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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 黃慶璨 | |
dc.contributor.author | Yu-Ling Chen | en |
dc.contributor.author | 陳昱伶 | zh_TW |
dc.date.accessioned | 2021-05-19T17:42:18Z | - |
dc.date.available | 2021-08-29 | |
dc.date.available | 2021-05-19T17:42:18Z | - |
dc.date.copyright | 2019-02-15 | |
dc.date.issued | 2019 | |
dc.date.submitted | 2019-02-14 | |
dc.identifier.citation | 1. Bayer ME, Blumberg BS, Werner B: Particles associated with Australia antigen in the sera of patients with leukaemia, Down's Syndrome and hepatitis. Nature 1968, 218:1057-1059.
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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/7368 | - |
dc.description.abstract | 諾羅病毒為全球流行之非細菌性腸胃道致病菌。由於缺乏細胞株生產減毒或去活的諾羅病毒疫苗,諾羅病毒疫苗主要以類病毒顆粒為基礎發展。諾羅病毒衣殼蛋白質VP1之突出區(P (protruding) domain),會構成由12個雙體化P蛋白質所組成之P粒子(P particle),其抗原形態與病毒衣殼蛋白質VP1相同。因突出區具有三個多出來的環狀結構,能嵌入外來抗原,先前已做為外來抗原呈現平台。本研究欲使用分離自台灣本土株,GII.4型諾羅病毒之突出區作為P蛋白質多抗原呈現平台之基礎。首先在表現部分,利用不具有內毒素疑慮、培養成本低廉且易於放大培養之畢赤氏酵母菌Pichia pastoris,經醱酵槽培養,胞內P蛋白質產量可達220 mg/L。其次,在純化策略方面,利用P蛋白質本身的電性及原態具有的組胺酸,本研究發展出二套無標籤純化策略:(1)利用宿主蛋白質與P蛋白質對管柱的吸附落差,P蛋白質可經由離子交換管柱及疏水性管柱純化得到,但最終回收後產量僅有2.5%。為進一步提升產量,(2)利用親和層析管柱(His-Trap)能與原態暴露在外之組胺酸吸附的特性,P蛋白質可利用親和層析管柱及離子交換管柱純化,回收率為28.1%,純度可達82.1%。此外,藉由VP1蛋白質原態所具有的組胺酸,及VP1能組成顆粒之特性,原態之VP1顆粒亦能藉由親和層析管柱及膠體層析管柱純化,回收率為20%,純度可超過90%。純化出之VP1蛋白質經粒徑分析儀及穿透式電子顯微鏡檢測,VP1能成功組成具有生物功能之粒子,能與成人唾液之HBGA (human histo-blood group antigen)結合。與帶有組胺酸標籤(His-tag)之P蛋白質(P-His)相似,純化出之原態P蛋白質,經粒徑分析儀測定及穿透式電子顯微鏡觀測,二種P粒子皆呈現小型P粒子(small P particle)之三角形及四角形形態,顯示以酵母菌表現之台灣流行株GII.4型諾羅病毒P蛋白質,能構成由6個雙體化P蛋白質組成之小型P粒子。前人文獻指出,小型P粒子僅出現在C端突變之P蛋白質。而本研究之P蛋白質未經末端修飾即呈現小型P粒子,經與其它GII.4菌株序列比對,發現其中四個胺基酸對P粒子的形成可能扮演關鍵角色。當以綠色螢光蛋白質模擬外來抗原,呈現於P蛋白質的表面頂端,結果發現嵌合型P蛋白質不但能成功組成嵌合小型P粒子,亦能發出綠色螢光,顯示台灣分離株諾羅病毒P蛋白質能做為外來抗原呈現平台。本研究為首篇提供諾羅病毒P蛋白質酵母菌大量生產、無標籤簡易純化及確立小型P粒子亦能作為外來抗原呈現平台之研究。 | zh_TW |
dc.description.abstract | Norovirus (NoV) is one of the leading causes of acute nonbacterial gastroenteritis outbreaks worldwide. Due to the lack of a reliable and efficient cell culture system for producing inactivated or attenuated whole NoV vaccines, the development of NoV vaccines relies largely on virus-like particles (VLPs) formed by the major capsid protein VP1 or subviral particles formed by the exterior protrusion (P) domain of VP1. The P particle is composed of 12 P dimers and revealed the same antigenic types as VLP. Additionally, due to the presence of three outermost surface loops in the P domain, the P particle could serve as a platform for carrying foreign antigens. The goal of this study is to provide the fundamental understanding of different constructs of P particles formed by the P domain of NoV strain GII.4 isolated from Taiwan to establish the multiple antigen presentation platform. The P domain was expressed in Pichia pastoris, a well-known expression