Kretzschmar H A, Neumann M, Riethmüller G, Prusiner S B
Institute of Neuropathology, University of Munich, Germany.
J Gen Virol. 1992 Oct;73 ( Pt 10):2757-61. doi: 10.1099/0022-1317-73-10-2757.
Transmissible mink encephalopathy (TME) is a rare disease which is presumably transmitted to ranch-raised mink from scrapie-infected sheep offal or bovine spongiform encephalopathy-infected cattle products. Although the infectious agent of TME has not been isolated, there is circumstantial evidence that TME is caused by prions. The experimental host range of TME includes sheep, cattle, monkeys and hamsters. However, TME has never been transmitted to mice. Since experiments in transgenic animals have shown that the prion protein (PrP) gene modulates the susceptibility, incubation time and neuropathology of prion-induced disease, we have started to analyse the mink PrP gene. PrP, as deduced from a genomic DNA sequence, consists of 257 amino acids and overall shows similarity of 84 to 90% with the sequences of the PrPs of other mammalian species. It remains to be determined whether these differences in the primary structure of PrP will explain the peculiar host range of TME.
传染性水貂脑病(TME)是一种罕见疾病,据推测是牧场养殖的水貂通过感染羊瘙痒病的绵羊内脏或感染牛海绵状脑病的牛产品感染所致。尽管尚未分离出TME的传染因子,但有间接证据表明TME是由朊病毒引起的。TME的实验宿主范围包括绵羊、牛、猴子和仓鼠。然而,TME从未传染给小鼠。由于转基因动物实验表明,朊病毒蛋白(PrP)基因可调节朊病毒诱导疾病的易感性、潜伏期和神经病理学,我们已开始分析水貂PrP基因。根据基因组DNA序列推导,PrP由257个氨基酸组成,与其他哺乳动物物种PrP序列的总体相似度为84%至90%。PrP一级结构的这些差异是否能解释TME独特的宿主范围,仍有待确定。