1991) ‘Must Scientific Diagrams Be Eliminable? The Case of Path Analysis’, Biology and Philosophy 6: 155–80.
Güntert, P. et al. (1991) ‘Efficient Computation of Three-dimensional Protein Structures in Solution from Nuclear Magnetic Resonance Data Using the Program DIANA and the Supporting Programs CALIBA, HABAS and GLOMSA’, J. Mol. Biol. 217: 517–30.
Huang, Z. et al. (1994) ‘Proposed Three-dimensional Structure for the Cellular Prion Protein’, PNAS USA 91(15): 7139–43.
Huang, Z. et al. (1996) ‘Structures of Prion Proteins and Conformational Models for Prion Diseases’, Curr. Top. Microbiol. Immunol. 207: 49–67.
James, T. L. et al. (1997) ‘Solution Structure of a 142-residue Recombinant Prion Protein Corresponding to the Infectious Fragment of the Scrapie Isoform’, PNAS USA 94(19): 10086–91.
Johnson, C. K. (1965) OR TEP: a FORTRAN Thermal-ellipsoid Plot Program for Crystal Structure Illustrations. ONRL Report No. 3794. Oak Ridge, Tenn.: Oak Ridge National Laboratory.
Kaneko, K. et al. (1997) ‘Evidence for Protein X Binding to a Discontinuous Epitope on the Cellular Prion Protein during Scrapie Prion Propagation’, PNAS USA 94: 10069–74.
Kay, L. E. (2000) Who Wrote the Book of Life? A History of the Genetic Code. Chicago: University of Chicago Press.
Keyes, M. E. (1999) ‘The Prion Challenge to the “Central Dogma” of Molecular Biology, 1965–1991. Part I: Prelude to Prions’ and ‘Part II: The Problem with Prions’, Studies in History and Philosophy of Biological and Biomedical Sciences 30 (1 and 2): 1–19, 181–218.
Koradi, R. et al. (1996) ‘MOLMOL: a Program for Display and Analysis of Macromolecular Structures’, Journal of Molecular Graphics 14(1): 51–5.
Kuhn, T. S. (1977) The Essential Tension: Selected Studies in Scientific Tradition and Change. Chicago: University of Chicago Press.
Lacroute, F. (1971) ‘Non-Mendelian Mutation Allowing Ureidosuccinic Acid Uptake in Yeast’, J. Bacteriol. 106: 519–22.
Lakoff, G. and M. Johnson (1980) Metaphors We Live By. Chicago: University of Chicago Press.
Latour, B. (1993) ‘Le “Pédofil” De Boa Vista - Montage Photo-Philosophique’, in B. Latour (ed.) La Clef de Berlin. Paris: La Découverte: 171–225.
Latour, B. and S. Woolgar (1979) Laboratory Life: the Social Construction of Scientific Facts. Beverly Hills: Sage Publications.
Levinthal, C. (1966) ‘Molecular Model-Building by Computers’, Scientific American 214: 42–52.
Lynch, M. (1985) ‘Discipline and the Material Form of Images’, Social Studies of Science 15(1): 37–66.
Lynch, M. (1998) ‘The Production of Scientific Images: Vision and Re-Vision in the History, Philosophy, and Sociology of Science’, Communication and Cognition 31(2–3): 213–28.
Martz, E. and E. Francoeur (2001) ‘History of Visualization of Biological Macromolecules’, http://www.umass.edu/microbio/rasmol/history.htm (latest revision 9/2001).
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(5233): 93–5.
Maunoury, M. T. et al. (1999) ‘Observer la science en action ou, comment les sciences de l’information permettent de suivre l’évolution et la convergence des concepts de prion et d’hérédité non mendélienne dans la littérature’, Médecine/Sciences 15(4): 577–82.
Merz, P. et al. (1981) ‘Abnormal Fibrils from Scrapie-infected Brain’, Acta Neuropathologica 54: 63–74.
Merz, P. et al. (1984) ‘Infection-Specific Particle from the Unconventional Slow Virus Diseases’, Science 225: 437–40.
Morange, M. (1998) A History of Molecular Biology. Cambridge: Harvard University Press.
