Griffith, J. S. Self-replication and scrapie. Nature215, 1043–1044 (1967). CASPubMed Google Scholar
Wickner, R. B., Edskes, H. K., Shewmaker, F. & Nakayashiki, T. Prions of fungi: inherited structures and biological roles. Nature Rev. Microbiol.5, 611–618 (2007). CAS Google Scholar
Collinge, J. & Clarke, A. R. A general model of prion strains and their pathogenicity. Science318, 930–936 (2007). CASPubMed Google Scholar
Nemecek, J., Nakayashiki, T. & Wickner, R. B. A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen. Proc. Natl Acad. Sci. USA106, 1892–1896 (2009). CASPubMedPubMed Central Google Scholar
Wickner, R. B. [_URE3_] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science264, 566–569 (1994). The first experimental proof that a non-Mendelian element (in this case [URE3]) in yeast can be explained by the 'protein only' or prion hypothesis. CASPubMed Google Scholar
Michelitsch, M. D. & Weissman, J. S. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl Acad. Sci. USA97, 11910–11915 (2000). Google Scholar
Alberti, S., Halfmann, R., King, O., Kapila, A. & Lindquist, S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell137, 146–158 (2009). A comprehensive study that reveals the diversity of potential prions in yeast and provides direct experimental proof for [MOT3+], the prion form of the transcriptional co-repressor Mot3. CASPubMedPubMed Central Google Scholar
Cox, B. Ψ, a cytoplasmic suppressor of super-suppression in yeast. Heredity20, 505–521 (1965). Google Scholar
Culbertson, M. R., Charnas, L., Johnson, M. T. & Fink, G. R. Frameshifts and frameshift suppressors in Saccharomyces cerevisiae. Genetics86, 745–764 (1977). CASPubMedPubMed Central Google Scholar
Patino, M. M., Liu, J. J., Glover, J. R. & Lindquist, S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science273, 622–626 (1996). CASPubMed Google Scholar
Paushkin, S. V., Kushnirov, V. V., Smirnov, V. N. & Ter-Avanesyan, M. D. Propagation of the yeast prion-like [PSI+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J.15, 3127–3134 (1996). CASPubMedPubMed Central Google Scholar
Chen, B., Newnam, G. P. & Chernoff, Y. O. Prion species barrier between the closely related yeast proteins is detected despite coaggregation. Proc. Natl Acad. Sci. USA104, 2791–2796 (2007). Using the [PSI+] yeast prion system, the authors show that the barrier to interspecies prion transmission occurs at the point of conformational replication rather than by the binding of two different conformers. CASPubMedPubMed Central Google Scholar
Eaglestone, S. S., Cox, B. S. & Tuite, M. F. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism. EMBO J.18, 1974–1981 (1999). CASPubMedPubMed Central Google Scholar
True, H. L., Berlin, I. & Lindquist, S. L. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature431, 184–187 (2004). CASPubMed Google Scholar
True, H. L. & Lindquist, S. L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature407, 477–483 (2000). An analysis of a range of phenotypes that differentiate [PSI+] from [psi−] cells. The authors propose that the [PSI+] prion provides the means to uncover hidden genetic variation and produce new heritable phenotypes.
