Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways

FEBS Journal

Volumn 275, Issue 9, 2008, Pages 2021-2031

  El Moustaine, Driss ^a,b,c   Perrier, Veronique ^a,b,c   Smeller, Laszlo ^d   Lange, Reinhard ^a,b,c   Torrent, Joan ^a,b,c  

^a UNIV MONTPELLIER   (France)

^b INSERM   (France)

^c PSL RESEARCH UNIVERSITY   (France)

^d SEMMELWEIS UNIVERSITY   (Hungary)

Author keywords

Amyloid fibrils; Conformational transition; High pressure; Prion protein; Protein aggregation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMYLOID; POLYPEPTIDE; PRION PROTEIN; THIOFLAVINE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; ISOELECTRIC POINT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; REACTION ANALYSIS; SPECTROSCOPY; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID; BIREFRINGENCE; COLORING AGENTS; CONGO RED; HYDROGEN-ION CONCENTRATION; LIGHT; MICROSCOPY, POLARIZATION; PRESSURE; PRIONS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION; SOLUBILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SPECTRUM ANALYSIS;

EID: 42449160594     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06356.x     Document Type: Article

References (39)

1. Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136 144.
2. Baskakov IV, Legname G, Prusiner SB Cohen FE (2001) Folding of prion protein to its native alpha-helical conformation is under kinetic control. J Biol Chem 276, 19687 19690.
3. Wildegger G, Liemann S Glockshuber R (1999) Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat Struct Biol 6, 550 553.
4. Baskakov IV, Legname G, Baldwin MA, Prusiner SB Cohen FE (2002) Pathway complexity of prion protein assembly into amyloid. J Biol Chem 277, 21140 21148.
5. Baskakov IV (2007) The reconstitution of mammalian prion infectivity de novo. Febs J 274, 576 587.
6. Baskakov IV Breydo L (2007) Converting the prion protein: what makes the protein infectious. Biochim Biophys Acta 1772, 692 703.
7. Caughey B Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26, 267 298.
8. Chiesa R Harris DA (2001) Prion diseases: what is the neurotoxic molecule? Neurobiol Dis 8, 743 763.
9. Kazlauskaite J, Young A, Gardner CE, Macpherson JV, Venien-Bryan C Pinheiro TJ (2005) An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells. Biochem Biophys Res Commun 328, 292 305.
10. Simoneau S, Rezaei H, Sales N, Kaiser-Schulz G, Lefebvre-Roque M, Vidal C, Fournier JG, Comte J, Wopfner F, Grosclaude J et al. (2007) In vitro and in vivo neurotoxicity of prion protein oligomers. PLoS Pathog 3, e125.
11. Jackson GS, Hosszu LL, Power A, Hill AF, Kenney J, Saibil H, Craven CJ, Waltho JP, Clarke AR Collinge J (1999) Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 283, 1935 1937.
12. Swietnicki W, Morillas M, Chen SG, Gambetti P Surewicz WK (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39, 424 431.
13. Leffers KW, Schell J, Jansen K, Lucassen R, Kaimann T, Nagel-Steger L, Tatzelt J Riesner D (2004) The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites. J Mol Biol 344, 839 853.
14. Leffers KW, Wille H, Stohr J, Junger E, Prusiner SB Riesner D (2005) Assembly of natural and recombinant prion protein into fibrils. Biol Chem 386, 569 580.
15. Rezaei H, Choiset Y, Eghiaian F, Treguer E, Mentre P, Debey P, Grosclaude J Haertle T (2002) Amyloidogenic unfolding intermediates differentiate sheep prion protein variants. J Mol Biol 322, 799 814.
16. Smeller L, Roemich H Lange R (2006) Proteins under high pressure. Biochim Biophys Acta 1764, 329 330.
17. Mozhaev VV, Heremans K, Frank J, Masson P Balny C (1996) High pressure effects on protein structure and function. Proteins 24, 81 91.
