|Raymond, G. - NIAID/NIH ROCKY MTN LAB|
|Bossers, A. - INSTITUE ANLM SCI &HEALTH|
|Raymond, L. - NIAID/NIH ROCKY MTN LAB|
|Bryant, P Kruger|
|Miller, M. - COLORADO DIV OF WILDLIFE|
|Williams, E. - DEPT VET SCI UNV WYOMING|
|Smits, M. - INSTITUE ANML SCI &HEALTH|
|Caughey, B. - NIAID/NIH ROCKY MTN. LAB.|
Submitted to: EMBO Journal
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: July 13, 2000
Publication Date: N/A
Interpretive Summary: Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) of deer and elk. CWD shares some characteristics of a diverse group of diseases affecting humans, cats, and food producing animals such as sheep and cattle. Most of these diseases affect a single species and are not transmissible to humans or other animal species. In contrast, bovine spongiform encephalopathy is associated with a novel human neurologic disease. The disease is believed to originate by exposure of human protein to an abnormal form of a pathogenic bovine protein. In this paper, a laboratory test was developed to examine the susceptibility of human, cattle, and sheep proteins to the pathogenic proteins from CWD-affected deer or elk. The CWD proteins readily affected normal deer or elk proteins but had little effect on proteins from humans, sheep, or cattle. These results suggest humans, sheep, and cattle may have a low susceptibility to CWD.
Technical Abstract: Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) of deer and elk and little is known about its transmissibility to other species. An important factor controlling interspecies TSE susceptibility is prion protein (PrP) homology between the source and recipient species/genotypes. Furthermore, the efficiency with which the protease-resistant PrP (PrP-res) of one species induces the in vitro conversion of the normal PrP (PrP- sen) of another species to the protease-resistant state correlates with the cross-species transmissibility of TSE agents. Here we show that the CWD-associated PrP-res (PrPCWD) of cervids readily induces the conversion of cervid PrP-sen molecules to the protease- resistant state in accordance with the known transmissibility of CWD between cervids. In contrast, PrPCWD induced conversions of human and bovine PrP-sen were much less efficient, and, conversion of ovine PrP-sen was intermediate. These data correlate with the cross species transmissibility of TSE and the results demonstrate a barrier at the molecular level that should limit the susceptibility of these non cervid species to CWD.