Common pathogenic mutations PRNP in Gerstmann–Sträussler–Scheinker syndrome (GSS) are clustered at PrP95-105.

All the nonsense PRNP mutations producing truncated PrP fragment with PrP 95-105 exhibited tremendous amyloid phenotypes.

The high affinity binding between PrP95-105 and Aβ oligomers might be the underlying mechanism of the predominant amyloid phenotype of GSS.

Soluble PrP-Aβ oligomer complexes might be the central common pathogenic event of both prion diseases and Alzheimer’s disease.