18. Royer CA (2002) Revisiting volume changes in pressure-induced protein unfolding. Biochim Biophys Acta 1595, 201 209.
19. Kim YS, Randolph TW, Seefeldt MB Carpenter JF (2006) High-pressure studies on protein aggregates and amyloid fibrils. Methods Enzymol 413, 237 253.
20. Silva JL, Cordeiro Y Foguel D (2006) Protein folding and aggregation: two sides of the same coin in the condensation of proteins revealed by pressure studies. Biochim Biophys Acta 1764, 443 451.
21. Silva JL, Foguel D Royer CA (2001) Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem Sci 26, 612 618.
22. Cordeiro Y, Kraineva J, Ravindra R, Lima LM, Gomes MP, Foguel D, Winter R Silva JL (2004) Hydration and packing effects on prion folding and beta-sheet conversion: high-pressure spectroscopy and pressure perturbation calorimetry studies. J Biol Chem 279, 32354 32359.
23. Torrent J, Alvarez-Martinez MT, Harricane MC, Heitz F, Liautard JP, Balny C Lange R (2004) High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation. Biochemistry 43, 7162 7170.
24. Torrent J, Alvarez-Martinez MT, Heitz F, Liautard JP, Balny C Lange R (2003) Alternative prion structural changes revealed by high pressure. Biochemistry 42, 1318 1325.
25. Torrent J, Alvarez-Martinez MT, Liautard JP, Balny C Lange R (2005) The role of the 132-160 region in prion protein conformational transitions. Protein Sci 14, 956 967.
26. Torrent J, Alvarez-Martinez MT, Liautard JP Lange R (2006) Modulation of prion protein structure by pressure and temperature. Biochim Biophys Acta 1764, 546 551.
27. Torrent J, Balny C Lange R (2006) High pressure modulates amyloid formation. Protein Pept Lett 13, 271 277.
28. Dzwolak W (2006) Tuning amyloidogenic conformations through cosolvents and hydrostatic pressure: when the soft matter becomes even softer. Biochim Biophys Acta 1764, 470 480.
29. Meersman F, Dobson CM Heremans K (2006) Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions. Chem Soc Rev 35, 908 917.
30. Bemporad F, Calloni G, Campioni S, Plakoutsi G, Taddei N Chiti F (2006) Sequence and structural determinants of amyloid fibril formation. Acc Chem Res 39, 620 627.
31. Rousseau F, Schymkowitz J Serrano L (2006) Protein aggregation and amyloidosis: confusion of the kinds? Curr Opin Struct Biol 16, 118 126.
32. Krebs MR, Devlin GL Donald AM (2007) Protein particulates: another generic form of protein aggregation? Biophys J 92, 1336 1342.
33. Cordeiro Y, Kraineva J, Gomes MP, Lopes MH, Martins VR, Lima LM, Foguel D, Winter R Silva JL (2005) The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. Biophys J 89, 2667 2676.
34. Barducci A, Chelli R, Procacci P Schettino V (2005) Misfolding pathways of the prion protein probed by molecular dynamics simulations. Biophys J 88, 1334 1343.
35. Hirschberger T, Stork M, Schropp B, Winklhofer KF, Tatzelt J Tavan P (2006) Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations. Biophys J 90, 3908 3918.
36. Kuznetsov IB Rackovsky S (2004) Comparative computational analysis of prion proteins reveals two fragments with unusual structural properties and a pattern of increase in hydrophobicity associated with disease-promoting mutations. Protein Sci 13, 3230 3244.
37. Bocharova OV, Breydo L, Parfenov AS, Salnikov VV Baskakov IV (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J Mol Biol 346, 645 659.
38. Van EldikR, Asano T Le NobleWJ (1989) Activation and reaction volume in solution 2. Chem Rev 89, 549 688.
39. Rezaei H, Marc D, Choiset Y, Takahashi M, Hui BonHoa G, Haertle T, Grosclaude J Debey P (2000) 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, 2833 2839.