Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions

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

Volumn 108, Issue 48, 2011, Pages

  Klingeborn, Mikael ^a,b   Race, Brent ^a   Meade White, Kimberly D ^a   Chesebro, Bruce ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

Amyloid; Creutzfeldt Jakob disease; Neurodegeneration; Protein aggregation; Protein polymerization

Indexed keywords

PRION PROTEIN; PROTEASE RESISTANT PRION PROTEIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ATAXIA; BRAIN HOMOGENATE; CELL FREE SYSTEM; CONTROLLED STUDY; DILUTION; FEMALE; GENE AMPLIFICATION; HAMSTER; HISTOPATHOLOGY; HYPERACTIVITY; INCUBATION TIME; KYPHOSIS; MOUSE; NEUROPATHOLOGY; NONHUMAN; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MISFOLDING CYCLIC AMPLIFICATION; QUANTITATIVE ANALYSIS; SCRAPIE; SOMNOLENCE; TITRIMETRY; TRANSGENIC MOUSE; VIRUS INFECTIVITY; VIRUS STRAIN; WEIGHT REDUCTION;

ANIMALS; BRAIN; CELL-FREE SYSTEM; CRICETINAE; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; MICE; MICE, TRANSGENIC; NUCLEIC ACID AMPLIFICATION TECHNIQUES; PRIONS; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 82755197344     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111255108     Document Type: Article

References (49)

