Characterization of orange-spotted grouper HSP90AB and its relationship with nervous necrosis virus
碩士 === 國立成功大學 === 生物科技研究所碩博士班 === 98 === 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 characte...
| Main Authors: | , |
|---|---|
| Other Authors: | |
| Format: | Others |
| Language: | zh-TW |
| Published: |
2010
|
| Online Access: | http://ndltd.ncl.edu.tw/handle/37434766673510180028 |
| Summary: | 碩士 === 國立成功大學 === 生物科技研究所碩博士班 === 98 === 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.
|
|---|