Conformational Change in Hamster Scrapie Prion Protein (PrP27-30) Associated with Proteinase K Resistance and Prion Infectivity

Journal of Veterinary Medical Science

Kenta TERUYA¹  Masuhiro TAKATA²  Sachiko Y. SUZUKI²  Shirou MOHRI²  Takashi YOKOYAMA²  Morikazu SHINAGAWA² 

[1] Division of Prion Biology, Department of Prion Research, Tohoku University Graduate School of Medicine;Prion Disease Research Center, National Institute of Animal Health

关键词: prion;    small PrP27-30 aggregates;    spectroscopic analysis;    thioflavin T;    transmissibility;   

DOI  :  10.1292/jvms.70.159

学科分类：兽医学

来源: Japanese Society of Veterinary Science

【 摘 要 】

References(24)Cited-By(2)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.

【 授权许可】

Unknown