Segments in the Amyloid Core that Distinguish Hamster from Mouse Prion Fibrils.

In this study, cross-seeding assay was used to identify the segments involved in the amyloid fibril formation of full-length hamster prion protein, SHaPrP(23-231). Our results showed that the residues in the segments 108-127, 172-194 (helix 2 in PrPC) and 200-227 (helix 3 in PrPC) are in the amyloid core of hamster prion fibrils. The segment 127-143, but not 107-126 (which corresponds to hamster sequence 108-127), was previously reported to be involved in the amyloid core of full-length mouse prion fibrils. Our results indicate that hamster prion protein and mouse prion protein use different segments to form the amyloid core in amyloidogenesis. The sequence-dependent core formation can be used to explain the seeding barrier between mouse and hamster.
PMID: 30603982 [PubMed - as supplied by publisher]

Source: Neurochemical Research - January 2, 2019 Category: Neuroscience Authors: Shen HC, Chen YH, Lin YS, Chu BK, Liang CS, Yang CC, Chen RP Tags: Neurochem Res Source Type: research