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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 | Ting-Yu Lin | en |
dc.contributor.author | 林庭羽 | zh_TW |
dc.date.accessioned | 2021-06-16T13:33:18Z | - |
dc.date.available | 2018-07-25 | |
dc.date.copyright | 2013-07-25 | |
dc.date.issued | 2013 | |
dc.date.submitted | 2013-07-19 | |
dc.identifier.citation | Abaitua F, O'Hare P (2008) Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein. J. Virol., 82, 5234-5244.
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/62198 | - |
dc.description.abstract | Epstein-Barr virus (EB病毒) 屬於人類疱疹病毒科,其生活史包含了潛伏期及溶裂期。EB病毒在溶裂期會依序表現極早期、早期及晚期基因,而藉由這些蛋白質的共同表現才能產生具有感染性的病毒顆粒。極早期蛋白質Rta與Zta為兩個病毒的轉錄因子,能促進複製蛋白質的表現、協助病毒基因體的複製及生成組裝病毒顆粒所需要的結構性蛋白質。先前研究指出Zta能結合在溶裂期複製起始點 (oriLyt) 上,並協助聚集複製蛋白質以組裝成完整的複製複合體。除了Zta之外,還需要其他六種複製蛋白質的共同參與才能順利開啟複製,而本研究主要以病毒的引子酶 (primase) BSLF1作為主要研究目標。首先,藉由共免疫沉澱分析及GST pull-down證明了Rta與BSLF1能直接結合,且BSLF1會與Rta蛋白質N端190個胺基酸片段及N190-415片段結合。接著,利用293T細胞進行免疫螢光染色分析,發現Rta會與BSLF1及BBLF2/3共同位在細胞核內,而Rta各別會與BSLF1或BBLF2/3主要分布在細胞質中。此外,觀察以TPA及sodium butyrate (SB/TPA) 誘導病毒進入溶裂期36小時的P3HR1細胞,發現Rta會與BSLF1及BBLF2/3呈點狀分布於細胞核內,顯示病毒在進行複製時Rta會位在複製複合體中。而在先前的研究中,預測了BSLF1可能具有去泛素化酵素的活性,本研究也利用體外去泛素化酵素活性分析證明BSLF1具有截切泛素的能力,而在細胞中過量表現BSLF1時能移除Rta上的泛素化修飾。此外,不論在P3HR1或293T細胞中過量表現BSLF1都能增加Rta在細胞中的含量,顯示BSLF1移除Rta上的泛素化修飾可能有助於增加Rta的穩定性。最後,本研究發現BSLF1會降低Rta活化BMRF1及BMLF1啟動子的能力,推測可能與調節病毒溶裂期基因的表現量相關。綜合以上結果,本研究發現BSLF1能夠移除Rta上的泛素化修飾並進而調節Rta的功能。此外,Rta也被發現會與BSLF1及BBLF2/3共同分布在細胞核內,顯示Rta可能參與在病毒的溶裂複製上。 | zh_TW |
dc.description.abstract | Epstein-Barr virus (EBV) is a human herpesvirus with two distinct life cycles, latent and lytic. During the lytic cycle, EBV expesses the immediate-early, early and late genes in order to produce infectious virus particles. Rta and Zta are two transcription factors expressed during the immediate-early stage, and both of them are required to trigger sequential events including expression of replication proteins, amplification of viral genome and synthesis of structural proteins. Previous study showed that Zta acts as an oriLyt-binding protein, facilitating the assembly of viral replication machinary.Besides Zta, there are other six proteins involved in lytic replication. In this study, we aim to explore the functions of BSLF1, which is a primase. GST pull-down and coimmunoprecipitation studies reveal that Rta interacts with BSLF1, and the interaction involves the N-terminal and the middle region in Rta. Moreover, indirect immunofluorescence analysis indicates that Rta, BSLF1 and BBLF2/3, a primase-associated protein, colocalize in the nucleus, while Rta and BSLF1 or BBLF2/3 colocalize mainly in the cytoplasm in 293T cells. Furthermore, Rta, BSLF1 and BBLF2/3 colocalize in the nucleus at 36 hr after lytic induction in P3HR1 cells, indicating that Rta may be involved in the replication complex. In addition, BSLF1 has been shown to function as a deubiquitinase (DUB). Overexpression of BSLF1 decreases the ubiquitination of Rta and increases the stability of Rta. BSLF1 also reduces the transactivation activity of Rta which may modulate the expression of lytic genes. Taken together, this study demonstrates that BSLF1 is capable of deubiquitinating Rta and modulating the functions of Rta. BSLF1 also interacts with BBLF2/3 and Rta, suggesting that Rta is involved in lytic replication. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T13:33:18Z (GMT). No. of bitstreams: 1 ntu-102-R00b22002-1.pdf: 3155797 bytes, checksum: 960af8b742ec1edd991e0e545a8f9429 (MD5) Previous issue date: 2013 | en |
