|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine >
Peer-reviewed Journal Articles, etc >
A domain responsible for spontaneous conversion of bank vole prion protein
| Title: | A domain responsible for spontaneous conversion of bank vole prion protein |
| Authors: | Kobayashi, Atsushi Browse this author | | Matsuura, Yuichi Browse this author →KAKEN DB | | Takeuchi, Atsuko Browse this author →KAKEN DB | | Yamada, Masahito Browse this author →KAKEN DB | | Miyoshi, Ichiro Browse this author →KAKEN DB | | Mohri, Shirou Browse this author →KAKEN DB | | Kitamoto, Tetsuyuki Browse this author →KAKEN DB |
| Keywords: | prion | | prion disease | | bank vole | | misfolding |
| Issue Date: | Mar-2019 |
| Publisher: | John Wiley & Sons |
| Journal Title: | Brain pathology |
| Volume: | 29 |
| Issue: | 2 |
| Start Page: | 155 |
| End Page: | 163 |
| Publisher DOI: | 10.1111/bpa.12638 |
| Abstract: | Bank vole is a small rodent that shows high susceptibility to infection with diverse prion strains. To determine whether the increased susceptibility of bank voles to prion diseases can be attributed to the intrinsic nature of bank vole prion protein (PrP) or to host factors other than PrP, we produced transgenic mice overexpressing bank vole PrP. These transgenic mice spontaneously developed neurological illness with spongiform changes and the accumulation of abnormal PrP in the brain. Then, we produced transgenic mice overexpressing chimeric mouse/bank vole PrP, which differs from mouse PrP only at two residues located at the C-terminus, to determine the minimum essential domain for the induction of spontaneous generation of abnormal PrP. These transgenic mice also developed spontaneous neurological illness with spongiform changes and the accumulation of abnormal PrP in the brain. In addition, knock-in mice expressing bank vole PrP at the same level as that of wild-type mice did not develop spontaneous disease but showed high susceptibility to infection with diverse prion strains, similarly to bank voles. Taken together, these findings show that bank vole PrP has a high propensity for the conformational conversion both in spontaneous disease and in prion infection, probably due to the characteristic structural properties of the C-terminal domain. |
| Rights: | This is the peer reviewed version of the following article: Atsushi K. et al, "A domain responsible for spontaneous conversion of bank vole prion protein, which has been published in final form at https://doi.org/10.1111/bpa.12638. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/76862 |
| Appears in Collections: | 獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 小林 篤史
|
