Bovine Spongiform Encephalopathy (BSE) is a new fatal degenerative dis
ease of the Central Nervous System, belonging to the unconventional sl
ow virus diseases. These diseases are characterised by the formation a
nd accumulation of the amyloid protein PrP in the brain of affected in
dividuals. Thus, the development of antisera which immunostain PrP can
be useful for the diagnosis of BSE. We have screened a number of poly
clonal antisera prepared against the proteinase K resistant portion of
PrP (PrP27-30) purified from brains of 263K scrapie-infected hamster,
and ME7 scrapie-infected mouse. Moreover, we prepared polyclonal anti
bodies against peptides corresponding to 4 different regions of the bo
vine PrP purified from brainstems and cortices of five clinically susp
ected cases of BSE. Antisera showed that the band pattern of bovine Pr
P27-30 (PrP(BSE)) differs from that of PrP27-30 purified from brains o
f hamsters with experimental scrapie (PrP263K) and from brains of pati
ents dying of CJD (PrP(CJD). The amount of PrP(BSE) in affected brain
was at least 10-fold less than that found in CJD brains and 10000-fold
less than in scrapie-infected hamsters.