Matthew E.C. Bourkas

Aug 1, 2024 | jci.org | Surabhi Mehra |Matthew E.C. Bourkas |Lech Kaczmarczyk |Erica Stuart

AbstractMost cases of human prion disease arise due to spontaneous misfolding of WT or mutant prion protein, yet recapitulating this event in animal models has proven challenging. It remains unclear whether spontaneous prion generation can occur within the mouse lifespan in the absence of protein overexpression and how disease-causing mutations affect prion strain properties. To address these issues, we generated knockin mice that express the misfolding-prone bank vole prion protein (BVPrP).

Sep 29, 2023 | biorxiv.org | Daniel Walsh |Judy R Rees |Surabhi Mehra |Matthew E.C. Bourkas

AbstractPrion diseases uniquely manifest in three distinct forms: inherited, sporadic, and infectious. Wild-type prions are responsible for the sporadic and infectious versions, while mutant prions cause inherited variants like fatal familial insomnia (FFI) and familial Creutzfeldt-Jakob disease (fCJD). Although some drugs can prolong prion incubation times up to four-fold in rodent models of infectious prion diseases, no effective treatments for FFI and fCJD have been found.

Sep 27, 2023 | biorxiv.org | Surabhi Mehra |Matthew E.C. Bourkas |Lech Kaczmarczyk |Erica Stuart

AbstractMost cases of human prion disease arise due to spontaneous misfolding of wild-type or mutant prion protein. Though recapitulating spontaneous prion conversion in animal models has proven challenging, transgenic mice expressing the misfolding-prone bank vole prion protein (BVPrP) recreate certain key aspects of sporadic and genetic prion disease.