Structural studies of prion proteins and prions

Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases

Volumn 9789400727748, Issue , 2012, Pages 289-317

  Legname, Giuseppe ^a   Giachin, Gabriele ^a   Benetti, Federico ^a  

^a SISSA   (Italy)

Author keywords

Antibody labeling; Atomic force microscopy; Disease linked mutations; Electron microscopy; Fourier transform infrared spectroscopy; Limited proteolysis; NMR; Prion; Prion diseases; Prion protein; Small angle X ray scattering; X ray fiber diffraction

Indexed keywords

EID: 84883150934     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-94-007-2774-8_9     Document Type: Chapter

References (143)

1. Adrover M, Pauwels K, Pringent S, De Chiara C, Xu Z, Chapuis C, Pastore A, Rezaei H (2010) Prion fibrillization is mediated by a native structural element which comprises the helices H2 and H3. J Biol Chem 285:21004-21012
2. Aguzzi A, Sigurdson C, Heikenwaelder M (2008) Molecular mechanisms of prion pathogenesis. Annu Rev Pathol 3:11-40
3. Alper T, Cramp WA, Haig DA, Clarke MC (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214:764-766
4. Anderson M, Bocharova OV, Makarava N, Breydo L, Salnikov VV, Baskakov IV (2006) Polymorphism and ultrastructural organization of prion protein amyloid fibrils: An insight from high resolution atomic force microscopy. J Mol Biol 358:580-596
5. Antonyuk SV, Trevitt CR, Strange RW, Jackson GS, Sangar D, Batchelor M, Cooper S, Fraser C, Jones S, Georgiou T, Khalili-Shirazi A, Clarke AR, Hasnain SS, Collinge J (2009) Crystal structure of human prion protein bound to a therapeutic antibody. Proc Natl Acad Sci USA 106:2554-2558
6. Apetri AC, Surewicz K, Surewicz WK (2004) The effect of disease-associated mutations on the folding pathway of human prion protein. J Biol Chem 279:18008-18014
7. Ashok A, Hegde RS (2009) Selective processing and metabolism of disease-causing mutant prion proteins. PLoS Pathog 5:e1000479
8. Bae SH, Legname G, Serban A, Prusiner SB, Wright PE, Dyson HJ (2009) Prion proteins with pathogenic and protective mutations show similar structure and dynamics. Biochemistry 48:8120-8128
9. Baker HE, Poulter M, Crow TJ, Frith CD, Lofthouse R, Ridley RM (1991) Aminoacid polymorphism in human prion protein and age at death in inherited prion disease. Lancet 337:1286
10. Balguerie A, Dos Reis S, Ritter C, Chaignepain S, Coulary-Salin B, Forge V, Bathany K, Lascu I, Schmitter JM, Riek R, Saupe SJ (2003) Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. EMBO J 22:2071-2081
11. Bellinger-Kawahara C, Diener TO, Mckinley MP, Groth DF, Smith DR, Prusiner SB (1987) Purified scrapie prions resist inactivation by procedures that hydrolyze, modify, or shear nucleic acids. Virology 160:271-274
12. Benetti F, Amenitsch H, Vos M, Peters P, Legname G, Requena JR (2010) SAXS study of Syrian hamster prion fibrils and recombinant truncated prion protein in the presence of transition metals (in press). In: Sartori BRM, Amenitsch H, Bernstorff S (ed) Annual report of the Austrian SAXS beamline 2009. Institute of Biophysics and Nanosystems Research
13. Graz Bertho G, Bouvier G, Hui Bon Hoa G, Girault JP (2008) The key-role of tyrosine 155 in the mechanism of prion transconformation as highlighted by a study of sheep mutant peptides. Peptides 29:1073-1084
14. Bessen RA, Marsh RF (1992) Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66:2096-2101
15. Bessen RA, Marsh RF (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68:7859-7868
16. Bignami A, Parry HB (1971) Aggregations of 35-nanometer particles associated with neuronal cytopathic changes in natural scrapie. Science 171:389-399
