Molecular characterization of chicken prion proteins by C-terminal-specific monoclonal antibodies.

Abstract

We obtained seven monoclonal antibodies (mAbs) against chicken cellular prion protein (ChPrP(C)) by immunizing BALB/c mice with recombinant prion protein (rChPrP). Of the seven mAbs, two mAbs (6 and 26) could recognize rChPrP, but not ChPrP(C), in chicken brain lysate via Western blot (WB) analysis. Three C-terminal linear epitopes (AAANQTEVEM, RWWS and SPVPQD) were identified in ChPrP amino acids by pepspot analysis with five mAbs. The mAbs recognizing the C-terminal epitopes in ChPrP(C) predominantly reacted with the N-terminal truncated ChPrP(C) in WB analysis, which differed from the reaction with N-terminal proline/glycine-rich repeats recognizing rabbit polyclonal antibody. These mAbs will soon be available as a useful tool to characterize the biology of ChPrP(C) in birds.