dc.description.tableofcontents | 謝辭………………………………………………………………………………………i
摘要 ii Abstract iii 壹、前言 1 一、 EB病毒 (Epstein-Barr virus) 的發現 1 二、 EB病毒的結構 1 三、 EB病毒的致病性 2 四、 EB毒的生活史 2 潛伏期 (Latency) 2 溶裂期 (Lytic cycle) 3 五、 EB病毒的極早期蛋白質 4 轉錄因子Rta 4 轉錄因子Zta 6 六、 EB病毒的溶裂期複製 8 七、 EB病毒的BSLF1蛋白質 9 八、 泛素化修飾 (ubiquitination) 與去泛素化修飾 (deubiquitination) 10 泛素化修飾調控的生理功能 11 病毒對宿主泛素化系統的抗衡 11 疱疹病毒科病毒的去泛素化酵素 13 九、 研究目的 14 貳、材料與方法 15 一、 細胞株培養 (cell culture) 15 二、 質體與抗體 15 三、 質體DNA萃取 15 四、 大腸桿菌轉型作用 (transformation) 15 五、 細胞轉染 (cell transfection) 16 六、 蛋白質誘導表現 16 七、 Glutathione S-transferase (GST) pull-down assay 16 八、 免疫螢光染色分析 (Immunofluorescence analysis) 17 九、 免疫沉澱法 (Immunoprecipitation, IP) 17 十、 變性免疫沉澱法 (denature immunoprecipitation, denature IP) 17 十一、西方點墨法分析 (Western blot analysis) 18 十二、體外去泛素化酵素活性分析 18 十三、變性蛋白質純化法 (Ni-NTA denature protein purification) 19 十四、SDS-PAGE膠體蛋白質染色分析 19 十五、抗體製備 19 十六、冷光報導基因分析 (Luciferase reporter assay) 20 參、結果 21 一、 BSLF1重組蛋白質的表現與純化 21 二、 BSLF1與Rta的相互結合 22 三、 Rta與複製蛋白質的免疫螢光分析 23 四、 BSLF1對Rta泛素化修飾的影響 25 五、 BSLF1對Rta的轉錄活性及穩定性的影響 27 肆、討論 29 Rta參與在複製複合體內 29 BSLF1進核的可能原因 30 BSLF1調控Rta的泛素化修飾 31 BSLF1影響Rta的穩定性及轉錄活性 32 伍、圖表 34 表1、 本研究使用的質體 34 表2、 本研究使用的抗體 37 圖1、 EB病毒的生活史 39 圖2、 EB病毒的溶裂期複製 (lytic replication) 40 圖3、 His-BSLF1-C蛋白質的表現與純化 41 圖4、 以抗BSLF1抗體偵測BSLF1融合蛋白質的表現 42 圖5、 BSLF1與Rta在細胞內結合 43 圖6、 BSLF1與Rta結合區域的分析 44 圖7、 BSLF1與Rta在體外結合 45 圖8、 GFP-BSLF1與Rta在293T細胞中的免疫螢光分析 47 圖9、 GFP-BBLF2/3與Rta在293T細胞中的免疫螢光分析 48 圖10、 GFP-BSLF1、GFP-BBLF2/3與Rta在P3HR1細胞中的免疫螢光分析.49 圖11、Rta、Zta與Flag-BSLF1在293T細胞中的免疫螢光分析 51 圖12、Flag-BSLF1與HA-BBLF2/3在293T細胞中的免疫螢光分析 52 圖13、BSLF1的體外去泛素化活性分析 53 圖14、BSLF1會減少Rta的polyUb修飾 54 圖15、BSLF1會減少Rta的K63-linked polyUb修飾 55 圖16、BSLF1會減少Rta的monoUb修飾 56 圖17、過量表現GFP-BSLF1會穩定Rta在細胞中的含量 57 圖18、BSLF1會降低Rta的轉錄活性 58 圖19、BSLF1 的DUB活性區突變株對Rta泛素化修飾的影響 59 陸、參考文獻 60 柒、附錄 ……………………………………………………………………………...76 附錄1、 泛素化修飾與其生理意義 77 附錄2、 溶裂複製起始點 (oriLyt) 78 附錄3、 Rta在病毒溶裂複製中的角色 79 附錄4、 EB病毒的Rta、Zta、複製蛋白質與宿主蛋白質之間的交互作用 80 附錄5、 Rta、Zta與複製蛋白質之間的交互作用 81 | |
dc.language.iso | zh-TW | |
dc.title | EB病毒BSLF1蛋白質的功能性分析 | zh_TW |
dc.title | Functional Analysis of BSLF1 of Epstein-Barr Virus | en |
dc.type | Thesis | |
dc.date.schoolyear | 101-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 劉世東(Shih-Tung Liu),張沛鈞(Pey-Jium Chang),張世宗(Shih-Chung Chang),廖憶純(Yi-Chun Liao) | |
dc.subject.keyword | EB病毒,Rta,BSLF1,BBLF2/3,去泛素化修飾, | zh_TW |
dc.subject.keyword | Epstein-Barr virus,Rta,BSLF1,BBLF2/3,deubiquitinase (DUB), | en |
dc.relation.page | 81 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2013-07-19 | |
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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