system with several advantages including high cell density fermentation at low cost and non-risk of endotoxin. The production of NoV P protein reached 220 mg/L as a soluble form in fermentation cultures. The overexpression P protein provided the cornerstone for the development of tag-free P protein purification schemes. For purification of tag-free P protein, based on the charge and the surface histidine in native NoV, two purification schemes were developed: (1) The host cell proteins and the target P protein were separated by the difference of the binding strength to the chromatography column. Using anion-exchange and hydrophobic interaction chromatography purification schemes, NoV P protein with high purity was obtained. However, the P protein recovery was 2.5%. (2) Using the HisTrap affinity column and anion-exchange column, the native NoV P protein was purified, and recovery and purity were 28.1% and 82.1%, respectively. Besides, the NoV major capsid protein VP1 was also purified using the HisTrap affinity column and gel filtration column. The purity of NoV VP1 protein was over 90% and the recovery was 20%. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) analysis of the purified NoV VP1 revealed that VP1 proteins were self-assembled into particles, and these particles remained HBGA binding ability as evidenced by saliva binding assay. Similar to P-His protein, the P protein also formed biologically functional small P particle composed by six of P dimer. The purified P-His and P protein, analyzed by TEM and DLS, were also revealed triangle-, square- and ring-shaped. Previous studies showed that the small P particles were only found with C-terminus modification. Without terminal modification, small P particles were formed in this study. The amino acid sequence analysis showed only four different amino acids between the P domain in this study and other investigated GII.4 strains, suggesting that these amino acids might play an important role in P particle formation. To extend the application of the small P particle, the green fluorescent protein was used to mimic the foreign antigen and inserted into NoV P loop2 distal end. From gel filtration and fluorescent microscopy, the chimera small P proteins were self-assembly into chimera small P particles and showed green fluorescence. It was indicated that these Taiwan native small P particle can be an antigen presentation platform. This study was the first report of NoV P protein covering overexpression in P. pastoris, easy handling tag-free purification schemes, and formation of small P particles without terminal modification as foreign antigen displaying platform. | en |
dc.description.provenance | Made available in DSpace on 2021-05-19T17:42:18Z (GMT). No. of bitstreams: 1 ntu-108-D01b22006-1.pdf: 7383874 bytes, checksum: c462f61c6e60691c4e9f0500a41f3091 (MD5) Previous issue date: 2019 | en |
