Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein

The agent responsible for transmissible spongiform encephalopathies (TSEs) is thought to be a malfolded, protease-resistant version (PrPres) of the normal cellular prion protein (PrP). The interspecies transmission of bovine spongiform encephalopathy (BSE) to mice was studied. Although all of the mi...

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Published in:Science (American Association for the Advancement of Science) Vol. 275; no. 5298; pp. 402 - 405
Main Authors: Lasmezas, C.I. (Commissariat a l'Energie Atomique, Fontenay-aux-Roses, France.), Deslys, J.P, Robain, I, Jaegly, A, Beringue, V, Peyrin, J.M, Fournier, J.G, Hauw, J.J, Rossier, J, Dormont, D
Format: Journal Article
Language:English
Published: Washington, DC American Society for the Advancement of Science 17-01-1997
American Association for the Advancement of Science
The American Association for the Advancement of Science
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Summary:The agent responsible for transmissible spongiform encephalopathies (TSEs) is thought to be a malfolded, protease-resistant version (PrPres) of the normal cellular prion protein (PrP). The interspecies transmission of bovine spongiform encephalopathy (BSE) to mice was studied. Although all of the mice injected with homogenate from BSE-infected cattle brain exhibited neurological symptoms and neuronal death, more than 55 percent had no detectable PrPres. During serial passage, PrPres appeared after the agent became adapted to the new host. Thus, PrPres may be involved in species adaptation, but a further unidentified agent may actually transmit BSE
Bibliography:9718385
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ISSN:0036-8075
1095-9203
DOI:10.1126/science.275.5298.402