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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/78223完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張麗冠(Li-Kwan Chang) | |
| dc.contributor.author | Hsiao-Han Tsai | en |
| dc.contributor.author | 蔡曉涵 | zh_TW |
| dc.date.accessioned | 2021-07-11T14:46:39Z | - |
| dc.date.available | 2021-07-05 | |
| dc.date.copyright | 2016-07-05 | |
| dc.date.issued | 2016 | |
| dc.date.submitted | 2016-06-27 | |
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Non-structural protein 4A of Hepatitis C virus accumulates on mitochondria and renders the cells prone to undergoing mitochondria-mediated apoptosis. J Gen Virol 87 (Pt 7):1935-1945. Nutter, L. M., S. P. Grill, J. S. Li, R. S. Tan, and Y. C. Cheng. 1987. Induction of virus enzymes by phorbol esters and n-butyrate in Epstein-Barr virus genome-carrying Raji cells. Cancer Res 47 (16):4407-4412. Obita, T., T. Muto, T. Endo, and D. Kohda. 2003. Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences. J Mol Biol 328 (2):495-504. Ohman, T., J. Rintahaka, N. Kalkkinen, S. Matikainen, and T. A. Nyman. 2009. Actin and RIG-I/MAVS signaling components translocate to mitochondria upon influenza A virus infection of human primary macrophages. J Immunol 182 (9):5682-5692. Ordureau, A., S. A. Sarraf, D. M. Duda, J. M. Heo, M. P. Jedrychowski, V. O. Sviderskiy, J. L. Olszewski, J. T. Koerber, T. Xie, S. A. Beausoleil, J. A. Wells, S. P. Gygi, B. A. Schulman, and J. W. Harper. 2014. Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis. Mol Cell 56 (3):360-375. Pal, A. D., N. P. Basak, A. S. Banerjee, and S. Banerjee. 2014. Epstein-Barr virus latent membrane protein-2A alters mitochondrial dynamics promoting cellular migration mediated by Notch signaling pathway. Carcinogenesis 35 (7):1592-1601. Parker, B. D., A. Bankier, S. Satchwell, B. Barrell, and P. J. Farrell. 1990. Sequence and transcription of Raji Epstein-Barr virus DNA spanning the B95-8 deletion r | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/78223 | - |
| dc.description.abstract | Epstein-Barr Virus (EB 病毒) 屬於人類疱疹病毒科，其生活史包括潛伏期 (latent life cycle) 與溶裂期 (lytic cycle)，而極早期蛋白質 Rta 是促使 EB 病毒進入溶裂期的關鍵轉錄因子之一。本實驗室在先前的研究中發現 Rta 蛋白質在 EB 病毒潛伏期時會分布於粒線體。粒線體參與了許多細胞生理途徑，如能量的產生、細胞死亡、宿主免疫反應的誘導和老化等；而粒線體自噬 (mitophagy) 為維持粒線體網絡健康的重要機制。本研究欲證實 Rta 蛋白質上是否具有粒線體導向序列 (mitochondria targeting sequence，MTS)，並初步探討 Rta 蛋白質位於粒線體上的意義及其扮演的角色。首先以具有病毒潛伏的 P3HR1 細胞、B95-8 細胞及 293-2089 細胞為材料，利用免疫螢光染色分析探討 Rta 於細胞中的分佈情形，結果證實 Rta 蛋白質位於粒線體；同時利用粒線體分離分析結果指出，細胞中 Rta 蛋白質在細胞質與粒線體中皆有表現。接著利用 293T 細胞為材料，轉染入不同 Rta 片段之建構質體，可藉由觀察其進粒線體與否推定出 MTS 為 Rta 蛋白質之 N 端第 68 至 90 胺基酸片段，並由生物資訊軟體預測出其具有 α 螺旋體結構。接著以共免疫沉澱分析證明了 Rta 蛋白質會與粒線體外膜蛋白導入受體 (import receptor) Tom20 結合。而後以 ATP 測定分析結果發現，在 293T 細胞表現 Rta 後會使細胞中的 ATP 產量提高。最後，以 carbonyl cyanide m-chlorophenyl hydrazine (CCCP) 處理 293T 細胞，誘導粒線體損害進而引發粒線體自噬，結果發現 Rta 蛋白質的表現可能會促進粒線體自噬。總和以上所述，本研究首度證實 Rta 含有一 α 螺旋體結構的 MTS，可位於粒線體並影響粒線體的功能。 | zh_TW |
