The mystery of misfolded prions


John Paul Glaves

Transmission is a big question for scientists studying prion disease. Misfolded prions are associated with mad cow and chronic wasting disease. What makes the misfolded prion infectious within a species, and what stops it from being transmitted between different species?
In his research, University of Alberta biochemist John Paul Glaves studied fragments of peptide fibrils or threadlike strands from elk and hamsters. Elk are susceptible to chronic wasting disease, but it’s very hard for hamsters to develop prion disease.
Glaves outlined his surprising results in a poster presented at the recent Prion Conference in Edmonton.
We’ve taken small fragments of the prion protein that have been known to form fibrils, and we’ve basically generated those based on different species. So there’s a small amount of variability in the sequences that we’ve chosen… we’re highlighting residues number 127 to 147 of the prion protein. You can just basically drop these small fragments of the prion protein in water and they spontaneously form fibrils.”
Glaves goes on to explain that, although there are only four changes in the 20 residue pepties, the researchers found there are gross morphological differences between the fibrils of elk and hamsters.
“What we hope to do,” he says, “is gain some high resolution information about these fibrils so we can see each individual residue and how it contributes to fibril formation. Then we can start to dissect whether these variations in sequences that we see between species… are important for so-called species barriers and transmission between different species.”
The next step for Glaves and his colleagues is to expand their research to other species and different parts of the prion protein. √

~ Cheryl Croucher

Explore posts in the same categories: Cheryl Croucher, Edmonton Tech Community, Edmonton Technology

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