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朊蛋白最新研究成果
【字体: 大 中 小 】 时间:2008年09月01日 来源:生物通
编辑推荐:
来自法国食品安全管理局的研究小组,鉴定了朊蛋白的一个新特性,这一特性导致朊蛋白能引起不同寻常的羊痒病。这一结果发表在8月29日PloS Pathogens上,这一结果将为阮蛋白种间传播的多样性特征提供新的研究思路。
原文摘要:A C-Terminal Protease-Resistant Prion Fragment Distinguishes Ovine ''CH1641-Like'' Scrapie from Bovine Classical and L-Type BSE in Ovine Transgenic Mice.
Abstract
The protease-resistant prion protein (PrPres) of a few natural scrapie isolates identified in sheep, reminiscent of the experimental isolate CH1641 derived from a British natural scrapie case, showed partial molecular similarities to ovine bovine spongiform encephalopathy (BSE). Recent discovery of an atypical form of BSE in cattle, L-type BSE or BASE, suggests that also this form of BSE might have been transmitted to sheep. We studied by Western blot the molecular features of PrPres in four “CH1641-like” natural scrapie isolates after transmission in an ovine transgenic model (TgOvPrP4), to see if “CH1641-like” isolates might be linked to L-type BSE. We found less diglycosylated PrPres than in classical BSE, but similar glycoform proportions and apparent molecular masses of the usual PrPres form (PrPres #1) to L-type BSE. However, the “CH1641-like” isolates differed from both L-type and classical BSE by an abundant, C-terminally cleaved PrPres product (PrPres #2) specifically recognised by a C-terminal antibody (SAF84). Differential immunoprecipitation of PrPres #1 and PrPres #2 resulted in enrichment in PrPres #2, and demonstrated the presence of mono- and diglycosylated PrPres products. PrPres #2 could not be obtained from several experimental scrapie sources (SSBP1,
(生物通 张欢)