Variably protease-sensitive prionopathy: mass spectrometry analysis of the pathogenic prion protein provides a new perspective.

ABSTRACT: Variably protease-sensitive prionopathy (VPSPr) is a rare and complex prion disease that differs from sporadic Creutzfeldt-Jakob disease (sCJD) in its clinical and histopathological phenotypes. VPSPr also features a variety of fragments generated by the disease-causing prion protein (PrP^D). However, accurately determining the number and sequence of these fragments has been challenging when relying solely on epitope mapping with existing antibodies. To address these challenges, we performed mass spectrometry analyses and designed epitope mapping experiments to determine the primary structure and verify the presence or absence of the anchor in the VPSPr proteinase K-resistant and deglycosylated PrP^D fragments. All three N-terminus fragments, with reported molecular weig

SUBMITTER: Nemani SK 

PROVIDER: S-EPMC12345132 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature