Abstract
The agent that causes bovine spongiform encephalopathy (BSE) may be infecting small ruminants, which could have serious implications for human health. To distinguish BSE from scrapie and to examine the molecular characteristics of the protease-resistant prion protein (PrPres), we used a specifically designed Western blot method to test isolates from 648 sheep and 53 goats. During 2002–2009, classical non-Nor98 transmissible spongiform encephalopathy had been confirmed among ≈1.7 million small ruminants in France. Five sheep and 2 goats that showed a PrPres pattern consistent with BSE, or with the CH1641 experimental scrapie source, were identified. Later, bioassays confirmed infection by the BSE agent in 1 of the 2 goats. Western blot testing of the 6 other isolates showed an additional C-terminally cleaved PrPres product, with an unglycosylated band at ≈14 kDa, similar to that found in the CH1641 experimental scrapie isolate and different from the BSE isolate.
Highlights
The agent that causes bovine spongiform encephalopathy (BSE) may be infecting small ruminants, which could have serious implications for human health
We describe the molecular findings obtained for a large series of Transmissible spongiform encephalopathies (TSEs) infections in France identified in small ruminants by active surveillance during 2002–2009 and for CH1641-like isolates in sheep and in 1 goat
Active Surveillance Findings during 2002–2009 Since active surveillance of TSEs in small ruminants began in France in 2002, a total of 1,231 small ruminant (1,153 sheep and 78 goats) samples have been confirmed as TSE-positive by Western blot using Sha 31 antibody; >1.7 million animals have been tested by rapid tests (1,152,065 sheep and 685,634 goats) (Table)
Summary
The agent that causes bovine spongiform encephalopathy (BSE) may be infecting small ruminants, which could have serious implications for human health. To distinguish BSE from scrapie and to examine the molecular characteristics of the protease-resistant prion protein (PrPres), we used a designed Western blot method to test isolates from 648 sheep and 53 goats. Biological characterization of the BSE agent in inbred wild-type mice appeared to be reliable, because it showed uniform features in mice [8] The identification of uniform molecular features of PrPres by Western blot in human variant CJD paved the way to a similar approach for detecting possible BSE in small ruminants [12]. Discriminant molecular features of the prion protein can be investigated by immunohistochemical analysis [18] or ELISA [19] In all of these studies, it was assumed that the strain information was closely associated with the structural features of PrPd
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