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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張世宗 | |
| dc.contributor.author | Kuo-Che Hung | en |
| dc.contributor.author | 洪國哲 | zh_TW |
| dc.date.accessioned | 2021-07-11T14:37:22Z | - |
| dc.date.available | 2022-08-30 | |
| dc.date.copyright | 2017-08-30 | |
| dc.date.issued | 2017 | |
| dc.date.submitted | 2017-08-10 | |
| dc.identifier.citation | 1. Taubenberger, J. K., and Morens, D. M. (2008) The pathology of influenza virus infections. Annual review of pathology 3, 499-522
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/77917 | - |
| dc.description.abstract | 新型H7N9禽流感病毒的特色為高重症率與高死亡率，而流感病毒蛋白質PB1-F2是造成高重症率的因子之一。PB1-F2為病毒聚合酶PB1基因根據另外一個轉譯閱讀框架而轉譯出的蛋白質。研究指出PB1-F2可增進PB1聚合酶的活性，亦可藉由改變粒線體之膜電位而造成細胞凋亡，或者破壞宿主抵禦病毒入侵的機制，進而造成肺部的二次性細菌感染。本研究發現將新型H7N9流感病毒之PB1-F2基因於HEK293細胞表現時，其表現量可因加入蛋白酶體之抑制劑MG132，而有顯著上升的現象，顯示半衰期短暫的H7N9 PB1-F2蛋白質於細胞內的穩定性可能是由蛋白酶體所調控。進一步將PB1-F2分子上可能會被泛素化的所有離胺酸突皆變為精胺酸時，此PB1-F2的突變株於細胞中仍會被快速的降解，除非同時以MG132來處理細胞，才能偵測到PB1-F2的表現，顯示其降解可能並不需要經過泛素化。本研究亦於大腸桿菌中，成功表現及純化出N端為麥芽糖結合蛋白 (Maltose-binding protein, MBP) 與C端為PB1-F2的融合重組蛋白質 (MBP-F2)。將MBP-F2或MBP分別與20S蛋白酶體進行反應後，實驗結果顯示MBP-F2受到蛋白酶體的降解速率比MBP降解速率為慢，此結果與細胞實驗結果不同，詳細的反應機制尚須進一步探討。 | zh_TW |
| dc.description.abstract | The novel avian influenza virus H7N9 is known to have high morbidity and mortality. Influenza protein PB1-F2 is one of the factor that contributes to sever symptoms. PB1-F2 is translated from the alternative open reading frame of the viral PB1 polymerase gene segment. Previous studies showed that PB1-F2 could enhance the activity of PB1 polymerase, and could enter mitochondria intermembrane space to alter the membrane potential which results in cell apoptosis. It could also interact with mitochondrial antiviral signaling protein, damage the immunity of host cells, and cause secondary bacterial lung infection. This study found that the H7N9 PB1-F2 protein expression in HEK293 cell line was elevated by treated with proteasome inhibitor MG132, indicating that the stability of short-lived H7N9 PB1-F2 protein in cells might be regulated by proteasome. Furthermore, the PB1-F2 mutant without containing any potential ubiquitination lysine residues, which were replaced by arginines, was still degraded rapidly unless treated cells with MG132, demonstrating that the degradation of PB1-F2 might be ubiquitination-independent. In addition, the maltose binding protein (MBP) conjugated with a C-terminal PB1-F2 fusion protein (MBP-F2) was successfully expressed and purified by using Escherichia coli expression system. The purified MBP or MBP-F2 was then incubated with 20S proteasome respectively. The data showed that the degradation of MBP-F2 catalyzed by 20S proteasome in vitro was slower than that of MBP, revealing a different result observed in cellular experiments. More detailed investigation about the relationship between PB1-F2 and proteasome need to be further explored. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-11T14:37:22Z (GMT). No. of bitstreams: 1 ntu-106-R04b22002-1.pdf: 2760236 bytes, checksum: 78315901ce88d1541940f333cfdce34e (MD5) Previous issue date: 2017 | en |
| dc.description.tableofcontents | 目錄 i
摘要 iii Abstract iv 縮寫表 v 第一章 緒論 1 1.1. 流感病毒 1 1.1.1. 禽流感病毒 3 1.1.2. 新型H7N9病毒 4 1.2. Polymerase basic protein- frame 2 (PB1-F2) 5 1.2.1. PB1-F2蛋白質的發現 5 1.2.2. PB1-F2蛋白質的結構 6 1.2.3. PB1-F2在細胞凋亡機制上游以及細胞先天免疫功能調節的角色 6 1.2.4. PB1-F2蛋白質可以調控PB1聚合酶的活性 8 1.2.5. PB1-F2蛋白質可以增進細菌二次感染宿主的機會 8 1.2.6. 依賴蛋白酶體的降解機制以及PB1-F2的泛素化 8 1.3. 研究動機 9 第二章 材料與方法 11 2.1. PB1-F2基因來源 11 2.2. 大腸桿菌菌株 11 2.2.1. 大腸桿菌DH5α 11 2.2.2. 大腸桿菌BL21(DE3) 11 2.2.3. 大腸桿菌Rosetta(DE3) 12 2.2.4. 大腸桿菌Origami(DE3) 12 2.2.5. 大腸桿菌Tuner(DE3) 12 2.3. 人類細胞株 12 2.4. PB1-F2重組蛋白質表現質體建立 13 2.4.1. PB1-F2突變株建立 14 2.5. 重組蛋白質表現 14 2.6. 重組蛋白質純化 15 2.7. 細胞轉染 16 2.8. 變性免疫沉澱法 16 2.9. 免疫染色分析 17 2.10. 胞外20S蛋白酶體降解試驗 17 第三章 結果 19 3.1. PB1-F2蛋白質在HEK293細胞中的穩定性 19 3.1.1. HEK 293細胞表現質體建構 19 3.1.2. V5-F2-His和GFP-F2重組蛋白質在HEK293細胞內的穩定度分析 19 3.2. PB1-F2在細胞中的表現與探討其蛋白酶體降解機制 20 3.2.1. 免疫沉澱分析泛素化之GFP-F2重組蛋白質 20 3.2.2. PB1-F2突變株建立 20 3.2.3. PB1-F2野生株與突變株在HEK293細胞當中的表現量 21 3.3. PB1-F2與20S蛋白酶體的胞外試驗 21 3.3.1. 大腸桿菌表現質體建構 21 3.3.2. His-F2-His在不同株大腸桿菌當中的表現情況 22 3.3.3. MBP-F2表現與純化 22 3.3.4. MBP表現與純化 23 3.3.5. 20S蛋白酶體表現與純化 23 3.3.6. PB1-F2與20S蛋白酶體的胞外試驗 23 3.3.7. TEV蛋白酶表現與純化 25 3.3.8. MBP-F2與TEV蛋白酶的反應與F2-His的純化 25 第四章 討論 26 4.1. PB1-F2重組蛋白質在細胞內的穩定度 26 4.2. PB1-F2重組蛋白質的表現與純化 27 4.3. PB1-F2的胞外試驗 28 參考文獻 30 圖與表 36 附錄 54 | |
| dc.language.iso | zh-TW | |
| dc.title | 新型H7N9流感病毒蛋白質PB1-F2與蛋白酶體之關聯性研究 | zh_TW |
| dc.title | Study of the Relationship between the Novel Avian Influenza A(H7N9) Virus PB1-F2 Protein and Proteasome | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 105-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 廖憶純,陳慧文,鄭貽生 | |
| dc.subject.keyword | 新型H7N9流感病毒,PB1-F2,蛋白?體, | zh_TW |
| dc.subject.keyword | H7N9 influenza virus,PB1-F2,proteasome, | en |
| dc.relation.page | 60 | |
| dc.identifier.doi | 10.6342/NTU201702950 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2017-08-10 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科技學系 | zh_TW |
| 顯示於系所單位： | 生化科技學系 | |
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| ntu-106-R04b22002-1.pdf 目前未授權公開取用 | 2.7 MB | Adobe PDF |
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