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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張麗冠 | |
dc.contributor.author | Yun-Ting Weng | en |
dc.contributor.author | 翁筠婷 | zh_TW |
dc.date.accessioned | 2021-07-11T14:46:10Z | - |
dc.date.available | 2021-10-17 | |
dc.date.copyright | 2016-10-17 | |
dc.date.issued | 2016 | |
dc.date.submitted | 2016-07-12 | |
dc.identifier.citation | Adams, A. 1987. Replication of latent Epstein-Barr virus genomes in Raji cells. J Virol 61 (5):1743-1746.
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/78211 | - |
dc.description.abstract | Rta 為Epstein-Barr virus (EBV) 溶裂極早期基因的產物,是溶裂期表現的轉錄因子。Tripartite-motif 5 alpha (TRIM5α) 具有泛素E3 連接酶 (ubiquitin E3 ligase)的活性, 為反轉錄病毒的限制因子 (restriction factor) , 在免疫缺乏病毒 (immunodeficiency virus) 的物種特異性上扮演重要的角色。先前的研究發現TRIM5α 能夠促進自噬作用 (autophagy) , 並和選擇性自噬作用 (selective autophagy) 的連接蛋白 (adaptor) sequestosome 1 (SQSTM1, p62) 直接結合,而減少TRIM5α 表現量會造成細胞自噬作用減少。根據本實驗室的研究,人類TRIM5α(huTRIM5α) 會與Rta 結合,並促進Rta 的泛素化,使Rta 被送入proteasome 進行降解,導致Rta 促使的轉錄活化作用減少。而將TRIM5α 基因抑制後,病毒顆粒的產量會上升,顯示TRIM5α 影響EBV 的溶裂循環。根據上述,本研究將證明TRIM5α 能促使Rta 被細胞自噬作用降解。首先,證明TRIM5α 和Rta 在細胞質作用,並能增加Rta 被K63-linked 泛素化修飾。由於p62 辨認待降解物質的根據之一是K63-linked 泛素化修飾,下一步便利用免疫共沈澱,發現Rta 會與p62 結合。免疫螢光染色的結果顯示Rta、TRIM5α 及p62 三者互相疊合。而利用有EBV 潛伏的TRIM5α-knockdown 細胞株進行免疫共沈澱及免疫螢光染色,發現TRIM5α 被抑制會造成Rta 與p62 的交互作用減少,證明TRIM5α 促進Rta 與p62的結合。此外,在TRIM5α 大量表現的細胞株中,Rta 能夠進入autolysosome 降解。最後,以藥物處理促使進入溶裂期的細胞進行自噬作用後,TRIM5α 未被抑制的細胞株其Rta 表現量明顯低於TRIM5α 被抑制的細胞株,顯示TRIM5α 能夠促使Rta 被自噬作用降解 。 | zh_TW |
dc.description.abstract | The Epstein-Barr virus (EBV) Rta protein, known as a viral transcription activator, is one of the vital keys for activating EBV lytic cycle. Tripartite-motif 5 alpha (TRIM5α) a restriction factor with the activity of ubiquitin E3 ligase causes the species-specificity of immunodeficiency virus within primates. Previous studies have been showed that TRIM5α promotes autophagy and interacts with Sequestosome 1(SQSTM1, p62), a selective autophagy adaptor. Our recent studies indicated that Rta binds to TRIM5α and promotes ubiquitination of Rta, resulting in the suppression of Rta’s transactivation activity. Knockdown of the expression of TRIM5α also increased virion production, suggesting that TRIM5α affects the EBV lytic cycle. The aim of this study is to investigate the mechanism by which TRIM5α affects Rta function via autophagy. First of all, TRIM5α and Rta colocalize at cytoplasm. Moreover, TRIM5α promotes K63-linked ubiquitination of Rta, and K63-linked ubiquitin chain is a substrate recognaizad by p62. Furthermore, p62 interacts with Rta and TRIM5α. Inhibiting the expression of TRIM5α by lentivirus introduced P3HR1 cells reduced the interaction between p62 and Rta. Showing that TRIM5α promotes interaction of p62 and Rta. Additionally, expressing TRIM5α in the cells induces the colocalization of Rta and autolysosome. Finally, the levels of Rta are siginificantly reduced in P3HR1 cells after treatment of inducing autophagy, but not in TRIM5α-knockdown cells during the EBV lytic cycle. Overall, this study demonstrates that TRIM5α induces Rta degradation by autophagy. | en |
