Abstract
Prion diseases are caused by the misfolding of the cellular prion protein, PrPC, which adopts a β-sheet rich conformation when converted into the infectious state, PrPSc. Here, we present our approach to design structure-based vaccines that present specific antigenic sequences in a structurally controlled format. The prion domain of the fungal HET-s protein is unrelated to the mammalian prion protein, but adopts a similar, β-sheet rich conformation. This innocuous scaffold protein was engineered as a carrier to express PrPSc surface epitopes in a structurally controlled manner.
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