17. Biverstahl H, Andersson A, Graslund A, Maler L (2004) NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein. Biochemistry 43:14940-14947
18. Borchelt DR, Taraboulos A, Prusiner SB (1992) Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J Biol Chem 267:16188-16199
19. Bots GT, De Man JC, Verjaal A (1971) Virus-like particles in brain tissue from two patients with Creutzfeldt-Jakob disease. Acta Neuropathol 18:267-270
20. Bueler H, Aguzzi A, Sailer A, Greiner RA, Autenried P, Aguet M, Weissmann C (1993) Mice devoid of PrP are resistant to scrapie. Cell 73:1339-1347
21. Burns CS, Aronoff-Spencer E, Legname G, Prusiner SB, Antholine WE, Gerfen GJ, Peisach J, Millhauser GL (2003) Copper coordination in the full-length, recombinant prion protein. Biochemistry 42:6794-6803
22. Calzolai L, Zahn R (2003) Influence of pH on NMR structure and stability of the human prion protein globular domain. J Biol Chem 278:35592-35596
23. Calzolai L, Lysek DA, Guntert P, Von Schroetter C, Riek R, Zahn R, Wuthrich K (2000) NMR structures of three single-residue variants of the human prion protein. Proc Natl Acad Sci USA 97:8340-8345
24. Calzolai L, Lysek DA, Perez DR, Guntert P, Wuthrich K (2005) Prion protein NMR structures of chickens, turtles, and frogs. Proc Natl Acad Sci USA 102:651-655
25. Campana V, Sarnataro D, Zurzolo C (2005) The highways and byways of prion protein trafficking. Trends Cell Biol 15:102-111
26. Caughey B (1991) Cellular metabolism of PrP. Prion Diseases in Humans and Animals Conference, London
27. Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS (1991) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30:7672-7680
28. Caughey B, Raymond GJ, Bessen RA (1998) Strain-dependent differences in b-sheet conformations of abnormal prion protein. J Biol Chem 273:32230-32235
29. Chesebro B (1992) PrP and the scrapie agent. Nature 356:560
30. Chesebro B, Trifilo M, Race R, Meade-White K, Teng C, Lacasse R, Raymond L, Favara C, Baron G, Priola S, Caughey B, Masliah E, Oldstone M (2005) Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308:1435-1439
31. Chiesa R, Piccardo P, Ghetti B, Harris DA (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21:1339-1351
32. Christen B, Perez DR, Hornemann S, Wuthrich K (2008) NMR structure of the bank vole prion protein at 20 °C contains a structured loop of residues 165-171. J Mol Biol 383:306-312
33. Christen B, Hornemann S, Damberger FF, Wuthrich K (2009) Prion protein NMR structure from Tammar Wallaby ( Macropus eugenii ) shows that the b 2-a 2 loop is modulated by long-range sequence effects. J Mol Biol 389:833-845
34. Cohen FE, Prusiner SB (1998) Pathologic conformations of prion proteins. Annu Rev Biochem 67:793-819
35. Collinge J (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 24:519-550
36. Collinge J, Palmer MS, Dryden AJ (1991) Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease. Lancet 337:1441-1442
37. David-Ferreira JF, David-Ferreira KL, Gibbs CJ Jr, Morris JA (1968) Scrapie in mice: Ultrastructural observations in the cerebral cortex. Proc Soc Exp Biol Med 127:313-320
38. Demarco ML, Daggett V (2004) From conversion to aggregation: protofibril formation of the prion protein. Proc Natl Acad Sci USA 101:2293-2298
39. Demarco ML, Silveira J, Caughey B, Daggett V (2006) Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models. Biochemistry 45:15573-15582
40. Diener TO, Mckinley MP, Prusiner SB (1982) Viroids and prions. Proc Natl Acad Sci USA 79:5220-5224
41. Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE, Dyson HJ (1997) Structure of the recombinant full-length hamster prion protein PrP(29-231): the N-terminus is highly flexible. Proc Natl Acad Sci USA 94:13452-13457
42. Dossena S, Imeri L, Mangieri M, Garofoli A, Ferrari L, Senatore A, Restelli E, Balducci C, Fiordaliso F, Salio M, Bianchi S, Fioriti L, Morbin M, Pincherle A, Marcon G, Villani F, Carli M, Tagliavini F, Forloni G, Chiesa R (2008) Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model. Neuron 60:598-609
43. Eghiaian F, Grosclaude J, Lesceu S, Debey P, Doublet B, Treguer E, Rezaei H, Knossow M (2004) Insight into the PrP C ? PrP Sc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants. Proc Natl Acad Sci USA 101:10254-10259
44. Fischer M, Rulicke T, Raeber A, Sailer A, Moser M, Oesch B, Brandner S, Aguzzi A, Weissmann C (1996) Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 15:1255-1264
45. Gasset M, Baldwin MA, Fletterick RJ, Prusiner SB (1993) Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc Natl Acad Sci USA 90:1-5
46. Godsave SF, Wille H, Kujala P, Latawiec D, Dearmond SJ, Serban A, Prusiner SB, Peters PJ (2008) Cryo-immunogold electron microscopy for prions: toward identification of a conversion site. J Neurosci 28:12489-12499
47. Goormaghtigh E, Cabiaux V, Ruysschaert J-M (1990) Secondary structure and dosage of soluble membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur J Biochem 193:409-420
48. Gorodinsky A, Harris DA (1995) Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin. J Cell Biol 129:619-627
49. Gossert AD, Bonjour S, Lysek DA, Fiorito F, Wuthrich K (2005) Prion protein NMR structures of elk and of mouse/elk hybrids. Proc Natl Acad Sci USA 102:646-650
50. Govaerts C, Wille H, Prusiner SB, Cohen FE (2004) Evidence for assembly of prions with lefthanded b-helices into trimers. Proc Natl Acad Sci USA 101:8342-8347
51. Haire LF, Whyte SM, Vasisht N, Gill AC, Verma C, Dodson EJ, Dodson GG, Bayley PM (2004) The crystal structure of the globular domain of sheep prion protein. J Mol Biol 336:1175-1183
52. Hegde RS, Mastrianni JA, Scott MR, Defea KA, Tremblay P, Torchia M, Dearmond SJ, Prusiner SB, Lingappa VR (1998) A transmembrane form of the prion protein in neurodegenerative disease. Science 279:827-834
53. Hegde RS, Tremblay P, Groth D, Dearmond SJ, Prusiner SB, Lingappa VR (1999) Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 402:822-826
54. Heske J, Heller U, Winklhofer KF, Tatzelt J (2004) The C-terminal globular domain of the prion protein is necessary and sufficient for import into the endoplasmic reticulum. J Biol Chem 279:5435-5443
55. Hill AF, Antoniou M, Collinge J (1999) Protease-resistant prion protein produced in vitro lacks detectable infectivity. J Gen Virol 80(Pt 1):11-14
56. Hornemann S, Von Schroetter C, Damberger FF, Wuthrich K (2009) Prion protein-detergent micelle interactions studied by NMR in solution. J Biol Chem 284:22713-22721
57. Hsiao KK, Scott M, Foster D, Groth DF, Dearmond SJ, Prusiner SB (1990) Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 250:1587-1590
58. Hsiao K, Dlouhy SR, Farlow MR, Cass C, Da Costa M, Conneally PM, Hodes ME, Ghetti B, Prusiner SB (1992) Mutant prion proteins in Gerstmann-Straüssler-Scheinker disease with neurofibrillary tangles. Nat Genet 1:68-71
59. Hsiao KK, Groth D, Scott M, Yang SL, Serban H, Rapp D, Foster D, Torchia M, Dearmond SJ, Prusiner SB (1994) Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc Natl Acad Sci USA 91:9126-9130
60. Huang Z, Prusiner SB, Cohen FE (1995) Scrapie prions: A three-dimensional model of an infectious fragment. Fold Des 1:13-19