dc.description.provenance | Made available in DSpace on 2021-07-11T14:46:10Z (GMT). No. of bitstreams: 1 ntu-105-R03b22050-1.pdf: 173961618 bytes, checksum: 40d3493bac5e2744d2634b67e75dbebe (MD5) Previous issue date: 2016 | en |
dc.description.tableofcontents | 目錄
摘要 ii 英文摘要 iii 常用縮寫表 iv 前言 1 一、Epstein-Barr virus (EBV) 1 二、EBV的遺傳物質及結構 1 三、EBV的生活史 2 四、EBV的極早期蛋白質─Rta 4 五、自噬作用 (Autophagy) 6 六、泛素與泛素化 (Ubiquitin and ubiquitination) 11 七、Tripartite motif 5 alpha (TRIM5α) 14 研究目的 18 材料與方法 19 一、菌種及細胞株 19 二、質體與抗體 19 三、大腸桿菌轉型作用 (transformation) 19 四、質體DNA的萃取 19 五、細胞轉染 (transfection) 20 六、免疫沉澱分析 (immunoprecipitation, IP) 20 七、變性免疫沉澱分析 (Denature immunoprecipitation, denature IP) 20 八、免疫螢光染色 (immunefluorescence, IF) 21 九、溶酶體 (lysosome) 染色 21 十、西方墨點法分析 (western blot analysis) 21 結果 23 1. TRIM5α與Rta在細胞質結合 23 2. Rta與自噬作用的連接蛋白p62結合 23 (1) K63 linkage為Rta主要的泛素化鏈結形式 23 (2) Rta與p62結合 24 (3) Rta與TRIM5α和p62結合 24 (4) TRIM5α促進Rta與p62結合 24 3. Rta 會進入自噬作用降解路徑 25 (1) Rta 會進入溶酶體 25 (2) Rta與自噬體及自噬溶酶體結合 25 4. 誘導自噬作用導致 Rta 表現量降低 26 (1) 溶裂極早期誘導自噬作用導致 Rta 表現量降低 26 (2) 溶裂期中誘導自噬作用無法降低 Rta 表現量 27 討論 28 TRIM5α與Rta和p62兩者或三者間於細胞質作用 28 K63 linkage 為Rta泛素化修飾的主要方式 29 TRIM5α對於Rta和p62兩者間交互作用非常重要 30 TRIM5α促進Rta及溶酶體的結合 31 TRIM5α促進Rta進入自噬溶酶體 31 於溶裂期初始誘導自噬作用能有效降低Rta表現量 32 圖表 34 表1、本研究使用之質體 34 表2、本研究使用之抗體及胞器染劑 36 圖1、EBV的生活史 37 圖2、TRIM5α與Rta於293T 細胞及P3HR1細胞的位置 38 圖3、TRIM5α與Rta於293EBV(2089)細胞的位置 39 圖4、將泛素K48及K63分別突變後對Rta的泛素化影響 40 圖5、Rta與p62 在細胞內的結合 41 圖6、Rta與 p62 的免疫螢光分析 42 圖7、Rta、TRIM5α及p62在293T細胞中的免疫螢光分析 43 圖8、Rta、TRIM5α及p62在P3HR1細胞中的免疫螢光分析 44 圖9、Rta與內生p62在細胞內的結合 45 圖10、抑制 TRIM5α表現量檢視Rta與p62的位置 46 圖11、抑制抑制 TRIM5α表現量檢視Rta與lysosome的位置 47 圖12、 測試自噬作用進程的報導質體 48 圖13、檢視 GFP-C1-Redmonomer-LC3 與 Rta 在細胞內的結合 49 圖14、溶裂期初誘導自噬作用後內生Rta的表現量 50 圖15、溶裂期中誘導自噬作用後內生Rta的表現量 51 圖16、TRIM5α能直接或間接將Rta送入自噬作用降解 52 圖17、內生Rta與內生p62在細胞內的結合 53 參考文獻 54 附錄1、TRIM5α促進泛素化Rta的累積 72 附錄2、TRIM蛋白質家族的結構簡圖 73 附錄3、選擇性自噬作用 74 附錄4、mTOR於自噬作用中扮演的角色 75 附錄5、自噬作用進程的marker 75 附錄6、p62所參與的各種選擇性自噬作用 (selective autophagy) 76 附錄7、p62的功能區及生理功能 77 附錄8、TRIM5α在自噬作用中扮演的角色 78 | |
dc.language.iso | zh-TW | |
dc.title | TRIM5α 藉由細胞自噬作用調控 Epstein-Barr Virus 的
Rta蛋白質 | zh_TW |
dc.title | Regulation of Rta of Epstein-Barr Virus by TRIM5α via
Autophagy | en |
dc.type | Thesis | |
dc.date.schoolyear | 104-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 劉世東,張世宗,莊健盈 | |
dc.subject.keyword | Epstein-Barr Virus (EB病毒),Rta,TRIM5α,autophagy, | zh_TW |
dc.subject.keyword | EBV,Rta,TRIM5α,autophagy, | en |
dc.relation.page | 78 | |
dc.identifier.doi | 10.6342/NTU201600806 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2016-07-13 | |
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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