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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 鄭益謙(Ivan-Chen Cheng) | |
dc.contributor.author | Chieh-Li Liu | en |
dc.contributor.author | 劉玠澧 | zh_TW |
dc.date.accessioned | 2021-06-17T08:19:42Z | - |
dc.date.available | 2024-08-27 | |
dc.date.copyright | 2019-08-27 | |
dc.date.issued | 2019 | |
dc.date.submitted | 2019-08-13 | |
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Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/1702246 Veerapen, V. P., van Zyl, A. R., Wigdorovitz, A., Rybicki, E. P., & Meyers, A. E. (2018). Novel expression of immunogenic foot-and-mouth disease virus-like particles in Nicotiana benthamiana. Virus Res, 244, 213-217. doi:10.1016/j.virusres.2017.11.027 Vidal, M., Cairo, J., Mateu, M. G., & Villaverde, A. (1991). Molecular cloning and expression of the VP1 gene of foot-and-mouth disease virus C1 in E. coli: effect on bacterial cell viability. Appl Microbiol Biotechnol, 35(6), 788-792. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/1369359 Wang, C., Castro, A. F., Wilkes, D. M., & Altenberg, G. A. (1999). Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: comparison of fusions to glutathione S-transferase, thioredoxin and maltose-binding protein. Biochem J, 338 ( Pt 1), 77-81. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/9931301 Wang, J. H., Liang, C. M., Peng, J. M., Shieh, J. J., Jong, M. H., Lin, Y. L., . . . Liang, S. M. (2003). Induction of immunity in swine by purified recombinant VP1 of foot-and-mouth disease virus. Vaccine, 21(25-26), 3721-3729. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/12922103 Xiao, Y., Chen, H. Y., Wang, Y., Yin, B., Lv, C., Mo, X., . . . Tian, K. (2016). Large-scale production of foot-and-mouth disease virus (serotype Asia1) VLP vaccine in Escherichia coli and protection potency evaluation in cattle. BMC Biotechnol, 16(1), 56. doi:10.1186/s12896-016-0285-6 Xie, Q. C., McCahon, D., Crowther, J. R., Belsham, G. J., & McCullough, K. C. (1987). Neutralization of foot-and-mouth disease virus can be mediated through any of at least three separate antigenic sites. J Gen Virol, 68 ( Pt 6), 1637-1647. doi:10.1099/0022-1317-68-6-1637 Yang, M., Xu, W., Goolia, M., & Zhang, Z. (2014). Characterization of monoclonal antibodies against foot-and-mouth disease virus serotype O and application in identification of antigenic variation in relation to vaccine strain selection. Virol J, 11, 136. doi:10.1186/1743-422X-11-136 Yang, P. C., Chu, R. M., Chung, W. B., & Sung, H. T. (1999). Epidemiological characteristics and financial costs of the 1997 foot-and-mouth disease epidemic in Taiwan. Vet Rec, 145(25), 731-734. Retrieved from https://www.ncbi.nlm.nih.gov/pubmed/10972111 Zhang, W., Yang, F., Zhu, Z., Yang, Y., Wang, Z., Cao, W., . . . Zheng, H. (2019). Cellular DNAJA3, a Novel VP1-Interacting Protein, Inhibits Foot-and-Mouth Disease Virus Replication by Inducing Lysosomal Degradation of VP1 and Attenuating Its Antagonistic Role in the Beta Interferon Signaling Pathway. J Virol, 93(13). doi:10.1128/JVI.00588-19 | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/74094 | - |
