Delayed progression of prion disease in mice by polyarginine-facilitated prevention of PrP^Sc propagation in the spleen.

ABSTRACT: Prions are infective agents composed of abnormally folded prion proteins (PrP^Sc), which are pathogenic isoforms of normal cellular prion proteins (PrP^C) that cause incurable, transmissible, neurodegenerative conditions in mammals called prion diseases. The spread of PrP^Sc within a host is facilitated by the lymphoreticular system, which uptakes and propagates PrP^Sc in the periphery and transmits them to the central nervous system. Our previous study showed that poly-l-arginine (PLR), a cationic amino acid polymer, inhibits PrP^Sc accumulation in neuroblastoma cells with persistent prion infection (ScN2a). Here, we report the beneficial effect of PLR against prions. In the in vitro prion infection experiment, PLR efficiently reduced the

SUBMITTER: Lee S 

PROVIDER: S-EPMC12047483 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature