Use of hybrid mammalian-yeast prions to identify factors that inhibit protein aggregation

2006 Pilot Project Read More


Principal Investigator: David Harris, MD, PhD (formerly WUSTL Cell Biology & Physiology)
Collaborator: Heather True-Krob, PhD (WUSTL Cell Biology & Physiology)


Prion proteins are involved in fatal neurodegenerative brain illnesses including Jacob-Creutzfeld Disease and “Mad Cow” disease. These diseases are like other neurodegenerative diseases in that the primary pathology starts with abnormal accumulation of proteins within brain cells. This project is a collaboration between two Hope Center faculty members: David Harris is an established prion neuroscientis; Heather True is a yeast cell biologist. Together, they have developed an innovative technique which uses yeast to screen many thousands of genes at a time, to find those genes which potentially inhibit protein misfolding and aggregation.


Tank EM, Harris DA, Desai AA, True HL. Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Molecular Cell Biology (2007).

Kalastavadi T, True HL. Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochemistry (2008).


Updated October 2012


Hope Center Investigators

Heather True-Krob