文章基本信息

标题：Recombinant Human Prion Protein Inhibits Prion Propagation in vitro
本地全文：下载
作者：Jue Yuan ; Yi-An Zhan ; Romany Abskharon 等
期刊名称：Scientific Reports
电子版ISSN：2045-2322
出版年度：2013
卷号：3
期号：1
DOI：10.1038/srep02911
语种：English
出版社：Springer Nature
摘要：Prion diseases are associated with the conformational conversion of the cellular prion protein (PrP^C) into the pathological scrapie isoform (PrP^Sc) in the brain. Both the in vivo and in vitro conversion of PrP^C into PrP^Sc is significantly inhibited by differences in amino acid sequence between the two molecules. Using protein misfolding cyclic amplification (PMCA), we now report that the recombinant full-length human PrP (rHuPrP23-231) (that is unglycosylated and lacks the glycophosphatidylinositol anchor) is a strong inhibitor of human prion propagation. Furthermore, rHuPrP23-231 also inhibits mouse prion propagation in a scrapie-infected mouse cell line. Notably, it binds to PrP^Sc, but not PrP^C, suggesting that the inhibitory effect of recombinant PrP results from blocking the interaction of brain PrP^C with PrP^Sc. Our findings suggest a new avenue for treating prion diseases, in which a patient's own unglycosylated and anchorless PrP is used to inhibit PrP^Sc propagation without inducing immune response side effects.