臺灣博碩士論文加值系統

根據文獻記載愛德華氏菌屬（Genus Edwardsiella）中有2菌種常造成水生動物嚴重病症感染。其菌種之一，愛德華氏菌E. tarda已在世界各地造成多種魚類尤其是吳郭魚、鰻魚、鯉魚與比目魚等典型愛德華氏菌症之危害。之二菌種愛德華氏菌E. ictaluri在美國所造成的鯰魚腸敗血症及其他如越南等亞洲國家的鯰魚、淡水魚均已被證實為最重要的傳染病病原菌之ㄧ。有鑑於此，研發有效對抗愛德華氏菌症及鯰魚腸敗血症疫苗是有其迫切必要性。近年來研究指出某些細菌的外膜蛋白如3-甘油醛磷酸脫氫酶 (glyceraldehydes-3-phosphate dehydrogenase；GAPDH）可成為魚類抵抗愛德華氏菌及弧菌之有效疫苗的候選蛋白。然而愛德華氏菌E. ictaluri來源的外膜蛋白GAPDH作為疫苗候選蛋白之疫苗效力未被研究。因此本研究即利用大腸桿菌表現系統進行愛德華氏菌E. ictaluri來源的 37 kDa GAPDH之表現，並以鎳離子螯合親和層析法純化此重組融合候選蛋白。根據胺基酸及核苷酸序列的比對分析資料庫中OT9606Z005S株（愛德華氏菌E. ictaluri）來源的 37 kDa GAPDH與其他革蘭氏陰性菌及愛德華氏菌E. ictaluri、E. tarda有高達74–100%的相似度，且以西方墨點轉漬進行候選蛋白的免疫原性分析，結果發現兔抗候選蛋白血清與候選重組蛋白GAPDH有很強的反應。另以此候選重組蛋白（30μg fish-1）混以佐劑ISA 763A、福馬林不活化愛德華氏菌E. ictaluri全菌細胞及生理食鹽水作為陰性對照進行吳郭魚活體對愛德華氏菌E. ictaluri死菌菌苗與候選重組蛋白，包括相對存活百分比(RPS)及其增強魚類抗體等相關性免疫反應效力評估。實驗魚隻在免疫後第四及十二週，分別進行血清凝集、溶菌酶活性及特異性抗體測定。結果在免疫後第四及十二週所有免疫組血清凝集力價均有顯著增加，其值在log2 值2.3 到 11.5之間，而免疫混合候選重組蛋白GAPDH組在免疫後第四週及十二週之特異性抗體力價log2 值顯著高於其他免疫對照組。另一方面，免疫候選重組蛋白GAPDH與福馬林不活化全菌細胞混合組在第十二週時以愛德華氏菌E. tarda攻毒來評估其疫苗之保護效力結果，其相對存活百分達71.4%。綜合以上實驗結果顯示愛德華氏菌E. ictaluri來源的候選重組蛋白GAPDH確實可有效保護實驗吳郭魚不受愛德華氏菌E. tarda的感染。因此未來愛德華氏菌E. ictaluri來源的候選重組蛋白GAPDH將可於愛德華氏菌E. ictaluri、E. tarda之多價疫苗研發時之首選標的物。

Genus Edwardsiella had a two species that have often been reported as causative agents of serious infection in aquatic animal. Edwardsiella tarda, causal agent of classical edwardsiellosis in several kinds of fish, especially tilapia, eel, carp and flounder in the world. Besides, E. ictaluri is known to be the causative agent of enteric septicemia of catfish (ESC) in the United States of American (USA) and has been isolated from other freshwater fish in Vietnam and other Asian countries. For these reasons, the developing an effective vaccination strategy to edwardsiellosis and ESC in fish is a necessary. Recent studies indicate that the outer membrane protein like glyceraldehydes–3–phosphate dehydrogenase (GAPDH) can be an effective vaccine candidate against E. tarda or Vibrio anguillarum infected fish. However, vaccine efficacy of GAPDH from E. ictaluri has not been investigated. This study, the gene-coding 37 kilodalton GAPDH of E. ictaluri was determined and over expressed by using the Escherichia coli expression system. The recombinant fusion of GAPDH proteins were purified with nickel (Ni-NTA agarose) chelate affinity chromatography. Alignment analysis based on the amino acid and nucleotide sequences indicate that the GAPDH from E. ictaluri strain OT9606Z005S had highly homologous 74–100% of identities with several products of GAPDH from E. tarda and other gram-negative bacterial species within the Enterobacteriaceae family. To analyze the immunogenicity of this protein, Western blotting of rabbit serum against GAPDH protein reveals that the rabbit serum reacted strongly with recombinant GAPDH proteins. An efficacious E. ictaluri vaccine was evaluated using a recombinant GAPDH protein (30μg fish–1) from E. ictaluri and formalin-killed whole cells (WC) of E. ictaluri, both of which, emulsified in the ISA 763A adjuvant, and phosphate-buffered saline as the negative control. A vaccine study was conducted by intraperitoneal injection in tilapia Oreochromis niloticus in order to determine protection in terms of Relative Percent Survival (RPS). At 4 and 12 weeks after immunization, immune responses were measured in term of serum agglutinating production, the lysozyme activity, and the specific antibody level. The fish sera agglutination titer all of vaccine groups increased significant (P < 0.05) during 4 weeks and 12 weeks post-vaccination, within the range of log2 values of 2.3 to 11.5. The lysozyme activity level of fish had no significant difference among the fish in the control and post-vaccinations for 4 weeks. The specific mean antibody titer log2 level of groups vaccinated with GAPDH at 4 weeks and 12 weeks were significantly higher than that of non-vaccination fish (the control group). On the other hand, the fish immunized with mixed recombinant GAPDH and WC at 12 weeks were challenged with the E. tarda strain OT980–27 to assess vaccine efficacy with RPS values exceeding 71.4%. The result showed that GAPDH from E. ictaluri effectively protected tilapia from experimental E. tarda infection. Therefore, E. ictaluri GAPDH should be considered as a multi-purpose candidate vaccine against E. ictaluri and E. tarda.