61. Ilc G, Giachin G, Jaremko M, Jaremko L, Benetti F, Plavec J, Zhukov I, Legname G (2010) NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. PLoS One 5:e11715
62. James TL, Liu H, Ulyanov NB, Farr-Jones S, Zhang H, Donne DG, Kaneko K, Groth D, Mehlhorn I, Prusiner SB, Cohen FE (1997) Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci USA 94:10086-10091
63. Kaneko K, Vey M, Scott M, Pilkuhn S, Cohen FE, Prusiner SB (1997a) COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc Natl Acad Sci USA 94:2333-2338
64. Kaneko K, Zulianello L, Scott M, Cooper CM, Wallace AC, James TL, Cohen FE, Prusiner SB (1997b) Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 94:10069-10074
65. Kimberlin RH (1990) Scrapie and possible relationships with viroids. Semin Virol 1:153-162
66. Knaus KJ, Morillas M, Swietnicki W, Malone M, Surewicz WK, Yee VC (2001) Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat Struct Biol 8:770-774
67. Kobayashi A, Hizume M, Teruya K, Mohri S, Kitamoto T (2009) Heterozygous inhibition in prion infection: the stone fence model. Prion 3:27-30
68. Kovacs GG, Trabattoni G, Hainfellner JA, Ironside JW, Knight RS, Budka H (2002) Mutations of the prion protein gene phenotypic spectrum. J Neurol 249:1567-1582
69. Kozin SA, Bertho G, Mazur AK, Rabesona H, Girault JP, Haertle T, Takahashi M, Debey P, Hoa GH (2001) Sheep prion protein synthetic peptide spanning helix 1 and b-strand 2 (residues 142-166) shows b-hairpin structure in solution. J Biol Chem 276:46364-46370
70. Kozin SA, Lepage C, Hui Bon Hoa G, Rabesona H, Mazur AK, Blond A, Cheminant M, Haertle T, Debey P, Rebuffat S (2004) Solution structure of synthetic 21mer peptide spanning region 135-155 (in human numbering) of sheep prion protein http://www.pdb.org/pdb/explore/ explore.do?structureId=1S4T
71. Kuwata K, Li H, Yamada H, Legname G, Prusiner SB, Akasaka K, James TL (2002) Locally disordered conformer of the hamster prion protein: A crucial intermediate to PrP Sc ? Biochemistry 41:12277-12283
72. Latarjet R, Muel B, Haig DA, Clarke MC, Alper T (1970) Inactivation of the scrapie agent by near monochromatic ultraviolet light. Nature 227:1341-1343
73. Lee S, Antony L, Hartmann R, Knaus KJ, Surewicz K, Surewicz WK, Yee VC (2010) Conformational diversity in prion protein variants influences intermolecular b-sheet formation. EMBO J 29:251-262
74. Legname G, Baskakov IV, Nguyen HO, Riesner D, Cohen FE, Dearmond SJ, Prusiner SB (2004) Synthetic mammalian prions. Science 305:673-676
75. Legname G, Nguyen HO, Baskakov IV, Cohen FE, Dearmond SJ, Prusiner SB (2005) Strainspecified characteristics of mouse synthetic prions. Proc Natl Acad Sci USA 102:2168-2173
76. Legname G, Nguyen HO, Peretz D, Cohen FE, Dearmond SJ, Prusiner SB (2006) Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci USA 103:19105-19110
77. Li J, Mei FH, Xiao GF, Guo CY, Lin DH (2007) 1 H, 13 C and 15 N resonance assignments of rabbit prion protein (91-228). J Biomol NMR 38:181
78. Liemann S, Glockshuber R (1999) Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochemistry 38:3258-3267
79. Liu H, Farr-Jones S, Ulyanov NB, Llinas M, Marqusee S, Groth D, Cohen FE, Prusiner SB, James TL (1999) Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry 38:5362-5377
80. Lopez Garcia F, Zahn R, Riek R, Wuthrich K (2000) NMR structure of the bovine prion protein. Proc Natl Acad Sci USA 97:8334-8339
81. Lysek DA, Schorn C, Nivon LG, Esteve-Moya V, Christen B, Calzolai L, Von Schroetter C, Fiorito F, Herrmann T, Guntert P, Wuthrich K (2005) Prion protein NMR structures of cats, dogs, pigs, and sheep. Proc Natl Acad Sci USA 102:640-645
