BOUND TO WORK

Abstract

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 (PrP Sc , prion protein scrapie) exerts a bad influence on normal prion protein (PrP C , prion protein cellular), making it too turn bad. To have such an influence, the infectious prion presumably has to first bind with PrP C . 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 PrP C is expressed in mice and the animals are given infectious prions, PrP C dimer binds PrP Sc in ...