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PRION INSIGHTS
For the first time in live animals, researchers have shown that a form of normal prion protein binds to abnormal prion protein--the cause of Creutzfeldt-Jakob disease, mad cow disease, and other prion diseases. Their experiments also indicate how infectious prions might be inhibited. It has been proposed that prion disease spreads when infectious prion protein (PrPSc, prion protein scrapie) exerts a bad influence on normal prion protein (PrPC, prion protein cellular), making it too turn bad. To have such an influence, the infectious prion presumably has to first bind with PrPC. This interaction has been demonstrated in vitro, but because of technical obstacles, researchers have not previously been able to show that it occurs in living animals. Adriano Aguzzi, professor of neuropathology at the University of Zurich, and coworkers now find that when a dimeric form of PrPC is expressed in mice and the animals are given infectious prions, PrPC dimer binds PrPSc in vivo and slows the onset of prion disease in the mice [Cell, 113, 49 (2003)]. The dimer apparently ties up PrPSc's binding site, slowing the rate at which it can bind to natural PrPC in the brain and convert it into additional infectious prions. The study thus helps confirm the protein-only hypothesis of prion disease and points the way toward potential therapeutics. A number of agents that fight prion disease have been found previously, but none of these "worked when prions were applied directly to the brain" as the prion dimer does, Aguzzi says. The challenge will be to find drugs capable of reaching the brain, where PrPSc does its damage. "We are trying hard to get there," Aguzzi says. "Preliminary results, not included in the Cell paper, are very encouraging."
DOUBLE VISION PrPC dimer expressed in mice by Aguzzi and coworkers. |
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