82. Maddelein ML, Dos Reis S, Duvezin-Caubet S, Coulary-Salin B, Saupe SJ (2002) Amyloid aggregates of the HET-s prion protein are infectious. Proc Natl Acad Sci USA 99:7402-7407
83. Manuelidis L, Fritch W (1996) Infectivity and host responses in Creutzfeldt-Jakob disease. Virology 216:46-59
84. Mashima T, Matsugami A, Nishikawa F, Nishikawa S, Katahira M (2009) Unique quadruplex structure and interaction of an RNA aptamer against bovine prion protein. Nucleic Acids Res 37:6249-6258
85. Mckinley MP, Bolton DC, Prusiner SB (1983) A protease-resistant protein is a structural component of the scrapie prion. Cell 35:57-62
86. Mckinley MP, Meyer RK, Kenaga L, Rahbar F, Cotter R, Serban A, Prusiner SB (1991a) Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 65:1340-1351
87. Mckinley MP, Taraboulos A, Kenaga L, Serban D, Stieber A, Dearmond SJ, Prusiner SB, Gonatas N (1991b) Ultrastructural localization of scrapie prion proteins in cytoplasmic vesicles of infected cultured cells. Lab Invest 65:622-630
88. Megy S, Bertho G, Kozin SA, Debey P, Hoa GH, Girault JP (2004) Possible role of region 152-156 in the structural duality of a peptide fragment from sheep prion protein. Protein Sci 13:3151-3160
89. Meyer RK, Mckinley MP, Bowman KA, Braunfeld MB, Barry RA, Prusiner SB (1986) Separation and properties of cellular and scrapie prion proteins. Proc Natl Acad Sci USA 83:2310-2314
90. Mills NL, Surewicz K, Surewicz WK, Sonnichsen FD (2009) Residue 129 polymorphism and conformational dynamics of familial prion diseases associated with the human prion protein variant D178N. doi:10.2210/pdb2k1d/pdb http://www.pdb.org/pdb/explore/explore. do?structureId=2K1D
91. Mishra RS, Bose S, Gu Y, Li R, Singh N (2003) Aggresome formation by mutant prion proteins: the unfolding role of proteasomes in familial prion disorders. J Alzheimers Dis 5:15-23
92. Muramoto T, Dearmond SJ, Scott M, Telling GC, Cohen FE, Prusiner SB (1997) Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an a-helix. Nat Med 3:750-755
93. Nguyen JT, Inouye H, Baldwin MA, Fletterick RJ, Cohen FE, Prusiner SB, Kirschner DA (1995) X-ray diffraction of scrapie prion rods and PrP peptides. J Mol Biol 252:412-422
94. Novitskaya V, Makarava N, Bellon A, Bocharova OV, Bronstein IB, Williamson RA, Baskakov IV (2006) Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J Biol Chem 281:15536-15545
95. Onisko B, Fernandez EG, Freire ML, Schwarz A, Baier M, Camina F, Garcia JR, Rodriguez-Segade Villamarin S, Requena JR (2005) Probing PrP Sc structure using chemical cross-linking and mass spectrometry: Evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate. Biochemistry 44:10100-10109
96. Palmer MS, Dryden AJ, Hughes JT, Collinge J (1991) Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352:340-342
97. Pan K-M, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, Prusiner SB (1993) Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90:10962-10966
98. Parchi P, Zou W, Wang W, Brown P, Capellari S, Ghetti B, Kopp N, Schulz-Schaeffer WJ, Kretzschmar HA, Head MW, Ironside JW, Gambetti P, Chen SG (2000) Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci USA 97:10168-10172
99. Peretz D, Williamson RA, Matsunaga Y, Serban H, Pinilla C, Bastidas RB, Rozenshteyn R, James TL, Houghten RA, Cohen FE, Prusiner SB, Burton DR (1997) A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform. J Mol Biol 273:614-622
100. Perez DR, Damberger FF, Wuthrich K (2010) Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. J Mol Biol 400:121-128