1. Chesebro B (2003) Introduction to the transmissible spongiform encephalopathies or prion diseases. Br Med Bull 66:1-20.
2. Brandner S, et al. (1996) Normal host prion protein (PrPC) is required for scrapie spread within the central nervous system. Proc Natl Acad Sci USA 93:13148-13151.
3. Büeler H, et al. (1993) Mice devoid of PrP are resistant to scrapie. Cell 73:1339-1347. (Pubitemid 23201147)
4. Rohwer RG (1991) The scrapie agent: "a virus by any other name". Transmissible Spongiform Encephalopathies, Scrapie, BSE and Related Disorders, Current Topics in Microbiology and Immunology, ed Chesebro BW (Springer, New York), Vol 172, pp 195-232.
5. Griffith JS (1967) Self-replication and scrapie. Nature 215:1043-1044.
6. Bolton DC, McKinley MP, Prusiner SB (1982) Identification of a protein that purifies with the scrapie prion. Science 218:1309-1311.
7. Prusiner SB (1982) Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
8. Merz PA, Somerville RA, Wisniewski HM, Iqbal K (1981) Abnormal fibrils from scrapieinfected brain. Acta Neuropathol 54:63-74.
9. Prusiner SB, et al. (1983) Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358. (Pubitemid 14202913)
10. Diringer H, et al. (1983) Scrapie infectivity, fibrils and low molecular weight protein. Nature 306:476-478. (Pubitemid 14235568)
11. McKinley MP, Bolton DC, Prusiner SB (1983) A protease-resistant protein is a structural component of the scrapie prion. Cell 35:57-62. (Pubitemid 14240218)
12. Chesebro B (1998) BSE and prions: Uncertainties about the agent. Science 279:42-43.
13. Chesebro B (1999) Prion protein and the transmissible spongiform encephalopathy diseases. Neuron 24:503-506.
14. Dormont D (1999) Agents that cause transmissible subacute spongiform encephalopathies. Biomed Pharmacother 53:3-8.
15. Kocisko DA, et al. (1994) Cell-free formation of protease-resistant prion protein. Nature 370:471-474. (Pubitemid 24263553)
16. Saborio GP, Permanne B, Soto C (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411:810-813. (Pubitemid 32588105)
17. Colby DW, et al. (2007) Prion detection by an amyloid seeding assay. Proc Natl Acad Sci USA 104:20914-20919.
18. Atarashi R, et al. (2008) Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nat Methods 5:211-212.
19. Caughey B, Baron GS, Chesebro B, Jeffrey M (2009) Getting a grip on prions: Oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem 78:177-204.
20. Kim JI, et al. (2010) Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem 285:14083-14087.
21. Castilla J, Saá P, Hetz C, Soto C (2005) In vitro generation of infectious scrapie prions. Cell 121:195-206. (Pubitemid 40546388)
22. Deleault NR, Harris BT, Rees JR, Supattapone S (2007) Formation of native prions from minimal components in vitro. Proc Natl Acad Sci USA 104:9741-9746. (Pubitemid 47175337)
23. Wang F, Wang X, Yuan CG, Ma J (2010) Generating a prion with bacterially expressed recombinant prion protein. Science 327:1132-1135.
24. Weber P, et al. (2006) Cell-free formation of misfolded prion protein with authentic prion infectivity. Proc Natl Acad Sci USA 103:15818-15823. (Pubitemid 44657550)
25. Prusiner SB, et al. (1980) Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent. Biochemistry 19:4883-4891.
26. Prusiner SB, et al. (1982) Measurement of the scrapie agent using an incubation time interval assay. Ann Neurol 11:353-358. (Pubitemid 12133693)
27. Somerville RA, Carp RI (1983) Altered scrapie infectivity estimates by titration and incubation period in the presence of detergents. J Gen Virol 64:2045-2050. (Pubitemid 13048395)
28. Castilla J, et al. (2008) Crossing the species barrier by PrP(Sc) replication in vitro generates unique infectious prions. Cell 134:757-768.
29. Kurt TD, et al. (2007) Efficient in vitro amplification of chronic wasting disease PrPRES. J Virol 81:9605-9608. (Pubitemid 47311509)
30. Meyerett C, et al. (2008) In vitro strain adaptation of CWD prions by serial protein misfolding cyclic amplification. Virology 382:267-276.
31. Kercher L, Favara C, Chan CC, Race R, Chesebro B (2004) Differences in scrapie-induced pathology of the retina and brain in transgenic mice that express hamster prion protein in neurons, astrocytes, or multiple cell types. Am J Pathol 165:2055-2067. (Pubitemid 39578383)
32. Bruce ME (2003) TSE strain variation. Br Med Bull 66:99-108.
33. Green KM, et al. (2008) Accelerated high fidelity prion amplification within and across prion species barriers. PLoS Pathog 4:e1000139.
34. Weber P, Reznicek L, Mitteregger G, Kretzschmar H, Giese A (2008) Differential effects of prion particle size on infectivity in vivo and in vitro. Biochem Biophys Res Commun 369:924-928.
35. Weissmann C (1991) Spongiform encephalopathies. The prion's progress. Nature 349:569-571.
36. Wilham JM, et al. (2010) Rapid end-point quantitation of prion seeding activity with sensitivity comparable to bioassays. PLoS Pathog 6:e1001217.
37. May BC, Govaerts C, Prusiner SB, Cohen FE (2004) Prions: So many fibers, so little infectivity. Trends Biochem Sci 29:162-165. (Pubitemid 38472018)
38. Deleault NR, Kascsak R, Geoghegan JC, Supattapone S (2010) Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro. Biochemistry 49:3928-3934.
39. Piro JR, et al. (2011) Seeding specificity and ultrastructural characteristics of infectious recombinant prions. Biochemistry 50:7111-7116.
40. Barron RM, et al. (2007) High titers of transmissible spongiform encephalopathy infectivity associated with extremely low levels of PrPSc in vivo. J Biol Chem 282:35878-35886. (Pubitemid 350277109)
41. Silveira JR, et al. (2005) The most infectious prion protein particles. Nature 437:257-261. (Pubitemid 41294488)
42. Weber P, et al. (2007) Generation of genuine prion infectivity by serial PMCA. Vet Microbiol 123:346-357. (Pubitemid 47096769)
43. Makarava N, et al. (2010) Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol 119:177-187.
44. Castilla J, et al. (2008) Cell-free propagation of prion strains. EMBO J 27:2557-2566.
45. Race R, Oldstone M, Chesebro B (2000) Entry versus blockade of brain infection following oral or intraperitoneal scrapie administration: Role of prion protein expression in peripheral nerves and spleen. J Virol 74:828-833. (Pubitemid 30036219)
46. Meade-White K, et al. (2007) Resistance to chronic wasting disease in transgenic mice expressing a naturally occurring allelic variant of deer prion protein. J Virol 81:4533-4539. (Pubitemid 46668651)
47. Dougherty R (1964) Animal virus titration techniques. Techniques in Experimental Virology, ed Harris R (Academic, New York), pp 169-224.
48. Kascsak RJ, et al. (1987) Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 61:3688-3693. (Pubitemid 18011463)
49. Meade-White KD, et al. (2009) Characteristics of 263K scrapie agent in multiple hamster species. Emerg Infect Dis 15:207-215.