title: Distribution of a pathological form of prion protein in the brainstem and cerebellum in classical and atypical cases of bovine spongiform encephalopathy.
abstract: This study evaluated the distribution and signal intensity of a prion protein resistant to proteolysis (PrP(res)) in the brainstem and cerebellum of cattle affected with classical and atypical forms of bovine spongiform encephalopathy (BSE) using a Western immunoblotting technique. In both classical and atypical cases of BSE, a stronger signal was detected in the more rostral brainstem regions relative to the obex. In classical and H-type cases a significant decrease in the PrP(res) signal was found in the cerebellum when compared to that in the obex, whereas L-type BSE cases were characterised by signals of similar intensity in these regions. The uniform distribution of PrP(res) in the region rostral to the obex suggests that when autolysed samples are being tested for BSE, both classical and atypical forms are detectable, even when this target site is missing or cannot be clearly identified. The findings indicate that both the obex and rostral brainstem can be used for BSE diagnosis whereas use of the more caudal brainstem regions and cerebellum is not recommended.
authors.affiliation: National Veterinary Research Institute, Partyzantow 57, 24-100 Pulawy, Poland. ppolak@piwet.pulawy.pl
authors.forename: Miroslaw P
authors.initials: MP
authors.lastname: Polak
authors.forename: Jan F
authors.initials: JF
authors.lastname: Zmudzinski
mesh_terms: D000818:Animals; D001933:Brain Stem; D002417:Cattle; D002531:Cerebellum; D016643:Encephalopathy, Bovine Spongiform / Q000473:pathology*; D018620:PrPSc Proteins / Q000302:isolation & purification* / Q000472:pathogenicity
chemical_list: D018620:PrPSc Proteins