Conformational change in hamster scrapie prion protein (PrP27-30) associated with proteinase K resistance and prion infectivity.
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.
Suzuki
Sachiko Y
SY
Prion Disease Research Center, National Institute of Animal Health, Ibaraki, Japan.
Takata
Masuhiro
M
Teruya
Kenta
K
Shinagawa
Morikazu
M
Mohri
Shirou
S
Yokoyama
Takashi
T
D000468:Alkalies; D000818:Animals; D006224:Cricetinae; D019286:Endopeptidase K / Q000378:metabolism*; D005260:Female; D006358:Hot Temperature; D008647:Mesocricetus; D018622:PrP 27-30 Protein / Q000737:chemistry* / Q000378:metabolism* / Q000472:pathogenicity; D011487:Protein Conformation; D011489:Protein Denaturation
D000468:Alkalies; D018622:PrP 27-30 Protein; D019286:Endopeptidase K