請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/25086
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 李佳音 | |
dc.contributor.author | Yu-Huei Chan | en |
dc.contributor.author | 詹于慧 | zh_TW |
dc.date.accessioned | 2021-06-08T06:01:57Z | - |
dc.date.copyright | 2011-08-10 | |
dc.date.issued | 2011 | |
dc.date.submitted | 2011-08-05 | |
dc.identifier.citation | 劉以葭。2007。探討腸炎弧菌幾丁質酶A所扮演的角色及功能。國立台灣大學農業化學系碩士論文
張絜雯。2009。胞外絲胺酸蛋白酶對腸炎弧菌生物膜生成及遊走能力之影響。國立台灣大學農業化學系碩士論文 劉嘉玲等人。2009。2009年臺灣沿岸港埠鄰近海域致病性弧菌屬分布調查。衛生署疾病管制局疫情報導。第 27 卷,第 4 期, 42-49。 Anguiano-Beltran, C., Lizarraga-Partida, M.L., and Searcy-Bernal, R. (2004). Effect of Vibrio alginolyticus on larval survival of the blue mussel Mytilus galloprovincialis. Dis Aquat Organ 59, 119-123. Balebona, M.C., Andreu, M.J., Bordas, M.A., Zorrilla, I., Morinigo, M.A., and Borrego, J.J. (1998). Pathogenicity of Vibrio alginolyticus for cultured gilt-head sea bream (Sparus aurata L.). Appl Environ Microbiol 64, 4269-4275. Benitez, J.A., Spelbrink, R.G., Silva, A., Phillips, T.E., Stanley, C.M., Boesman-Finkelstein, M., and Finkelstein, R.A. (1997). Adherence of Vibrio cholerae to cultured differentiated human intestinal cells: an in vitro colonization model. Infect Immun 65, 3474-3477. Booth, B.A., Boesman-Finkelstein, M., and Finkelstein, R.A. (1983). Vibrio cholerae soluble hemagglutinin/protease is a metalloenzyme. Infect Immun 42, 639-644. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254. Burnet, F.M. (1948). The mucinase of V. cholerae. Aust J Exp Biol Med Sci 26, 71-80. Bullock, W. O., Fernandez, J. M. and Short, J. M. (1987) XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques 5, 376-379 Cabello, F.C., Espejo, R.T., Hernandez, M.C., Rioseco, M.L., Ulloa, J., and Vergara, J.A. (2007). Vibrio parahaemolyticus O3:K6 epidemic diarrhea, Chile, 2005. Emerg Infect Dis 13, 655-656. Cai, S.H., Wu, Z.H., Jian, J.C., and Lu, Y.S. (2007). Cloning and expression of the gene encoding an extracellular alkaline serine protease from Vibrio alginolyticus strain HY9901, the causative agent of vibriosis in Lutjanus erythopterus. J Fish Dis 30, 493-500. Fabbri, A., Falzano, L., Frank, C., Donelli, G., Matarrese, P., Raimondi, F., Fasano, A., and Fiorentini, C. (1999). Vibrio parahaemolyticus thermostable direct hemolysin modulates cytoskeletal organization and calcium homeostasis in intestinal cultured cells. Infect Immun 67, 1139-1148. Finkelstein, R.A., Boesman-Finkelstein, M., Chang, Y., and Hase, C.C. (1992). Vibrio cholerae hemagglutinin/protease, colonial variation, virulence, and detachment. Infect Immun 60, 472-478. Finkelstein, R.A., Boesman-Finkelstein, M., and Holt, P. (1983). Vibrio cholerae hemagglutinin/lectin/protease hydrolyzes fibronectin and ovomucin: F.M. Burnet revisited. Proc Natl Acad Sci U.S.A 80, 1092-1095. Fuqua, C., Parsek, M.R., and Greenberg, E.P. (2001). Regulation of gene expression by cell-to-cell communication: acyl-homoserine lactone quorum sensing. Annu Rev Genet 35, 439-468. Gode-Potratz C.J. and McCarter L.L.