Fig. 10
From: Bona fide atypical scrapie faithfully reproduced for the first time in a rodent model
Imunohistochemical and biochemical analysis of sheep inoculated with ShTgSPON compared to atypical scrapie. a PrPres Immunohistochemistry showed a fine granular deposition pattern, particularly abundant in the outer molecular layer of the cerebellar cortex that is identical to that observed in sheep inoculated intrecerebrally with atypical scrapie isolate (Anti PrPres antibody 8G8, 1:1000). b Western blotting comparison of a healthy sheep brain homogenate (Ov NBH), a classical scrapie isolate (SSBP/1), two different isolates of atypical (Nor98-like) ovine scrapie (01: Cerebellum O-1233 AHQ/AHQ; 02: Cerebellum O-1238 AHQ/AHQ) and the prions extracted from ShTgSPON inoculated AHQ/AHQ sheep after digestion with proteinase K (PK). Anti PrP antibody 12B2, 1:5000. Electrophoretic migration profile of PrPSc detected in different brain areas of one of the sheep inoculated with diseased-TgShI112 brain homogenate (ShTgSPON), shows a 7–10 kDa band characterisitc of atypical prion disease of sheep, similar to atypical scrapie isolates from sheep used here to compare. Some variability can be observed among the different brain areas regarding the exact size of this low molecular weight band, matching with subtle differences among the two different atypical scrapie isolates used for comparison, likely due to the presence of fragments with ragged ends after PK digestion more evident in low molecular weight products. MW: Molecular weight