Spontaneous and BSE-prion-seeded amyloid formation of full length recombinant bovine prion protein
| Autor: | Dimitrios Papathanassiou, Giannantonio Panza, Christian Dumpitak, Dieter Willbold, Jürgen Weiss, Eva Birkmann, Jan Stöhr, Detlev Riesner |
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| Rok vydání: | 2008 |
| Předmět: |
Gene isoform
Models Molecular Amyloid PrPSc Proteins Protein Conformation animal diseases Biophysics Hamster Scrapie Biology Biochemistry law.invention Protein structure law Cricetinae Animals Molecular Biology Cell Biology In vitro Recombinant Proteins Encephalopathy Bovine Spongiform Recombinant DNA Cattle |
| Zdroj: | Biochemical and biophysical research communications. 373(4) |
| ISSN: | 1090-2104 |
| Popis: | The conversion of the cellular isoform of the prion protein into the pathogenic isoform PrP(Sc) is the key event in prion diseases. The disease can occur spontaneously genetically or by infection. In earlier studies we presented an in vitro conversion system which simulates the structural transition in recPrP by varying low concentrations of SDS at constant NaCl. In the present study we adopted the conversion system from experimental Scrapie in hamster to bovine recPrP and generated amyloid fibrils. The intermediate state which is optimal for fibril formation is a soluble, beta-rich state. The system was extended using BSE-prions as seeds and led to an acceleration of fibril formation by orders of magnitude. This seeded amyloid formation assay avoids any PK-treatment, is therefore able to detect even PK-sensitive PrP(Sc) and does not require cellular components. |
| Databáze: | OpenAIRE |
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