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Cell-free formation of protease-resistant prion protein
Open accessAbstract
THE infectious agent (or 'prion') of the transmissible spongiform encephalopathies (TSEs) such as scrapie resembles a virus in that it replicates in vivo and has distinct strains1, but it was postulated long ago to contain only protein2,3. More recently, PrPSc, a pathogenic, scrapie-associated form of the host-encoded prion protein (PrP), was identified as a possible primary TSE agent protein4–6. PrPSc is defined biochemically by its insolubility and resistance to proteases7 and is derived post-translationally from normal, protease-sensitive PrP (PrPc)8,9. The conversion seems to involve conformational change rather than covalent modification10–13. However, the conversion mechanism and the relationship of PrPSc formation to TSE agent replication remain unclear. Here we report the conversion of PrPc to protease-resistant forms similar to PrPSc in a cell-free system composed of substantially purified constituents. This conversion was selective and required the presence of preexisting PrPSc, providing direct evidence that PrPSc derives from specific PrPc–PrPSc interactions.
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Cited by
Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J., & Hill, A. F. (1996) · Nature · doi:10.1038/383685a0 · Cited by 1,735
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Self-citationCaughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Self-citationPrion Diseases of Humans and Animals: Their Causes and Molecular Basis
Collinge, J. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.519 · Cited by 1,344
The most infectious prion protein particles
Silveira, J. R., Raymond, G. J., Hughson, A. G., Race, R. E., Sim, V. L., Hayes, S. F., & Caughey, B. (2005) · Nature · doi:10.1038/nature03989 · Cited by 899
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Metadata
- Authors
- Kocisko, D. A., Come, J. H., Priola, S. A., Chesebro, B., Raymond, G. J., Lansbury, P. T., & Caughey, B.
- Venue
- Nature
- Published
- 1994-08
- Volume
- 370
- Issue
- 6489
- Pages
- 471-474
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1992084965
- Cited by
- 883
- References
- 0
- FWCI
- 15.69
- Type
- journal article
- Language
- en
- Open access
- green
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- Kocisko, D. A., Come, J. H., Priola, S. A., Chesebro, B., Raymond, G. J., Lansbury, P. T., & Caughey, B. (1994). Cell-free formation of protease-resistant prion protein. Nature. https://doi.org/10.1038/370471a0
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