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研究生： 黃育慈
論文名稱： 重組鱟血漿凝集素之細菌及配體結合功能分析
Functional Caracterization of Bacteria and Ligand Binding Activities of Recombinant Tachypleus Plasma Lectin
指導教授： 張大慈
張壯榮
口試委員: 張晃猷
王雯靜
張壯榮
鄭兆珉
學位類別： 碩士
Master
系所名稱： 生命科學暨醫學院 - 生物科技研究所
Biotechnology
論文出版年： 2013
畢業學年度： 101
語文別： 英文
論文頁數： 123
中文關鍵詞： 鱟血漿凝集素
相關次數： 點閱：4  下載：0 
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    • 中文摘要
    鱟是古老的無脊椎海洋動物，缺乏後天性免疫系統，因此完全依賴由血漿及血球組成的先天性免疫系統抵抗病原菌入侵。由台灣品種鱟 (Taiwanese Tachypleus tridentatus) 的血漿中分離之血漿凝集素具有辨識革蘭氏陽性和陰性菌、以及其他病源菌相關分子型態(pathogen associated molecular patterns, PAMPs) 的能力。以往利用嗜甲醇酵母菌 (Pichia pastoris) 可於胞外表現鱟血漿凝集素，但其表現量及產率皆低；而目前尚無利用原核生物系統表現並純化可溶性鱟血漿凝集素的成功案例。本研究利用蛋白質工程技術設計及修飾重組鱟血漿凝集素胜肽序列，並利用大腸桿菌表現此新穎之重組蛋白。其生物功能性分析顯示重組鱟血漿凝集素可識別特定的細菌及病原相關分子型態、亦能結合多種臨床分離之病源菌，並發現此結合細菌的能力可能與病源菌細胞壁中特殊醣分子相關。此外，本研究亦首次發現重組鱟血漿凝集素具有抑制綠膿桿菌生長的能力。本論文探討重組鱟血漿凝集素與細菌、病原菌及糖類的特定分子交互作用關係，將有助於發展偵測臨床微生物致病菌或內毒素殘留的新穎方法。
     

    Table of Contents 中文摘要…………………………………………………………………………..…..I Abstract…......................................................... II Acknowledgement III Abbreviation XI Chapter 1 Introduction 1 1.1 Innate immunity of invertebrates 1 1.2 Horseshoe crab 3 1.3 Hemolymph coagulation 4 1.4 Endotoxin detection assay–from Limulus amebocyte lysate (LAL) to recombinant Factor C (rFC) 6 1.5 Endotoxin removal kit-ToxinEraser and EndoTrap® 8 1.6 Tachylectin 9 1.7 Tachypleus plasma lectin 1 and Tachypleus plasma lectin 2 12 1.8 Starch binding domain (SBD) 16 1.9 Solubility-enhancing peptide (SEP) 16 1.10 ySBD-SEP-TPL2 17 1.11 Characteristics and detection methods of clinically important pathogens 18 1.12 Research motivation 23 Chapter 2 Materials and methods 25 2.1 Microbial strains, media and plasmid 25 2.2 Construction of plasmid 25 2.3 Competent cell preparation 26 2.4 Escherichia coli heat-shock transformation 27 2.5 Confirmation of colonies by in situ PCR 27 2.6 Mini-preparation of plasmid 28 2.7 Small scale expression of recombinant TPL2 in E. coli 28 2.8 Purification of recombinant SEP-TPL2 and removal endotoxin 29 2.9 Protein buffer exchange 30 2.10 Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) 30 2.11 Bicinchoninic acid (BCA) assay 30 2.12 Enzyme-linked imunosorbent assay (ELISA) for PAMPs 31 2.13 Enzyme-linked immunosorbent assay (ELISA) for bacteria 31 2.14 Magnetic reduction (MR) assay 33 2.15 Inhibition and competitive ELISA 33 2.16 Antibacterial activity assay 34 2.17 Analytical ultracentrifugation 34 2.18 Mass spectrometry determination 35 2.19 Statistical analysis 35 Chapter 3 Results 36 3.1 Small scale expression of recombinant TPL2 36 3.2 Design of different recombinant TPL2 36 3.3 Construction of pET23a-n7-tpl2 and pET23a-c7-tpl2 37 3.4 Small scale expression of recombinant TPL2 37 3.5 Purification of SEP-TPL2 and removal endotoxin 38 3.6 Binding activity of SEP-TPL2 to PAMPs 39 3.7 Bacteria-binding activity of SEP-TPL2 40 3.8 Clinically isolated bacteria recognition of SEP-TPL2 41 3.9 L-rhamnose binding activity of SEP-TPL2 42 3.10 Binding activity of SEP-TPL2 to L-rhamnose 43 3.11 Binding activity of SEP-TPL2 to Rhamnosoft® HP 43 3.12 Antibacterial activity of SEP-TPL2 45 3.13 Determination of SEP-TPL2 forms 45 Chapter 4 Discussion 47 4-1 Expression and purification of TPL2 47 4-2 PAMP-binding activity of TPL2 48 4-3 Bacteria-binding activity of TPL2 49 4-4 Functional roles of rhamnose in pathogens 50 4-5 Antibacterial activity of SEP-TPL2 54 4-6 Characterization of SEP-TPL2 forms 55 4-7 Application of SEP-TPL2 for endotoxin detection kit and endotoxin removal kit 56 4-8 Comparison between SEP-TPL2 and rhamnose binding lectins (RBLs) 57 4-9 Conclusion 58 References… 61 Figures…… 72 Tables…….. 