Williams, I., Richardson, J., Starkey, A. & Stansfield, I. Genome-wide prediction of stop codon readthrough during translation in the yeast Saccharomyces cerevisiae. Nucleic Acids Res.32, 6605–6616 (2004). CASPubMedPubMed Central Google Scholar
Wilson, M. A., Meaux, S., Parker, R. & van Hoof, A. Genetic interactions between [PSI+] and nonstop mRNA decay affect phenotypic variation. Proc. Natl Acad. Sci. USA102, 10244–10249 (2005). CASPubMedPubMed Central Google Scholar
Palanimurugan, R., Scheel, H., Hofmann, K. & Dohmen, R. J. Polyamines regulate their synthesis by inducing expression and blocking degradation of ODC antizyme. EMBO J.23, 4857–4867 (2004). CASPubMedPubMed Central Google Scholar
Namy, O. et al. Epigenetic control of polyamines by the prion [PSI+]. Nature Cell Biol.10, 1069–1075 (2008). The authors show that [PSI+] enhances the synthesis of antizyme, a regulator of polyamine synthesis, through a −1 frameshift event. This in turn leads to the modulation of the levels of polyamines in the yeast cell that can lead to a range of phenotypes, including some of those described in reference 17. CASPubMed Google Scholar
Namy, O., Duchateau-Nguyen, G. & Rousset, J. P. Translational readthrough of the PDE2 stop codon modulates cAMP levels in Saccharomyces cerevisiae. Mol. Microbiol.43, 641–652 (2002). CASPubMed Google Scholar
Du, Z., Park, K. W., Yu, H., Fan, Q. & Li, L. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nature Genet.40, 460–465 (2008). This article describes a yeast prion that is formed by a key chromatin remodelling factor and thus reveals a possible link between global transcriptional regulation and the ability of Swi1 to undergo conformational conversion. CASPubMed Google Scholar
Patel, B. K., Gavin-Smyth, J. & Liebman, S. W. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nature Cell Biol.11, 344–349 (2009). CASPubMed Google Scholar
Hongay, C., Jia, N., Bard, M. & Winston, F. Mot3 is a transcriptional repressor of ergosterol biosynthetic genes and is required for normal vacuolar function in Saccharomyces cerevisiae. EMBO J.21, 4114–4124 (2002). CASPubMedPubMed Central Google Scholar
Lempiäinen, H. & Shore, D. Growth control and ribosome biogenesis. Curr. Opin. Cell Biol.21, 855–863 (2009). PubMed Google Scholar
Courchesne, W. E. & Magasanik, B. Regulation of nitrogen assimilation in Saccharomyces cerevisiae: roles of the URE2 and GLN3 genes. J. Bacteriol.170, 708–713 (1988). CASPubMedPubMed Central Google Scholar
Cunningham, T. S., Andhare, R. & Cooper, T. G. Nitrogen catabolite repression of DAL80 expression depends on the relative levels of Gat1p and Ure2p production in Saccharomyces cerevisiae. J. Biol. Chem.275, 14408–14414 (2000). CASPubMed Google Scholar
Rai, R., Tate, J. J. & Cooper, T. G. Ure2, a prion precursor with homology to glutathione _S_-transferase, protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity. J. Biol. Chem.278, 12826–12833 (2003). CASPubMed Google Scholar
Rogoza, T. et al. Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1. Proc. Natl Acad. Sci. USA107, 10573–10577 (2010). CASPubMedPubMed Central Google Scholar
Saupe, S. J. A short history of small s: a prion of the fungus Podospora anserina. Prion1, 110–115 (2007). PubMedPubMed Central Google Scholar
Coustou, V., Deleu, C., Saupe, S. & Begueret, J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl Acad. Sci. USA94, 9773–9778 (1997). CASPubMedPubMed Central Google Scholar
Paoletti, M. & Saupe, S. J. Fungal incompatibility: evolutionary origin in pathogen defense? Bioessays31, 1201–1210 (2009). CASPubMed Google Scholar