101. Piccardo P, Dlouhy SR, Lievens PM, Young K, Bird TD, Nochlin D, Dickson DW, Vinters HV, Zimmerman TR, Mackenzie IR, Kish SJ, Ang LC, De Carli C, Pocchiari M, Brown P, Gibbs CJ Jr, Gajdusek DC, Bugiani O, Ironside J, Tagliavini F, Ghetti B (1998) Phenotypic variability of Gerstmann-Straüssler-Scheinker disease is associated with prion protein heterogeneity. J Neuropathol Exp Neurol 57:979-988
102. Premzl M, Delbridge M, Gready JE, Wilson P, Johnson M, Davis J, Kuczek E, Marshall Graves JA (2005) The prion protein gene: identifying regulatory signals using marsupial sequence. Gene 349:121-134
103. Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216:136-144
104. Prusiner SB (1997) Biology of prions. In: Rosenberg RN, Prusiner SB, Dimauro S, Barchi RL (eds) The molecular and genetic basis of neurological disease, 2nd edn. Butterworth Heinemann
105. Stoneham Prusiner SB (1998) Prions. Proc Natl Acad Sci USA 95:13363-13383
106. Prusiner SB, Scott MR, Dearmond SJ, Cohen FE (1998) Prion protein biology. Cell 93:337-348
107. Requena JR (2009) Structure of mammalian prions. Future Virol 4:295-307
108. Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wüthrich K (1996) NMR structure of the mouse prion protein domain PrP(121-231). Nature 382:180-182
109. Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F (2008) Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein 2 helical 180-195 segment, and comparisonwith full length 2-helix-derived peptides. J. Pept. Sci. 14:1096-1102
110. Sajnani G, Pastrana MA, Dynin I, Onisko B, Requena JR (2008) Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry. J Mol Biol 382:88-98
111. Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, Mcfarlane HT, Madsen AO, Riekel C, Eisenberg D (2007) Atomic structures of amyloid cross-b spines reveal varied steric zippers. Nature 447:453-457
112. Sim VL, Caughey B (2009) Ultrastructures and strain comparison of under-glycosylated scrapie prion fibrils. Neurobiol Aging 30:2031-2042
113. Smirnovas V, Kim JI, Lu X, Atarashi R, Caughey B, Surewicz WK (2009) Distinct structures of scrapie prion protein (PrP Sc )-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange. J Biol Chem 284:24233-24241
114. Spassov S, Beekes M, Naumann D (2006) Structural differences between TSEs strains investigated by FT-IR spectroscopy. Biochim Biophys Acta 1760:1138-1149
115. Swietnicki W, Petersen RB, Gambetti P, Surewicz WK (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem 273:31048-31052
116. Taraboulos A, Raeber AJ, Borchelt DR, Serban D, Prusiner SB (1992) Synthesis and trafficking of prion proteins in cultured cells. Mol Biol Cell 3:851-863
117. Taubner LM, Bienkiewicz EA, Copie V, Caughey B (2010) Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. J Mol Biol 395:475-490
118. Telling GC (2000) Prion protein genes and prion diseases: studies in transgenic mice. Neuropathol Appl Neurobiol 26:209-220
119. Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, Dearmond SJ, Prusiner SB (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83:79-90
120. Telling GC, Scott M, Prusiner SB (1996) Deciphering prion diseases with transgenic mice. In: Gibbs CJ Jr (ed) Bovine spongiform encephalopathy: the BSE dilemma. Springer Verlag, New York
121. Vanik DL, Surewicz WK (2002) Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form. J Biol Chem 277:49065-49070
122. Vey M, Pilkuhn S, Wille H, Nixon R, Dearmond SJ, Smart EJ, Anderson RG, Taraboulos A, Prusiner SB (1996) Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci USA 93:14945-14949
123. Viles JH, Cohen FE, Prusiner SB, Goodin DB, Wright PE, Dyson HJ (1999) Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc Natl Acad Sci USA 96:2042-2047
