Abstract
Prions, once dismissed as an impossibility, have now gained wide recognition as extraordinary pathogens that cause a number of infectious, genetic and sporadic disorders. Prions are composed only of a protein which is encoded by a chromosomal gene. This protein, designated PrP, is converted from a normal benign form into a disease causing form by a change in conformation. Prions cause bovine spongiform encephalopathy in cattle, scrapie in sheep, and four fatal CNS diseases in humans. Currently, there is no known treatment for prion diseases, and the fear that prions have passed from cattle to humans may be justified.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Alper, T., Cramp, W.A., Haig, D.A. and Clarke, M.C. Does the agent of scrapie replicate without nucleic acid? Nature 214: 764–766 (1967).
Anderson, R.M., Donnelly, C.A., Ferguson, N.M., Woolhouse, M.E.J., Watt, C.J., Udy, H.J., MaWhinney, S., Dunstan, S.P., Southwood, T.R.E., Wilesmith, J.W., Ryan, J.B.M., Hoinville, L.J., Hillerton, J.E., Austin, A.R. and Wells, G.A.H. Transmission dynamics and epidemiology of BSE in British cattle. Nature 382: 779–788 (1996).
Bessen, R. A. and Marsh, R.F. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J Gen Virol 73: 329–334 (1992).
Bolton, D.C., McKinley, M.P. and Prusiner, S.B. Identification of a protein that purifies with the scrapie prion. Science 218: 1309–1311 (1982).
Bruce, M., Chree, A., McConnell, I., Foster, J., Pearson, G. and Fraser, H. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Phil Trans R Soc LondB 343: 405–411 (1994).
Büeler, H., Aguzzi, A., Sailer, A., Greiner, R.-A., Autenried, P., Aguet, M. and Weissmann, C. Mice devoid of PrP are resistant to scrapie. Cell 73: 1339–1347 (1993).
Cousens, S.N., Vynnycky, E., Zeidler, M., Will, R.G. and Smith, P.G. Predicting the CJD epidemic in humans. Nature 385: 197–198 (1997).
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. J Comp Pathol 78: 293–299 (1968).
Gajdusek, D.C. Unconventional viruses and the origin and disappearance of kuru. Science 197: 943–960 (1977).
Hsiao, K., Baker, H.F., Crow, T.J., Poulter, M., Owen, F., Terwilliger, J.D., Westaway, D., Ott, J. and Prusiner, S.B. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 338: 342–345 (1989).
Huang, Z., Prusiner, S.B. and Cohen, F.E. Scrapie prions: a three-dimensional model of an infectious fragment. Folding & Design 1: 13–19 (1996).
Lasmézas, C.I., Deslys, J.-P., Demaimay, R., Adjou, K.T., Lamoury, F., Dormont, D., Robain, O., Ironside, J. and Hauw, J.-J. BSE transmission to macaques. Nature 381: 743–744 (1996).
Prusiner, S.B. Novel proteinaceous infectious particles cause scrapie. Science 216: 136–144 (1982).
Prusiner, S.B. Prions. Sci Am 251: 50–59 (1984).
Prusiner, S.B. The prion diseases. Sci Am 272: 48–57 (1995).
Prusiner, S.B, Prions, in: Fields Virology, B.N. Fields, D.M. Knipe and P.M. Howley, eds., Raven Press, New York (1996).
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R. and Wüthrich, K. NMR structure of the mouse prion protein domain PrP (121-231). Nature 382: 180–182 (1996).
Telling, G.C., Scott, M., Mastrianni, J., Gabizon, R., Torchia, M., Cohen, F.E., DeArmond, S.J. and Prusiner, S.B. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83: 79–90 (1995).
Telling, G.C., Haga, T., Torchia, M., Tremblay, P., DeArmond, S.J. and Prusiner, S.B. Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes & Dev 10: 1736–1750 (1996).
Telling, G.C., Parchi, P., DeArmond, S.J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J., Lugaresi, E., Gambetti, P. and Prusiner, S.B. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 214: 2079–2082 (1996).
Westaway, D., Goodman, P.A., Mirenda, C.A., McKinley, M.P., Carlson, G.A. and Prusiner, S.B. Distinct prion proteins in short and long scrapie incubation period mice. Cell 51: 651–662 (1987).
Wickner, R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264: 566–569 (1994).
Will, R.G., Ironside, J.W., Zeidler, M., Cousens, S.N., Estibeiro, K., Alperovitch, A., Poser, S., Pocchiari, M., Hofman, A. and Smith, P.G. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347: 921–925 (1996).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Prusiner, S.B. (1998). Prion Biology and Diseases — Fatal Conformations of Proteins during a Journey from Heresy to Orthodoxy. In: Morrison, D.R.O. (eds) Prions and Brain Diseases in Animals and Humans. NATO ASI Series, vol 295. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1896-3_14
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1896-3_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1898-7
Online ISBN: 978-1-4899-1896-3
eBook Packages: Springer Book Archive