dc.description.tableofcontents | 摘要 I
Abstract III 目錄 V 圖目錄 VIII 表目錄 X 第一章 前言 1 1.類病毒顆粒疫苗 1 1.1類病毒顆粒疫苗的發展優勢 1 1.2類病毒顆粒的結構分類 1 2.諾羅病毒介紹 2 2.1諾羅病毒之流行病學 2 2.2諾羅病毒的研究挑戰及替代的研究方案 3 2.3諾羅病毒分子生物學特性及分類 5 2.4諾羅病毒之細胞趨性 6 2.4.1 HBGA之生合成路徑 6 2.4.2人類諾羅病毒與不同HBGAs之結合特異性 7 3.諾羅病毒類病毒顆粒 (VP1) 10 3.1諾羅病毒VP1結構 10 3.2諾羅病毒類病毒顆粒之生產與純化 10 3.3諾羅病毒疫苗 11 4.諾羅病毒P 11 4.1 P粒子 (P particle) 12 4.2小型P粒子(Small P particle) 13 4.3諾羅病毒P粒子做為多抗原呈現平台 13 4.3.1多抗原呈現平台 13 4.3.2 P粒子攜帶外來抗原的策略 14 4.3.3 P 粒子成為疫苗的利基及攜帶外來抗原的例子 14 4.4 P蛋白質之生產與純化 15 5.嗜甲醇酵母菌(Methylotrophic yeast) 18 5.1甲醇代謝調控路徑(MUT pathway) 18 5.2 Pichia pastoris 表現系統 19 5.2.1菌株與甲醇表現型 20 6.研究動機及具體目標 21 6.1研究動機 21 6.2研究目標 22 第二章 材料與方法 24 1.培養機與藥品 24 2 菌株與培養條件 25 2.1細菌 25 2.2真菌 25 2.3菌種保存 26 3.質體建構 26 4. P. pastoris轉形 30 4.1 P. pastoris勝任細胞製備 30 4.2轉形DNA置備 30 4.3電穿孔轉形 30 5. P. pastoris 轉形株篩選與培養 31 5.1抗藥性濃度梯度篩選 31 5.2搖瓶培養 31 5.3醱酵槽培養 31 6.轉形株螢光顯微鏡觀察 32 7.異源蛋白質產物純化 32 7.1蛋白質萃取 32 7.2親和層析純化 33 7.3離子交換純化 33 7.4疏水性層析純化 34 7.5膠體過濾法 34 8.異源蛋白質分析 37 8.1西方墨點法 37 8.2 LC-MS/MS 38 8.3 Indirect ELISA 38 8.4唾液結合測試 (Saliva-binding assay) 39 8.5穿透式電子顯微鏡 40 8.6粒徑分析 40 第三章、結果 43 一、序列分析與結構模擬 43 1.胺基酸序列分析 43 2.結構模擬 43 3.不同菌株之序列比對 43 二、組胺酸標籤(6xHis)之P蛋白質生產、純化及顆粒分析 50 1. P. pastoris生產 50 2.以組胺酸標籤(6xHis)純化 50 3.物性分析 50 4.功能性分析 51 三、原態P蛋白質之生產、純化及顆粒分析 55 1. P. pastoris生產 55 1.1.高表現量P轉形株篩選 55 1.2搖瓶培養 55 1.3醱酵槽培養 55 2.開發無標籤純化策略 61 2.1策略一:利用雜蛋白質與目標蛋白質對管柱之吸附落差純化 61 2.2策略二:利用原態之組氨酸純化 66 3.物性分析 73 4.功能性分析 73 四、嵌有綠色螢光之原態P蛋白質生產及物性功能性分析 79 1. P. pastoris生產 79 2.物性與功能性分析 79 五、組胺酸標籤(6xHis) VP1蛋白質之生產與純化 83 1. P. pastoris生產 83 2.以組胺酸標籤(6xHis)純化 83 六、原態VP1蛋白質之生產、純化及顆粒分析 85 1. P. pastoris生產 85 2.利用原態之組氨酸純化 85 3.物性分析 86 4.功能性分析 86 第四章、討論 92 1. P蛋白質產量之比較 92 2.無純化標籤之純化策略探討 92 2.1 P蛋白質之純化策略討論 92 2.1.1策略一:利用蛋白質之吸附落差純化 93 2.1.2策略二:利用原態之組氨酸純化 93 2.2. VP1蛋白質之純化策略討論 94 3.類病毒顆粒之顆粒性與生物功能性探討 95 3.1. P蛋白質之顆粒性探討 95 3.2. VP1蛋白質之顆粒性探討 95 3.3. VP1、P與P-6xHis與HBGA之結合差異討論 97 3.4.組胺酸(6xHis)對P蛋白質之影響 98 4. P蛋白質之延伸應用性 99 第五章、總結 101 第六章、未來工作與展望 102 第七章、參考文獻 105 附錄 117 | |
dc.language.iso | zh-TW | |
dc.title | 利用畢赤氏酵母菌醱酵生產台灣GII.4 2006b型諾羅病毒類病毒顆粒及小型P粒子之純化與性質研究 | zh_TW |
dc.title | Expression, purification and characterization of Taiwan-native norovirus GII.4 2006b virus-like particle and small P particle in Pichia pastoris | en |
dc.type | Thesis | |
dc.date.schoolyear | 107-1 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 張世宗,楊啟伸,許瑞祥,張沛鈞 | |
dc.subject.keyword | 諾羅病毒,類病毒顆粒,小型P粒子,嵌合型P粒子,畢赤氏酵母菌,醱酵培養,無標籤純化, | zh_TW |
dc.subject.keyword | Norovirus,Virus-like particle,small P particle,chimera P particle,Pichia pastoris,fermentation cultures,tag-free purification, | en |
dc.relation.page | 133 | |
dc.identifier.doi | 10.6342/NTU201900497 | |
dc.rights.note | 同意授權(全球公開) | |
dc.date.accepted | 2019-02-14 | |
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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