124. Viles JH, Donne D, Kroon G, Prusiner SB, Cohen FE, Dyson HJ, Wright PE (2001) Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. Biochemistry 40:2743-2753
125. Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH (2008) Amyloid fibrils of the HET-s(218-289) prion form a b solenoid with a triangular hydrophobic core. Science 319:1523-1526
126. Wen Y, Li J, Yao W, Xiong M, Hong J, Peng Y, Xiao G, Lin D (2010) Unique structural characteristics of the rabbit prion protein. J Biol Chem 285(41):31682-31693
127. Wille H, Michelitsch MD, Guenebaut V, Supattapone S, Serban A, Cohen FE, Agard DA, Prusiner SB (2002) Structural studies of the scrapie prion protein by electron crystallography. Proc Natl Acad Sci USA 99:3563-3568
128. Wille H, Govaerts C, Borovinskiy A, Latawiec D, Downing KH, Cohen FE, Prusiner SB (2007) Electron crystallography of the scrapie prion protein complexed with heavy metals. Arch Biochem Biophys 467:239-248
129. Wille H, Bian W, Mcdonald M, Kendall A, Colby DW, Bloch L, Ollesch J, Borovinskiy AL, Cohen FE, Prusiner SB, Stubbs G (2009) Natural and synthetic prion structure from X-ray fiber diffraction. Proc Natl Acad Sci USA 106:16990-16995
130. Williamson RA, Peretz D, Pinilla C, Ball H, Bastidas RB, Rozenshteyn R, Houghten RA, Prusiner SB, Burton DR (1998) Mapping the prion protein using recombinant antibodies. J Virol 72:9413-9418
131. Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol 16:973-978
132. Windl O, Dempster M, Estibeiro JP, Lathe R, De Silva R, Esmonde T, Will R, Springbett A, Campbell TA, Sidle KC, Palmer MS, Collinge J (1996) Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: A systematic analysis of predisposing mutations and allelic variation in the PRNP gene. Hum Genet 98:259-264
133. Wopfner F, Weidenhofer G, Schneider R, Von Brunn A, Gilch S, Schwarz TF, Werner T, Schatzl HM (1999) Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J Mol Biol 289:1163-1178
134. Worrall BB, Herman ST, Capellari S, Lynch T, Chin S, Gambetti P, Parchi P (1999) Type 1 protease resistant prion protein and valine homozygosity at codon 129 of PRNP identify a subtype of sporadic Creutzfeldt-Jakob disease. J Neurol Neurosurg Psychiatry 67:671-674
135. Young K, Piccardo P, Kish SJ, Ang LC, Dlouhy S, Ghetti B (1998) Gerstmann-Sträussler-Scheinker disease (GSS) with a mutation at prion protein (PrP) residue 212. J Neuropathol Exp Neurol 57:518
136. Zahn R (2003) The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site. J Mol Biol 334:477-488
137. Zahn R, Von Schroetter C, Wuthrich K (1997) Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett 417:400-404
138. Zahn R, Liu A, Luhrs T, Riek R, Von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K (2000) NMR solution structure of the human prion protein. Proc Natl Acad Sci USA 97:145-150
139. Zahn R, Guntert P, Von Schroetter C, Wuthrich K (2003) NMR structure of a variant human prion protein with two disulfide bridges. J Mol Biol 326:225-234
140. Zanusso G, Farinazzo A, Prelli F, Fiorini M, Gelati M, Ferrari S, Righetti PG, Rizzuto N, Frangione B, Monaco S (2004) Identification of distinct N-terminal truncated forms of prion protein in different Creutzfeldt-Jakob disease subtypes. J Biol Chem 279:38936-38942
141. Zhang Y, Swietnicki W, Zagorski MG, Surewicz WK, Sonnichsen FD (2000) Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem 275:33650-33654
142. Zimmermann K, Turecek PL, Schwarz HP (1999) Genotyping of the prion protein gene at codon 129. Acta Neuropathol 97:355-358
143. Zou WQ, Capellari S, Parchi P, Sy MS, Gambetti P, Chen SG (2003) Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J Biol Chem 278:40429-40436