Prion protein oligomerization

Current Alzheimer Research

Volumn 5, Issue 6, 2008, Pages 572-578

  Rezaei, H ^a  

^a INRA Institut National de la Recherche Agronomique   (France)

Author keywords

Amyloid; Catalyse; Kinetic intermediate; Nucleus, seed; Oligomerization; Protein misassembly; Soluble oligomers; Transmissible spongiform encephalopathies

Indexed keywords

PRION PROTEIN;

AMYLOIDOSIS; BETA SHEET; BIOLOGICAL ACTIVITY; CONFORMATIONAL TRANSITION; CREUTZFELDT JAKOB DISEASE; GERSTMANN STRAUSSLER SCHEINKER SYNDROME; HUMAN; IN VIVO STUDY; KURU; NONHUMAN; OLIGOMERIZATION; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; REVIEW;

EID: 58049195811     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720508786898497     Document Type: Review

References (65)

1. Prusiner SB, Prions. Proc Natl Acad Sci USA 95(23): 13363-83 (1998).
2. Prusiner SB, McKinley MP, Bowman KA, Bolton DC, Bendheim PE, Groth DF, et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35(2 Pt 1): 349-58 (1983).
3. Pergami P, Jaffe H, Safar J. Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form. Anal Biochem 236(1): 63-73 (1996).
4. Rezaei H, Choiset Y, Eghiaian F, Treguer1 E, Mentre P, Debey P, et al. High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur J Biochem 267(10): 2833-9 (2000).
5. Volkel D, Blankenfeldt W, Schomburg D. Large-scale production, purification and refolding of the full-length cellular prion protein from Syrian golden hamster in Escherichia coli using the glutathione S-transferase-fusion system. Eur J Biochem 251(1-2): pp. 462-71 (1998).
6. Mehlhorn I, Groth D, Stöckel J, Moffat B, Reilly D, Yansura D, et al. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35(17): 5528-37 (1996).
7. McKinley MP, Bolton DC, Prusiner SB. A protease-resistant protein is a structural component of the scrapie prion. Cell 35(1): 57-62 (1983).
8. Bendheim PE, Bolton DC, Seligman SJ, Bablanian G, Windsor D, Scala LJ, et al. Purification and partial characterization of the normal cellular homologue of the scrapie agent protein. J Infect Dis 158(6): 1198-208 (1988).
9. Lansbury PT, Jr, Costa PR, Griffiths JM, Simon EJ, Auger M, Halverson KJ, et al. Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Biol 2(11): 990-8 (1995).
10. Sunde M, Serpella CL, Bartlama M, Frasera PE, Pepysa MB, Blakea CF et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J Mol Biol 273(3): 729-39 (1997).
11. Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Caughey B, et al. The most infectious prion protein particles. Nature 437(7056): 257-61 (2005).
12. Eigen M. Prionics or the kinetic basis of prion diseases. Biophys Chem 63(1): A1-18 (1996).
13. Griffith JS. Self-replication and scrapie. Nature 215(5105): 1043-4 (1967).
14. Bolton DC, Bendheim PE. A modified host protein model of scrapie. Ciba Found Symp 135: 164-81 (1988).
15. Come JH, Fraser PE and Lansbury PT, Jr. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc Natl Acad Sci USA 90(13): 5959-63 (1993).
16. Lansbury PT Jr and Caughey B. The chemistry of scrapie infection: implications of the 'ice 9' metaphor. Chem Biol 2(1): 1-5 (1995).
17. Watzky MA and Finke RG. Transition metal nanocluster formation kinetic and mechanistic studies. A new mechanism when hydrogen is the reductant: slow, continuous nucleation and fast autocatalytic surface growth. J Am Chem Soc 119: 10382-10400 (1997).
18. Safar J, Roller PP, Gajdusek DC and Gibbs CJ Jr. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J Biol Chem 268(27): 20276-84 (1993).
19. Safar J, Roller PP, Gajdusek DC and Gibbs CJ Jr. Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33(27): 8375-83 (1994).
