A prion protein missense variant is integrated in kuru plaque cores in patients with Gerstmann-Sträussler syndrome.
Kuru plaques are the pathologic hallmark in Gerstmann-Sträussler syndrome (GSS). To demonstrate that prion protein (PrP) is a component of kuru plaque cores, we fractionated and sequenced kuru plaque core derived peptides, following digestion with Achromobacter lyticus protease I. We identified 3 PrP-derived peptides by reverse-phase high-performance liquid chromatography and found a fragment of digests derived from a missense variant of PrP. The variant PrP was also present in the prion rod fraction in patients with GSS. This substitution may play a major role in cerebral amyloidogenesis.
Kitamoto
T
T
Department of Neuropathology, Kyushu University, Fukuoka, Japan.
Yamaguchi
K
K
Doh-ura
K
K
Tateishi
J
J
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D007562:Creutzfeldt-Jakob Syndrome / Q000378:metabolism / Q000473:pathology; D014644:Genetic Variation; D016098:Gerstmann-Straussler-Scheinker Disease / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D018620:PrPSc Proteins; D011328:Prions / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
D018620:PrPSc Proteins; D011328:Prions; D014764:Viral Proteins