(2011). Quorum sensing and silencing in Vibrio parahaemolyticus. J Bacteriol 191, 6911-6917. Gomez-Leon, J., Villamil, L., Lemos, M.L., Novoa, B., and Figueras, A. (2005). Isolation of Vibrio alginolyticus and Vibrio splendidus from aquacultured carpet shell clam (Ruditapes decussatus) larvae associated with mass mortalities. Appl Environ Microbiol 71, 98-104. Goshima, K., Honda, T., Hirata, M., Kikuchi, K., and Takeda, Y. (1977). Stopping of the spontaneous beating of mouse and rat myocardial cells in vitro by a toxin from Vibrio parahaemolyticus. J Mol Cell Cardiol 9, 191-213. Hervio-Heath, D., Colwell, R.R., Derrien, A., Robert-Pillot, A., Fournier, J.M., and Pommepuy, M. (2002). Occurrence of pathogenic vibrios in coastal areas of France. J Appl Microbiol 92, 1123-1135. Higgins, D.A., Pomianek, M.E., Kraml, C.M., Taylor, R.K., Semmelhack, M.F., and Bassler, B.L. (2007). The major Vibrio cholerae autoinducer and its role in virulence factor production. Nature 450, 883-886. Hillen, W., and Berens, C. (1994). Mechanisms underlying expression of Tn10 encoded tetracycline resistance. Annu Rev Microbiol 48, 345-369. Honda, T., Goshima, K., Takeda, Y., Sugino, Y., and Miwatani, T. (1976). Demonstration of the cardiotoxicity of the thermostable direct hemolysin (lethal toxin) produced by Vibrio parahaemolyticus. Infect Immun 13, 163-171. Horsburgh, M.J., Aish, J.L., White, I.J., Shaw, L., Lithgow, J.K., and Foster, S.J. (2002). sigmaB modulates virulence determinant expression and stress resistance: characterization of a functional rsbU strain derived from Staphylococcus aureus 8325-4. J Bacteriol 184, 5457-5467. Irving, J.A., Steenbakkers, P.J., Lesk, A.M., Op den Camp, H.J., Pike, R.N., and Whisstock, J.C. (2002). Serpins in prokaryotes. Mol Biol Evol 19, 1881-1890. Janda, J.M., Powers, C., Bryant, R.G., and Abbott, S.L. (1988). Current perspectives on the epidemiology and pathogenesis of clinically significant Vibrio spp. Clin Microbiol Rev 1, 245-267. Jaques, S., and McCarter, L.L. (2006). Three new regulators of swarming in Vibrio parahaemolyticus. J Bacteriol 188, 2625-2635. Ji, G., Beavis, R.C., and Novick, R.P. (1995). Cell density control of staphylococcal virulence mediated by an octapeptide pheromone. Proc Natl Acad Sci U.S.A. 92, 12055-12059. Jobling, M.G., and Holmes, R.K. (1997). Characterization of hapR, a positive regulator of the Vibrio cholerae HA/protease gene hap, and its identification as a functional homologue of the Vibrio harveyi luxR gene. Mol Microbiol 26, 1023-1034. Jude, B.A., Martinez, R.M., Skorupski, K., and Taylor, R.K. (2009). Levels of the secreted