Establishment of bovine prion peptide-based monoclonal antibodies for identifying bovine prion.

Abstract

To obtain high titer monoclonal antibodies (McAbs) which can react with mammalian prion protein (PrP), Balb/C mice were immunized with bovine (Bo) PrP peptide (BoPrP 209-228 aa) coupled to keyhole limpet hemocyanin (KLH). The hybridoma cell lines secreting monoclonal antibodies against the peptide were established by cell fusion and cloning. The obtained McAbs were applied to detect recombinant human, bovine and hamster PrP, cellular prion protein (PrP(c)) in normal bovine brain and pathogenic scrapie prion protein (PrP(Sc)) accumulated in the medulla oblongata of bovine spongiform encephalopathy(BSE)specimen with Western blot and immunohistochemical detection, respectively. The current procedure might offer a simple, feasible method to raise high titer antibodies for studying biological features of PrP in mammals, as well as detection of transmissible spongiform encephalopathy (TSE) and diagnosis of BSE, in particular.