Retrospective analysis of sheep scrapie by western blotting with formalin-fixed paraffin-embedded (FFPE) tissues.
An abnormal isoform of prion protein (PrP(Sc)) was extracted from formalin-fixed paraffin-embedded (FFPE) tissues from sheep and analyzed by western blotting. PrP(Sc) immunoreactivity against anti-PrP monoclonal antibody T2, which recognizes discontinuous PrP sequences, differed amongst individual scrapie sheep cases. This may reflect structural differences in PrP(Sc) that have been formalin-fixed prior to their extraction. This study indicates that western blotting by using FFPE tissues is useful for the retrospective analysis of transmissible spongiform encephalopathies in which only formalin-fixed samples are available and in conducting transmissible spongiform encephalopathies surveillance where freezing system is insufficient.
Prion Disease Research Center, National Institute of Animal Health, Tsukuba 305-0856, Japan.
Gantsetseg
G
Dorj
Hiroyuki
H
Okada
Kohtaro
K
Miyazawa
Kentaro
K
Masujin
Kumiko
K
Kimura
Shirou
S
Mohri
Takashi
T
Yokoyama
D000818:Animals; D015153:Blotting, Western / Q000379:methods / Q000662:veterinary*; D005557:Formaldehyde; D016612:Paraffin Embedding / Q000662:veterinary; D018620:PrPSc Proteins / Q000302:isolation & purification*; D012189:Retrospective Studies; D012608:Scrapie / Q000473:pathology*; D012756:Sheep; D016707:Tissue Fixation / Q000662:veterinary
D018620:PrPSc Proteins; D005557:Formaldehyde