s. These results help explain why stable inheritance of prions is rare; while many proteins have stretches of amino acids similar to the aggregation sequence, few also contain sequences that permit inheritance. Osherovich and colleagues were able to create an artificial prion by fusing the oligopeptide repeats to an expanded polyglutamine tract.

By creating artificial hybrid prions, Osherovich and colleagues showed that the two discrete elements of prion-forming domains are portable and work together regardless of their origins. The authors suggest that other artificial prions could be used as a model system to study different types of aggregation sequences, such as those found in the human prion protein responsible for Creutzfeldt-Jakob's disease or the misshapen plaques of proteins that contribute to Alzheimer's disease.

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Contact: Philip Bernstein
pbernstein@plos.org
415-624-1210
Public Library of Science
23-Mar-2004

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