Scrapie-infected cells, isolated prions, and recombinant prion protein: a comparative study

Biopolymers. 2004 May-Jun 5;74(1-2):163-7. doi: 10.1002/bip.20064.

Abstract

Fourier -transform infrared microscopic spectra of scrapie-infected nervous tissue measured at high spatial resolution (approximately 6 microm) were compared with those obtained from the purified, partly proteinase K digested scrapie isoform of the prion protein isolated from nervous tissue of hamsters infected with the same scrapie strain (263K) to elucidate similarities/dissimilarities between prion structure investigated in situ and ex vivo. A further comparison is drawn to the recombinant Syrian hamster prion protein SHaPrP(90-232) after in vitro conformational transition from the predominantly alpha-helical isoform to beta-sheet-rich structures. It is shown that prion protein structure can be investigated within tissue and that detectability of regions with elevated beta-sheet content as observed in microspectra of prion-infected tissue strongly depends on spatial resolution of the experiment.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cricetinae
  • Endopeptidase K / metabolism
  • Ganglia, Spinal / metabolism
  • In Vitro Techniques
  • Mesocricetus
  • Prion Diseases / metabolism
  • Prions / chemistry*
  • Protein Conformation
  • Protein Isoforms
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Scrapie / metabolism*
  • Spectroscopy, Fourier Transform Infrared / methods*

Substances

  • Prions
  • Protein Isoforms
  • Recombinant Proteins
  • Endopeptidase K