Brain tissue from a case of
bovine spongiform encephalopathy (BSE) from Alberta was subjected to a Western immunoblotting technique to ascertain the molecular profile of any disease-specific, abnormal
prion protein, that is,
prion protein that is
protease-resistant (
PrP(res)). This technique can discriminate between isolates from BSE, ovine
scrapie, and sheep experimentally infected with BSE. Isolates of brain tissue from the BSE case in Alberta, 3 farmed elk with
chronic wasting disease (CWD) from different parts of Saskatchewan, and 1 farmed white-tailed deer with CWD from Edmonton, Alberta, were examined alongside isolates of brain tissue from BSE, ovine
scrapie, and sheep experimentally infected with BSE from the United Kingdom (UK). The molecular weights of
PrP(res) and the cross reactions to 2 specific
monoclonal antibodies (mAbs) were determined for each sample. The BSE isolates from Canada and the UK had very similar
PrP(res) molecular weights and reacted with only 1 of the 2 mAbs. The
PrP(res) isolated from both elk and white-tailed deer with CWD had a higher molecular weight profile than did the corresponding
PrP(res) from the
scrapie and BSE isolates. The
PrP(res) from CWD cases cross reacted with both mAbs, a property shared with
PrP(res) in isolates from
scrapie but not with
PrP(res) isolates from BSE or sheep experimentally infected with BSE. The results from this study seem to confirm that the
PrP(res) isolated from the BSE case in Alberta has similar molecular properties to the
PrP(res) isolated from a BSE case in the UK, and that it differs in its molecular and immunological characteristics from the CWD and
scrapie cases studied.