Conformational change in hamster scrapie prion protein (PrP27-30) associated with proteinase K resistance and prion infectivity

Sachiko Y. Suzuki, Masuhiro Takata, Kenta Teruya, Morikazu Shinagawa, Shirou Mohri, Takashi Yokoyama

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)159-165
Number of pages7
JournalJournal of Veterinary Medical Science
Volume70
Issue number2
DOIs
Publication statusPublished - 2008 Feb

Keywords

  • Prion
  • Small PrP27-30 aggregates
  • Spectroscopic analysis
  • Thioflavin T
  • Transmissibility

ASJC Scopus subject areas

  • veterinary(all)

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