Monday, August 26, 2013

Did you know: New mouse models faithfully recapitulate human prion diseases

Research performed at the Whitehead Institute in Massachusetts has led to the creation of mouse models for both Creutzfeldt-Jakob disease (CJD) and fatal familial insomnia (FFI), two fatal prion diseases that effect humans. As with other prion diseases CJD and FFI are caused by mutations in the prion protein that result in a misfolded protein. This misfolded protein can induce normal prion protein (PrP) to assume this shape and build up in clumps of protein containing many misfolded prion proteins.

Immunohistochemical staining of cerebellar tissue of a
patient that died of CJD in the US.


Previous to this report, entitled: 'Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases' animal models that mimic the disease process in humans were not available. In order to create these the models the scientists used a knock-in approach where the mutated human prion sequence for each disease replaced the normal mouse PrP. They found that as a result of this approach the effect of FFI mutation was neuronal loss in the thalamus and CJD mice exhibit spongiosis in the hippocampus and cerebellum as is seen in humans.


This report in PNAS is just the latest exciting development in prion disease research. We at BMG LABTECH have been glad we can play a small part in prion research when our FLUOstar Omegas are used in RTQuIC assays that can be used to screen for the presence of misfolded PrP in a variety of samples from several species.