| dc.description.abstract | Epstein-Barr virus (EBV) is a human herpesvirus with two distinct life cycles, latent and lytic. Rta, an immediate-early protein, is an important transcription factor required for initiating the lytic cycle of EBV. Our preliminary study found that Rta is localized at mitochondria during EBV latency. Mitochondrium is a multifunctional organelle with diverse roles including energy production, apoptosis, elicitation of host immune response, and aging. Moreover, mitochondria autophagy (mitophagy) is a critical mechanism to maintain mitochondrial health and homeostasis. This study aims to investigate whether Rta contains mitochondria targeting sequence (MTS), and examine roles of Rta in mitochondria. First, immunofluorescence analysis indicated that Rta colocalizes with mitochondria in P3HR1 cells, B95-8 cells and 293-2089 cells during both EBV latency and lytic cycle. Mitochondria isolation assay was performed and indicated that Rta expresses both in cytosolic and mitochondrial fraction. Mutagenesis and bioinformatic analyses demonstrated that an MTS is localized between amino acid residues 68 to 90 in Rta, which forms an amphipathic α-helix structure. Co-immunoprecipitation assay further indicated that Rta binds to Tom20, an import receptor on mitochondrial outer membrane. ATP determination assay also revealed that overexpressing Rta increases ATP levels in 293T cells. Finally, treatment of carbonyl cyanide m-chlorophenyl hydrazine (CCCP) to 293T cells with expression of Rta affects mitophagy. Taken together, this study demonstrates that Rta is a mitochondrion-targeted protein that contains an amphipathic α-helical MTS, which may affect the functions of mitochondria. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-11T14:46:39Z (GMT). No. of bitstreams: 1 ntu-105-R00b22020-1.pdf: 4263063 bytes, checksum: bcfa36c8c1dc3cdb568f7c483528b430 (MD5) Previous issue date: 2016 | en |
| dc.description.tableofcontents | 謝辭 i
摘要 ii Abstract iii 第一章、 前言 1 一、 Epstein-Barr virus (EB 病毒) 的發現及其致病性 1 二、 EB 病毒的遺傳物質及結構 2 三、 EB 病毒的生活史 2 潛伏期 (Latency)…………………………………………………………3 溶裂期 (Lytic cycle)………………………………………………………3 四、 EB 病毒的極早期蛋白質 5 Zta 蛋白質…………………………………………………………………5 Rta 蛋白質…………………………………………………………………7 Rta 轉錄活性的調控………………………………………………………7 Rta 參與細胞生理途徑…………………………………………………10 五、 粒線體 (mitochondria) 的生理重要性 11 粒線體藉氧化磷酸化合成 ATP…………………………………………12 粒線體參與細胞凋亡 (apoptosis)………………………………………12 粒線體與免疫系統的關聯………………………………………………14 粒線體自噬 (mitophagy)…………………………………………………14 六、 粒線體導向序列 (mitochondrial targeting signal, MTS) 15 七、 病毒對粒線體功能的調節 16 1. 