Vibrio cholerae attachment factor GbpA are modulated by quorum-sensing-induced proteolysis. J Bacteriol 191, 6911-6917. Kang, S., Barak, Y., Lamed, R., Bayer, E.A., and Morrison, M. (2006). The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors. Mol Microbiol 60, 1344-1354. Kawase, T., Miyoshi, S., Sultan, Z., and Shinoda, S. (2004). Regulation system for protease production in Vibrio vulnificus. FEMS Microbiol Lett 240, 55-59. Kim, S.K., Yang, J.Y., and Cha, J. (2002). Cloning and sequence analysis of a novel metalloprotease gene from Vibrio parahaemolyticus 04. Gene 283, 277-286. Kirn, T.J., Jude, B.A., and Taylor, R.K. (2005). A colonization factor links Vibrio cholerae environmental survival and human infection. Nature 438, 863-866. L, S.K., Hilli, L., Orlowski, J., Kupperman, J.L., Baral, M., and R, F.W. (2006). Efficacy of probiotics and nutrients in functional gastrointestinal disorders: a preliminary clinical trial. Dig Dis Sci 51, 2134-2144. Lee, C.Y., Cheng, M.F., Yu, M.S., and Pan, M.J. (2002). Purification and characterization of a putative virulence factor, serine protease, from Vibrio parahaemolyticus. FEMS Microbiol Lett 209, 31-37. Lee, C.Y., Su, S.C., and Liaw, R.B. (1995). Molecular analysis of an extracellular protease gene from Vibrio parahaemolyticus. Microbiology 141, 2569-2576. Ling, M.M., and Robinson, B.H. (1997). Approaches to DNA mutagenesis: an overview. Anal Biochem 254, 157-178. Makino, K., Oshima, K., Kurokawa, K., Yokoyama, K., Uda, T., Tagomori, K., Iijima, Y., Najima, M., Nakano, M., Yamashita, A., et al. (2003). Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V cholerae. Lancet 361, 743-749. Martinez-Urtaza, J., Simental, L., Velasco, D., DePaola, A., Ishibashi, M., Nakaguchi, Y., Nishibuchi, M., Carrera-Flores, D., Rey-Alvarez, C., and Pousa, A. (2005). Pandemic Vibrio parahaemolyticus O3:K6, Europe. Emerg Infect Dis 11, 1319-1320. McCarter, L.L. (1998). OpaR, a homolog of Vibrio harveyi LuxR, controls opacity of Vibrio parahaemolyticus. J Bacteriol 180, 3166-3173. McDougald, D., Rice, S.A., and Kjelleberg, S. (2001). SmcR-dependent regulation of adaptive phenotypes in Vibrio vulnificus. J Bacteriol 183, 758-762. Miyamoto, Y., Kato, T., Obara, Y., Akiyama, S., Takizawa, K., and Yamai, S. (1969). In vitro hemolytic characteristic of Vibrio parahaemolyticus: its close correlation with human pathogenicity. J Bacteriol 100, 1147-1149. Miyashiro, T., Wollenberg, M.S., Cao, X., Oehlert, D., and Ruby, E.G. (2010). A single qrr gene is necessary and sufficient for LuxO-mediated regulation in Vibrio fischeri. Mol Microbiol 77, 1556-1567. Miyoshi, S., Nakazawa, H., Kawata, K., Tomochika, K., Tobe, K., and Shinoda, S. (1998). Characterization of the hemorrhagic reaction caused by Vibrio vulnificus metalloprotease, a member of the thermolysin