Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 21, Issue 7, Pages 2608-2616Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.21.7.2608-2616.2001
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Funding
- NCRR NIH HHS [P41 RR001614, RR01614] Funding Source: Medline
- NIA NIH HHS [P01 AG002132, AG02132, AG10770, P01 AG010770] Funding Source: Medline
- NINDS NIH HHS [K08 NS02048-02, NS14069] Funding Source: Medline
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An abridged prion protein (PrP) molecule of 106 amino acids, designated PrP106, is capable of forming infectious miniprions in transgenic mice (S. Supattapone, P. Bosque, T. Muramoto, H. Wille, C. Aagaard, D. Peretz, H.-O. B. Nguyen, C. Heinrich, M. Torchia, J. Safar, F. E. Cohen, S. J. DeArmond, S. B. Prusiner, and M. Scott, Cell 96:869-878, 1999). We removed additional sequences from PrP106 and identified a 61-residue peptide, designated PrP61, that spontaneously adopted a protease-resistant conformation in neuroblastoma cells. Synthetic PrP61 bearing a carboxy-terminal lipid moiety polymerized into protease resistant, beta -sheet-enriched amyloid fibrils at a physiological salt concentration. Transgenic mice expressing low levels of PrP61 died spontaneously with ataxia. Neuropathological examination revealed accumulation of protease resistant PrP61 within neuronal dendrites and cell bodies, apparently causing apoptosis, PrP61 may be a useful model for deciphering the mechanism by which PrP molecules acquire protease resistance and become neurotoxic.
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