98 Appendices… 105   List of Figures Fig. 1-1 Structures of bacterial cell wall and pathogen associated molecular patterns (PAMPs) 3 Fig. 1-2 Innate immune system of horseshoe crab 4 Fig. 1-3 Schematic illustration of hemolymph coagulation cascade system in Lmulus 6 Fig. 1-4 Schematic illustration of endotoxin detection mechanisms in LAL system and rFC system 8 Fig. 1-5 Three dimensional structures of (A) TL-2 and (B) TL-5A 11 Fig. 1-6 Sequence alignment of tachylectins and Tachypleus plasma lectins 15 Fig. 1-7 Scanning electron micrographs of pathogens 20 Fig. 3-1 Plasmid map and cartoon maps of recombinant TPL2 73 Fig. 3-2 Small-scale expression of recombinant TPL2s 76 Fig. 3-3 Purification of SEP-TPL2 77 Fig. 3-4 Purification of endotoxin-free SEP-TPL2 78 Fig. 3-5 Molecular weight determination of SEP-TPL2 79 Fig. 3-6 Binding activity of SEP-TPL2 to LPS 80 Fig. 3-7 Binding activity of SEP-TPL2 to S. aureus LTA and S. faecalis LTA 81 Fig. 3-8 Comparison of PAMP-binding activity between SEP-TPL2 and endotoxin-free SEP-TPL2 82 Fig. 3-9 Binding activity of SEP-TPL2 to Gram-negative bacteria 83 Fig. 3-10 Binding activity of SEP-TPL2 to Gram-positive bacteria 84 Fig. 3-11 Dose-dependent binding of SEP-TPL2 to bacteria 85 Fig. 3-12 Binding activity of SEP-TPL2 to clinically isolated bacteria 86 Fig. 3-13 Binding activity of SEP-TPL2 to L-rhamnose 88 Fig. 3-14 P. aeruginosa binding activity of SEP-TPL2 in the presence of L-rhamnose 89 Fig. 3-15 P. aeruginosa binding activity of SEP-TPL2 in the presence of Rhamnosoft® HP 90 Fig. 3-16 L. monocytogenes binding activity of SEP-TPL2 in the presence of Rhamnosoft® HP 92 Fig. 3-17 Binding activity of SEP-TPL2 to Rhamnosoft® HP 94 Fig. 3-18 Antibacterial activity of SEP-TPL2 95 Fig. 3-19 Characterization of SEP-TPL2 species by SDS-PAGE and analytical ultracentrifugation 96   List of Tables Table 1-1 Native tachylectins from Japanese T. tridentatus 12 Table 1-2 Fusion partners for solubility enhancement of recombinant proteins 17 Table 1-3 Summary of native and two recombinant TPL2s 18 Table 1-4 Summary of characteristics of pathogens 21 Table 1-5 Summary of pathogen detection methods 23 Table 3-1 Chemical structures of PAMPs of SEP-TPL2 binding bacteria 98 Table 4-1 Comparison among purification of TPL2 99 Table 4-2 Comparison PAMP binding activity between ySBD-SEP-TPL2 and SEP-TPL2 99 Table 4-3 Summary of antibiotic resistance of clinical pathogens 100 Table 4-4 Analytical methods of PAMP components of rhamnose-containing bacteria 101 Table 4-5 Summary of antibacterial lectins 102 Table 4-6 Prices of endotoxin detection kits 103 Table 4-7 Summary of tachylectins and Tachypleus plasma lectins 104 List of Appendices Appendix Fig. 1 Small scale expression of recombinant TPL2 105 Appendix Fig. 2 Amplification of DNA fragment encoding n7-tpl2 and c7-tpl2 by PCR 106 Appendix Fig. 3 Verification of pET23a-n7-tpl2 and pET23a-c7-tpl2 by in situ PCR 108 Appendix Fig. 4 Comparison of Roche blocking reagent and BSA in LPS-binding ELISA for blocking 110 Appendix Fig. 5 Comparison binding activity of ySBD-SEP-TPL2 and SEP-TPL2 to PAMPs 111 Appendix Fig. 6 Characterization of ySBD-SEP-TPL2 species by SDS-PAGE and analytical ultracentrifugation 112 Appendix Fig. 7 Structure of Rhamnosoft® HP 114 Appendix Fig. 8 Multiple sequence alignment of SEP-TPL2 and RBLs 115

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