Here we have performed systematic studies of purified resPrP<sup>D</sup> species extracted from GSS cases with the A117V (GSS<sup>A117V</sup>) and F198S (GSS<sup>F198S</sup>) PrP gene mutations.
A 16 kDa thermolysin-resistant signature was also found in GSS patients with P102L, A117V, H187R and F198S alleles and has coordinates similar to GSS stop codon mutations.
We conclude that GSSA117V is indeed a prion disease although the relative contributions of (Ctm)PrP and prion propagation in neurodegeneration and their pathogenetic interaction remains to be established.
Overall, Tg(A116V) mice recapitulate many clinicopathologic features of G</span>SS(A117V) that are distinct from CJD, supporting PrP(A116V) to carry specific phenotypic information.
The aim ofthis study was to characterize PrP in brain extracts, microsomal preparations, and purified fractions from A117V patients and to determine the N terminus of PrP(sc) species in both GSSA117V and F198S.
A 7-kDa prion protein (PrP) fragment, an integral component of the PrP region required for infectivity, is the major amyloid protein in Gerstmann-Sträussler-Scheinker diseaseA117V.