Bosque Patrick J, Ryou Chongsuk, Telling Glenn, Peretz David, Legname Giuseppe, DeArmond Stephen J, Prusiner Stanley B
Institute for Neurodegenerative Diseases, Department of Neurology, University of California, San Francisco, CA 94143, USA.
Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3812-7. doi: 10.1073/pnas.052707499.
Considerable evidence argues that consumption of beef products from cattle infected with bovine spongiform encephalopathy (BSE) prions causes new variant Creutzfeldt-Jakob disease. In an effort to prevent new variant Creutzfeldt-Jakob disease, certain "specified offals," including neural and lymphatic tissues, thought to contain high titers of prions have been excluded from foods destined for human consumption [Phillips, N. A., Bridgeman, J. & Ferguson-Smith, M. (2000) in The BSE Inquiry (Stationery Office, London), Vol. 6, pp. 413-451]. Here we report that mouse skeletal muscle can propagate prions and accumulate substantial titers of these pathogens. We found both high prion titers and the disease-causing isoform of the prion protein (PrP(Sc)) in the skeletal muscle of wild-type mice inoculated with either the Me7 or Rocky Mountain Laboratory strain of murine prions. Particular muscles accumulated distinct levels of PrP(Sc), with the highest levels observed in muscle from the hind limb. To determine whether prions are produced or merely accumulate intramuscularly, we established transgenic mice expressing either mouse or Syrian hamster PrP exclusively in muscle. Inoculating these mice intramuscularly with prions resulted in the formation of high titers of nascent prions in muscle. In contrast, inoculating mice in which PrP expression was targeted to hepatocytes resulted in low prion titers. Our data demonstrate that factors in addition to the amount of PrP expressed determine the tropism of prions for certain tissues. That some muscles are intrinsically capable of accumulating substantial titers of prions is of particular concern. Because significant dietary exposure to prions might occur through the consumption of meat, even if it is largely free of neural and lymphatic tissue, a comprehensive effort to map the distribution of prions in the muscle of infected livestock is needed. Furthermore, muscle may provide a readily biopsied tissue from which to diagnose prion disease in asymptomatic animals and even humans.
大量证据表明,食用感染牛海绵状脑病(BSE)朊病毒的牛的牛肉制品会引发新型克雅氏病。为预防新型克雅氏病,某些被认为含有高滴度朊病毒的“特定牛杂碎”,包括神经和淋巴组织,已被排除在供人类食用的食品之外[菲利普斯,N.A.,布里奇曼,J. & 弗格森 - 史密斯,M.(2000年),载于《疯牛病调查报告》(伦敦文书局),第6卷,第413 - 451页]。在此我们报告,小鼠骨骼肌能够传播朊病毒并积累大量此类病原体。我们在接种了Me7或落基山实验室鼠朊病毒株的野生型小鼠的骨骼肌中发现了高滴度的朊病毒以及致病形式的朊病毒蛋白(PrP(Sc))。特定肌肉积累了不同水平的PrP(Sc),后肢肌肉中观察到的水平最高。为确定朊病毒是在肌肉内产生还是仅仅在肌肉内积累,我们构建了仅在肌肉中表达小鼠或叙利亚仓鼠PrP的转基因小鼠。对这些小鼠进行肌肉内接种朊病毒会导致肌肉中形成高滴度的新生朊病毒。相比之下,对PrP表达靶向肝细胞的小鼠进行接种,朊病毒滴度较低。我们的数据表明,除了PrP表达量之外的因素决定了朊病毒对某些组织的嗜性。某些肌肉本身能够积累大量朊病毒这一点尤其令人担忧。因为通过食用肉类可能会发生大量的朊病毒饮食暴露,即使肉类基本不含神经和淋巴组织,所以需要全面努力绘制感染家畜肌肉中朊病毒的分布图。此外,肌肉可能提供一种易于活检的组织,用于在无症状动物甚至人类中诊断朊病毒疾病。