family. Infect Immun 66, 4851-4855. Miyoshi, S., Nitanda, Y., Fujii, K., Kawahara, K., Li, T., Maehara, Y., Ramamurthy, T., Takeda, Y., and Shinoda, S. (2008). Differential gene expression and extracellular secretion of the collagenolytic enzymes by the pathogen Vibrio parahaemolyticus. FEMS Microbiol Lett 283, 176-181. Miyoshi, S., Sonoda, Y., Wakiyama, H., Rahman, M.M., Tomochika, K., Shinoda, S., Yamamoto, S., and Tobe, K. (2002). An exocellular thermolysin-like metalloprotease produced by Vibrio fluvialis: purification, characterization, and gene cloning. Microb Pathog 33, 127-134. Naim, R., Yanagihara, I., Iida, T., and Honda, T. (2001). Vibrio parahaemolyticus thermostable direct hemolysin can induce an apoptotic cell death in Rat-1 cells from inside and outside of the cells. FEMS Microbiol Lett 195, 237-244. Nair, G.B., Ramamurthy, T., Bhattacharya, S.K., Dutta, B., Takeda, Y., and Sack, D.A. (2007). Global dissemination of Vibrio parahaemolyticus serotype O3:K6 and its serovariants. Clin Microbiol Rev 20, 39-48. Ng, W.L., and Bassler, B.L. (2009). Bacterial quorum-sensing network architectures. Annu Rev Genet 43, 197-222. Nishibuchi, M., and Kaper, J.B. (1995). Thermostable direct hemolysin gene of Vibrio parahaemolyticus: a virulence gene acquired by a marine bacterium. Infect Immun 63, 2093-2099. Nomura, T., Hamashima, H., and Okamoto, K. (2000). Carboxy terminal region of haemolysin of Aeromonas sobria triggers dimerization. Microb Pathog 28, 25-36. Ottaviani, D., Leoni, F., Rocchegiani, E., Santarelli, S., Canonico, C., Masini, L., Ditrani, V., and Carraturo, A. (2008). First clinical report of pandemic Vibrio parahaemolyticus O3:K6 infection in Italy. J Clin Microbiol 46, 2144-2145. Pesci, E.C., Milbank, J.B., Pearson, J.P., McKnight, S., Kende, A.S., Greenberg, E.P., and Iglewski, B.H. (1999). Quinolone signaling in the cell-to-cell communication system of Pseudomonas aeruginosa. Proc Natl Acad Sci U.S.A. 96, 11229-11234. Philippe, N., Alcaraz, J.P., Coursange, E., Geiselmann, J., and Schneider, D. (2004). Improvement of pCVD442, a suicide plasmid for gene allele exchange in bacteria. Plasmid 51, 246-255. Pompeani, A.J., Irgon, J.J., Berger, M.F., Bulyk, M.L., Wingreen, N.S., and Bassler, B.L. (2008). The Vibrio harveyi master quorum-sensing regulator, LuxR, a TetR-type protein is both an activator and a repressor: DNA recognition and binding specificity at target promoters. Mol Microbiol 70, 76-88. Raimondi, F., Kao, J.P., Fiorentini, C., Fabbri, A., Donelli, G., Gasparini, N., Rubino, A., and Fasano, A. (2000). Enterotoxicity and cytotoxicity of Vibrio parahaemolyticus thermostable direct hemolysin in in vitro systems. Infect Immun 68, 3180-3185. Rajamani, S., and Sayre, R.T. (2011). A sensitive fluorescence reporter for monitoring quorum sensing regulated protease