Innovation Anthology #230:
Transmission is a big question for scientists studying prion disease. What makes it 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 from elk and from hamsters.
Glaves outlined his surprising results in a poster presented at the recent Prion Conference in Edmonton.
JOHN PAUL GLAVES: We’re highlighting residues number 127 to 147 of the prion protein. And what we see is that when we just basically drop these small fragments of the prion protein into water and they spontaneously form fibrils. And even though there are only four changes in that 20 residue peptide, we see gross morphological differences between elk fibrils and hamster fibrils. And so what we’re hoping to do is gain some high resolution information about these fibrils so that we can see whether or not these variations in sequences that we see between species, whether those are important for so-called species barriers and transmission between different species.
The next step for John Paul Glaves and his colleagues is to expand their research to other species and more parts of the prion protein.
Thanks today to The Canadian Institutes of Health Research.
FOR INNOVATION ANTHOLOGY, I’M CHERYL CROUCHER
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Canadian Institutes of Health Research
Program Date: 2009-06-02