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Scrapie‐infected cells, isolated prions, and recombinant prion protein: A comparative study
Author(s) -
Kneipp J.,
Miller L. M.,
Spassov S.,
Sokolowski F.,
Lasch P.,
Beekes M.,
Naumann D.
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20064
Subject(s) - scrapie , gene isoform , recombinant dna , hamster , prion protein , in situ , chemistry , transmissible spongiform encephalopathy , proteinase k , ex vivo , microbiology and biotechnology , virology , mesocricetus , in vitro , bovine spongiform encephalopathy , biology , biochemistry , enzyme , pathology , gene , medicine , disease , organic chemistry
Fourier ‐transform infrared microscopic spectra of scrapie‐infected nervous tissue measured at high spatial resolution (∼6 μm) 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 α‐helical isoform to β‐sheet‐rich structures. It is shown that prion protein structure can be investigated within tissue and that detectability of regions with elevated β‐sheet content as observed in microspectra of prion‐infected tissue strongly depends on spatial resolution of the experiment. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004