production in Vibrio harveyi. J Microbiol Methods 84, 189-193. Ramos, J.L., Martinez-Bueno, M., Molina-Henares, A.J., Teran, W., Watanabe, K., Zhang, X., Gallegos, M.T., Brennan, R., and Tobes, R. (2005). The TetR family of transcriptional repressors. Microbiol Mol Biol Rev 69, 326-356. Robert-Pillot, A., Guenole, A., Lesne, J., Delesmont, R., Fournier, J.M., and Quilici, M.L. (2004). Occurrence of the tdh and trh genes in Vibrio parahaemolyticus isolates from waters and raw shellfish collected in two French coastal areas and from seafood imported into France. Int J Food Microbiol 91, 319-325. Rui, H., Liu, Q., Ma, Y., Wang, Q., and Zhang, Y. (2008). Roles of LuxR in regulating extracellular alkaline serine protease A, extracellular polysaccharide and mobility of Vibrio alginolyticus. FEMS Microbiol Lett 285, 155-162. Rui, H., Liu, Q., Wang, Q., Ma, Y., Liu, H., Shi, C., and Zhang, Y. (2009). Role of alkaline serine protease, asp, in Vibrio alginolyticus virulence and regulation of its expression by luxO-luxR regulatory system. J Microbiol Biotechnol 19, 431-438. Saka, H.A., Bidinost, C., Sola, C., Carranza, P., Collino, C., Ortiz, S., Echenique, J.R., and Bocco, J.L. (2008). Vibrio cholerae cytolysin is essential for high enterotoxicity and apoptosis induction produced by a cholera toxin gene-negative V. cholerae non-O1, non-O139 strain. Microb Pathog 44, 118-128. Sakurai, J., Honda, T., Jinguji, Y., Arita, M., and Miwatani, T. (1976). Cytotoxic effect of the thermostable direct hemolysin produced by Vibrio parahaemolyticus on FL cells. Infect Immun 13, 876-883. Sarkar, B.L., Kumar, R., De, S.P., and Pal, S.C. (1987a). Hemolytic activity of and lethal toxin production by environmental strains of Vibrio parahaemolyticus. Appl Environ Microbiol 53, 2696-2698. Sarkar, B.L., Kumar, R., De, S.P., and Pal, S.C. (1987b). Observation on a 65-kilodalton protein isolated from kanagawa positive strains of Vibrio parahaemolyticus. Can J Microbiol 33, 1113-1116. Schafer, A., Kalinowski, J., Simon, R., Seep-Feldhaus, A.H., and Puhler, A. (1990). High-frequency conjugal plasmid transfer from gram-negative Escherichia coli to various gram-positive coryneform bacteria. J Bacteriol 172, 1663-1666. Schauder, S., Shokat, K., Surette, M.G., and Bassler, B.L. (2001). The LuxS family of bacterial autoinducers: biosynthesis of a novel quorum-sensing signal molecule. Mol Microbiol 41, 463-476. Schwarz, W.H., and Zverlov, V.V. (2006). Protease inhibitors in bacteria: an emerging concept for the regulation of bacterial protein complexes? Mol Microbiol 60, 1323-1326. Shao, C.P., and Hor, L.I. (2001). Regulation of metalloprotease gene expression in Vibrio vulnificus by a Vibrio harveyi LuxR homologue. J Bacteriol 183, 1369-1375. Shaw, L., Golonka, E., Potempa, J., and Foster, S.J. (2004). The role and