The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Formation of native prions from minimal components in vitro
Open accessAbstract
The conformational change of a host protein, PrP C , into a disease-associated isoform, PrP Sc , appears to play a critical role in the pathogenesis of prion diseases such as Creutzfeldt–Jakob disease and scrapie. However, the fundamental mechanism by which infectious prions are produced in neurons remains unknown. To investigate the mechanism of prion formation biochemically, we conducted a series of experiments using the protein misfolding cyclic amplification (PMCA) technique with a preparation containing only native PrP C and copurified lipid molecules. These experiments showed that successful PMCA propagation of PrP Sc molecules in a purified system requires accessory polyanion molecules. In addition, we found that PrP Sc molecules could be formed de novo from these defined components in the absence of preexisting prions. Inoculation of samples containing either prion-seeded or spontaneously generated PrP Sc molecules into hamsters caused scrapie, which was transmissible on second passage. These results show that prions able to infect wild-type hamsters can be formed from a minimal set of components including native PrP C molecules, copurified lipid molecules, and a synthetic polyanion.
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Cites
Novel Proteinaceous Infectious Particles Cause Scrapie
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Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
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Eight prion strains have PrPSc molecules with different conformations
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Scrapie prion protein contains a phosphatidylinositol glycolipid
STAHL, N. (1987) · Cell · doi:10.1016/0092-8674(87)90150-4 · Cited by 1,112
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The most infectious prion protein particles
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Cell-free formation of protease-resistant prion protein
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In Vitro Generation of Infectious Scrapie Prions
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Non-genetic propagation of strain-specific properties of scrapie prion protein
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Bellingham, S. A., Guo, B. B., Coleman, B. M., & Hill, A. F. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00124 · Cited by 412
A Test for Creutzfeldt–Jakob Disease Using Nasal Brushings
Orrú, C. D., Bongianni, M., Tonoli, G., Ferrari, S., Hughson, A. G., Groveman, B. R., Fiorini, M., Pocchiari, M., Monaco, S., Caughey, B., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1315200 · Cited by 355
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking
Atarashi, R., Wilham, J. M., Christensen, L., Hughson, A. G., Moore, R. A., Johnson, L. M., Onwubiko, H. A., Priola, S. A., & Caughey, B. (2008) · Nature Methods · doi:10.1038/nmeth0308-211 · Cited by 314
Ugalde, C. L., Finkelstein, D. I., Lawson, V. A., & Hill, A. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13772 · Cited by 92
Metadata
- Authors
- Deleault, N. R., Harris, B. T., Rees, J. R., & Supattapone, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-06-05
- Volume
- 104
- Issue
- 23
- Pages
- 9741-9746
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2067540111
- Cited by
- 631
- References
- 49
- FWCI
- 20.95
- Type
- journal article
- Language
- en
- Open access
- green
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- Deleault, N. R., Harris, B. T., Rees, J. R., & Supattapone, S. (2007). Formation of native prions from minimal components in vitro. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0702662104
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