Conformational Change in Hamster Scrapie Prion Protein (PrP27-30) Associated with Proteinase K Resistance and Prion Infectivity
| Autor: | Kenta Teruya, Morikazu Shinagawa, Takashi Yokoyama, Shirou Mohri, Masuhiro Takata, Sachiko Y. Suzuki |
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| Rok vydání: | 2008 |
| Předmět: |
Protein Denaturation
Conformational change Hot Temperature Mesocricetus General Veterinary Amyloid Protein Conformation Sonication Hamster Scrapie Alkalies Biology Proteinase K Transmissibility (vibration) PrP 27-30 Protein nervous system diseases chemistry.chemical_compound Biochemistry chemistry Cricetinae biology.protein Animals Female Thioflavin Endopeptidase K |
| Zdroj: | Journal of Veterinary Medical Science. 70:159-165 |
| ISSN: | 1347-7439 0916-7250 |
| DOI: | 10.1292/jvms.70.159 |
| Popis: | The scrapie prion protein (PrP27-30) is a crucial component of the prion and is responsible for its transmissibility. Structural information on this protein is limited because it is insoluble and shows aggregated properties. In this study, PrP27-30 was effectively dispersed using sonication under the weak alkaline condition. Subsequently, the small PrP27-30 aggregates were subjected to different pH, heat, and denaturing conditions. The loss of proteinase K (PK) resistance of PrP27-30 and prion infectivity were monitored along with spectroscopic changes. Prion inactivation could not be achieved by the loss of PK resistance alone; a significant loss of the PrP27-30 amyloid structure, which was represented by a decrease in thioflavin T fluorescence, was required for the loss of transmissibility. |
| Databáze: | OpenAIRE |
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