ABSTRACT (Chinese) I
ABSTRACT (English) III
ACKNOWLEDGEMENTS V
TABLE OF CONTENTS VII
LIST OF TABLES X
LIST OF FIGURES XI
LIST OF ABBREVIATIONS XV
1. INTRODUCTION 1
2. LITERATURE REVIEW 7
2.1 Enteric septicemia of catfish disease 7
2.1.1 Biochemical characteristic of E. ictaluri 8
2.1.2 Clinical signs 11
2.1.3 Pathogenesis 12
2.1.4 Transmission 14
2.1.5 Diagnostic 15
2.1.5.1 Isolation and bacteriological identification 15
2.1.5.2 Fluorescent antibody technique (FAT) 15
2.1.5.3 Enzyme-linked immunosorbent assay (ELISA) 16
2.1.5.4 Histopathology 17
2.1.5.5 Molecular techniques 18
2.1.5.5.1 Polymerase chain reaction (PCR) methods 18
2.1.5.5.2 Loop-mediated isothermal amplification method (LAMP) 19
2.1.6 Prevention and therapy 19
2.2 Immune response 20
2.3 The fish immune system 25
2.3.1 Innate immunity 25
2.3.1.1 Macrophages 26
2.3.1.2 Lysozyme 26
2.3.1.3 Complement system 27
2.3.1.4 Interferons (IFNs) 28
2.3.2 The adaptive immune 29
2.3.2.1 Humoral responses 29
2.3.2.2 Antibodies 30
2.3.2.3 Cell-mediated immunity T-cells 30
2.3.2.4 Factors affecting the immune response in fish 30
2.4 Characterization of Outer membrane proteins (OMPs) 31
3. MATERIALS AND METHODS 35
3.1 Primer design 35
3.2 Plasmid constructs used in this thesis 35
3.3 Bacterial strain 36
3.4 DNA extraction and purification of template for PCR 37
3.5. Cloning and sequencing of E. ictaluri GAPDH gene 38
3.5.1 Amplified the E. ictaluri GAPDH gene using PCR assay 38
3.5.2 Gel-purified PCR products 38
3.5.3 Cloning of the GAPDH fragment into pET 151/D-TOPO vector 39
3.5.4 Extraction and purified plasmids from bacterial cells 40
3.5.5 Agarose gel electrophoresis of plasmid DNA 40
3.5.6 Sequence analysis 41
3.6 Expression of GAPDH protein and purification 41
3.6.1 Expression of E. ictaluri GAPDH protein 41
3.6.2. Purification of recombinant protein 42
3.7 Quantification of recombinant protein 43
3.8 Sodium dodecyl sulphate - polyacrylamide gel electrophoresis (SDS-PAGE) analysis 43
3.9 Rabbit antiserum against recombinant GAPDH proteins 44
3.10 Western blot assay 44
3.11 Vaccine preparation 45
3.11.1 Preparation of formalin kill whole cell (WC) of E. ictaluri OT9606Z005S 45
3.11.2 Preparation of purified recombinant GAPDH vaccine 46
3.12 Fish 46
3.13 Vaccine administration 47
3.14 Challenge 47
3.15 Lysozyme activity assay 48
3.16 Enzyme-linked immunosorbent assay 48
3.17 Agglutination activity of serum 49
3.18 Statistic analysis 50
4. RESULTS AND DISCUSSIONS 51
4.1 Isolated and identified bacteria 51
4.2 Determination of GAPDH gene by PCR 51
4.3 Cloning and nucleotide sequence of GAPDH gene 52
4.4 Expression and purification of recombinant GAPDH 60
4.5 Western blot analysis 62
4.6 Lysozyme activity 65
4.7 Agglutination of serum assay 68
4.8 ELISA antibody titers of fish post-vaccination 72
4.9 Effective protection of the recombinant GAPDH proteins 72
4.10 General discussion 80
5. CONCLUSIONS AND RECOMMENDATIONS 84
REFERENCES 86
BIOSKETCH OF AUTHOR 111

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