Greenwald, J. et al. The mechanism of prion inhibition by HET-S. Mol. Cell38, 889–899 (2010). The authors show that the inhibition of the fibrillization ofP. anserinaHET-s by the closely related HET-S protein is not encoded by the structural differencesper se. Instead, it reflects an effect on the stability and oligomerization properties of the mixed aggregates formed between the two proteins. CASPubMedPubMed Central Google Scholar
Sondheimer, N. & Lindquist, S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell5, 163–172 (2000). CASPubMed Google Scholar
Derkatch, I. L., Bradley, M. E., Hong, J. Y. & Liebman, S. W. Prions affect the appearance of other prions: the story of [PIN+]. Cell106, 171–182 (2001). CASPubMed Google Scholar
Osherovich, L. Z. & Weissman, J. S. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion. Cell106, 183–194 (2001). CASPubMed Google Scholar
Resende, C. G., Outeiro, T. F., Sands, L., Lindquist, S. & Tuite, M. F. Prion protein gene polymorphisms in Saccharomyces cerevisiae. Mol. Microbiol.49, 1005–1017 (2003). CASPubMed Google Scholar
Nakayashiki, T., Kurtzman, C. P., Edskes, H. K. & Wickner, R. B. Yeast prions [_URE3_] and [PSI+] are diseases. Proc. Natl Acad. Sci. USA102, 10575–10580 (2005). This paper opens up the debate about the impact of yeast prions on the host and argues that because neither the [URE3] nor [PSI+] prions are present in 70 different wild strains, they must have a negative effect on the host. CASPubMedPubMed Central Google Scholar
Derkatch, I. L. et al. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc. Natl Acad. Sci. USA101, 12934–12939 (2004). CASPubMedPubMed Central Google Scholar
Derkatch, I. L. et al. Dependence and independence of [PSI+] and [PIN+]: a two-prion system in yeast? EMBO J.19, 1942–1952 (2000). CASPubMedPubMed Central Google Scholar
Dalstra, H. J., Swart, K., Debets, A. J., Saupe, S. J. & Hoekstra, R. F. Sexual transmission of the [Het-S] prion leads to meiotic drive in Podospora anserina. Proc. Natl Acad. Sci. USA100, 6616–6621 (2003). CASPubMedPubMed Central Google Scholar
Ter-Avanesyan, M. D. et al. Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol. Microbiol.7, 683–692 (1993). CASPubMed Google Scholar
Griswold, C. K. & Masel, J. Complex adaptations can drive the evolution of the capacitor [_PSI_], even with realistic rates of yeast sex. PLoS Genet.5, e1000517 (2009). PubMedPubMed Central Google Scholar
Joseph, S. B. & Kirkpatrick, M. Effects of the [PSI+] prion on rates of adaptation in yeast. J. Evol. Biol.21, 773–780 (2008). CASPubMed Google Scholar
Brundin, P., Melki, R. & Kopito, R. Prion-like transmission of protein aggregates in neurodegenerative diseases. Nature Rev. Mol. Cell Biol.11, 301–307 (2010). CAS Google Scholar
Meyer-Luehmann, M. et al. Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host. Science313, 1781–1784 (2006). CASPubMed Google Scholar
Ren, P. H. et al. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nature Cell Biol.11, 219–225 (2009). CASPubMed Google Scholar
Li, J. Y. et al. Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nature Med.14, 501–503 (2008). CASPubMed Google Scholar
Aguzzi, A. Cell biology: Beyond the prion principle. Nature459, 924–925 (2009). CASPubMed Google Scholar
Glabe, C. G. Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. Neurobiol. Aging27, 570–575 (2006). CASPubMed Google Scholar
Si, K., Choi, Y. B., White-Grindley, E., Majumdar, A. & Kandel, E. R. Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation. Cell140, 421–435 (2010). CASPubMed Google Scholar
Fowler, D. M. et al. Functional amyloid formation within mammalian tissue. PLoS Biol.4, e6 (2006). PubMed Google Scholar
Berson, J. F. et al. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol.161, 521–533 (2003). CASPubMedPubMed Central Google Scholar
