Characterization of a TnMAVS protein from Tetraodon nigroviridis

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• 作者：Zhiming  ; Xiang^a ;   ; ^b ;   ; ¹ ; Lin  ; Qi^a ;   ; ¹ ; Weijian  ; Chen^a ; Chuanfu  ; Dong^a ; Zhaoyu  ; Liu^a ; Dong  ; Liu^a ; Mengli  ; Huang^a ; Wei  ; Li^a ; Gan  ; Yang^a ; Shaoping  ; Weng^a ; Jianguo  ; He^a ;   ; ^{lsshjg@mail.sysu.edu.cn}
• 关键词：TnMAVS ; Interferon-sensitive response element ; NF-kB ; ISKNV
• 刊名：Developmental & Comparative Immunology
• 出版年：2011
• 出版时间：November 2011
• 年：2011
• 卷：35
• 期：11
• 页码：1103-1115
• 全文大小：3051 K

文摘

A growing family of cellular proteins encoding for caspase activation and the recruitment domain (CARD) plays a crucial role in immunity by sensing viral infections and signaling antiviral immune defenses. We obtained a MAVS-like protein (named TnMAVS) from Tetradon nigroviridis, which contains a CARD domain, a pro-rich domain, and a TM domain similar to human MAVS. A fluorescence assay showed that TnMAVS was located in the cytoplasm and near by the membrane, and not the mitochondria in FHM cells. As such, it was considered as a new member of MAVS. The TnMAVS was highly expressed in the liver and muscle of T. nigroviridis. In the spleen, TnMAVS was down-regulated when the fish was treated with polyinosinic:polycytidylic acid or challenged with ISKNV, but was not affected by PGN or LPS. The dual luciferase reporter assay revealed that TnMAVS overexpression resulted in the activation of the interferon-sensitive response element and NF-κB signal pathways. In addition, a characteristic TRAF3-associated peptide PVQD was found in the TnMAVS sequence. Co-immunoprecipitation assays indicated that TnMAVS could interact with zfTRAF3 in eukaryotic cells.