| First Author | Kaneko K | Year | 2000 |
| Journal | J Mol Biol | Volume | 295 |
| Issue | 4 | Pages | 997-1007 |
| PubMed ID | 10656806 | Mgi Jnum | J:61411 |
| Mgi Id | MGI:1354881 | Doi | 10.1006/jmbi.1999.3386 |
| Citation | Kaneko K, et al. (2000) A synthetic peptide initiates Gerstmann-Straussler-Scheinker (GSS) disease in transgenic mice. J Mol Biol 295(4):997-1007 |
| abstractText | The molecular basis of the infectious, inherited and sporadic forms of prion diseases is best explained by a conformationally dimorphic protein that can exist in distinct normal and disease-causing isoforms. We identified a 55-residue peptide of a mutant prion protein that can be refolded into at least two distinct conformations. When inoculated intracerebrally into the appropriate transgenic mouse host, 20 of 20 mice receiving the beta-form of this peptide developed signs of central nervous system dysfunction at approximately 360 days, with neurohistologic changes that are pathognomonic of Gerstmann-Straussler-Scheinker disease. By contrast, eight of eight mice receiving a non-beta-form of the peptide failed to develop any neuropathologic changes more than 600 days after the peptide injections. We conclude that a chemically synthesized peptide refolded into the appropriate conformation can accelerate or possibly initiate prion disease. Copyright 2000 Academic Press. |
