Conformational change in hamster scrapie prion protein (PrP27-30) associated with proteinase K resistance and prion infectivity |
| |
Authors: | Suzuki Sachiko Y Takata Masuhiro Teruya Kenta Shinagawa Morikazu Mohri Shirou Yokoyama Takashi |
| |
Affiliation: | Prion Disease Research Center, National Institute of Animal Health, Ibaraki, Japan. |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|