regulation of the extracellular proteases of Staphylococcus aureus. Microbiology 150, 217-228. Showalter, R.E., Martin, M.O., and Silverman, M.R. (1990). Cloning and nucleotide sequence of luxR, a regulatory gene controlling bioluminescence in Vibrio harveyi. J Bacteriol 172, 2946-2954. Takahashi, A., Iida, T., Naim, R., Naykaya, Y., and Honda, T. (2001). Chloride secretion induced by thermostable direct haemolysin of Vibrio parahaemolyticus depends on colonic cell maturation. J Med Microbiol 50, 870-878. Tang, G., Iida, T., Yamamoto, K., and Honda, T. (1997). Analysis of functional domains of Vibrio parahaemolyticus thermostable direct hemolysin using monoclonal antibodies. FEMS Microbiol Lett 150, 289-296. Tang, G.Q., Iida, T., Yamamoto, K., and Honda, T. (1995). Ca(2+)-independent cytotoxicity of Vibrio parahaemolyticus thermostable direct hemolysin (TDH) on Intestine 407, a cell line derived from human embryonic intestine. FEMS Microbiol Lett 134, 233-238. Tsou, A.M., and Zhu, J. (2010). Quorum sensing negatively regulates hemolysin transcriptionally and posttranslationally in Vibrio cholerae. Infect Immun 78, 461-467. Vaitkevicius, K., Lindmark, B., Ou, G., Song, T., Toma, C., Iwanaga, M., Zhu, J., Andersson, A., Hammarstrom, M.L., Tuck, S., et al. (2006). A Vibrio cholerae protease needed for killing of Caenorhabditis elegans has a role in protection from natural predator grazing. Proc Natl Acad Sci U.S.A. 103, 9280-9285. Wang, H., and Griffiths, M.W. (2009). Mg2+-free buffer elevates transformation efficiency of Vibrio parahaemolyticus by electroporation. Lett Appl Microbiol 48, 349-354. Winzer, K., Hardie, K.R., and Williams, P. (2002). Bacterial cell-to-cell communication: sorry, can't talk now - gone to lunch! Curr Opin Microbiol 5, 216-222. Xavier, K.B., and Bassler, B.L. (2003). LuxS quorum sensing: more than just a numbers game. Curr Opin Microbiol 6, 191-197. Yanagihara, I., Nakahira, K., Yamane, T., Kaieda, S., Mayanagi, K., Hamada, D., Fukui, T., Ohnishi, K., Kajiyama, S., Shimizu, T., et al. (2010). Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. J Biol Chem 285, 16267-16274. Yu, M.S., Yap, M.N., and Lee, C.Y. (2000). Metal content and biochemical analyses of a recombinant collagenase PrtV from Vibrio parahaemolyticus. Microbiol Immunol 44, 805-813. Zhu, J., and Mekalanos, J.J. (2003). Quorum sensing-dependent biofilms enhance colonization in Vibrio cholerae. Dev Cell 5, 647-656. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/25086 | - |
