Laboratories of Molecular Genetics, Institute of Biotechnology, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan 70101, Taiwan.
Fish Shellfish Immunol. 2010 May-Jun;28(5-6):895-904. doi: 10.1016/j.fsi.2010.02.004. Epub 2010 Feb 11.
The heat shock proteins (HSPs) family which consists of HSP90, HSP70, and low molecular mass HSPs are involved in chaperone activity. Here, we report the cloning and characterization of HSP90AB gene from orange-spotted grouper, Epinephelus coioides. The full-length of grouper HSP90AB was 727 amino acids and possessed an ATPase domain as well as an evolutionarily conserved molecular chaperone. The HSP90AB-green fluorescent protein fusion protein was evenly distributed in the cytoplasm. Immunohistochemistry (IHC) and real-time polymerase chain reaction (PCR) analyses indicated that the expression of grouper HSP90AB was marginally increased following nodavirus infection. Grouper E. coioides that received HSP90 inhibitor geldanamycin (GA) showed an increase in HSP90AB expression and growth of nodavirus supporting nodavirus replication.
热休克蛋白（HSPs）家族由 HSP90、HSP70 和低分子量 HSPs 组成，参与伴侣活性。在这里，我们报道了来自橘点石斑鱼（Epinephelus coioides）的 HSP90AB 基因的克隆和特性。石斑鱼 HSP90AB 的全长为 727 个氨基酸，具有 ATP 酶结构域和进化上保守的分子伴侣。HSP90AB-绿色荧光蛋白融合蛋白均匀分布在细胞质中。免疫组织化学（IHC）和实时聚合酶链反应（PCR）分析表明，石斑鱼 HSP90AB 的表达在神经坏死病毒感染后略有增加。接受 HSP90 抑制剂格尔德霉素（GA）处理的石斑鱼 E. coioides 表现出 HSP90AB 表达增加和神经坏死病毒支持的生长，从而促进了神经坏死病毒的复制。
