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研究生:阮崇海
研究生(外文):Nguyen,Trong Hai
論文名稱:利用昆蟲桿狀病毒載體系統於昆蟲及哺乳細胞表現豬環狀病毒蛋白
論文名稱(外文):Expression of Porcine circovirus Type 2 Capsid Protein in Insect and Mammalian Cells Using Baculovirus Expression Vector System
指導教授:鄭力廷鍾曜吉鄭達智鄭達智引用關係
指導教授(外文):Li-Ting ChengYao-Chi ChungPhilip T. Cheng
學位類別:碩士
校院名稱:國立屏東科技大學
系所名稱:熱帶農業暨國際合作系
學門:農業科學學門
學類:一般農業學類
論文種類:學術論文
論文出版年:2013
畢業學年度:101
論文頁數:96
中文關鍵詞:豬環狀病毒第2型重組昆蟲桿狀病毒衣殼蛋白哺乳細胞新型疫苗第2型之衣核蛋白
外文關鍵詞:Porcine circovirus type 2recombinant baculoviruscapsid proteinmammalian cellsnovel vaccine
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學號: M10022017
論文題目: 利用昆蟲桿狀病毒載體系統於昆蟲及哺乳細胞表現豬環狀病毒蛋白
總頁數: 96
學校名稱: 國立屏東科技大學 系(所)別: 熱帶農業暨國際合作系
畢業時間及摘要別: 一百零一學年度第二學期碩士學位論文摘要
研究生: 阮崇海 指導教授: 鄭力廷博士
鍾曜吉博士
鄭達智博士
論文摘要內容:
豬環狀病毒第2型 (PCV2)離乳後多系統消耗性綜合症 (PMWS)主要病源,且為當代養豬產業新興疾病 ,常造成養豬國家經濟上重大損失。因此,在多數的養豬國家急需迫切發展一有效疫苗來控制此疾病。近年,新型疫苗之開發多以較具吸引力之昆蟲桿狀病毒表現系統為。故本研究利用秋行軍蟲 (Sf9)細胞表現昆蟲桿狀病毒攜帶 PCV2 之開放閱讀框架2 (ORF2)基因,該基因片段經轉錄轉譯後為PCV2之衣核蛋白,且被證實為一重要免疫原;隨後利用巨細胞病毒啟動子轉錄帶有 ORF2基因之重組桿狀病毒,並於中國倉鼠卵巢 (CHO)細胞中表現病毒衣殼蛋白。將成功轉染至Sf9細胞及CHO細胞之重組桿狀病毒,觀察其細胞病變及綠螢光表現情形。此外,利用聚丙烯醯胺膠體 (SDS-PAGE)證實其重組蛋白表現位置與產量,以及使用西方墨點法 (Western blot)以His-tag及陽性血清 (PCV2)證實其抗原性。本研究結果顯示,已成功表現PCV2之重組衣殼蛋白於昆蟲細胞表現系統;但目前正極力將重組衣殼蛋白表現於哺乳細胞表現系統內。未來將發展一有效且新型之PCV2疫苗,得以控制PCV2之威脅。

Student ID: M10022017
Title of thesis: Expression of Porcine circovirus Type 2 Capsid Protein in Insect and Mammalian Cells Using Baculovirus Expression Vector System
Total page: 96
Name of institute: Department of Tropical Agriculture and International Cooperation
Graduate date: June 28th, 2013 Degree conferred: Master
Name of student: Nguyen, Trong Hai Advisors: Li-Ting Cheng, Ph.D.
Yao-Chi Chung, Ph.D.
Philip Ta Cheng, Ph.D.
The content of abstract in this thesis:
Porcine circovirus type 2 (PCV2) has been known as the primary causative agent of post-weaning multisystemic wasting syndrome, an emerging swine disease which causes tremendous economic losses. Thus, development of a highly efficient vaccine to control this pathogen is an urgent need for the swine industry in many countries. Recently, baculovirus has emerged as an attractive gene expression system for novel vaccine technology production. In this study, recombinant baculovirus carrying open reading frame 2 gene of PCV2 first was developed to express PCV2 capsid protein, the most important immunogen of PCV2, in Spodoptera frugiperda (Sf9) cells. Additionally, the recombinant baculovirus with the presence of cytomegalovirus promoter as protein transcriptional control in mammalian cells was generated and subsequently utilized to transduce Chinese hamster ovary (CHO) cells for expression of the capsid protein. Efficiency of recombinant virus transfection and infection in Sf9 cells was investigated by inspecting the appearance of cytopathic effect on the cells and also by comparing with positive control expressing green fluorescence. The capsid protein expressed then was evaluated by SDS-PAGE and Western blot using both antibody against His-tag and PCV2. Result shows that baculovirus expression vector system (BEVS) can be employed to successfully express the PCV2 capsid protein in insect cells system. Current efforts are focused on the expression of the capsid protein in a mammalian cells system. Continuing study is needed for developing an effective novel vaccine for PCV2 infection management.

