Interaction between G-protein-coupled receptor 125 and Enterovirus 71 2C protein

• Main Authors: Lin tzu-yao, 林紫瑤
• Other Authors: Horng jim-tong
• Format: Others
• Language: zh-TW
• Published: 2007
• Online Access: http://ndltd.ncl.edu.tw/handle/71391276151803299195

碩士 === 長庚大學 === 基礎醫學研究所 === 95 === Enterovirus 71 (EV71) is a member of the picornaviridae family and contains a single-stranded RNA genome of positive polarity. The human enterovirus is classified into five species: the poliovirus (PV), coxsakievirus A, coxsakievirus B, echovirus, and other enteroviruses. Their genomes are highly homologous and share similar biochemical properties. One of the general features is that infection with those viruses results in membrane rearrangements. These membrane rearrangements are triggered by the viral preprotein 2BC and mature protein 2C. The 2C protein is one of the most highly conserved viral proteins among picornaviruses. Genetic analyses have implicated the PV 2C contribute to host cell membrane rearrangement and RNA replication during viral replication. Previously, we performed yeast-two hybrid to search cellular proteins that interact with N-terminal region of EV71 2C protein. We found that the EV71 2C protein might interact with G-protein-coupled receptor 125 (GPR125). In this study, we constructed four fragments of GPR125 for antibody production, but none of them had antigenecity. By immunoflourescence microscopic study, the GPR125 was localized with ER marker calregulin but not Golgi marker GM130. Using cyclohexamide to inhibit nascent protein synthesis, GPR125 was localized in the ER, suggesting that GPR125 is an ER protein at steady-state. Reduced production of GPR125 by RNA interference reduced the synthesis of EV71-encoded viral proteins. Thus, GPR125 is important for EV71 production.