Fig. 4

Western blots analysis and interpretation of protease K-treated PrP^Sc (PrP^res) from Norwegian reindeer and moose diagnosed with CWD, and from a bovine with classical BSE (BSE-C). a Replica blots analysed with mAbs recognizing different epitopes on PrP, as indicated below each blot. The epitopes of the mAbs are shown in c The positions of molecular weight (MW) markers are indicated on the right of the blots (in kilodaltons). Reindeer CWD is detected by the N-terminal mAb 12B2, while moose CWD and BSE-C are not. With mAb 9A2 all samples show a three-banding pattern representing di-, mono- and un-glycosylated PrP^res, whose molecular weight is lower in moose than in reindeer (“Main fragment” in b and c). In contrast, mAbs directed to more C-terminal epitopes, L42 and SAF84, recognize additional low molecular weight PrP^res fragments at ~ 13 and 16 kDa, detected in moose (referred to as CTF16 and CTF13 in b and c), which are glycosylated too (51). b Cartoons representing PrP^res fragments detected in moose with CWD. Main, CTF16, CTF13 fragments are represented separately, with their di-glycosylayed (D), mono-glycosylated (M) and un-glycosylated (U) bands. On the right, the cartoons representing the different PrP^res fragments detected in moose PrP^Sc are joined to show the interpretation of the complex WB patterns observed with SAF84 and L42. The position of the cartoons is in accord with the position of the bands in the blots shown in a. c. Cartoons representing full-length PrP and the different PrP^res fragments detected in moose, with the position of the epitopes recognised by the mAbs used in a (ovine PrP numbering: SAF84, aa 167–173; L42, aa 148–153; 9A2, aa 99–101; 12B2, aa 93–97). Note that the 12B2 epitope is shaded in the main PrP^res fragment to indicate the variability in the N-terminal Proteinase K-cleavage observed in moose with CWD. Yellow circles labelled with “N” represent the position of N-linked sugars. The GPI anchor is represented at the C-terminus