Related Experiment Video
Updated: May 25, 2026
Detection of Abnormal Prion Protein by Immunohistochemistry
Published on: May 5, 2023
Novel assay with fluorescence-labelled PrP peptides for differentiating L-type atypical and classical BSEs, and
Kazuo Kasai1, Akiyoshi Hirata, Takafumi Ohyama
1Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki, Japan.
Abstract:
Characteristic differences of prions may account for the conformational diversity of the pathogenic isoform of prion protein (PrP(Sc)). Here, we applied a protein detection procedure by using fluorescent-labelled peptides for detecting PrP(Sc). Five prion protein (PrP) related peptides were found to change significantly their fluorescent intensities with prion-affected animal samples. Their reactivity was different among atypical L-BSE, classical BSE and scrapie. The pull-down assay revealed that they precipitated PrP(Sc) specifically. These findings suggest that fluorescent intensity changes depend on peptide-PrP(Sc) binding. This novel approach may distinguish the fine structural differences in PrP(Sc), which were not detected by the pull-down assay.