Maji, S. K. et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science325, 328–332 (2009). CASPubMedPubMed Central Google Scholar
Aguzzi, A., Baumann, F. & Bremer, J. The prion's elusive reason for being. Annu. Rev. Neurosci.31, 439–477 (2008). CASPubMed Google Scholar
Mallucci, G. R. et al. Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron53, 325–335 (2007). CASPubMed Google Scholar
White, M. D. et al. Single treatment with RNAi against prion protein rescues early neuronal dysfunction and prolongs survival in mice with prion disease. Proc. Natl Acad. Sci. USA105, 10238–10243 (2008). CASPubMedPubMed Central Google Scholar
Steele, A. D., Lindquist, S. & Aguzzi, A. The prion protein knockout mouse: a phenotype under challenge. Prion1, 83–93 (2007). PubMedPubMed Central Google Scholar
Isaacs, J. D., Jackson, G. S. & Altmann, D. M. The role of the cellular prion protein in the immune system. Clin. Exp. Immunol.146, 1–8 (2006). CASPubMedPubMed Central Google Scholar
Wilson, D. A. & Nixon, R. A. Sniffing out a function for prion proteins. Nature Neurosci.12, 7–8 (2009). CASPubMed Google Scholar
Malaga-Trillo, E. et al. Regulation of embryonic cell adhesion by the prion protein. PLoS Biol.7, e55 (2009). PubMed Google Scholar
Bremer, J. et al. Axonal prion protein is required for peripheral myelin maintenance. Nature Neurosci.13, 310–318 (2010). CASPubMed Google Scholar
Westergard, L., Christensen, H. M. & Harris, D. A. The cellular prion protein (PrPC): its physiological function and role in disease. Biochim. Biophys. Acta1772, 629–644 (2007). CASPubMedPubMed Central Google Scholar
Shmerling, D. et al. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell93, 203–214 (1998). CASPubMed Google Scholar
Baumann, F. et al. Lethal recessive myelin toxicity of prion protein lacking its central domain. EMBO J.26, 538–547 (2007). CASPubMedPubMed Central Google Scholar
Mallucci, G. et al. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science302, 871–874 (2003). CASPubMed Google Scholar
Brandner, S. et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature379, 339–343 (1996). CASPubMed Google Scholar
Chesebro, B. et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science308, 1435–1439 (2005). CASPubMed Google Scholar
Nicoll, A. J. & Collinge, J. Preventing prion pathogenicity by targeting the cellular prion protein. Infect. Disord. Drug Targets9, 48–57 (2009). CASPubMed Google Scholar
Radford, H. E. & Mallucci, G. R. The role of GPI-anchored PRPC in mediating the neurotoxic effect of scrapie prions in neurons. Curr. Issues Mol. Biol.12, 119–128 (2009). PubMed Google Scholar
Büeler, H. et al. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol. Med.1, 19–30 (1994). PubMed Google Scholar
Masel, J., Jansen, V. A. & Nowak, M. A. Quantifying the kinetic parameters of prion replication. Biophys. Chem.77, 139–152 (1999). CASPubMed Google Scholar
Haslberger, T., Bukau, B. & Mogk, A. Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem. Cell Biol.88, 63–75 (2010). CASPubMed Google Scholar
Jones, G. W. & Tuite, M. F. Chaperoning prions: the cellular machinery for propagating an infectious protein? Bioessays27, 823–832 (2005). CASPubMed Google Scholar
Prusiner, S. et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell63, 673–686 (1990). CASPubMed Google Scholar
Manson, J. C., Clarke, A. R., McBride, P. A., McConnell, I. & Hope, J. PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration3, 331–340 (1994). CASPubMed Google Scholar
Laurent, M. Bistability and the species barrier in prion diseases: stepping across the threshold or not. Biophys. Chem.72, 211–222 (1998). CASPubMed Google Scholar
