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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 蕭信宏(Shin-Hong Shiao) | |
| dc.contributor.author | Sheng-Yu Kuan | en |
| dc.contributor.author | 官聲友 | zh_TW |
| dc.date.accessioned | 2022-11-25T06:33:12Z | - |
| dc.date.copyright | 2021-08-31 | |
| dc.date.issued | 2021 | |
| dc.date.submitted | 2021-08-06 | |
| dc.identifier.citation | Aliota, M.T., Walker, E.C., Uribe Yepes, A., Dario Velez, I., Christensen, B.M., and Osorio, J.E. (2016). The wMel Strain of Wolbachia Reduces Transmission of Chikungunya Virus in Aedes aegypti. PLOS Neglected Tropical Diseases 10, e0004677. Alphey, L. (2014). Genetic control of mosquitoes. Annu Rev Entomol 59, 205-224. Amuzu, H.E., Tsyganov, K., Koh, C., Herbert, R.I., Powell, D.R., and McGraw, E.A. (2018). Wolbachia enhances insect-specific flavivirus infection in Aedes aegypti mosquitoes. Ecol Evol 8, 5441-5454. Anders, K.L., Indriani, C., Ahmad, R.A., Tantowijoyo, W., Arguni, E., Andari, B., Jewell, N.P., Rances, E., O'Neill, S.L., Simmons, C.P., et al. (2018). The AWED trial (Applying Wolbachia to Eliminate Dengue) to assess the efficacy of Wolbachia-infected mosquito deployments to reduce dengue incidence in Yogyakarta, Indonesia: study protocol for a cluster randomised controlled trial. Trials 19, 302-302. Balinsky, C.A., Schmeisser, H., Ganesan, S., Singh, K., Pierson, T.C., and Zoon, K.C. (2013). Nucleolin interacts with the dengue virus capsid protein and plays a role in formation of infectious virus particles. J Virol 87, 13094-13106. Basha, E., O'Neill, H., and Vierling, E. (2012). Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions. Trends Biochem Sci 37, 106-117. Benoit, J.B., Lopez-Martinez, G., Patrick, K.R., Phillips, Z.P., Krause, T.B., and Denlinger, D.L. (2011). Drinking a hot blood meal elicits a protective heat shock response in mosquitoes. Proc Natl Acad Sci U S A 108, 8026-8029. Benoit, J.B., Lopez-Martinez, G., Phillips, Z.P., Patrick, K.R., and Denlinger, D.L. (2010). Heat shock proteins contribute to mosquito dehydration tolerance. J Insect Physiol 56, 151-156. Bian, G., Xu, Y., Lu, P., Xie, Y., and Xi, Z. (2010). The Endosymbiotic Bacterium Wolbachia Induces Resistance to Dengue Virus in Aedes aegypti. PLOS Pathogens 6, e1000833. Borovsky, D. (2003). Biosynthesis and control of mosquito gut proteases. IUBMB Life 55, 435-441. Borovsky, D., Carlson, D.A., Griffin, P.R., Shabanowitz, J., and Hunt, D.F. (1990). Mosquito oostatic factor: a novel decapeptide modulating trypsin-like enzyme biosynthesis in the midgut. Faseb j 4, 3015-3020. Bradley, T.J. (1987). Physiology of Osmoregulation in Mosquitoes. Annual Review of Entomology 32, 439-462. Briegel, H., and Lea, A.O. (1979). Influence of the endocrine system on tryptic activity in female Aedes aegypti. Journal of Insect Physiology 25, 227-230. Calderón-Arguedas, O., Troyo, A., Solano, M.E., Avendaño, A., and Beier, J.C. (2009). Urban