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Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.
Open accessAbstract
Limited proteolysis of the scrapie prion protein (PrPSc) generates PrP 27-30, which polymerizes into amyloid. By attenuated total reflection-Fourier transform infrared spectroscopy, PrP 27-30 polymers contained 54% beta-sheet, 25% alpha-helix, 10% turns, and 11% random coil; dispersion into detergent-lipid-protein-complexes preserved infectivity and secondary structure. Almost 60% of the beta-sheet was low-frequency infrared-absorbing, reflecting intermolecular aggregation. Decreased low-frequency beta-sheet and increased turn content were found after SDS/PAGE, which disassembled the amyloid polymers, denatured PrP 27-30, and diminished scrapie infectivity. Acid-induced transitions were reversible, whereas alkali produced an irreversible transition centered at pH 10 under conditions that diminished infectivity. Whether PrPSc synthesis involves a transition in the secondary structure of one or more domains of the cellular prion protein from alpha-helical, random coil, or turn into beta-sheet remains to be established.
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Cited by
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Self-citationMayeux, R., Ottman, R., Maestre, G., Ngai, C., Tang, M.-X., Ginsberg, H., Chun, M., Tycko, B., & Shelanski, M. (1995) · Neurology · doi:10.1212/wnl.45.3.555 · Cited by 590
Ellis, R. J., Olichney, J. M., Thal, L. J., Mirra, S. S., Morris, J. C., Beekly, D., & Heyman, A. (1996) · Neurology · doi:10.1212/wnl.46.6.1592 · Cited by 561
Myers, R. H., Schaefer, E. J., Wilson, P. W. F., D'Agostino, R., Ordovas, J. M., Espino, A., Au, R., White, R. F., Knoefel, J. E., Cobb, J. L., et al. (1996) · Neurology · doi:10.1212/wnl.46.3.673 · Cited by 346
Lautenschlager, N. T., Cupples, L. A., Rao, V. S., Auerbach, S. A., Becker, R., Burke, J., Chui, H., Duara, R., Foley, E. J., Glatt, S. L., et al. (1996) · Neurology · doi:10.1212/wnl.46.3.641 · Cited by 298
Metadata
- Authors
- Gasset, M., Baldwin, M. A., Fletterick, R. J., & Prusiner, S. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-01
- Volume
- 90
- Issue
- 1
- Pages
- 1-5
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1997441257
- Cited by
- 307
- References
- 0
- FWCI
- 10.49
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Gasset, M., Baldwin, M. A., Fletterick, R. J., & Prusiner, S. B. (1993). Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.1.1
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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