中文要摘 1
English Abstract 2
Acknowledgements 4
Table of Contents 5
List of Tables 8
List of Figures 9
1. Introduction 11
2. Literature Review 13
2.1 Characterization of PCV2 13
2.2 PCV2-associated diseases (PCVAD) 14
2.2.1 Post-weaning multisystemic wasting syndrome (PMWS) 14
2.2.2 Porcine dermatitis and nephropathy syndrome (PDNS) 16
2.2.3 Porcine respiratory disease complex (PRDC) 19
2.2.4 Reproductive failure (RF) 22
2.2.5 Granulomatous enteritis (GE) 24
2.2.6 Congenital tremor (CT) 25
2.3 Baculovirus expression vector system 25
2.3.1 Principle of the baculovirus expression vector system 26
2.3.2 The development of baculovirus vectors over time 28
3. Materials and Methods 33
3.1 Materials 33
3.2 Construction of recombinant donor plasmid
for expression of PCV2 34
3.2.1 Purification of plasmid DNA by Plasmid
miniprep Kit (BioKit) 34
3.2.2 Measurement of plasmid DNA concentration 35
3.2.3 Amplification of ORF2 by Polymerase
chain reaction (PCR) 35
3.2.4 Digestion of pFastBac HTa plasmid and ORF2
gene by BamH I and Hind III restriction enzyme 37
3.2.5 Isolation of digestion product by Clean/Gel
Extraction Kit (BioKit) 37
3.2.6 Ligation of ORF2 gene and linear pFastBac HTa 39
3.2.7 Transformation of ligated plasmid into
E. coli DH5α competent cells 39
3.3 Construction of recombinant donor plasmid for PCV2
capsid protein expression in mammalian cells 40
3.4 Transposition of desired insert to bacmid DNA 41
3.5 Isolation of recombinant bacmid DNA 42
3.5.1 Preparation 42
3.5.2 Isolation of bacmid DNA protocol 42
3.6 Verification of recombinant bacmid DNA by PCR 44
3.7 Cell culture 46
3.7.1 Recovery of cryopreserved cultures procedure 46
3.7.2 Monolayer cell culture procedure 46
3.7.3 Cryopreservation of cell cultures procedure 48
3.8 Transfection of Sf9 cells with recombinant bacmid DNA 49
3.9 Harvest and storage of recombinant Baculovirus 50
3.10 Amplification of viral stocks 50
3.10.1 Multiplicity of infection for virus amplification 50
3.10.2 Infection of insect cells with recombinant
baculovirus particles 50
3.10.3 Titering virus stock by end point dilution assay 51
3.11 Investigation of recombinant PCV2 capsid
protein by Western blot 52
3.11.1 Extraction of protein 52
3.11.2 Preparation of sodium dodecyl sulfate polyacrylamide
gel electrophoresis (SDS – PAGE) 52
3.11.3 Western blot protocol 54
4. Results and Discussion 56
4.1 Construction of recombinant plasmids for PCV2
capsid protein expression using BEVS 56
4.1.1 Cloning recombinant plasmids for the capsid
protein expression in insect cells 56
4.1.2 Cloning recombinant plasmids for the capsid
protein expression in mammalian cells 57
4.1.3 Cloning recombinant plasmids for expression of green
fluorescent protein in insect and mammalian cells 58
4.2 Creation of recombinant bacmid DNA 59
4.3 Isolation and verification of the recombinant bacmids 61
4.4 Generation of recombinant baculovirus 61
4.5 Amplification of recombinant virus 62
4.6 Investigation of recombinant baculovirus titer 65
4.7 Optimization of transduction of CHO cells
with recombinant baculovirus 66
4.7.1 Optimization of incubation time and virus
dosage for transduction 66
4.7.2 Optimization of incubation temperature
and surrounding solution 70
4.8 Expression of PCV2 capsid protein 73
4.8.1 Expression of PCV2 capsid protein in insect cells 73
4.8.2 Expression of PCV2 capsid protein in mammalian cells 75
Discussion 76
5. Conclusions 82
6. References 83
Biosketch of Author 95

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