mosquito species (Diptera: Culicidae) of dengue endemic communities in the Greater Puntarenas area, Costa Rica. Rev Biol Trop 57, 1223-1234. Carlton, J.M. (2018). Malaria parasite evolution in a test tube. Science 359, 159-160. CDC (2019). Center for Disease Control and Prevention. Zika virus. https://www.cdc.gov/zika/index.html. CDC (2020a). Center for Disease Control and Prevention. Dengue virus. https://www.cdc.gov/dengue/index.html. CDC (2020b). Centers for Disease Control, R.O.C.(Taiwan).Taiwan National Infectious Disease Statistics System. https://nidss.cdc.gov.tw/en/Home/Index. Chakrabarti, N., Tajkhorshid, E., Roux, B.t., and Pomès, R. (2004). Molecular Basis of Proton Blockage in Aquaporins. Structure 12, 65-74. Christophers, S.R. (1960). Aëdes aegypti (L.) the Yellow Fever Mosquito: its Life History, Bionomics and Structure. (The Syndics of the Cambridge University Press). Clare, D.K., and Saibil, H.R. (2013). ATP-driven molecular chaperone machines. Biopolymers 99, 846-859. Clum S, Ebner KE, and R., P. (1997). Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3(Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B. J Biol Chem 272, 30715-30723. Colpitts, T.M., Barthel, S., Wang, P., and Fikrig, E. (2011). Dengue virus capsid protein binds core histones and inhibits nucleosome formation in human liver cells. PLoS One 6, e24365. Corsi, A.K., and Schekman, R. (1996). Mechanism of polypeptide translocation into the endoplasmic reticulum. J Biol Chem 271, 30299-30302. Cowman, A.F., Berry, D., and Baum, J. (2012). The cellular and molecular basis for malaria parasite invasion of the human red blood cell. J Cell Biol 198, 961-971. de Alwis, R., Williams, K.L., Schmid, M.A., Lai, C.Y., Patel, B., Smith, S.A., Crowe, J.E., Wang, W.K., Harris, E., and de Silva, A.M. (2014). Dengue viruses are enhanced by distinct populations of serotype cross-reactive antibodies in human immune sera. PLoS Pathog 10, e1004386. Deplazes Zemp, A., Lefort, F., Müller, P., Romeis, J., Rüegsegger, A., Schoenenberger, N., and Spehn, E. (2020). Gene drives: benefits, risks, and possible applications. 15, 1-7. Dorigatti, I., McCormack, C., Nedjati-Gilani, G., and Ferguson, N.M. (2018). Using Wolbachia for Dengue Control: Insights from Modelling. Trends Parasitol 34, 102-113. Drake, L.L., Boudko, D.Y., Marinotti, O., Carpenter, V.K., Dawe, A.L., and Hansen, I.A. (2010). The Aquaporin gene family of the yellow fever mosquito, Aedes aegypti. PLoS One 5, e15578-e15578. Drake, L.L., Rodriguez, S.D., and Hansen, I.A. (2015). Functional characterization of aquaporins and aquaglyceroporins of the yellow fever mosquito, Aedes aegypti. Sci Rep 5, 7795-7795. Flores, H.A., and O'Neill, S.L. (2018). Controlling vector-borne diseases by releasing modified mosquitoes. Nat Rev Microbiol 16, 508-518. Glasner, D.R., Puerta-Guardo, H., Beatty, P.R., and Harris, E. (2018). The Good, the Bad, and the Shocking: The Multiple Roles of Dengue Virus