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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 | Shih-Wei Hsu | en |
dc.contributor.author | 徐詩媁 | zh_TW |
dc.date.accessioned | 2021-06-16T13:25:40Z | - |
dc.date.available | 2018-08-08 | |
dc.date.copyright | 2013-08-08 | |
dc.date.issued | 2013 | |
dc.date.submitted | 2013-07-23 | |
dc.identifier.citation | Allday MJ, Crawford DH, Griffin BE (1989) Epstein-Barr virus latent gene expression during the initiation of B cell immortalization. J Gen Virol 70: 1755-1764
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/62061 | - |
dc.description.abstract | Epstein-Barr Virus (EB病毒) 屬於人類皰疹病毒,其生活史包括潛伏期 (Latent life cycle) 與溶裂期 (Lytic cycle)。在病毒進入溶裂期時,病毒會大量複製其遺傳物質與蛋白質,組裝成完整的病毒顆粒以感染其他細胞。在病毒成熟的過程中,外鞘蛋白質 (Capsid protein) 的產生及組裝是非常重要的一環,卻是溶裂期中最少被研究的部份。皰疹病毒科的外鞘殼體為正二十面體,在EB病毒中,病毒外殼由主要外鞘蛋白質VCA (major capsid protein) 與次要外鞘蛋白質BORF1和BDLF1 (minor capsid protein) 組成。Tripartite-motif 5 alpha (TRIM5α) 是反轉錄病毒的限制因子 (restriction factor),為具有泛素E3連接酶 (ubiquitin E3 ligase) 活性的細胞蛋白質,先前研究發現TRIM5α會與反轉錄病毒之外鞘蛋白質結合,使其提早解體而影響病毒的感染。本研究首先發現人類的TRIM5α能透過C端的B30.2功能區與EB病毒的外鞘蛋白質BORF1及VCA直接結合,另外TRIM5α在細胞外及細胞內皆會促進BORF1的泛素化修飾,而TRIM5α的SUMO-interacting motifs (SIMs) 對於增進BORF1的泛素化修飾扮演重要之角色。此外,若在細胞中過量表現TRIM5α會導致BORF1的濃度降低,而利用shRNA將細胞內的TRIM5α抑制後發現,BORF1蛋白質的表現量則會增加。最後利用P3HR1細胞收集EB病毒顆粒,發現將TRIM5α抑制後EB病毒產生的量會大幅的增加。綜合以上結果,本研究發現TRIM5α會藉由影響EB病毒的外鞘蛋白質,進而抑制EB病毒溶裂期的發展。 | zh_TW |
dc.description.abstract | Epstein-Barr virus (EBV) is a human herpesvirus that contains two distinct life cycles, latency and lytic cycle. During the lytic cycle, EBV encodes a series of proteins that are necessary for viral lytic DNA replication, capsid assembly and viral maturation to produce infectious viral particles. The production and assembly of capsid proteins are important to the maturation of EBV virion, but the mechanism is unclear. The capsids of herpesviruses have a common icosahedral structure. In EBV, the capsid contains a major capsid protein, VCA and two minor capsid proteins, BORF1 and BDLF1. Tripartite-motif 5 alpha (TRIM5α) that possesses the ubiquitin E3 ligase activity is a restriction factor of retroviruses. Previous study showed that TRIM5α binds the retroviral capsids and disrupts viral structure to accelerate uncoating of capsids, which influences the replication of retroviruses. This study demonstrates that TRIM5α binds to EBV capsid proteins, BORF1 and VCA, through the C-terminal B30.2 domain. Moreover, TRIM5α promotes the ubiquitination of BORF1 in vitro and in vivo and the SUMO-interaction motifs in TRIM5α are important to the ubiquitination of BORF1. Furthermore, over-expressing of TRIM5α reduces the amount of BORF1, while knocking down of TRIM5α enhances the level of BORF1. Finally, inhibition the expression of TRIM5α enhances EBV lytic progression and promotes virion production. Taken together, this study demonstrates that TRIM5α targets to EBV capsid proteins to inhibit the lytic progression. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T13:25:40Z (GMT). No. of bitstreams: 1 ntu-102-R00b22006-1.pdf: 28705426 bytes, checksum: 4d7ed3e498afcc5dfbe76af598ef9e26 (MD5) Previous issue date: 2013 | en |
dc.description.tableofcontents | 目錄
誌謝 i 中文摘要 ii Abstract iii 目錄 v 圖目錄 viii 表目錄 ix 前言 1 一、Epstein-Barr virus (EB病毒) 的發現與其相關疾病...........1 二、EB病毒的遺傳物質與結構特性..............1 三、EB病毒的生活史.................2 四、皰疹病毒 (herpesviruses) 的外鞘殼體............4 五、泛素與泛素化修飾 (ubiquitin and ubiquitination).......7 六、類泛素 (small ubiquitin-like modifier, SUMO)........9 七、TRIM5α蛋白質..................11 研究目的...............18 材料與方法............19 一、細胞株..................19 二、EB病毒的溶裂期誘導..................19 三、細菌...............19 四、質體與抗體...............20 五、質體DNA的萃取..................20 六、RNA的萃取及含量分析................20 七、細胞轉染 (Transfection) .................21 八、蛋白質的誘導表現...............21 九、Glutathione S-transferase (GST) pull-down assay....21 十、免疫沉澱分析 (Immunoprecipitation) ...........22 十一、變性免疫沉澱分析 (Denature immunoprecipitation, denature IP).....22 十二、試管內泛素化修飾分析 (In vitro ubiquitination assay) .............23 十三、西方點墨法分析 (Western blot analysis).............24 十四、免疫螢光染色分析 (Immunofluorescence analysis) .........24 十五、建立TRIM5α knock down細胞株............25 十六、病毒顆粒的定量分析 (Real-time quantitative PCR of EB virion) ........26 十七、EB病毒殼體破壞實驗 (Capsid destruction of EBV).............26 結果..........…28 一、TRIM5α在EB病毒溶裂期的表現..................28 二、TRIM5α與BORF1、BDLF1和VCA在細胞體內的結合.............28 三、TRIM5α與BORF1和VCA在細胞體外直接結合.................30 四、TRIM5α以C端的B30.2 domain與BORF1和VCA結合............31 五、TRIM5α與BORF1及VCA在細胞內的分佈位置............33 六、TRIM5α促進BORF1的泛素化修飾.................34 七、TRIM5α對BORF1穩定性的影響.................36 八、TRIM5α的SIM突變時無法增加BORF1的泛素化修飾.............37 九、BORF1與TRIM5αSUMO區域突變株的結合關係............39 十、BORF1的SUMO修飾與泛素化修飾之關係............40 十一、TRIM5α會增進EB病毒殼體的泛素化修飾並造成病毒殼體的瓦解............42 十二、TRIM5α對EB病毒溶裂期的影響............43 討論............45 圖表............54 附錄............88 附錄1、皰疹病毒的外鞘殼體結構............88 附錄2、HSV-1外鞘殼體組裝的過程............89 附錄3、HSV-1不同形式的外鞘殼體............90 附錄4、泛素連結系統............91 附錄5、泛素化的鏈結形式與功能............92 附錄6、SUMO修飾的過程............94 參考文獻............95 | |
dc.language.iso | zh-TW | |
dc.title | TRIM5α對EB病毒溶裂發展的影響 | zh_TW |
dc.title | Role of TRIM5α in the lytic progression of Epstein-Barr virus | en |
dc.type | Thesis | |
dc.date.schoolyear | 101-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 劉世東,張沛鈞,張世宗,廖憶純 | |
dc.subject.keyword | Epstein-Barr Virus (EB病毒),外鞘蛋白質,BORF1,VCA,TRIM5α,泛素化, | zh_TW |
dc.subject.keyword | Epstein-Barr Virus (EBV),capsid proteins,BORF1,VCA,TRIM5α,ubiquitination, | en |
dc.relation.page | 117 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2013-07-23 | |
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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