Fig. 1
From: Prion type 2 selection in sporadic Creutzfeldt–Jakob disease affecting peripheral ganglia
PrPSc aggregates in peripheral ganglia of sCJD patients detected by PET-blot and immunohistochemistry. Prion protein aggregates within several ganglia are visualized by conventional immunohistochemistry (A, C, E), and with the PET-blot technique (B, D, F). Membrane associated and cytoplasmic prion aggregates were detectable with both methods and are pointed out with arrowheads in black (membrane-associated) and white (cytoplasmic) in the area (C), magnified from A. Prion protein aggregates are shown in the trigeminal ganglion (A, B, C), nodose ganglion (D) and thoracic sympathetic trunk ganglion (F, E). Bars equal either 1 mm (A, E), 500 µm (B, D, F) or 50 µm (C). Western blot analysis (G) reveals the presence of CJD type 2 prion aggregates in a sympathetic trunk ganglion, a trigeminal ganglion and a celiac ganglion of a MV2 CJD patient. The typical three-banded pattern with a diglycosylated, monoglycolsylated and unglycosylated fragment are visible; the latter having a size of ~ 21 kDa in CJD type 1 and ~ 19 kDa in CJD type 2 brain homogenates (see CJD type 1 and 2). Immunodetection was performed using the monoclonal anti-prion antibody 3F4