Nonstructural Protein 1 in Protection and Pathogenesis. Annu Rev Virol 5, 227-253. Graf, R., and Briegel, H. (1989). The synthetic pathway of trypsin in the mosquito Aedes aegypti L. (Diptera: Culicidae) and in vitro stimulation in isolated midguts. Insect Biochemistry 19, 129-137. Guzhova, I., and Margulis, B. (2006). Hsp70 Chaperone as a Survival Factor in Cell Pathology. In International Review of Cytology (Academic Press), pp. 101-149. Guzman, M.G., Alvarez, M., and Halstead, S.B. (2013). Secondary infection as a risk factor for dengue hemorrhagic fever/dengue shock syndrome: an historical perspective and role of antibody-dependent enhancement of infection. Arch Virol 158, 1445-1459. Guzman, M.G., and Harris, E. (2015). Dengue. The Lancet 385, 453-465. Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579. Hartl, F.U., and Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858. Hastings, A.K., Uraki, R., Gaitsch, H., Dhaliwal, K., Stanley, S., Sproch, H., Williamson, E., MacNeil, T., Marin-Lopez, A., Hwang, J., et al. (2019). Aedes aegypti NeSt1 Protein Enhances Zika Virus Pathogenesis by Activating Neutrophils. J Virol 93. Hennessy, F., Nicoll, W.S., Zimmermann, R., Cheetham, M.E., and Blatch, G.L. (2005). Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions. Protein Sci 14, 1697-1709. Ivanyi-Nagy, R., Lavergne, J.-P., Gabus, C., Ficheux, D., and Darlix, J.-L. (2008). RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. Nucleic Acids Res 36, 712-725. Jung, J.S., Preston, G.M., Smith, B.L., Guggino, W.B., and Agre, P. (1994). Molecular structure of the water channel through aquaporin CHIP. The hourglass model. Journal of Biological Chemistry 269, 14648-14654. King, A.M., and MacRae, T.H. (2015). Insect heat shock proteins during stress and diapause. Annu Rev Entomol 60, 59-75. Kishor, A., Tandukar, B., Ly, Y.V., Toth, E.A., Suarez, Y., Brewer, G., and Wilson, G.M. (2013). Hsp70 is a novel posttranscriptional regulator of gene expression that binds and stabilizes selected mRNAs containing AU-rich elements. Mol Cell Biol 33, 71-84. Kishor, A., White, E.J.F., Matsangos, A.E., Yan, Z., Tandukar, B., and Wilson, G.M. (2017). Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions. J Biol Chem 292, 14122-14133. Li, X., Yang, J., Pu, Q., Peng, X., Xu, L., and Liu, S. (2019). Serine hydroxymethyltransferase controls blood-meal digestion in the midgut of Aedes aegypti mosquitoes. Parasit Vectors 12, 460. Lindenbach, B.D. (2007). Flaviviridae:The viruses and their replication. In Fields Virol, pp. 1101‐1152. Lu, S.J., Pennington, J.E., Stonehouse, A.R., Mobula, M.M., and Wells, M.A. (2006). Reevaluation of the role of early trypsin activity in the transcriptional activation of the late trypsin gene in the mosquito Aedes aegypti. Insect Biochem Mol Biol 36, 336-343. McMeniman, C.J., Lane, R.V., Cass, B.N., Fong, A.W.C., Sidhu, M., Wang, Y.