Despite the great effort aimed at uncovering the physiological function of cellular prion protein, its role remains unclear. The highly conserved amino acid sequence of PrP indicates its important function, but normally developing PrP knockout mice and cattle were prepared. Here we propose hypothesis that prion protein has no function or a redundant one and more importantly, that the conserved amino acid sequence of mammalian PrPs is not the result of their important function, but rather due to cytotoxicity of most mutations occurring in the PrP molecule. It is possible that the majority of mutations in PrP dramatically destabilizes the PrP(C) structure and causes a pathological change in conformation, so that natural selection favours individuals with non-mutated PrP.
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