Cavallo Giorgio, Lembo David, Cavallo Rossana
Dipar.to di Sanità Pubblica e di Microbiologia, University of Turin, Turin, Italy.
Riv Biol. 2010 May-Dec;103(2-3):343-70.
Prions result in fatal degeneration of the central nervous system (CNS) in the form of diseases known as transmissible spongiform encephalopathies (TSEs). The discovery in 1996 of a new variant of Creutzfeldt-Jakob disease (a human TSE) and experimental confirmation that it is caused by the prion strain responsible for bovine spongiform encephalopathy (BSE) has greatly spurred research in this field. The mechanism underlying prion propagation is now reasonably clear. Prions multiply, in fact, by stimulating their hosts to produce proteins that are initially normal, but acquire an abnormal, prion-like conformation during the coiling stage. A fuller understanding of this mechanism could lead to the employment of molecules capable of making prion proteins revert to the normal conformation in the treatment of both TSEs and other serious CNS disorders.
朊病毒会导致中枢神经系统（CNS）发生致命性退化，其疾病形式为传染性海绵状脑病（TSEs）。1996年发现了一种新型克雅氏病（一种人类TSE），并通过实验证实它是由导致牛海绵状脑病（BSE）的朊病毒株引起的，这极大地推动了该领域的研究。目前，朊病毒传播的潜在机制已较为明确。事实上，朊病毒通过刺激其宿主产生最初正常但在卷曲阶段获得异常的、朊病毒样构象的蛋白质来进行增殖。对这一机制更全面的理解可能会促使人们在治疗TSEs和其他严重的中枢神经系统疾病时使用能够使朊病毒蛋白恢复正常构象的分子。
