An international team led by researchers from IRTA-CReSA and CIC bioGUNE has shown that the fastest known prion strain, CWD-vole, maintains its properties even in the absence of glycosylation and membrane anchoring. Using a transgenic mouse model expressing the vole prion protein without GPI anchoring and with little glycosylation, the scientists managed to infect the animals in three consecutive passes. Subsequently, when this strain was reintroduced into mice with normal prion protein, its propagation speed and neuropathological characteristics were fully preserved.

This finding reinforces the hypothesis that the properties of prion strains are encoded in the misfolded structure of the protein, and do not necessarily depend on its post-translational modifications. Furthermore, it opens up new opportunities for the structural study of prions using recombinant proteins in the absence of glycans, a key strategy in research based on techniques such as cryo-EM.