dc.description.abstract | 腸炎弧菌(Vibrio parahaemolyticus)屬於革蘭氏陰性的細菌,生長於海洋及河川出海口。人類因為食用受汙染的魚或有殼海鮮類而受感染造成腹瀉症狀,或者是不慎傷口曝於受汙染的海水造成感染。Vibrio parahaemolyticus No. 93 為一株不具有 tdh 及 trh 溶血素之台灣臨床分離株。其胞外鹼性絲胺酸蛋白酶,PrtA(VPA0227),已證實為可能的致病因子。由於哈維氏弧菌(Vibrio harveyi)及溶藻弧菌(Vibrio alginolyticus)之胞外蛋白酶受 LuxR 同源性蛋白質所調控,而且弧菌屬中 LuxO-LuxR 系統具有高度保留性,在 PrtA 啟動子上游具有 LuxR 結合的保守序列。本研究目的為探討腸炎弧菌 No. 93 的胞外蛋白酶 PrtA 是否會受 LuxR 之同源蛋白質, OpaR(VP2516),所調控。本研究以先決條件分析(Precondition assay)得知腸炎弧菌之胞外蛋白酶活性受 LuxO-OpaR 系統影響。分別構築腸炎弧菌LuxO 和 OpaR 的突變株和補償株,在 Heart Infusion soft Agar 上觀察遊走能力的表現型態,證實 OpaR 會抑制腸炎弧菌的遊走能力。然而受測試菌的菌落透明度均無明顯地變化。此外, Q-PCR的結果顯示 prtA 和 vppC 的轉錄表現時間不同,分別在 3 和 6 小時其轉錄表現量最高,胞外蛋白酶 prtV 則是以穩定的方式持續表現。突變株 | zh_TW |
dc.description.provenance | Made available in DSpace on 2021-06-08T06:01:57Z (GMT). No. of bitstreams: 1 ntu-100-R98623006-1.pdf: 2180441 bytes, checksum: f231820a57cca717e7a3720d18f83465 (MD5) Previous issue date: 2011 | en |
dc.description.tableofcontents | 論文審定書…………………………………………………………………..i
中文摘要…………………………………………………………………….ii 英文摘要……………………………………………………………………iv 目錄………………………………………………………………………....vi 表次………………………………………………………………………….x 圖次…………………………………………………………………………xi 附圖次……………………………………………………………………...xii 縮寫表……………………………………………………………………..xiii 腸炎弧菌基因體序列代碼………………………………………………..xiv 壹、 前言 1 一、 腸炎弧菌(Vibrio parahaemolyticus)……………………..………1 1.1 概論 1 1.2 性狀 2 1.3 毒力因子 3 二、 胞外蛋白酶(Extracellular protease)……………………………..4 1.1 概論 4 1.2 弧菌屬(Vibrio spp.)之相關研究 5 1.3 弧菌屬中 LuxR 同源基因對於胞外蛋白酶調控的研究 6 1.4 溶藻弧菌 LuxR 同源基因對於胞外蛋白酶調控的研究 6 1.5 創傷弧菌 SmcR 對於胞外蛋白酶調控的研究 8 1.6 霍亂弧菌 HapR 對於胞外蛋白酶調控的研究 8 1.7 腸炎弧菌胞外蛋白酶調控的研究 9 1.8 其他細菌胞外蛋白酶調控之研究 10 三、 定額感應系統(Quorum sensing system)………………………11 1.1 概述 11 1.2 哈維氏弧菌(Vibrio harveyi)的定額感應系統概述 11 1.3 哈維氏弧菌 LuxR 的研究 12 1.4 腸炎弧菌 OpaR 的研究 13 1.5 各種自誘物質之簡介 14 四、 其他細菌定額感應系統的概述 14 五、 研究目的與動機 15 貳、 實驗材料與方法 16 一、 實驗材料 16 1 實驗菌株、質體與引子 16 2 培養基與培養條件 16 3 化學藥品與材料來源 17 4 儀器 17 二、 實驗方法 18 1 DNA 技術 18 2 RNA 技術 22 3 蛋白質技術 25 4 分析腸炎弧菌野生株與突變株基本生理特性與基因表現 29 5 建構突變株 31 6 建構補償株 36 7 生物資訊庫軟體分析 39 8 統計分析 40 參、 實驗結果 41 一、 腸炎弧菌之胞外蛋白酶活性受定額感應系統影響 41 二、 弧菌屬中同源蛋白質之序列比對 41 三、 建構腸炎弧菌 NO. 93 之突變株 42 四、 建構腸炎弧菌 NO. 93 之補償株 44 五、 觀察菌株遊走能力與菌落透明度之差異 44 六、 比較菌株生長速率與胞外蛋白酶活性表現 45 七、 抑制劑對菌株胞外蛋白酶活性之影響 45 八、 隨時間觀察腸炎弧菌 NO. 93 胞外蛋白酶基因轉錄之差異 46 九、 比較菌株間胞外蛋白酶基因轉錄之差異 47 十、 以西方墨點法比較菌株間胞外蛋白酶表現之差異 48 肆、 討論 49 一、 小型RNA分子於弧菌屬中之重要性 49 二、 胞外蛋白酶受抑制劑之影響 49 三、 胞外蛋白酶於腸炎弧菌表現之消長情形 51 四、 定額感應系統對腸炎弧菌 NO. 93 之影響 52 伍、 結論 53 陸、 參考文獻 54 柒、 表 70 捌、 圖 76 玖、 附錄圖 98 | |
dc.language.iso | zh-TW | |
dc.title | 腸炎弧菌胞外蛋白酶 PrtA 調控機制之研究 | zh_TW |
dc.title | The regulation of extracellular protease PrtA from Vibrio parahaemolyticus | en |
dc.type | Thesis | |
dc.date.schoolyear | 99-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 彭雲明,賴信志,羅凱尹 | |
dc.subject.keyword | 腸炎弧菌,胞外蛋白酶, | zh_TW |
dc.subject.keyword | Vibrio parahaemolyticus,extracellular protease, | en |
dc.relation.page | 100 | |
dc.rights.note | 未授權 | |
dc.date.accepted | 2011-08-05 | |
dc.contributor.author-college | 生物資源暨農學院 | zh_TW |
dc.contributor.author-dept | 農業化學研究所 | zh_TW |
顯示於系所單位: | 農業化學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-100-1.pdf 目前未授權公開取用 | 2.13 MB | Adobe PDF |
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。