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Depleting Neuronal PrP in Prion Infection Prevents Disease and Reverses Spongiosis
Giovanna Mallucci, Andrew Dickinson, Jacqueline Linehan, Peter-Christian Klöhn, Sebastian Brandner and John Collinge
New Series, Vol. 302, No. 5646 (Oct. 31, 2003), pp. 871-874
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/3835558
Page Count: 4
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The mechanisms involved in prion neurotoxicity are unclear, and therapies preventing accumulation of PrPSc, the disease-associated form of prion protein (PrP), do not significantly prolong survival in mice with central nervous system prion infection. We found that depleting endogenous neuronal PrPc in mice with established neuroinvasive prion infection reversed early spongiform change and prevented neuronal loss and progression to clinical disease. This occurred despite the accumulation of extraneuronal PrPSc to levels seen in terminally ill wild-type animals. Thus, the propagation of non-neuronal PrPSc is not pathogenic, but arresting the continued conversion of PrPc to PrPSc within neurons during scrapie infection prevents prion neurotoxicity.
Science © 2003 American Association for the Advancement of Science