A multidisciplinary team led by researchers from CIC bioGUNE and in collaboration with partners of the NEURO-COOP project, has demonstrated that the recombinant mouse prion protein (recPrP), although it can be transformed into its infectious form without the need for cofactors, shows a higher conversion efficiency in vitro when cofactors are present. Using protein misfolding shaking amplification (PMSA) models, the researchers were able to generate infectious prions from recPrP without additions, although the presence of RNA or lipids facilitated the emergence of more stable and efficient structures.

The study reveals that the infectious capacity of prions does not strictly depend on external cofactors, but these do influence the structural conformation of the misfolded protein. Moreover, prions generated without cofactors were able to cause disease in mice, confirming their authenticity.

These findings open new avenues for producing infectious prions under controlled conditions and studying their structural properties without interference, which has important implications for research on neurodegenerative diseases and for the development of diagnostic tools based on recombinant proteins.