Sindi, S. S. & Serio, T. R. Prion dynamics and the quest for the genetic determinant in protein-only inheritance. Curr. Opin. Microbiol.12, 623–630 (2009). CASPubMedPubMed Central Google Scholar
Legname, G. et al. Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc. Natl Acad. Sci. USA103, 19105–19110 (2006). CASPubMedPubMed Central Google Scholar
Tanaka, M., Collins, S. R., Toyama, B. H. & Weissman, J. S. The physical basis of how prion conformations determine strain phenotypes. Nature442, 585–589 (2006). CASPubMed Google Scholar
Kimberlin, R. H. & Walker, C. A. Evidence that the transmission of one source of scrapie agent to hamsters involves separation of agent strains from a mixture. J. Gen. Virol.39, 487–496 (1978). CASPubMed Google Scholar
Marsh, R. F. & Hanson, R. P. in Slow Transmissible Diseases of the Nervous System (eds Prusiner, S. B. & Hadlow, W. J.) 451–460 (Academy Press, New York, 1979). Google Scholar
Dickinson, A. G. in Slow Virus Diseases of Animals and Man (ed. Kimberlin, R. H.) 209–241 (North-Holland Publishing Company, Amsterdam, 1976). Google Scholar
Derkatch, I. L., Bradley, M. E., Zhou, P. & Liebman, S. W. The PNM2 mutation in the prion protein domain of SUP35 has distinct effects on different variants of the [PSI+] prion in yeast. Curr. Genet.35, 59–67 (1999). CASPubMed Google Scholar
Ghaemmaghami, S. et al. Continuous quinacrine treatment results in the formation of drug-resistant prions. PLoS Pathog.5, e1000673 (2009). Quinacrine treatment induces the loss of some prion strains while promoting the amplification of others. PubMedPubMed Central Google Scholar
Manuelidis, L., Fritch, W. & Xi, Y. G. Evolution of a strain of CJD that induces BSE-like plaques. Science277, 94–98 (1997). CASPubMed Google Scholar
Li, J., Browning, S., Mahal, S. P., Oelschlegel, A. M. & Weissmann, C. Darwinian evolution of prions in cell culture. Science327, 869–872 (2010). The frequency of prion strain mutations can be influenced by selective pressures, including host identity and exposure to chemical treatments. CASPubMed Google Scholar
Bruce, M. E. Scrapie strain variation and mutation. Br. Med. Bull.49, 822–838 (1993). CASPubMed Google Scholar
Angers, R. C. et al. Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science328, 1154–1158 (2010). The frequency of prion strain mutation in chronic wasting disease has been linked to a change in PrP sequence that does not seem to alter the conformation of the prion form. CASPubMedPubMed Central Google Scholar
Bessen, R. A. & Marsh, R. F. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J. Gen. Virol.73, 329–334 (1992). PubMed Google Scholar
Dickinson, A. G. & Outram, G. W. in Virus Nonconventionnels et Affections du Systeme Nerveux Central (eds Court, L. A. & Cathala, F.) 3–16 (Masson, Paris, 1983). Google Scholar
Parchi, P. et al. Incidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with mixed phenotype and co-occurrence of PrPSc types: an updated classification. Acta Neuropathol.118, 659–671 (2009). CASPubMedPubMed Central Google Scholar
Cali, I. et al. Co-existence of scrapie prion protein types 1 and 2 in sporadic Creutzfeldt-Jakob disease: its effect on the phenotype and prion-type characteristics. Brain132, 2643–2658 (2009). PubMedPubMed Central Google Scholar
Bruce, M., Fraser, H., McBride, P., Scott, J. & Dickinson, A. in Prion Diseases of Humans and Animals (eds Prusiner, S., Collinge, J., Powell, J. & Anderton, B.) 497–508 (Ellis Horwood, New York, 1992). Google Scholar
Bartz, J. C., Bessen, R. A., McKenzie, D., Marsh, R. F. & Aiken, J. M. Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathy. J. Virol.74, 5542–5547 (2000). CASPubMedPubMed Central Google Scholar
Dickinson, A. G. et al. Extraneural competition between different scrapie agents leading to loss of infectivity. Nature253, 556 (1975). CASPubMed Google Scholar
Dickinson, A. G., Fraser, H., Meikle, V. M. & Outram, G. W. Competition between different scrapie agents in mice. Nature New Biol.237, 244–245 (1972). CASPubMed Google Scholar
Dickinson, A. G. & Outram, G. W. in Slow Transmissible Diseases of The Nervous System (eds Prusiner, S. B. & Hadlow, W. J.) 13–31 (Academic Press, New York, 1979). Google Scholar
Shikiya, R. A., Ayers, J. I., Schutt, C. R., Kincaid, A. E. & Bartz, J. C. Coinfecting prion strains compete for a limiting cellular resource. J. Virol.84, 5706–5714 (2010). CASPubMedPubMed Central Google Scholar
Bradley, M. E., Edskes, H. K., Hong, J. Y., Wickner, R. B. & Liebman, S. W. Interactions among prions and prion “strains” in yeast. Proc. Natl Acad. Sci. USA99 (Suppl. 4), 16392–16399 (2002). CASPubMedPubMed Central Google Scholar
Morales, R., Abid, K. & Soto, C. The prion strain phenomenon: molecular basis and unprecedented features. Biochim. Biophys. Acta1772, 681–691 (2007). CASPubMed Google Scholar
Goldfarb, L. et al. Patients wth Creutzfeldt-Jakob disease and kuru lack the mutation in the PRIP gene found in Gerstmann-Sträussler syndrome, but they show a different double-allele mutation in the same gene. Am. J. Hum. Genet.45, A189 (1989). Google Scholar
Owen, F., Poulter, M., Collinge, J. & Crow, T. J. Codon 129 changes in the prion protein gene in Caucasians. Am. J. Hum. Genet.46, 1215–1216 (1990). CASPubMedPubMed Central Google Scholar
Liemann, S. & Glockshuber, R. Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry38, 3258–3267 (1999). CASPubMed Google Scholar
Hosszu, L. L. et al. The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC. J. Biol. Chem.279, 28515–28521 (2004). CASPubMed Google Scholar
Apetri, A. C., Vanik, D. L. & Surewicz, W. K. Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90–231. Biochemistry44, 15880–15888 (2005). CASPubMed Google Scholar
Baskakov, I. V., Legname, G., Baldwin, M. A., Prusiner, S. B. & Cohen, F. E. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem.277, 21140–21148 (2002). CASPubMed Google Scholar
Come, J. & Lansbury, P. Predisposition of prion protein homozygotes to Creutzfeldt-Jakob disease can be explained by a nucleation-dependent polymerization mechanism. J. Am. Chem. Soc.116, 4109–4110 (1994). CAS Google Scholar
Tahiri-Alaoui, A., Gill, A. C., Disterer, P. & James, W. Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: implications for disease susceptibility to Creutzfeldt-Jakob disease. J. Biol. Chem.279, 31390–31397 (2004). CASPubMed Google Scholar
Tahiri-Alaoui, A., Sim, V. L., Caughey, B. & James, W. Molecular heterosis of prion protein β-oligomers. A potential mechanism of human resistance to disease. J. Biol. Chem.281, 34171–34178 (2006). CASPubMed Google Scholar
Jeong, B. H. et al. Association of sporadic Creutzfeldt-Jakob disease with homozygous genotypes at PRNP codons 129 and 219 in the Korean population. Neurogenetics6, 229–232 (2005). CASPubMed Google Scholar
Westaway, D. et al. Distinct prion proteins in short and long scrapie incubation period mice. Cell51, 651–662 (1987). CASPubMed Google Scholar
Dickinson, A. G., Meikle, V. M. & 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). CASPubMed Google Scholar
Foster, J. D. & Dickinson, A. G. The unusual properties of CH1641, a sheep-passaged isolate of scrapie. Vet. Rec.123, 5–8 (1988). CASPubMed Google Scholar
Goldmann, W., Hunter, N., Smith, G., Foster, J. & Hope, J. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol.75, 989–995 (1994). CASPubMed Google Scholar
Gordon, W. ARS91–53: Report of Scrapie Seminar, 53–68 (US Department of Agriculture, 1964).
