Antibody to DNA detects scrapie but not normal prion protein.

ABSTRACT: Prion diseases, a group of fatal neurodegenerative disorders, are characterized by the presence of the abnormal scrapie isoform of prion protein (PrP(Sc)) in affected brains. A conformational change is believed to convert the normal cellular prion protein into PrP(Sc). Detection of PrP(Sc) for diagnosis and prophylaxis is impaired because available Abs recognizing epitopes on PrP fail to distinguish between PrP(Sc) and normal cellular prion protein. Here, we report that an anti-DNA Ab, OCD4, as well as gene 5 protein, a well established DNA-binding protein, capture PrP from brains affected by prion diseases in both humans and animals but not from unaffected controls. OCD4 appears to immunoreact with DNA (or a DNA-associated molecule) that forms a conformation-dependent complex with PrP in

SUBMITTER: Zou WQ 

PROVIDER: S-EPMC337061 | biostudies-literature | 2004 Feb

REPOSITORIES: biostudies-literature