Doppel蛋白研究进展  

Advances on research of Doppel protein

作　　者：丁天兵[1] 邢玉洁[2] 魏波[2] 秦克锋[1] 

机构地区：[1]第四军医大学微生物学教研室,陕西西安710032 [2]第四军医大学口腔医学系13队

出　　处：《中国病原生物学杂志》2006年第6期457-461,共5页Journal of Pathogen Biology

基　　金：国家自然科学基金项目(No.3008006)

摘　　要：朊蛋白PrPC的错误折叠形式即PrPSc,它是瘙痒症感染因子的主要组成部分,也是可传播性海绵样脑病(TSE)的致病因子,但是PrPSc既不引发免疫应答也不产生炎症反应。编码细胞水平的PrPC蛋白的基因Prnp20年前就已经被克隆,但是其基因序列及功能仍不清楚。直到1999年才发现了一种新蛋白,命名为Doppel(Dpl),此蛋白与PrPC在生化和结构方面有不少相似性,其一级结构与PrPCC端的2/3有25%的同源性。尽管有关Dpl的研究尚处于萌芽状态,但它的发现已经解释了朊蛋白生物学上的一些谜团,而且对其生理功能也有了一定的了解。本文综述了近年来对Dop-pel蛋白的研究进展。PrP^Sc, the misfolding form of PrP^C protein, is the main component of scrapie infections and causing agent of transmissible spongiform encephalopathy （TSE）. Neither does it induce immune responses of the hosts, nor does it produce inflammatory reactions. The gene encoding PrP^C, Prnp, was cloned twenty years ago; however, its genetic structure and physiological function were not clearly defined. Until 1999 when a new protein, designated Doppel （Dpl）, was first identified when physiological functions of PrPc were investigated by using corresponding knout-out mice. Dpl shares significant homology with PrP^C on biochemistry and structure-the two thirds of C terminus in primary structure has 25% homology with PrP^C. Although the research work about Dpl is now still in its infancy, some new findings elucidated some of the mysteries on prion biological and physiological functions. This article reviews the recent research advances on Doppel protein.

关 键 词：DOPPEL PrP^C 结构 功能 综述 

分 类 号：R37[医药卫生—病原生物学]