AI Article Synopsis
- Prion disease results from a change in the normal prion protein (PrP(C)) to a harmful form (PrP(Sc)), posing a risk to large populations due to new variants like Creutzfeldt-Jakob disease.
- There are currently no effective treatments or preventive measures for prion disease, highlighting a significant health concern.
- Research has shown that immunizing with recombinant PrP and using anti-PrP antibodies can extend the incubation period after prion exposure, suggesting that immune system stimulation could be a key therapeutic approach for prion diseases and similar neurodegenerative disorders.
Article Abstract
Prion disease is characterized by a conformational change of the normal form of the prion protein (PrP(C)) to the scrapie-associated form (PrP(Sc)). Since the emergence of new variant Creutzfeldt-Jakob disease a potentially large human population is at risk for developing prion disease. Currently, no effective treatment or form of post-exposure prophylaxis is available for prion disease. We recently showed that active immunization with recombinant PrP prolongs the incubation period of scrapie. Here we show that anti-PrP antibodies following prion exposure are effective at increasing the incubation period of the infection. Stimulation of the immune system is an important therapeutic target for the prion diseases, as well as for other neurodegenerative illnesses characterized by abnormal protein conformation.
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| http://dx.doi.org/10.1016/s0304-3940(02)01192-8 | DOI Listing |
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