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American Journal of Pathology, Vol 152, 1415-1420, Copyright © 1998 by American Society for Investigative Pathology

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An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy

P Piccardo, JP Langeveld, AF Hill, SR Dlouhy, K Young, G Giaccone, G Rossi, M Bugiani, O Bugiani, RH Meloen, J Collinge, F Tagliavini and B Ghetti
Indiana University School of Medicine, Indianapolis, USA.

Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity (from strong immunopositivity to lack of reactivity) when challenged with PrP from diverse species. We have produced an antibody (anti-PrP95-108) raised against a synthetic peptide corresponding to residues 95 to 108 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (ie, cattle, sheep, hamsters, and mice). This is probably due to the fact that the epitope recognized by this antibody includes residues 100 to 108 of human PrP, a sequence that is also present in PrP of several other species. Thus, this reagent is valuable not only for the study of human prion diseases but also for analysis of the possible relationship between human and animal disorders.

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