Shibuya, S., Higuchi, J., Shin, R. W., Tateishi, J. & Kitamoto, T. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann. Neurol.43, 826–828 (1998). CASPubMed Google Scholar
Westaway, D. et al. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev.8, 959–969 (1994). CASPubMed Google Scholar
Kaneko, K. et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl Acad. Sci. USA94, 10069–10074 (1997). CASPubMedPubMed Central Google Scholar
Perrier, V. et al. Dominant-negative inhibition of prion replication in transgenic mice. Proc. Natl Acad. Sci. USA99, 13079–13084 (2002). CASPubMedPubMed Central Google Scholar
Geoghegan, J. C,. Miller, M. B,. Kwak, A. H,. Harris, B. T. & Supattapone, S. Trans- dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor. PLoS Pathog.5, e1000535 (2009). Using PrP purified from mammalian cells and the protein misfolding cyclic amplification approach, the authors show that dominant-negative inhibition of prion propagation by a PrP mutant can be recapitulatedin vitroin the absence oftransfactors. PubMedPubMed Central Google Scholar
Lee, C. I., Yang, Q., Perrier, V. & Baskakov, I. V. The dominant-negative effect of the Q218K variant of the prion protein does not require protein X. Protein Sci.16, 2166–2173 (2007). Using recombinant protein purified from bacteria, the authors show that the Gln218Lys variant of PrP interferes with amyloid formation by wild-type PrPin vitro, and their studies suggest that the inhibition occurs not by an effect on binding but rather by a effect on conformational conversion. CASPubMedPubMed Central Google Scholar
Masel, J. & Jansen, V. A. Designing drugs to stop the formation of prion aggregates and other amyloids. Biophys. Chem.88, 247–259 (2000). Google Scholar
DePace, A. H., Santoso, A., Hillner, P. & Weissman, J. S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell93, 1241–1252 (1998). CASPubMed Google Scholar
Young, C. & Cox, B. Extrachromosomal elements in a super-suppression system of yeast I. A nuclear gene controlling the inheritance of the extrachromosomal elements. Heredity26, 413–422 (1971). Google Scholar
Doel, S. M., McCready, S. J., Nierras, C. R. & Cox, B. S. The dominant _PNM2_− mutation which eliminates the Ψ factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics137, 659–670 (1994). CASPubMedPubMed Central Google Scholar
King, C. Y. Supporting the structural basis of prion strains: induction and identification of [_PSI_] variants. J. Mol. Biol.307, 1247–1260 (2001). CASPubMed Google Scholar
Kochneva-Pervukhova, N. V. et al. Mechanism of inhibition of Ψ+ prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein. EMBO J.17, 5805–5810 (1998). CASPubMedPubMed Central Google Scholar
Osherovich, L. Z., Cox, B. S., Tuite, M. F. & Weissman, J. S. Dissection and design of yeast prions. PLoS Biol.2, e86 (2004). PubMedPubMed Central Google Scholar
Zlotnik, I. & Rennie, J. C. Experimental transmission of mouse passaged scrapie to goats, sheep, rats and hamsters. J. Comp. Pathol.75, 147–157 (1965). CASPubMed Google Scholar
Pattison, I. in NINDB Monograph, No.2: Slow, Latent, and Temperate Virus Infections (eds Gajdusek D. C., Gibbs C. J. Jr & Alpers M. P.)249–257 (US National Institutes of Health, Bethesda, Maryland, 1965). Google Scholar
Collinge, J., Sidle, K. C., Meads, J., Ironside, J. & Hill, A. F. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature383, 685–690 (1996). CASPubMed Google Scholar
Bruce, M. E. et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature389, 498–501 (1997). CASPubMed Google Scholar
Marsh, R. F., Burger, D., Eckroade, R., Zu Rhein, G. M. & Hanson, R. P. A preliminary report on the experimental host range of the transmissible mink encephalopathy agent. J. Infect. Dis.120, 713–719 (1969). CASPubMed Google Scholar
Hill, A. F. et al. Species-barrier-independent prion replication in apparently resistant species. Proc. Natl Acad. Sci. USA97, 10248–10253 (2000). CASPubMedPubMed Central Google Scholar
Race, R. & Chesebro, B. Scrapie infectivity found in resistant species. Nature392, 770 (1998). CASPubMed Google Scholar
Dickinson, A. G., Fraser, H. & Outram, G. W. Scrapie incubation time can exceed natural lifespan. Nature256, 732–733 (1975). CASPubMed Google Scholar
