Mechanisms of prion protein assembly into amyloid

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 7, 2008, Pages 2409-2414

  Stöhr, Jan ^a   Weinmann, Nicole ^a   Wille, Holger ^b,c   Kaimann, Tina ^a   Nagel Steger, Luitgard ^a   Birkmann, Eva ^a   Panza, Giannantonio ^a   Prusiner, Stanley B ^b,c   Eigen, Manfred ^d   Riesner, Detlev ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Dimer; Fibril; Precursor state; Seeding

Indexed keywords

AMYLOID; PRION PROTEIN; THIOFLAVINE; CROSS LINKING REAGENT;

ARTICLE; CIRCULAR DICHROISM; CROSS LINKING; FLUORESCENCE; IN VITRO STUDY; KINETICS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; ULTRACENTRIFUGATION; ULTRASOUND; CHEMISTRY; DIMERIZATION; ELECTRON MICROSCOPY; METABOLISM; PRION; ULTRASTRUCTURE;

AMYLOID; CIRCULAR DICHROISM; CROSS-LINKING REAGENTS; DIMERIZATION; MICROSCOPY, ELECTRON; PRIONS; ULTRACENTRIFUGATION;

EID: 40649125572     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0712036105     Document Type: Article

References (38)

1. Prusiner SB (2007) in Fields Virology (Lippincott Williams & Wilkins, Philadelphia), 5th Ed, pp 3059-3091.
2. Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D (1992) Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis. J Gen Virol 73(Pt 4):1025-1029.
3. Safar JG, et al. (2005) Search for a prion-specific nucleic acid. J Virol 79:10796-10806.
4. Cohen FE, et al. (1994) Structural clues to prion replication. Science 264:530-531.
5. Eigen M (1996) Prionics or the kinetic basis of prion diseases. Biophys Chem 63:A1-A18.
6. Harper JD, Lansbury PT, Jr (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 66:385-407.
7. McKinley MP, Bolton DC, Prusiner SB (1983) A protease-resistant protein is a structural component of the scrapie prion. Cell 35:57-62.
8. Caughey B, Raymond GJ, Ernst D, Race RE (1991) N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 65:6597-6603.
9. Pan KM, et al. (1993) Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90:10962-10966.
10. Safar J, Roller PP, Gajdusek DC, Gibbs CJ, Jr (1993) Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci 2:2206-2216.
11. Prusiner SB, et al. (1983) Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358.
12. McKinley MP, et al. (1991) Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 65:1340-1351.
13. Legname G, et al. (2004) Synthetic mammalian prions. Science 305:673-676.
14. Legname G, et al. (2005) Strain-specified characteristics of mouse synthetic prions. Proc Natl Acad Sci USA 102:2168-2173.
15. Saborio GP, Permanne B, Soto C (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411:810-813.
16. Castilla J, Saa P, Hetz C, Soto C (2005) In vitro generation of infectious scrapie prions. Cell 121:195-206.
17. Deleault NR, Harris BT, Rees JR, Supattapone S (2007) From the Cover: Formation of native prions from minimal components in vitro. Proc Natl Acad Sci USA 104:9741-9746.
18. Leffers KW, et al. (2004) The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites. J Mol Biol 344:839-853.
19. Leffers KW, et al. (2005) Assembly of natural and recombinant prion protein into fibrils. Biol Chem 386:569-580.
20. Kaimann T, et al. (2007) Molecular model of an α-helical prion protein dimer and its monomeric subunits as derived from chemical cross-linking and molecular modeling calculations. J Mol Biol, 10.1016/j.jmb2007.11.035.
21. Bocharova OV, Breydo L, Salnikov VV, Gill AC, Baskakov IV (2005) Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease. Protein Sci 14:1222-1232.
22. Birkmann E, et al. (2006) Detection of prion particles in samples of BSE, scrapie by fluorescence correlation spectroscopy without proteinase K digestion. Biol Chem 387:95-102.
23. Post K, et al. (1998) Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation. Biol Chem 379:1307-1317.
24. Atarashi R, et al. (2007) Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat Methods 4:645-650.
25. Jansen K, et al. (2001) Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form. Biol Chem 382:683-691.
26. Liu H, et al. (1999) Solution structure of Syrian hamster prion protein rPrP(90 -231). Biochemistry 38:5362-5377.
27. Apetri AC, Surewicz WK (2003) Atypical effect of salts on the thermodynamic stability of human prion protein. J Biol Chem 278:22187-22192.
28. Govaerts C, Wille H, Prusiner SB, Cohen FE (2004) Evidence for assembly of prions with left-handed beta-helices into trimers. Proc Natl Acad Sci USA 101:8342-8347.
29. Masel J, Jansen VA (2004) Prion kinetics. Biophys J 87:728.
30. Eigen M (2001) BSE und das Prionen-Problem. Spek Wiss 4:40-49.
31. Safar JG, et al. (2005) Prion clearance in bigenic mice. J Gen Virol 86:2913-2923.
32. Thomzig A, Kratzel C, Lenz G, Kruger D, Beekes M (2003) Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie. EMBO Rep 4:530-533.
33. Colby DW, Zhang J, Wang S, Groth D, Legname G, Riesner D, Prusiner SB (2007) Prion detection by an amyloid seeding assay. Proc Natl Acad Sci USA 104:20914-20919.
34. Birkmann E, et al. (2007) Counting of single prion particles bound to a capture-antibody surface (surface-FIDA). Vet Microbiol 123:294-304.
35. Mehlhorn I, et al. (1996) High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35:5528-5537.
36. Safar J, et al. (1998) Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 4:1157-1165.
37. Casassa EF, Eisenberg H (1964) Thermodynamic analysis of multicomponent solutions. Adv Protein Chem 19:287-395.
38. Williamson RA, et al. (1998) Mapping the prion protein using recombinant antibodies. J Virol 72:9413-9418.