dc.description.abstract | 口蹄疫病毒(Foot-and-mouth disease virus, FMDV)為無封套病毒,以正二十面體的外殼蛋白包覆一條正向單股RNA作為遺傳物質。由於其廣泛的宿主種別和具有高度的傳染性,使口蹄疫的防檢疫倍受各國政府重視並制定諸多措施防範。台灣曾於1997年爆發嚴重的口蹄疫情,僅該年度就造成約3.78億美元的損失。時至今日台灣仍未正式恢復口蹄疫非疫區的地位,加上鄰國潛在的傳播威脅,擁有一套可供快速、大量處理血清抗體的診斷平台對於防檢疫無疑都具極大助益。本研究利用knock-out mutagenesis技術與類病毒空殼蛋白(VLPs)從實驗室既有的FMDV融合瘤中篩檢能夠識別O型口蹄疫病毒中和抗體決定位的單源抗體(MAb),考量不須操作活病毒與能兼顧抗原真實性的前提,最終使用哺乳動物細胞表現VLPs作為抗原,結合過去所篩選出的抗Site 1與Site 2 MAb,建構blocking ELSIA,復以此系統對經家畜衛生試驗所測定中和抗體力價(Serum neutralizing titer, SN titer)的97隻豬血清進行測試,結果顯示此系統與SN titer展現極高的關聯性,以抗Site 1 MAb作為tracer其相關性達到R2=0.67,在抗Site 2 MAb則為R2=0.63。根據上述結果,擬進一步拓展其應用性,結合以E.coli所生產SUMO fusion蛋白的VLPs作為抗原,藉以提升產量及降低成本,並透過大量血清樣品的測試,及生物統計分析對發揮更優化的效果,期許有朝一日能將此blocking ELISA實際應用於口蹄疫防檢疫的血清檢測。 | zh_TW |
dc.description.abstract | Foot-and-mouth disease virus (FMDV) is a non-enveloped virus with an icosahedral capsid containing a positive-sense single-strand RNA. Due to its wide host range and highly contagious activity, FMD is one of the most important diseases in animal husbandry industry in the world. In 1997, a devastating outbreak of FMD in Taiwan caused losses of about US$ 378 million. Until now, FMD has not been fully eradicated in Taiwan. Hence, the establishment of a fast and stable platform for massive serologic test as a tool of prevention and control measure is undoubtedly necessary. Recently, site 1 and site 2 have been regarded as the most immune-dominant neutralization sites. In order to use monoclonal antibodies (MAbs) specifically against the well-known neutralization sites from a previously produced MAbs panel, we established a screening system based on mutated Virus-like-particles (VLPs), which alleviates biosecurity concerns that viruses pose. Due to authentic antigenicity, the mammalian cell expression system, HTK, was chosen as the antigen for the MAb-based antibody blocking ELISA (bELISA). Preliminary results showed that the PI value of the bELISA tested on 97 swine serums exhibited high correlation to SN titer, with R2 values of 0.67 and 0.63 in site 1 and site 2, respectively. Considering cost and application, we intend to express our VLPs with SUMO fusion protein in E.coli, the more productive expression system. With further optimization, we believe that this bELISA platform we have established could not only be used for FMD researching, but also as a practical serological tool for FMD monitoring and prevention. | en |
dc.description.provenance | Made available in DSpace on 2021-06-17T08:19:42Z (GMT). No. of bitstreams: 1 ntu-108-R05629010-1.pdf: 6213765 bytes, checksum: 134e8ccb97bc06afd787617a95eeb713 (MD5) Previous issue date: 2019 | en |
dc.description.tableofcontents | 目 錄
口試委員會審定書 i 中文摘要 ii 英文摘要 iii 第一章 序言 1 第二章 文獻回顧 4 第一節 台灣口蹄疫發展歷史 4 第二節 口蹄疫病毒介紹 5 2-2.1 病毒結構蛋白 6 2-2.2 中和抗原決定位(Neutralizing sties) 7 第三節 FMD臨床症狀、傳播方式即診斷方法 8 2-3.1 臨床症狀 8 2-3.2 傳播方式 8 2-3.3 診斷方法 9 2.3.3.1 病毒分離(Virus isolation) 9 2-3.3.2 血清中和試驗(Serum neutralization test, SN test) 9 2-3.3.3 酵素連結免疫吸附試驗(Enzyme-Link Immunosorbent Assay,ELISA) 9 2-3.3.4 反轉錄定量聚合酶連鎖反應(Reverse Transcription -Polymerase Chain Reaction, RT-PCR) 10 第四節 類病毒空殼蛋白及突變策略 11 第五節 重組蛋白表現系統 12 2-5.1 真核細胞表現系統 12 2-5.2 原核細胞表現系統 13 第三章 材料與方法 15 第一節 質體建構 15 3-1.1 pcDNA-His-VP0、pcDNA-His-VP3、pcDNA-His-VP1質體建構 15 3-1.1.1 