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Understanding the structure of PrPSc and its strain variation has been one of the major challenges in prion disease biology. To study the strain-dependent conformations of PrPSc , we purified proteinase-resistant PrPSc (PrPRES ) from mouse brains with three different murine-adapted scrapie strains (Chandler, 22L, and Me7) and systematically tested the accessibility of epitopes of a wide range of anti-PrP and anti-PrPSc specific antibodies by indirect enzyme-linked immunosorbent assay (ELISA). We found that epitopes of most anti-PrP antibodies were hidden in the folded structure of PrPRES , even though these epitopes are revealed with guanidine denaturation. However, reactivities to a PrPSc -specific conformational C-terminal antibody showed significant differences among the three different prion strains. Our results provide evidence for strain-dependent conformational variation near the C termini of molecules within PrPSc multimers.IMPORTANCE It has long been apparent that prion strains can have different conformations near the N terminus of the PrPSc protease-resistant core. Here, we show that a C-terminal conformational PrPSc -specific antibody reacts differently to three murine-adapted scrapie strains. These results suggest, in turn, that conformational differences in the C terminus of PrPSc also contribute to the phenotypic distinction between prion strains.

PrP Sc -Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains

PrP ^Sc -Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains