High pressure, a tool to switch between soluble and fibrillar prion protein structures

Communicative and Integrative Biology

Volumn 5, Issue 1, 2012, Pages 30-33

  Torrent, Joan ^a,b,c,d   Lange, Reinhard ^b,c,d  

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

^b UNIV MONTPELLIER   (France)

^c INSERM   (France)

^d PSL RESEARCH UNIVERSITY   (France)

Author keywords

Amyloid; High pressure; Prion; Protein misfolding

Indexed keywords

EID: 84859075501     PISSN: None     EISSN: 19420889     Source Type: Journal    
DOI: 10.4161/cib.17969     Document Type: Article

References (19)

1. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44; PMID:6801762; DOI: 10.1126/science.6801762.
2. Cohen FE, Prusiner SB. Pathologic conformations of prion proteins. Annu Rev Biochem 1998; 67:793-819; PMID:9759504; DOI: 10.1146/annurev.biochem. 67.1.793.
3. 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 USA 1997; 94:9773-8; PMID:9275200; DOI: 10.1073/pnas.94.18.9773.
4. +]: an epigenetic modulator of translation termination efficiency. Annu Rev Cell Dev Biol 1999; 15:661-703; PMID:10611975; DOI: 10.1146/annurev.cellbio.15.1.661.
5. Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. Prions of yeast as heritable amyloidoses. J Struct Biol 2000; 130:310-22; PMID:10940235; DOI: 10.1006/jsbi.2000.4250.
6. Prusiner SB, DeArmond SJ. Prion diseases of the central nervous system. Monogr Pathol 1990; 32:86-122; PMID:2192281.
7. Carrell RW, Lomas DA. Conformational disease. Lancet 1997; 350:134-8; PMID:9228977; DOI: 10.1016/S0140-6736(97)02073-4.
8. Breydo L, Makarava N, Baskakov IV. Methods for conversion of prion protein into amyloid fibrils. Methods Mol Biol 2008; 459:105-15; PMID:18576151; DOI: 10.1007/978-1-59745-234-2_8.
9. Come JH, Fraser PE, Lansbury PT Jr. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc Natl Acad Sci USA 1993; 90:5959-63; PMID:8327467; DOI: 10.1073/pnas.90.13.5959.
10. Jarrett JT, Lansbury PT Jr. Seeding " one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73:1055-8; PMID:8513491; DOI: 10.1016/0092-8674(93)90635-4.
11. Torrent J, Alvarez-Martinez MT, Heitz F, Liautard JP, Balny C, Lange R. Alternative prion structural changes revealed by high pressure. Biochemistry 2003; 42:1318-25; PMID:12564935; DOI: 10.1021/bi0269916.
12. Torrent J, Alvarez-Martinez MT, Harricane MC, Heitz F, Liautard JP, Balny C, et al. High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation. Biochemistry 2004; 43:7162-70; PMID:15170353; DOI: 10.1021/bi049939d.
13. El Moustaine D, Perrier V, Smeller L, Lange R, Torrent J. Full-length prion protein aggregates to amyloid fibrils and spherical particles by distinct pathways. FEBS J 2008; 275:2021-31; PMID:18355314; DOI: 10.1111/j.1742-4658.2008.06356.x.
14. El Moustaine D, Torrent J, Lange R. Prion protein aggregation induced by copper (II) and heparan sulfate. Pressure dependent switch of reaction pathways. Z Naturforsch 2008; 63:745-55.
15. Brown P, Meyer R, Cardone F, Pocchiari M. Ultrahigh-pressure inactivation of prion infectivity in processed meat: a practical method to prevent human infection. Proc Natl Acad Sci USA 2003; 100:6093-7; PMID:12732724; DOI: 10.1073/pnas.1031826100.
16. Fernández García A, Heindl P, Voigt H, Buttner M, Wienhold D, Butz P, et al. Reduced proteinase K resistance and infectivity of prions after pressure treatment at 60°C. J Gen Virol 2004; 85:261-4; PMID:14718641; DOI: 10.1099/vir.0.19410-0.
17. El Moustaine D, Perrier V, Acquatella-Tran Van Ba I, Meersman F, Ostapchenko VG, Baskakov IV, et al. Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure. J Biol Chem 2011; 286:13448-59; PMID:21357423; DOI: 10.1074/jbc.M110.192872.
18. Bocharova OV, Breydo L, Salnikov VV, Gill AC, Baskakov IV. Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease. Protein Sci 2005; 14:1222-32; PMID:15802644; DOI: 10.1110/ps.041186605.
19. Torrent J, Alvarez-Martinez MT, Liautard JP, Balny C, Lange R. The role of the 132-160 region in prion protein conformational transitions. Protein Sci 2005; 14:956-67; PMID:15772306; DOI: 10.1110/ps.04989405.