聚合酶連鎖反應(PCR)增幅VP0、VP3、VP1基因 15 3-1.1.2 PCR產物濃縮純化(DNA clean & concentration, DCC) 16 3-1.1.3 Restriction Enzyme Digestion 17 3-1.1.4 Sticky-end ligation and transformation 17 3-1.1.5 Colony PCR 18 3-1.2 pcDNA-P1 5M點突變實驗 19 第二節 重組蛋白表現 21 3-2.1 Transient expression抗原表現 21 3-2.2 VLPs抗原大量表現21 3-3.3 Sucrose gradient ultracentrifuge純化VLPs與鑑定 21 3-2.3.1 Sucrose gradient ultracentrifuge分離promoter、pentamer及VLPs 21 3-2.3.2 VLPs-based sandwich ELISA 22 3-2.3.3 VLPs-based direct ELISA 22 3-2.3.4十二烷基硫酸鈉聚丙烯醯胺凝膠電泳(Sodium dodecyl sulfate -polyacrylamide gel electrophoresis, SDS-PAGE) 23 3-2.3.5西方墨點法 (Western blot, WB) 23 第三節 抗口蹄疫(FMD)單源抗體(MAb)特性鑑定 24 3-3.1 免疫螢光染色 (Immunofluorescene assay, IFA) 24 3-3.2 抗口蹄疫次單元(subunit protein)單源抗體鑑定 24 3-3.3 抗口蹄疫中和單源抗體識別neutralizing sites鑑定 24 3-3.4 抗O99 VLPs單源抗體鑑定 24 3-3.5 以Sucrose gradient fraction篩檢識別Virus-like-particles構形單源抗體 25 3-3.6 單源抗體Site 1與Site 2 steric effect比較 25 第四節 抗口蹄疫(FMD)阻斷型酵素連結免疫吸附法(bELISA)建立 26 3-4.1 單源抗體腹水純化 26 3-4.2 純化抗體蛋白定量 26 3-4.3 標定HRP (Horseradish peroxidase)純化抗體Tracer製備 26 3-4.4 Capture Ab篩選及血清量最優化 27 3-4.5 VLPs-based blocking ELISA與大量血清樣品測試 27 第五節 E. coli表現重組蛋白 28 3-5.1 pET-SUMO-VP0、pET-SUMO-VP3及pET-SUMO-VP1表現質體建構 28 3-5.2 TA cloning 28 3-5.3 SUMO重組蛋白表現 29 3-5.4超音波破菌 29 3-5.5表現重組蛋白純化 30 3-5.6重組蛋白移除SUMO fusion protein 30 第六節 其他實驗常用生物材料製備 31 3-5.1 重組牛痘病毒(T7)製備 31 3-5.2 勝任細胞製備 31 3-5.3 大量質體DNA萃取 32 第四章 結果 33 第一節 質體建構 33 4-1.1 PCR增幅His-VP0、His-VP3、His-VP1基因片段 33 4-1.2 pcDNA-His-VP0、pcDNA-His-VP3、pcDNA-His-VP1質體建構 33 4-1.3 5M突變pcDNA-mP1質體建構 33 第二節 重組抗原表現 34 4-2.1 His-VP0、His-VP3、His-VP1重組蛋白表現確認 34 4-2.2表現VLPs抗原sucrose gradient確認 34 第三節 口蹄疫單源抗體特性鑑定 34 4-3.1 抗口蹄疫次單元(subunit protein)單源抗體鑑定 35 4-3.2抗口蹄疫中和單源抗體辨識neutralizing sites鑑定 35 4-3.3 抗O/KM/99 (O99) VLPs單源抗體鑑定 36 4-3.4 識別Virus-like-particles構形單源抗體篩選 36 4-3.5單源抗體Site 1與Site 2 steric effect比較 37 第四節 VLPs-based blocking ELISA檢測系統建立 38 4-4.1 Capture Ab篩選及血清量最優化 38 4-4.2 少量血清樣品測試 38 4-4.3 大量血清樣品測試 39 第五節 E.coli表現重組蛋白 39 4-5.1 pET-SUMO-VP0、pET-SUMO-VP3、pET-SUMO-VP1與質體建構 39 4-5.2 pET-SUMO-VP0、pET-SUMO-VP3、pET-SUMO-VP1抗原表現 39 4-5.3 pET-SUMO-VP0、pET-SUMO-VP3、pET-SUMO-VP1純化40 4-5.4純化抗原SUMO protease酶切 41 第五章 討論42 第一節 單源抗體特性鑑定 43 5-1.1 抗口蹄疫次單元(subunit protein)單源抗體鑑定 43 5-1.2 抗口蹄疫中和單源抗體識別neutralizing sites鑑定 45 5-1.3 抗O99 VLPs單源抗體鑑定 47 第二節VLPs-based blocking ELISA建立 47 第三節 E.coli表現重組蛋白 50 第四節 結論 52 參考文獻 88 附錄 97 | |
dc.language.iso | zh-TW | |
dc.title | 以抗Site 1/Site 2單源抗體結合SUMO fusion蛋白所表現的口蹄疫類病毒空殼蛋白建構阻斷型ELISA | zh_TW |
dc.title | Advanced Development of FMDV Blocking ELISA based on Site1/Site2 MAbs and VLP Expressed by SUMO Fusion Protein | en |
dc.type | Thesis | |
dc.date.schoolyear | 107-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 楊平政,張惠雯,王金和,陳世平,潘居祥 | |
dc.subject.keyword | 口蹄疫,中和抗體決定位,單源抗體,SUMO fusion蛋白,阻斷型酵素連結免疫吸附試驗, | zh_TW |
dc.subject.keyword | Foot-and-Mouth Disease Virus,Neutralization Site,Monoclonal Antibody,SUMO Fusion Protein,Blocking ELISA, | en |
dc.relation.page | 100 | |
dc.identifier.doi | 10.6342/NTU201900694 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2019-08-14 | |
dc.contributor.author-college | 獸醫專業學院 | zh_TW |
dc.contributor.author-dept | 獸醫學研究所 | zh_TW |
顯示於系所單位: | 獸醫學系 |
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