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Detection of Abnormal Prion Protein by Immunohistochemistry
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Detection of Abnormal Prion Protein by Immunohistochemistry

Published on: May 5, 2023

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

Li Zhao1, XinSheng Hou, Rong Ji

  • 1Department of Laboratory Science of Microbiology, Shandong University, Jinan, 250012, China.

Science in China. Series C, Life Sciences
|September 4, 2009
PubMed

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.

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