In situ detection of cellular and abnormal isoforms of prion protein in brains of cattle with bovine spongiform encephalopathy and sheep with scrapie by use of a histoblot technique

To detect prion protein, brains from 5 cattle naturally affected with bovine spongiform encephalopathy (BSE) and 3 sheep naturally affected with scrapie were examined and compared with brains of normal cattle and Sheep using a histoblot technique. The technique enabled the in situ distinctive detection of the cellular (PrPC) and abnormal (PrPSc,) isoforms of the prion protein. In BSE- or scrapie-affected brains, the PrPC signal decreased, especially in those areas where the PrPSc signal was detected.