Prion protein self-peptides modulate prion interactions and conversion |
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| Authors: | Alan Rigter Jan Priem Drophatie Timmers-Parohi Jan PM Langeveld Fred G van Zijderveld Alex Bossers |
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| Affiliation: | (1) Department of Bacteriology and TSEs, Central Veterinary Institute (CVI) of Wageningen UR, Lelystad, 8200, AB, the Netherlands;(2) Pepscan Presto BV, Lelystad, 8243, RC, the Netherlands |
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| Abstract: | Background Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood. Selective self-interaction between PrP molecules forms a basis underlying the observed differences of the PrPC into PrPSc conversion process (agent replication). The importance of previously peptide-scanning mapped ovine PrP self-interaction domains on this conversion was investigated by studying the ability of six of these ovine PrP based peptides to modulate two processes; PrP self-interaction and conversion. |
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