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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/65370完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張麗冠 | |
| dc.contributor.author | Han-Ting Chen | en |
| dc.contributor.author | 陳菡亭 | zh_TW |
| dc.date.accessioned | 2021-06-16T23:39:04Z | - |
| dc.date.available | 2017-08-01 | |
| dc.date.copyright | 2012-08-01 | |
| dc.date.issued | 2012 | |
| dc.date.submitted | 2012-07-26 | |
| dc.identifier.citation | Adamson, A. L., and S. Kenney. 2001. Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J Virol 75 (5):2388-2399.
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/65370 | - |
| dc.description.abstract | Epstein-Barr virus是人類第四型皰疹病毒，病毒外殼由162個次蛋白衣 (capsomer)組合而成正二十面體 (icosahedron)。EB病毒外殼由主要外鞘蛋白質VCA (major capsid protein)與次要外鞘蛋白質BDLF1和BORF1 (minor capsid protein)組成，兩分子的BDLF1與一分子的BORF1組成三聚體 (triplex)，連結VCA 形成的五聚體或六聚體以組成次蛋白衣，並由具有NLS的BORF1分別將BDLF1或VCA帶入核內進行病毒顆粒的組裝。在病毒成熟的過程中，外鞘蛋白質的組裝是非常重要的一環，卻是溶裂循環中最少被研究的部分。SUMO (small ubiquitin-like modifier) 以共價鍵結方式連接在目標蛋白質上是一種轉譯後修飾，參與許多蛋白質的功能調控，包括蛋白質在細胞中分佈的位置、轉錄活性、穩定度及與其他蛋白質的交互作用等。本研究首先發現，BDLF1與BORF1皆受到SUMO蛋白質共價鍵修飾，接著利用GST pull-down證明BDLF1利用其N端的SUMO-interaction motifs (SIMs)與SUMO蛋白質結合；以BDLF1的SIM突變株進行功能性分析後發現，SIM會增加BDLF1受SUMO蛋白質的修飾、降低受泛素化的程度，同時增進BDLF1的蛋白質穩定性；最後利用螢光顯微鏡分析則發現，當BDLF1的SIM突變會改變BDLF1與BORF1的分佈，所以BDLF1的SIM可能在EB病毒顆粒的組裝上扮演重要的角色。 | zh_TW |
| dc.description.abstract | Epstein-Barr virus (EBV), also called human herpesvirus 4 (HHV-4), contains a common icosahedral structure with 162 capsomers. The capsids of EBV contain major capsid protein VCA and minor capsid proteins, BDLF1 and BORF1. The capsomers are composed of VCA pentamers or hexamers, which are linked together by triplexes that are formed by two copies of BDLF1 and one copy of BORF1. During the capsid assembly, BORF1, which exhibits nuclear localization signal sequence (NLS) brings VCA and BDLF1 into the nuclei. Assembly of capsid is required for the development of mature EBV virion but it is nevertheless the must unknown part of EBV lytic cycle. Targets covently attached by small ubiquitin-like modifier (SUMO) proteins is a kind of post-translational modification which involves in diverse functions of proteins including cellular localization, stability, transcriptional activity and protein-protein interaction. This study demonstrates that minor capsid proteins BDLF1 and BORF1 are both SUMOylated. A GST pulldown study identifies BDLF1 interacts noncolvently with SUMO through SUMO-interaction motifs (SIM) in the N-terminal region of BDLF1. Functional analysis of BDLF1 SIM mutants revealed that SIM integrity is required for increasing the SUMOylation level, decreasing the ubiquitination level as well as maintaining the stability of BDLF1. Futhermore, immunofluorescence analysis shows that BDLF1 SIM mutants exhibit different pattern with the colocalization of wt-BDLF1 and BORF1. These results indicate the SIM motifs in BDLF1 are likely to have a key function in the EBV capsid assembly. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-16T23:39:04Z (GMT). No. of bitstreams: 1 ntu-101-R99b22046-1.pdf: 3757444 bytes, checksum: 02ef87cf05dc9ed4251b62496eeca768 (MD5) Previous issue date: 2012 | en |
| dc.description.tableofcontents | 中文摘要 II
Abstract III 常用縮寫表 IV 目錄 V 前言 1 一、 EB病毒 (Epstein-Barr virus, EBV) 1 二、 EB病毒的生活史 1 三、 EB病毒的基因體 2 四、 第一型簡單皰疹病毒 (herpes simplex virus type 1, HSV-1)的外鞘殼體 3 五、 EB病毒的外鞘殼體 4 六、 類泛素 (small ubiquitin-like modifier, SUMO) 5 七、 SUMO-interacting motif (SIM) 6 八、 DNA病毒與SUMO修飾系統之間的關係 9 (一) 腺病毒科 9 (二) 皰疹病毒科 10 (三) 乳突病毒科 12 (四) 痘病毒科 13 研究目的 14 材料與方法 15 一、 大腸桿菌的轉型作用與質體 (transformation and plasmid) 15 二、 細胞株的培養 (cell culture) 15 三、 細胞轉染 (transfection) 15 四、 蛋白質的誘導表現 16 五、 西方點墨分析 (western blot analysis) 16 六、 Glutathione S-transferase (GST) pull down assay 16 七、 免疫沉澱分析 (Immunoprecipitation) 16 八、 免疫螢光染色 (Immumofluorescence) 17 九、 變性免疫沉澱法 (Denature-IP) 17 十、 即時定量聚合酶連鎖反應 (Quantitative real-time polymerase chain reaction, Q PCR) 17 結果 19 一、 EB病毒次要外鞘蛋白BDLF1會受SUMO的共價鍵修飾 19 二、 EB病毒次要外鞘蛋白BORF1受SUMO的共價鍵修飾 19 三、 SUMO會增強BDLF1與BORF1的結合 20 四、 BDLF1具有SUMO-interaction motifs (SIM) 20 五、 SIM會增加BDLF1受SUMO蛋白質的修飾 21 六、 SIM會影響BDLF1的穩定性 21 七、 SIM會影響BDLF1與 BORF1分佈的位置 22 討論 23 圖表 29 表一、本研究所用到的質體。 29 表二、本研究使用之抗體。 31 圖一、BDLF1會受SUMO的共價鍵修飾。 32 圖二、BDLF1及BORF1在生物體內皆會受SUMO的共價鍵修飾。 33 圖三、SUMO會增強BDLF1與BORF1的結合。 34 圖四、BDLF1具有SIMs。 35 圖五、SIM會增加BDLF1受SUMO蛋白質的修飾。 36 圖六、SIM會影響BDLF1的穩定性。 37 圖七、SIM會影響BDLF1與 BORF1分佈的位置。 39 附錄 40 附錄一、EB病毒感染人類的途徑。 40 附錄二、EB病毒的生活史。 41 附錄三、HSV-1病毒顆粒的組裝過程。 42 附錄四、EB病毒的結構及外鞘蛋白質。 43 附錄五、泛素化與SUMO蛋白質的共價修飾過程。 44 附錄六、SIM序列與SUMO蛋白質交互作用。 45 附錄七、SIM-SUMO的結合影響蛋白質功能。 46 附錄八、mSIM1與mSIM2仍然可以與BORF1結合。 47 附錄九、SUMOylation影響蛋白質功能的基本機制。 47 附錄十、SIM可能會影響BDLF1形成同型二聚體的能力。 48 附錄十一、SIM突變會降低病毒顆粒生成的數目。 49 參考文獻 50 | |
| dc.language.iso | zh-TW | |
| dc.title | Small Ubiquitin-like Modifier蛋白質對Epstein-Barr病毒外鞘蛋白質BDLF1的調控 | zh_TW |
| dc.title | Regulation of Epstein-Barr Virus Capsid Protein BDLF1 by Small Ubiquitin-like Modifier Proteins | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 100-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 劉世東,張沛鈞,張世宗 | |
| dc.subject.keyword | 人類第四型皰疹病毒,小類泛素,外鞘蛋白質, | zh_TW |
| dc.subject.keyword | Epstein-Barr virus,SUMO,BDLF1, | en |
| dc.relation.page | 64 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2012-07-26 | |
| 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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