Windl, O. et al. Breaking an absolute species barrier: transgenic mice expressing the mink PrP gene are susceptible to transmissible mink encephalopathy. J. Virol.79, 14971–14975 (2005). CASPubMedPubMed Central Google Scholar
Sigurdson, C. J. et al. A molecular switch controls interspecies prion disease transmission in mice. J. Clin. Invest.120, 2590–2599 (2010). The authors show that the barrier to interspecies prion transmission may be the structure of a loop in the PrP protein. CASPubMedPubMed Central Google Scholar
Chien, P., Weissman, J. S. & DePace, A. H. Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem.73, 617–656 (2004). CASPubMed Google Scholar
Sawaya, M. R. et al. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature447, 453–457 (2007). CASPubMed Google Scholar
Vanik, D. L., Surewicz, K. A. & Surewicz, W. K. Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol. Cell14, 139–145 (2004). CASPubMed Google Scholar
Nakayashiki, T., Ebihara, K., Bannai, H. & Nakamura, Y. Yeast [PSI+] “prions” that are crosstransmissible and susceptible beyond a species barrier through a quasi-prion state. Mol. Cell7, 1121–1130 (2001). CASPubMed Google Scholar
Chen, B. et al. Genetic and epigenetic control of the efficiency and fidelity of cross-species prion transmission. Mol. Microbiol.76, 1483–1499 (2010). CASPubMedPubMed Central Google Scholar
Edskes, H. K., McCann, L. M., Hebert, A. M. & Wickner, R. B. Prion variants and species barriers among Saccharomyces Ure2 proteins. Genetics181, 1159–1167 (2009). CASPubMedPubMed Central Google Scholar
Kadnar, M. L., Articov, G. & Derkatch, I. L. Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1. PLoS Genet.6, e1000824 (2010). Despite the absence of amino acid substitutions, the authors uncover a prion transmission barrier between fragments of the Rnq1 prion [RNQ+] ofS. cerevisiae, suggesting that protein conformation is the key determinant in prion compatibility. PubMedPubMed Central Google Scholar
Jones, E. M. & Surewicz, W. K. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell121, 63–72 (2005). CASPubMed Google Scholar
Tessier, P. M. & Lindquist, S. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nature Struct. Mol. Biol.16, 598–605 (2009). CAS Google Scholar
Pattison, I. H. & Jones, K. M. Modification of a strain of mouse-adapted scrapie by passage through rats. Res. Vet. Sci.9, 408–410 (1968). CASPubMed Google Scholar
Kimberlin, R. H., Walker, C. A. & Fraser, H. The genomic identity of different strains of mouse scrapie is expressed in hamsters and preserved on reisolation in mice. J. Gen. Virol.70, 2017–2025 (1989). PubMed Google Scholar
Kimberlin, R. H., Cole, S. & Walker, C. A. Temporary and permanent modifications to a single strain of mouse scrapie on transmission to rats and hamsters. J. Gen. Virol.68, 1875–1881 (1987). PubMed Google Scholar
Makarava, N., Ostapchenko, V. G., Savtchenko, R. & Baskakov, I. V. Conformational switching within individual amyloid fibrils. J. Biol. Chem.284, 14386–14395 (2009). CASPubMedPubMed Central Google Scholar
Si, K., Lindquist, S. & Kandel, E. R. A neuronal isoform of the Aplysia CPEB has prion-like properties. Cell115, 879–891 (2003). By using expression in yeast, the authors provide the first evidence of the existence of a prion-based mechanism in the sensory neurons ofAplysiaspp. (sea slug). In this case the translational regulator cytoplasmic polyadenylation element binding protein (CPEB) undergoes a conformational switch to a self-perpetuating amyloid that potentially affects synpatic efficiency and thus long-term facilitation. CASPubMed Google Scholar
Bernardi, G. Lessons from a small, dispensable genome: the mitochondrial genome of yeast. Gene354, 189–200 (2005). CASPubMed Google Scholar
Ross, E. D., Edskes, H. K., Terry, M. J. & Wickner, R. B. Primary sequence independence for prion formation. Proc. Natl Acad. Sci. USA102, 12825–12830 (2005). CASPubMedPubMed Central Google Scholar
Taneja, V., Maddelein, M. L., Talarek, N., Saupe, S. J. & Liebman, S. W. A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast. Mol. Cell27, 67–77 (2007). CASPubMedPubMed Central Google Scholar