State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Acta Biochim Biophys Sin (Shanghai). 2013 Jun;45(6):465-76. doi: 10.1093/abbs/gmt027. Epub 2013 Apr 11.
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform. However, pathogenic mutations, modifications as well as some cofactors, such as glycosaminoglycans, nucleic acids, and lipids, could modulate the conformational conversion process. Understanding the mechanism of conformational conversion of prion protein is essential for the biomedical research and the treatment of prion diseases. Particularly, the characterization of cofactors interacting with prion protein might provide new diagnostic and therapeutic strategies.
朊病毒病是一组传染性致命的神经退行性疾病。细胞朊蛋白（PrP(C)）构象转换为异常错误折叠的异构体（PrP(Sc)）是朊病毒病病理学中的关键事件。在正常情况下，高能量障碍将 PrP(C)与 PrP(Sc)异构体分离。然而，致病突变、修饰以及一些辅助因子，如糖胺聚糖、核酸和脂质，可以调节构象转换过程。了解朊蛋白构象转换的机制对于朊病毒病的生物医学研究和治疗至关重要。特别是，与朊蛋白相互作用的辅助因子的特征可能提供新的诊断和治疗策略。