-F., and Neill, S.L. (2009). Stable Introduction of a Life-Shortening lt;em gt;Wolbachia lt;/em gt; Infection into the Mosquito lt;em gt;Aedes aegypti lt;/em gt. Science 323, 141. Mitra, A., Menezes, M.E., Pannell, L.K., Mulekar, M.S., Honkanen, R.E., Shevde, L.A., and Samant, R.S. (2012). DNAJB6 chaperones PP2A mediated dephosphorylation of GSK3beta to downregulate beta-catenin transcription target, osteopontin. Oncogene 31, 4472-4483. Modis, Y., Ogata, S., Clements, D., and Harrison, S.C. (2004). Structure of the dengue virus envelope protein after membrane fusion. Nature 427, 313-319. Moreira, L.A., Iturbe-Ormaetxe, I., Jeffery, J.A., Lu, G., Pyke, A.T., Hedges, L.M., Rocha, B.C., Hall-Mendelin, S., Day, A., Riegler, M., et al. (2009). A Wolbachia symbiont in Aedes aegypti limits infection with dengue, Chikungunya, and Plasmodium. Cell 139, 1268-1278. Nascimento, O.J.M., and da Silva, I.R.F. (2017). Guillain–Barré syndrome and Zika virus outbreaks. Current Opinion in Neurology 30, 500-507. Netsawang, J., Noisakran, S., Puttikhunt, C., Kasinrerk, W., Wongwiwat, W., Malasit, P., Yenchitsomanus, P.T., and Limjindaporn, T. (2010). Nuclear localization of dengue virus capsid protein is required for DAXX interaction and apoptosis. Virus Res 147, 275-283. Neufeldt, C.J., Cortese, M., Acosta, E.G., and Bartenschlager, R. (2018). Rewiring cellular networks by members of the Flaviviridae family. Nat Rev Microbiol 16, 125-142. Ni, M., and Lee, A.S. (2007). ER chaperones in mammalian development and human diseases. FEBS Lett 581, 3641-3651. Noriega, F.G., Shah, D.K., and Wells, M.A. (1997). Juvenile hormone controls early trypsin gene transcription in the midgut of Aedes aegypti. Insect Mol Biol 6, 63-66. Park, S.H., Bolender, N., Eisele, F., Kostova, Z., Takeuchi, J., Coffino, P., and Wolf, D.H. (2007). The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol Biol Cell 18, 153-165. Pierson, T.C., and Diamond, M.S. (2012). Degrees of maturity: the complex structure and biology of flaviviruses. Curr Opin Virol 2, 168-175. Pierson, T.C., and Diamond, M.S. (2013). Flaviviruses. In Fields virology, D.M. Knipe, and P.M. Howley, eds., pp. 747-794. Qiu, X.B., Shao, Y.M., Miao, S., and Wang, L. (2006). The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63, 2560-2570. Ranford, J.C., Coates, A.R., and Henderson, B. (2000). Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev Mol Med 2, 1-17. Salazar, M.I., Richardson, J.H., Sanchez-Vargas, I., Olson, K.E., and Beaty, B.J. (2007). Dengue virus type 2: replication and tropisms in orally infected Aedes aegypti mosquitoes. BMC Microbiol 7, 9. Screaton, G., Mongkolsapaya, J., Yacoub, S., and Roberts, C. (2015). New insights into the immunopathology and control of dengue virus infection. Nat Rev Immunol 15, 745-759. Shiber, A., and Ravid, T. (2014). Chaperoning proteins for destruction: diverse roles of Hsp70 chaperones and their co-chaperones in targeting misfolded proteins to the proteasome. Biomolecules 4, 704-724. Shorter, J. (2011). The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6, e26319-e26319. Spring, J.H., Robichaux, S.R., and Hamlin, J.A. (2009). The role of aquaporins in excretion in insects. Journal of Experimental Biology 212, 358. Sreedharan, S., and Sankaranarayanan, K. (2019). Water channel activity of putative aquaporin-6 present in Aedes aegypti. Arch Insect Biochem Physiol 100, e21519. Taguwa, S., Maringer, K., Li, X., Bernal-Rubio, D., Rauch, J.N., Gestwicki, J.E., Andino, R., Fernandez-Sesma, A., and Frydman, J. (2015). Defining Hsp70 Subnetworks in Dengue Virus Replication Reveals Key Vulnerability in Flavivirus Infection. Cell 163, 1108-1123. Taguwa, S., Yeh, M.T., Rainbolt, T.K., Nayak, A., Shao, H., Gestwicki, J.E., Andino, R., and Frydman, J. (2019). Zika Virus Dependence on Host Hsp70 Provides a Protective Strategy against Infection and Disease. Cell Rep 26, 906-920 e903. Tan BH, Fu J, Sugrue RJ, Yap EH, Chan YC, and YH, T. (1996). Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity. Virology 216, 317-325. Tolle, M.A. (2009). Mosquito-borne diseases. Curr Probl Pediatr Adolesc Health Care 39, 97-140. Tsai, P.-J., and Teng, H.-J. (2016). Role of Aedes aegypti (Linnaeus) and Aedes albopictus (Skuse) in local dengue epidemics in Taiwan. BMC Infect Dis 16, 662-662. Vabulas, R.M., Raychaudhuri, S., Hayer-Hartl, M., and Hartl, F.U. (2010). Protein folding in the cytoplasm and the heat shock response. Cold Spring Harb Perspect Biol 2, a004390. Ventura, C.V., Maia, M., Bravo-Filho, V., Góis, A.L., and Belfort, R. (2016). Zika virus in Brazil and macular atrophy in a child with microcephaly. The Lancet 387. Walker, T., Johnson, P.H., Moreira, L.A., Iturbe-Ormaetxe, I., Frentiu, F.D., McMeniman, C.J., Leong, Y.S., Dong, Y., Axford, J., Kriesner, P., et al. (2011). The wMel Wolbachia strain blocks dengue and invades caged Aedes aegypti populations. Nature 476, 450-453. Wan, S.W., Wu-Hsieh, B.A., Lin, Y.S., Chen, W.Y., Huang, Y., and Anderson, R. (2018). The monocyte-macrophage-mast cell axis in dengue pathogenesis. J Biomed Sci 25, 77. Wang, S.-F., Wang, W.-H., Chang, K., Chen, Y.-H., Tseng, S.-P., Yen, C.-H., Wu, D.-C., and Chen, Y.-M.A. (2016a). Severe Dengue Fever Outbreak in Taiwan. Am J Trop Med Hyg 94, 193-197. Wang, S.F., Chang, K., Loh, E.W., Wang, W.H., Tseng, S.P., Lu, P.L., Chen, Y.H., and Chen, Y.A. (2016b). Consecutive large dengue outbreaks in Taiwan in 2014-2015. Emerg Microbes Infect 5, e123. Watkinson-Powell, B., and Alphey, N. (2017). Resistance to genetic insect control: Modelling the effects of space. Journal of Theoretical Biology 413, 72-85. Welsch, S., Miller, S., Romero-Brey, I., Merz, A., Bleck, C.K.E., Walther, P., Fuller, S.D., Antony, C., Krijnse-Locker, J., and Bartenschlager, R. (2009). Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell host microbe 5, 365-375. Werren, J.H., Baldo, L., and Clark, M.E. (2008). Wolbachia: master manipulators of invertebrate biology. Nat Rev Microbiol 6, 741-751. Whitehead, S.S. (2016). Development of TV003/TV005, a single dose, highly immunogenic live attenuated dengue vaccine; what makes this vaccine different from the Sanofi-Pasteur CYD™ vaccine? Expert Rev Vaccines 15, 509-517. WHO (2020). World malaria report 2020: 20 years of global progress and challenges (Geneva:World Health Organization). Woolfit, M., Iturbe-Ormaetxe, I., Brownlie, J.C., Walker, T., Riegler, M., Seleznev, A., Popovici, J., Rancès, E., Wee, B.A., Pavlides, J., et al. (2013). Genomic evolution of the pathogenic Wolbachia strain, wMelPop. Genome Biol Evol 5, 2189-2204. Xiao, X., Liu, Y., Zhang, X., Wang, J., Li, Z., Pang, X., Wang, P., and Cheng, G. (2014). Complement-Related Proteins Control the Flavivirus Infection of Aedes aegypti by Inducing Antimicrobial Peptides. PLOS Pathogens 10, e1004027. Xie, X., Zou, J., Zhang, X., Zhou, Y., Routh, A.L., Kang, C., Popov, V.L., Chen, X., Wang, Q.Y., Dong, H., et al. (2019). Dengue NS2A Protein Orchestrates Virus Assembly. Cell Host Microbe 26, 606-622 e608. Ye, Y.H., Carrasco, A.M., Frentiu, F.D., Chenoweth, S.F., Beebe, N.W., van den Hurk, A.F., Simmons, C.P., O'Neill, S.L., and McGraw, E.A. (2015). Wolbachia Reduces the Transmission Potential of Dengue-Infected Aedes aegypti. PLoS Negl Trop Dis 9, e0003894. Yu, I.M., Zhang, W., Holdaway, H.A., Li, L., Kostyuchenko, V.A., Chipman, P.R., Kuhn, R.J., Rossmann, M.G., and Chen, J. (2008). Structure of the Immature Dengue Virus at Low pH Primes Proteolytic Maturation. Science 319, 1834. Zhang, L., Fok, J.H., and Davies, F.E. (2014). Heat shock proteins in multiple myeloma. Oncotarget 5, 1132-1148. Zhang, Q., Hunke, C., Yau, Y.H., Seow, V., Lee, S., Tanner, L.B., Guan, X.L., Wenk, M.R., Fibriansah, G., Chew, P.L., et al. (2012). The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation. J Biol Chem 287, 40525-40534. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/82174 | - |
| dc.description.abstract | "登革熱為熱帶及亞熱帶地區嚴重的蚊媒疾病，全球每年大約有1億個登革熱感染病例，造成大約3萬人死亡。由於目前尚無安全有效的疫苗以及治療藥物，因此防疫大多仰賴噴灑殺蟲劑，但過量使用殺蟲劑又造成抗藥性的問題，因此積極開發新型替代性方案是當務之急。根據過去的文獻指出，人類的熱休克蛋白A8(heat shock protein A8, 又名熱休克蛋白70, HSC70)在登革病毒的感染扮演重要角色，但病媒蚊的熱休克蛋白對於登革病毒的影響則尚不清楚。因此，本研究以登革熱的主要病媒蚊-埃及斑蚊為研究模式，探討埃及斑蚊的熱休克蛋白參與登革病毒複製的功能性分析。我們以蛋白質序列比對的方式找到埃及斑蚊體內與人類HSC70類似的蛋白並命名為AaHsp70-403，再利用RNAi的方式抑制埃及斑蚊體內AaHsp70-403表現，並分析其對於登革病毒的影響。我們的結果顯示AaHsp70-403受到抑制後，會明顯抑制登革病毒的mRNA、蛋白質產生以及病毒感染力，我們也證實AaHsp70-403受到抑制會使capsid蛋白更容易產生不正常聚集，顯示AaHsp70-403為參與登革病毒複製的重要因子。而另一方面，我們也發現AaHsp70-403會透過調節埃及斑蚊trypsin及aquaporin的表現，進而影響吸血後對於血液的消化以及水份排出，最終會導致卵巢發育受影響而出現產卵異常的現象。我們的結果顯示埃及斑蚊的熱休克蛋白70對於登革病毒複製的控制以及病媒生殖調控扮演重要的角色。" | zh_TW |