Ottiger, M. et al. (1994) ‘The NMR Solution Structure of the Pheromone Er-2 from the Ciliated Protozoan Euplotes Raikovi’, Protein Science 3: 1515–26.
Pauling, L. et al. (1951) ‘The Structure of Proteins: Two Hydrogen-Bonded Helical Configurations of the Polypeptide Chain’, PNAS USA 37: 205–11.
Prusiner, S. (1982) ‘Novel Proteinaceous Infectious Particles Cause Scrapie’, Science 216: 136–44.
Prusiner, S. (1984) ‘Prions’, Scientific American 251: 48–57.
Prusiner, S. (1988) ‘Molecular Structure, Biology, and Genetics of Prions’, Advances in Virus Research 35: 83–136.
Prusiner, S. (1992) ‘Chemistry and Biology of Prions’, Biochemistry 31(49): 12277–88.
Prusiner, S. (1994) ‘Biology and Genetics of Prion Diseases’, Annu. Rev. Microbiol. 48: 655–86.
Prusiner, S. (1998) ‘Prions’, PNAS USA 95(23): 13363–83.
Prusiner, S. et al. (1983) ‘Scrapie Prions Aggregate to Form Amyloid-like Birefringent Rods’, Cell 35: 349–58.
Prusiner, S. et al. (1987) ‘On the Biology of Prions’, Acta Neuropathologica 72: 299–314.
Raeber, A. J. et al. (1998) ‘Transgenic and Knockout Mice in Research on Prion Diseases’, Brain Pathology 8: 715–33.
Rheinberger, H. J. (1997) Toward a History of Epistemic Things: Synthesizing Proteins in the Test Tube (Writing Science). Stanford: Stanford University Press.
Riek, R. et al. (1996) ‘NMR Structure of the Mouse Prion Protein PrP(121–231)’, Nature 382: 180–2.
Riek, R. et al. (1997) ‘NMR Characterization of the Full-length Recombinant Murine Prion Protein mPrP (23–231)’, FEBS Letters 413: 282–8.
Rudwick, M. J. S. (1976) ‘The Emergence of a Visual Language for Geological Science’, History of Science 14: 149–95.
Sarkar, S. S. (1996) ‘Thinking of Biology - Decoding “Coding” - Information and DNA’, Bioscience 46: 857–64.
Segal, J. (2002) ‘Les premiers “replieurs” français: Michel Goldberg à l’Institut Pasteur et Jeannine Yon à Orsay’, Revue pour l’histoire du CNRS 7: 50–6.
Shulamn, R. G. (2000) ‘D. C. Phillips’, Biographical Memoirs of the National Academy of Sciences. National Academy Press: 166–81 (or http://books.nap.edu/books/030907035X/html/166.html)
Soojung-Kim Pang, A. (1997) ‘Visual Representation and Post-Constructivist History of Science’, Historical Studies in the Physical and Biological Sciences 28: 139–71.
Thieffry, D. (1996) ‘E. coli as a Model System with which to Study Cell- differentiation’, Hist. Philos. Life Sci. 18: 163–93.
Thual, C. et al. (1999) ‘Structural Characterization of Saccharomyces cerevisiae Prion-like Protein Ure2’, J. Biol. Chem. 274(19): 13666–74.
Umland, T. C. et al. (2001) ‘The Crystal Structure of the Nitrogen Regulation Fragment of the Yeast Prion Protein Ure2p’, PNAS USA 98(4): 1459–64.
Wickner, R. B. (1994) ‘[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae’, Science 264(5158): 566–9.
Wickner, R. B. et al. (1995) ‘[PSI] and [URE3] as Yeast Prions’, Yeast 11(16): 1671–85.
Wüthrich, K. (2001) The Way to NMR Structures of Proteins’, Nature Structural Biology 8: 923–5.
Zahn, R. et al. (2000) ‘NMR Solution Structure of the Human Prion Protein’, PNAS USA 97(1): 145–50.
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Segal, J., Francoeur, E. (2004). Visualizing Prions: Graphic Representations and the Biography of Prions. In: Seguin, E. (eds) Infectious Processes. Science, Technology and Medicine in Modern History. Palgrave Macmillan, London. https://doi.org/10.1057/9780230524392_5
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