HSP90 (heat-shock protein 90) 為一個受溫度影響的蛋白，主要在協助細胞中的蛋白作摺疊、移動位置，或是協助病毒作組裝蛋白的工作，HSP90的伴隨蛋白 (chaperone)活性對於在細胞中執行其功能時極為重要。在本研究中主要分為兩部分，第一部分是針對點帶石斑魚HSP90AB進行功能特性的分析，比較了與其他物種在演化樹分類的差異、分析了點帶石斑魚HSP90AB在各組織的表現量分布情形，以及對HSP90AB伴隨蛋白的活性探討。第二部分則是探討HSP90AB與神經壞死病毒的關聯性，在先前的實驗工作中已初步證實點帶石斑魚HSP90AB與病毒的外鞘蛋白有結合的現象。現在更進一步利用病毒去感染石斑魚鰭細胞株，發現HSP90AB和病毒的外鞘蛋白分別在基因和蛋白層次上的表現皆有隨之上升。利用RNA干擾使HSP90AB的表現量下降，觀察到病毒的複製需要有HSP90AB的幫助。另外，將帶有綠螢光蛋白的HSP90AB質體轉染至石斑魚鰭細胞株中表現，發現在感染病毒後表現位置移動到靠近細胞核的位置。而Geldanamycin (GA)實驗和免疫共澱實驗結果證明HSP90AB誘導病毒外鞘蛋白的表現並不需要其自身的伴隨蛋白活性，而是藉由與病毒外鞘蛋白結合，進而誘導病毒外鞘蛋白大量表現。

HSP90 (heat-shock protein 90) is a temperature-dependent protein which possesses chaperone activity and involves in protein folding, translocation, or virus assembling in cell. The aim of the present study contains two portions. The first part is the characterization of orange-spotted grouper HSP90AB. The phylogenetic analysis of HSP90AB comparing with other HSP90 was conducted and the expression level from different tissues and chaperone acitivity of HSP90AB was examined. The second part is to evaluate the relationship between HSP90AB and nervous necrosis virus. Previous study in the lab has revealed that HSP90AB can interact with viral coat protein. In the present work shows that the expression of both HSP90AB and viral coat protein are increased in gene and protein level while in viral infection. RNA interference knockdown the expression of HSP90AB and shows low virus replication. In addition, HSP90AB-fused green fluorescent protein (GFP) indicates that HSP90AB will alter the position near the nucleus. At last, geldanamycin (GA) and co-immunoprecipitation experiment indicates that expression of viral coat protein can be induced by interacting with viral coat protein but does not require its own chaperone activity.

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