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| dc.description.tableofcontents | 致謝 i 中文摘要 ii Abstract iii 目錄 iv 圖目錄 viii 表目錄 ix 第一章 緒論 1 1.1 病媒蚊傳播疾病 (mosquito-borne disease) 1 1.1.1 瘧疾 (malaria) 1 1.1.2 茲卡病毒感染症 (Zika virus infection) 2 1.2 登革熱 (Dengue fever) 2 1.2.1 登革病毒 (Dengue virus; DENV) 2 1.2.2 臨床症狀 3 1.2.3 對付登革病毒之策略 3 1.2.4 台灣之登革熱 6 1.3 埃及斑蚊 (Aedes aegypti) 6 1.3.1 埃及斑蚊生活史 6 1.3.2 埃及斑蚊吸血後排水行為 7 1.3.3 埃及斑蚊吸血後消化行為 7 1.4 登革病毒生活史 8 1.4.1 宿主細胞內之複製 8 1.4.2 病媒蚊體內之複製 9 1.5 熱休克蛋白 (Heat Shock Protein; Chaperone) 9 1.5.1 熱休克蛋白重要性 9 1.5.2 熱休克蛋白定義與分類 10 1.5.3 熱休克蛋白70 10 1.6 實驗動機與假說 11 第二章 實驗材料與方法 12 2.1 實驗步驟與流程 12 2.1.1 埃及斑蚊飼養與繼代培養 12 2.1.2 細胞培養 (cell culture) 12 2.1.3 病毒製備 12 2.1.4 雙股RNA (double-stranded RNA; dsRNA) 13 2.1.4.1 質體建構 (plasmid constuction)與保存 13 2.1.4.2 雙股RNA合成 (dsRNA synthesis) 14 2.1.5 顯微注射 (microinjection) 14 2.1.5.1 病毒注射 (virus injection) 14 2.1.5.2 dsRNA注射 (dsRNA injection) 15 2.1.6 RNA萃取 (RNA extraction) 15 2.1.7 反轉錄作用 (Reverse transcription; RT) 15 2.1.8 聚合酶連鎖反應 (Polymerase chain reaction; PCR) 16 2.1.9 PCR篩選菌落法 (Colony polymerase chain reaction; Colony PCR) 16 2.1.10 即時定量聚合酶連鎖反應 (Real-time PCR; Quantitative PCR) 16 2.1.11 蛋白質萃取(Protein extraction) 17 2.1.12 西方點墨法 (Western blotting) 17 2.1.13 Focus forming assay (FFA) 18 2.1.14 產卵試驗 (Oviposition) 19 2.1.15 卵巢發育試驗 (Ovary development) 19 2.1.16 免疫沉澱試驗 (Immunoprecipitation assay) 19 2.1.17 組織免疫螢光染色實驗 (Immunofluorescent assay; IFA) 19 2.1.18 Coomassie blue staining 20 2.1.19 血液消化試驗 20 2.1.20 排水試驗 21 2.1.21 Filter trap assay 21 2.2 實驗試劑製備 21 第三章 結果 25 3.1 尋找與人類HspA8相似之埃及斑蚊Hsp70 25 3.2 埃及斑蚊Hsp70感染前後於各組織間RNA表現 25 3.3埃及斑蚊Hsp70與DENV2之關係 26 3.4 埃及斑蚊Hsp70與DENV2之交互關係 28 3.5 埃及斑蚊Hsp70-403對於產卵與卵巢發育之重要性 29 3.6埃及斑蚊Hsp70-403對於血液消化之重要性 31 3.7 埃及斑蚊Hsp70-403對於排水之重要性 32 3.8 埃及斑蚊Hsp70-403與其他AaHsp70之關係 33 第四章 討論 35 4.1 抑制AaHsp70-403對於病毒的影響 35 4.2 AaHsp70-403對於消化與排水的調控 35 4.3 吸血後AaHsp70的表現對於病毒的影響 36 4.4 AaHsp70-403與AaBip的關聯性 37 4.5 AaHsp70-403作為新型病蚊媒控制標的之可行性 37 附圖 39 附表 64 附錄 67 附錄一、人類與埃及斑蚊Hsp70之比較 68 附錄二、DENV2感染前後各組織間AaDnaJB6表現 69 附錄三、RNAi抑制AaDnaJB6效果 70 附錄四、抑制AaDnaJB6對DENV2 mRNA複製影響 72 附錄五、抑制AaDnaJB6對DENV2蛋白生合成無顯著影響 73 附錄六、抑制AaDnaJB6對DENV2感染力無顯著影響 74 參考資料 75 | |
| dc.language.iso | zh-TW | |
| dc.subject | 熱休克蛋白70 | zh_TW |
| dc.subject | 埃及斑蚊 | zh_TW |
| dc.subject | 生殖 | zh_TW |
| dc.subject | 病毒複製 | zh_TW |
| dc.subject | 登革病毒 | zh_TW |
| dc.subject | reproduction | en |
| dc.subject | Aedes aegypti | en |
| dc.subject | dengue virus | en |
| dc.subject | Hsp70 | en |
| dc.subject | virus replication | en |
| dc.title | 埃及斑蚊Hsp70在登革病毒複製與病媒生殖調控的雙重角色 | zh_TW |
| dc.title | Dual roles of Aedes aegypti Hsp70 in the control of dengue virus replication and mosquito reproduction | en |
| dc.date.schoolyear | 109-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 劉旻禕(Hsin-Tsai Liu),林志萱(Chih-Yang Tseng) | |
| dc.subject.keyword | 埃及斑蚊,登革病毒,熱休克蛋白70,病毒複製,生殖, | zh_TW |
| dc.subject.keyword | Aedes aegypti,dengue virus,Hsp70,virus replication,reproduction, | en |
| dc.relation.page | 86 | |
| dc.identifier.doi | 10.6342/NTU202102113 | |
| dc.rights.note | 未授權 | |
| dc.date.accepted | 2021-08-06 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 微生物學研究所 | zh_TW |
| dc.date.embargo-lift | 2026-08-05 | - |
| 顯示於系所單位： | 微生物學科所 | |
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