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Science 17 January 1997: Vol. 275. no. 5298, pp. 402 - 404 DOI: 10.1126/science.275.5298.402
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Reports
Transmission of the BSE Agent to Mice in the Absence of
Detectable Abnormal Prion Protein
Corinne I. Lasmézas,
*
Jean-Philippe Deslys,
Olivier Robain,
Alexandre Jaegly,
Vincent Beringue,
Jean-Michel Peyrin,
Jean-Guy Fournier,
Jean-Jacques Hauw,
Jean Rossier,
Dominique Dormont
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.
C. I. Lasmézas, J.-P. Deslys, A. Jaegly, V. Beringue, J.-M.
Peyrin, D. Dormont, Commissariat à l'Energie Atomique,
Service de Neurovirologie, DSV/DRM/SSA, B.P. 6, 60-68 avenue du
General Leclerc, 92265 Fontenay-aux-Roses Cedex, France.
O. Robain, Hôpital Saint Vincent de Paul, INSERM U 29, 74 avenue
Denfert-Rochereau, 75674 Paris Cedex 14, France.
J.-G. Fournier, Hôpital de la Salpétrière, INSERM U
153, 47 boulevard de l'Hôpital, 75651 Paris Cedex 13, France.
J.-J. Hauw, Hôpital de la Salpétrière, Laboratoire
Escourolle, INSERM U 360, 47 boulevard de l'Hôpital, 75651 Paris
Cedex 13, France.
J. Rossier, Ecole Supérieure de Physique et Chimie Industrielles,
CNRS URA 2054, 10 rue Vauquelin, 75231 Paris Cedex 5, France.
*
To whom correspondence should be addressed. E-mail:
CORINNE.LASMEZAS{at}cea.fr
Read the Full Text
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PNAS
98, 4142-4147
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- Prion infection impairs the cellular response to oxidative stress.
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PNAS
97, 13937-13942
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