Prion disease, a rare but fatal neurodegenerative disorder, is caused by prion, a prion protein with the wrong shape (PrPSc) that has the ability to induce the normal good prion protein (PrPC) to adapt to the wrong shape (PrPSc) and spread in the brain. However, we still don’t have a clear picture of how PrPSc converts and spreads, largely due to the lack of high-resolution structural information of PrPSc, hence impeding the developments of efficacious therapeutics against these currently incurable diseases. The main goal of this project is to develop methods for large scale production of high-quality human PrPSc for structural studies that will facilitate the structure-based drug design to treat human prion diseases.
About the Researcher:
My primary research focus has been on studying prion protein (PrP) misfolding associated with prion disease, which represents the prototypical protein misfolding-associated neurodegenerative disorder that affects both human and animals. Our lab has shown that infectious recombinant PrPSc (recPrPSc) can be generated from bacterially expressed non-infectious recombinant PrP (recPrP) in a novel in vitro protein misfolding system containing auxiliary cofactors. Our recent studies have demonstrated that recPrPSc share structural features with native PrPSc, suggesting that recPrPSc is a good resource for structural studies of infectious prions. Lately I have been working on developing the large-scale production system for generating high-quality recPrPSc in large quantity.
Dr. Wang is the recipient of:
- The CJD Foundation Grant, contributed by the Families of the CJD Foundation
- The Katie Dopirak Memorial Grant, contributed by the Pohl and Dopirak Family
- The Jeffrey A. Smith Memorial Grant, contributed by The Jeffrey and Mary Smith Family Foundation
- The Strides for CJD Grant, contributed by the Families of the CJD Foundation
- The Walter Williams Memorial Grant, contributed by Susan and Kyle Williams and the Aarons Law Firm