Interaction between various 14-3-3β segments and PrP In Vitro

VernacularTitle:信号蛋白14-3-3 β及其缺失突变体与朊蛋白体外相互作用的初步研究
Author: Ying-Hui LIU ¹ ; Yan-Ling HAN ; Juan SONG ; Ying WANG ; Wei ZHOU ; Bao-Yun ZHANG ; Chan TIAN ; Chao-Ping LI ; Jun HAN ; Xiao-Ping DONG
Author Information

1. 安徽理工大学医学院
Keywords: Protein,PrP; Prions; Molecular biology
From: Chinese Journal of Experimental and Clinical Virology 2010;24(3):165-167
CountryChina
Language:Chinese
Abstract: Objective To study the potential interaction between PrP protein.Methods The supernatant of health and scrapie-infected hamsters' brain homogenate was prepared,while various recombinant 14-3-3β or PrP proteins were purified.The possible molecular interaction between 14-3-3β proteins and PrP was tested by pull-down and immunoprecipitation assays.Results Both native PrPc and its protease-resistant isoform(PrPsc)formed complexes with 14-3-3β.The full-length recombinant 14-3-3β proteins interacted with PrP.The domain responsible for interacting 14-3-3β was located at N-terminal of 14-3-3β(residues 1 to 38).Conclusion The studies of the association of PrP with 14-3-3β may further provide insight into a potential role of 14-3-3β in the biological function of PrP and the pathogenesis of prion disease.