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Fig. 6 | Acta Neuropathologica Communications

Fig. 6

From: Bona fide atypical scrapie faithfully reproduced for the first time in a rodent model

Fig. 6

Western blotting comparison of a classical scrapie isolate (SSBP/1) and the prions extracted from diseased TgShI112 or atypical scrapie inoculated Tg338 (Ovine VRQ PrPC) and Tg501 (Ovine ARQ PrPC) mouse brains after digestion with proteinase K (PK). Electrophoretic migration profiles of prions from Tg338 and Tg501 mouse lines inoculated intracerebrally with ShTgSPON are similar and characterized by the presence of a 7–10 kDa band, also similar to the ovine atypical scrapie isolate inoculated in the same models. The detection of mildly PK-resistant high molecular weight bands in some of the samples may respond to some degree of variability due to the differences between the models in terms of PrP sequence, expression levels and slight variations in disease stage at culling. Along this line, variability due to the processing of the samples for the detection of the low molecular weight band could also explain the occasional presence of high molecular weight PrP fragments, given the low PK concentration and high sample amounts required. Since anatomopathological analysis did not show significant differences on plaque type and distribution between animals with or without them. Overall, all models challenged with ShTgSPON show the characteristic 7–10 kDa fragment resembling that from atypical scrapie, indicating the spontaneous formation of an atypical ovine prion in TgSh112I model. Anti PrP antibody 12B2, 1:5000. MW: Molecular weight

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