Abstract
Transmissible spongiform encephalopathies (TSEs) such as scrapie are neurodegenerative diseases that are characterized by the accumulation of a misfolded prion protein. During the pathogenesis, the normally α-helical prion protein (PrP C) refolds to the proteinase K-resistant abnormal form (PrP Sc), which is high in β-sheet content. In this study, dorsal root ganglia from the 263K hamster model of scrapie were cut into 8 μm thin sections and mounted onto an aluminium-coated glass slide. Single neuronal cells were mapped with synchrotron infrared microspectroscopy to study protein structure and X-ray fluorescence microprobe to determine metal accumulation. Both techniques provide a spatial resolution of 5–10 μm. Results showed that some IR spectra of the infected cells exhibited a significant frequency shift of the amide I band, where an increased peak intensity was observed at ∼1631 cm −1 (attributed to β-sheet) and a decreased peak intensity at ∼1658 cm −1 was also seen (attributed to α-helix). These shifts were not observed in non-infected cells. Adjacent sections were also stained with an antibody for the prion protein in order to confirm that the IR observations were associated with accumulated PrP Sc. Finally, the same cells were measured by X-ray fluorescence microprobe, which provided the first direct comparison of PrP Sc formation and metal ion accumulation. Results showed an accumulation of Fe in cells infected with PrP Sc.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.