20. Riesner D, Kellings K, Post K, Wille H, Serban H, Groth D, et al., Disruption of prion rods generates 10-nm spherical particles having high alpha-helical content and lacking scrapie infectivity. J Virol 70(3): 1714-22 (1996).
21. Zhang H, Stöckel J, Mehlhorn I, Groth D, Baldwin MA, Prusiner SB, et al. Physical studies of conformational plasticity in a recombinant prion protein. Biochemistry 36(12): 3543-53 (1997).
22. Swietnicki W, Petersen R, Gambetti P, Surewicz WK. pH-dependent stability and conformation of the recombinant human prion protein PrP(90-231). J Biol Chem 272(44): 27517-20 (1997).
23. Jackson GS, Hosszu LLP, Power A, Hill AF, Kenney J, Saibil H, et al. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 283(5409): 1935-7 (1999).
24. Baskakov IV, Legname G, Baldwin MA, Prusiner SB, Cohen FE, et al., Pathway complexity of prion protein assembly into amyloid. J Biol Chem 277(24): 21140-8 (2002).
25. Post K, Pitschke M, Schäfer O, Wille H, Appel TR, Kirsch D, et al. Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation. Biol Chem 379(11): 1307-17 (1998).
26. Stohr J, Weinmann N, Wille H, Kaimann T, Nagel-Steger L, Birkmann E, et al. Mechanisms of prion protein assembly into amyloid. Proc Natl Acad Sci USA 105(7): 2409-14 (2008).
27. Rezaei H, Choiset Y, Eghiaian F, Treguer E, Mentre P, Debey P, et al. Amyloidogenic unfolding intermediates differentiate sheep prion protein variants. J Mol Biol 322(4): 799-814 (2002).
28. Lu BY, Chang JY. Isolation and characterization of a polymerized prion protein. Biochem J 364(Pt 1): 81-7 (2002).
29. Rezaei H, Eghiaiana F, Perezc J, Doubleta B, Choisetd Y, Haertle T, et al. Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities. J Mol Biol 347(3): 665-79 (2005).
30. Legname G, Baskakov IV, Nguyen HOB, Riesner D, Cohen FE, DeArmond SJ, et al., Synthetic mammalian prions. Science 305(5684): 673-6 (2004).
31. Bessen RA, Kocisko DA, Raymond GJ, Nandan S, Lansbury PT, Caughey B, et al. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375(6533): 698-700 (1995).
32. Collinge J and Clarke AR. A general model of prion strains and their pathogenicity. Science 318(5852): 930-6 (2007).
33. Caughey B, Raymond GJ and Bessen RA. Strain-dependent differences in beta-sheet conformations of abnormal prion protein. J Biol Chem 273(48): 32230-5 (1998).
34. Somerville RA, Oberthür RC, Havekost U, MacDonald F, Taylor DM, Dickinson AG, et al. Characterization of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications. J Biol Chem 277(13): 11084-9 (2002).
35. Jones EM and Surewicz WK. Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 121(1): 63-72 (2005).
36. Sun Y, Makarava N, Lee CI, Laksanalamai P, Robb FT, Baskakov IV, et al., Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J Mol Biol 376(4): 1155-67 (2008).
37. Makarava N and Baskakov IV. The same primary structure of the prion protein yields two distinct self-propagating states. J Biol Chem (2008).
38. Eghiaian F, Daubenfeld T, Quenet Y, Audenhaege MV, Bouin AP, Rest GVD, et al. Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage. Proc Natl Acad Sci USA 104(18): 7414-9 (2007).
39. Oosawa F and Asakura S. Thermodynamics of the Polymerization of Protein. (1979) ed. 1971, New York: Academic Press. 223.
40. Oosawa F and Kasai M. A theory of linear and helical aggregations of macromolecules. J Mol Biol 4: 10-21 (1962).
41. Butler PJ. Assembly of tobacco mosaic virus particle. Nature 233(5314): 25-7 (1971).
42. Malfa R and Steinhardt J. A temperature-dependent latent-period in the aggregation of sickle-cell deoxyhemoglobin. Biochem Biophys Res Commun 59(3): 887-93 (1974).
