Scrapie-infected cells, isolated prions, and ...



Title Scrapie-infected cells, isolated prions, and recombinant prion protein: a comparative study
Author(s) J. Kneipp, Lisa M. Miller, S. Spassov, F. Sokolowski, P. Lasch, M. Beekes, D. Naumann
Journal Biopolymers
Date 2004
Volume 74
Issue 1/2
Start page 163
End page 167
Abstract Fourier-transform infrared microscopic spectra of scrapie-infected nervous tissue measured at high spatial resolution (~6 micro m) 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 SHaPrP90-232 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..

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