Journal
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume 35, Issue 11, Pages 1103-1115Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2011.03.029
Keywords
TnMAVS; Interferon-sensitive response element; NF-kB; ISKNV
Categories
Funding
- National Natural Science Foundation of China [U0631008]
- National Basic Research Program of China [2006CB101802]
- National High Technology Research and Development Program of China (863 Program) [2006AA09Z445, 2006AA100309]
- Guangdong Province Natural Science Foundation [20023002]
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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-kappa B 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. (C) 2011 Elsevier Ltd. All rights reserved.
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