43. Goldstein RF and Stryer L. Cooperative polymerization reactions. Analytical approximations, numerical examples, and experimental strategy. Biophys J 50(4): 583-99 (1986).
44. Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ and Prusiner SB. Structural clues to prion replication. Science 264(5158): 530-1 (1994).
45. Harper JD and Lansbury PT, Jr. 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 (1997).
46. Erickson HP and Pantaloni D. The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers. Biophys J 34(2): 293-309 (1981).
47. Manning GS. Polymer persistence length characterized as a critical length for instability caused by a fluctuating twist. Phys Rev A 34(1): 668-670 (1986).
48. Hvidt S, Nestler HM, Greaser ML and Ferry JD. Flexibility of myosin rod determined from dilute solution viscoelastic measurements. Biochemistry 21(17): 4064-73 (1982).
49. Obermann H, Mandelkow EM, Lange G and Mandelkow E. Microtubule oscillations. Role of nucleation and microtubule number concentration. J Biol Chem (1990). 265(8): 4382-8 (1982).
50. Wille H, Michelitsch MD, Guénebaut V, Supattapone S, Serban A, Cohen FE, et al. Structural studies of the scrapie prion protein by electron crystallography. Proc Natl Acad Sci USA 99(6): 3563-8 (2002).
51. Owen JP, Rees HC, Maddison BC, Terry LA, Thorne L, Jackman R, et al. Molecular profiling of ovine prion diseases by using thermolysin-resistant PrPSc and endogenous C2 PrP fragments. J Virol 81(19): 10532-9 (2007).
52. Fischer M, Rülicke T, Raeber A, Sailer A, Moser M, Oesch B, et al. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. Embo J 15(6): 1255-64 (1996).
53. Rogers M, Yehiely F, Scott M and Prusiner SB. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc Natl Acad Sci USA 90(8): 3182-6 (1993).
54. Morrissey MP and Shakhnovich EI. Evidence for the role of PrP(C) helix 1 in the hydrophilic seeding of prion aggregates. Proc Natl Acad Sci USA 96(20): 11293-8 (1999).
55. Enari M, Flechsig E and Weissmann C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc Natl Acad Sci USA 98(16): 9295-9 (2001).
56. Heppner FL, Musahl C, Arrighi I, Klein MA, Rülicke T, Oesch B, et al. Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science 294(5540): 178-82 (2001).
57. Peretz D, Williamson RA, Kaneko K, Vergara J, Leclerc E, et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412(6848): 739-43 (2001).
58. Feraudet C, Morel N, Simon S, Volland H, Frobert Y, Créminon C, et al. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. J Biol Chem 280(12): 11247-58 (2005).
59. Dima RI and Thirumalai D. Probing the instabilities in the dynamics of helical fragments from mouse PrPC. Proc Natl Acad Sci USA 101(43): 15335-40 (2004).
60. De Simone A, Zagari A and Derreumaux P. Water molecules as structural determinants among prions of low sequence identity. FEBS Lett 580(10): 2488-94 (2006).
61. Lu X and Wintrode PL. Surewicz WK. Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc Natl Acad Sci USA 104(5): 1510-5 (2007).
62. Morris AM, Watzky MA, Agar JN, Finke RG. Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth. Biochemistry 47(8): 2413-27 (2008).
63. Ridley RM, Baker1 HF, Windle CP and Cummings RM. Very long term studies of the seeding of beta-amyloidosis in primates. J Neural Transm 113(9): 1243-51 (2006).
64. Meyer-Luehmann M, Coomaraswamy J, Bolmont T, Kaeser S, Schaefer C, Kilger E, et al. Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 313(5794): 1781-4 (2006).
65. Kane MD, Lipinski WJ, Callahan MJ, Bian F, Durham RA, Schwarz RD, et al. Evidence for seeding of beta -amyloid by intracerebral infusion of Alzheimer brain extracts in beta -amyloid precursor protein-transgenic mice. J Neurosci 20(10): 3606-11 (2000).