病毒在宿主細胞中引發氧化壓力 (oxidative stress)………………16 2. 病毒調節宿主的粒線體膜電位 (mitochondrial membrane potential, MMP)……………………………………………………………………17 3. 病毒可調控細胞凋亡 (apoptosis)…………………………………18 4. 病毒影響粒線體相關的抗病毒免疫機制…………………………19 5. 病毒改變粒線體在細胞內的分布…………………………………19 6. 病毒造成宿主粒線體 DNA 耗竭 (mitochondrial DNA depletion).19 八、 EB 病毒與粒線體間的關係 20 九、 研究目的 21 第二章、 材料與方法 22 一、 細胞株 22 二、 EB 病毒的溶裂期誘導 22 三、 質體與抗體 23 四、 質體 DNA 的萃取 23 五、 細菌 23 六、 細菌轉型作用 (transformation) 23 七、 細胞轉染 (Transfection) 23 八、 免疫螢光染色分析 (Immunofluorescence analysis) 24 九、 粒線體的分離分析 25 十、 西方點墨法分析 (Western blot analysis) 25 十一、 免疫沈澱法 (Immunoprecipitation, IP) 26 十二、 加藥處理 26 十三、 ATP 測定分析 (ATP Determination assay) 26 第三章、 結果 28 一、 Rta 蛋白質存在於粒線體 28 二、 Rta 蛋白質會與 Tom20 結合 29 三、 Rta 的粒線體導向序列 (MTS) 分析 30 四、 Rta 的 N 端第 68 至 90 胺基酸之二級、三級結構預測 31 五、 MTS 上四個疏水性胺基酸突變使 Rta 無法進入粒線體 32 六、 Rta 蛋白質影響細胞內 ATP 的產量 32 七、 Rta 蛋白質影響粒線體自噬 (mitophagy) 33 第四章、 討論 34 圖表 41 表1、 本研究所使用之質體 41 表2、 本研究所使用之抗體 45 圖 1-1、EB 病毒的結構示意圖 46 圖 1-2、EB 病毒的生活史 47 圖 1-3、EB 病毒的溶裂期生活史 48 圖 1-4、EB 病毒極早期蛋白質 Rta 與 Zta 的表現 49 圖 1-5、Rta 蛋白質的功能區及入核訊號示意圖 50 圖 1-6、粒線體參與的生理途徑 51 圖 1-7、病毒可調節粒線體功能 52 圖 3-1、Rta 蛋白質與粒線體在 EB 病毒潛伏期的免疫螢光染色分析 53 圖 3-2、Rta 蛋白質與粒線體在 EB 病毒溶裂期的免疫螢光染色分析 54 圖 3-3、以粒線體分離分析 Rta 蛋白質的分布 56 圖 3-4、Rta 與 Tom20 在細胞內結合 57 圖 3-5、Rta 的刪除突變株在細胞中的分布 58 圖 3-6、Rta 及其刪除突變株的粒線體導向序列分析 60 圖 3-7、Rta 的突變株和粒線體在293T 細胞中的免疫螢光染色分析 62 圖 3-8、Rta 的 N 端片段之二級、三級結構預測 63 圖 3-9、Rta 及 Rta 的 MTS 突變株在細胞中的分布位置 64 圖 3-10、Rta 的 MTS 突變株和粒線體在293T 細胞中的免疫螢光染色分析 ………………………………………………………………………..65 圖 3-11、Rta 對細胞產生能量的影響 67 圖 3-12、Rta 對粒線體自噬的影響 68 圖 4-1、Rta 蛋白質與粒線體的關係 69 參考文獻……………………………………………………………………………..70 附錄 98 附錄 1、Rta 蛋白質在電子顯微鏡觀察下於 P3HR1 細胞內的分佈情形 (王文宏, 未發表) 98 附錄 2、粒線體內膜上的電子傳遞鍊與 ATP 合成酶 99 附錄 3、細胞凋亡的外在與內在途徑 101 附錄 4、粒線體參與的抗病毒免疫機制 103 附錄 5、粒線體的動態恆定以及質量管制 104 附錄 6、粒線體蛋白質的運輸機制 105 附錄 7、MTS 的結構特性及其與 Tom20 受體蛋白的相互作用 106 | |
| dc.language.iso | zh-TW | |
| dc.title | EB 病毒蛋白質 Rta 對粒線體的影響 | zh_TW |
| dc.title | Role of Rta of Epstein-Barr virus in mitochondria | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 104-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 劉世東(Shih-Tung Liu),莊健盈,張世宗,陳慧文 | |
| dc.subject.keyword | EB 病毒,Rta,粒線體,粒線體導向序列,粒線體自噬, | zh_TW |
| dc.subject.keyword | Epstein-Barr virus,Rta,mitochondria,mitochondria targeting sequence,mitophagy, | en |
| dc.relation.page | 106 | |
| dc.identifier.doi | 10.6342/NTU201600518 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2016-06-28 | |
| 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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