PrP及其缺失突变体与微管蛋白的体外相互作用的初步研究  

Interaction Analysis between Various PrP Fusion Proteins and the Tubulin In Vitro

作　　者：董辰方[1] 王小凡[1] 安润[2] 陈建明[1] 单冰[1] 韩露[1] 雷艳君[2] 韩俊[1] 董小平[1] 

机构地区：[1]中国疾病预防控制中心病毒病预防控制所传染病预防控制国家重点实验室,北京100052 [2]西安交通大学医学院,西安710061

出　　处：《病毒学报》2007年第1期28-32,共5页Chinese Journal of Virology

基　　金：国家自然科学基金委重点项目(编号:3011402);国家自然科学基金委重点项目(编号:30130070);国家自然科学基金委项目(编号:30571672);国家高技术研究发展计划(863计划)项目(编号:2001AA215391);欧盟项目(编号:QLRT200001441);国家科技攻关计划项目(编号:2003BA712A04-02)资助

摘　　要：为了进一步确定PrP蛋白与微管蛋白是否发生分子间相互作用以及PrP蛋白多肽链中与微管蛋白相互作用的区域,我们表达纯化了全长的PrP以及PrP蛋白缺失突变体,提取了兔脑组织中天然微管蛋白。利用pull-down及免疫共沉淀方法检测全长PrP及PrP蛋白缺失突变体与微管蛋白是否发生分子间相互作用。结果显示,全长His-PrP23-231能与微管蛋白发生体外相互作用,并首次证实了PrP与微管蛋白相互作用的区域位于PrP N端第23位至91位氨基酸。此研究为进一步研究PrP在神经细胞的主动转运机制以及Prion疾病的发病机制提供了一定的理论基础。In order to further study the potential interaction between PrP protein and the tubulin and identify the binding region in PrP with tubulin, native tubulin was extracted from rabbit brian tissues, while various recombinant PrP proteins were expressed and purified. The possible molecular interaction between various PrP fusion proteins and tubulin was tested by pull-down and immunoprecipitation assays. Remarkable molecular interaction between the full length PrP and tubulin was observed by pull-down and immunoprecipitation assays. Subsequently, the binding regions within PrP with tubulin were firstly mapped in the aa 23 - 91 region within N-terminus of PrP peptide. The studies of the association of PrP with tubulin may further provide insight into the unresolved mechanism of active transport of PrP protein in neurons and possible cellular pathways by which prion causes disease.

关 键 词：PrP蛋白 微管蛋白 分子间相互作用 

分 类 号：R373.9[医药卫生—病原生物学] Q78[医药卫生—基础医学]