Japanese encephalitis virus NS2B-NS3 protease binding to human brain proteins with dibasic residue repeat motifs

中國醫藥大學機構典藏 China Medical University Repository, Taiwan > 健康照護學院 > 營養學系暨碩士班 > 會議論文 > Item 310903500/18602

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题名:	Japanese encephalitis virus NS2B-NS3 protease binding to human brain proteins with dibasic residue repeat motifs
作者:	林振文
贡献者:	健康照護學院醫學檢驗生物技術學系
日期:	2005-11-04
上传时间:	2009-09-04 15:50:49 (UTC+8)
摘要:	Flavivirus NS2B-NS3 proteases are associated with neurovirulence, becoming an important target for insight into the virus-induced pathogenesis. In this study, a phage-displayed human brain cDNA library was used to detect possible interaction between brain proteins and the Japanese encephalitis virus (JEV) NS2B-NS3 protease. After six rounds of biopanning, eight high-affinity NS2B-NS3 protease-interacting phages were identified. Identified NS2B-NS3 protease-interacting brain proteins contained several repeats of the consensus motifs E(R/K)(R/K)K and G(R/K)(R/K) with the dibasic residues, being similar to the conserved cleavage sites among flavivirus proteases. In addition, three identified brain proteins (phage-24, 34, and 44) were predicted as the domain of trypsin inhibitor and basic region leucine zipper (bZIP) using the SMART genome search. Immunoprecipitation and cleavage of two brain fusion proteins (phage-24 and phage-46) by the NS2B-NS3 protease confirmed the specific interaction between identified brain proteins and the JEV NS2B-NS3 protease. Fluorogenic peptide substrate assays revealed dose-manner inhibitory effects of these two brain fusion proteins on the trans-cleavage activity of NS2B-NS3 protease. Moreover, in vitro signaling pathway assay revealed that the JEV NS2B-NS3 protease significantly inhibited the signaling pathway of activator protein 1(AP1), a member of the bZIP family. Our results provide an insight into the protein interaction network of the JEV NS2B-NS3 protease in human brain.
關聯:	The Seventh Chinese Laboratory Medicine Conference in Taipei
显示于类别:	[營養學系暨碩士班 ] 會議論文

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