NR AQLP
AU Kneipp,J.; Miller,L.M.; Spassov,S.; Sokolowski,F.; Lasch,P.; Beekes,M.; Naumann,D.
TI Scrapie-infected cells, isolated prions, and recombinant prion protein: a comparative study.
QU Biopolymers 2004 May-Jun 5; 74(1-2): 163-7
PT journal article
AB 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.
MH Animals; Comparative Study; Endopeptidase K/metabolism; Ganglia, Spinal/metabolism; Hamsters; In Vitro; Mesocricetus; Prion Diseases/metabolism; Prions/*chemistry; Protein Conformation; Protein Isoforms; Protein Structure, Secondary; Recombinant Proteins/chemistry/metabolism; Scrapie/*metabolism; Spectroscopy, Fourier Transform Infrared/*methods; Support, Non-U.S. Gov't
AD Robert Koch Institute, Nordufer 20, 13353 Berlin, Germany.
SP englisch
PO USA