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http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/79745完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 廖淑貞(Shwu-Jen Liaw) | |
| dc.contributor.author | Yueh-Ting Kuo | en |
| dc.contributor.author | 郭玥婷 | zh_TW |
| dc.date.accessioned | 2022-11-23T09:09:38Z | - |
| dc.date.available | 2021-11-05 | |
| dc.date.available | 2022-11-23T09:09:38Z | - |
| dc.date.copyright | 2021-11-05 | |
| dc.date.issued | 2021 | |
| dc.date.submitted | 2021-10-27 | |
| dc.identifier.citation | 1.Adeolu, M., et al., Genome-based phylogeny and taxonomy of the ‘Enterobacteriales’: proposal for Enterobacterales ord. nov. divided into the families Enterobacteriaceae, Erwiniaceae fam. nov., Pectobacteriaceae fam. nov., Yersiniaceae fam. nov., Hafniaceae fam. nov., Morganellaceae fam. nov., and Budviciaceae fam. nov. International Journal of Systematic and Evolutionary Microbiology, 2016. 66(12): p. 5575-5599. 2.Rózalski, A., Z. Sidorczyk, and K. Kotełko, Potential virulence factors of Proteus bacilli. Microbiology and molecular biology reviews : MMBR, 1997. 61(1): p. 65-89. 3.Jamil, R.T., L.A. Foris, and J. Snowden, Proteus Mirabilis Infections, in StatPearls. 2021, StatPearls Publishing Copyright © 2021, StatPearls Publishing LLC.: Treasure Island (FL). 4.Schaffer, J.N. and M.M. Pearson, Proteus mirabilis and Urinary Tract Infections. Microbiol Spectr, 2015. 3(5). 5.Armbruster, C.E. and H.L. Mobley, Merging mythology and morphology: the multifaceted lifestyle of Proteus mirabilis. Nat Rev Microbiol, 2012. 10(11): p. 743-54. 6.Armbruster, C.E., H.L.T. Mobley, and M.M. Pearson, Pathogenesis of Proteus mirabilis Infection. EcoSal Plus, 2018. 8(1): p. 10.1128/ecosalplus.ESP-0009-2017. 7.Sabbuba, N.A., E. Mahenthiralingam, and D.J. Stickler, Molecular epidemiology of Proteus mirabilis infections of the catheterized urinary tract. J Clin Microbiol, 2003. 41(11): p. 4961-5. 8.Jacobsen, S.M., et al., Complicated catheter-associated urinary tract infections due to Escherichia coli and Proteus mirabilis. Clin Microbiol Rev, 2008. 21(1): p. 26-59. 9.Mobley, H.L., et al., Construction of a flagellum-negative mutant of Proteus mirabilis: effect on internalization by human renal epithelial cells and virulence in a mouse model of ascending urinary tract infection. Infect Immun, 1996. 64(12): p. 5332-40. 10.Mobley, H.L., et al., Cytotoxicity of the HpmA hemolysin and urease of Proteus mirabilis and Proteus vulgaris against cultured human renal proximal tubular epithelial cells. Infect Immun, 1991. 59(6): p. 2036-42. 11.Chippendale, G.R., et al., Internalization of Proteus mirabilis by human renal epithelial cells. Infection and Immunity, 1994. 62(8): p. 3115-3121. 12.Mobley, H.L. and J.W. Warren, Urease-positive bacteriuria and obstruction of long-term urinary catheters. Journal of clinical microbiology, 1987. 25(11): p. 2216-2217. 13.Jacobsen, S.M. and M.E. Shirtliff, Proteus mirabilis biofilms and catheter-associated urinary tract infections. Virulence, 2011. 2(5): p. 460-5. 14.Coker, C., et al., Pathogenesis of Proteus mirabilis urinary tract infection. Microbes Infect, 2000. 2(12): p. 1497-505. 15.Drechsel, H., et al., Alpha-keto acids are novel siderophores in the genera Proteus, Providencia, and Morganella and are produced by amino acid deaminases. J Bacteriol, 1993. 175(9): p. 2727-33. 16.Harding, G.K.M. and A.R. Ronald, The management of urinary infections; what have we learned in the past decade? International Journal of Antimicrobial Agents, 1994. 4(2): p. 83-88. 17.Stamm, W.E. and S.R. Norrby, Urinary Tract Infections: Disease Panorama and Challenges. The Journal of Infectious Diseases, 2001. 183(Supplement_1): p. S1-S4. 18.Foxman, B. and R.R. Frerichs, Epidemiology of urinary tract infection: I. Diaphragm use and sexual intercourse. American journal of public health, 1985. 75(11): p. 1308-1313. 19.Stetson, D.B., Connections between antiviral defense and autoimmunity. Current opinion in immunology, 2009. 21(3): p. 244-250. 20.Iwasaki, A. and R. Medzhitov, Regulation of adaptive immunity by the innate immune system. Science, 2010. 327(5963): p. 291-5. 21.Reygaert, W., Innate Immune Response to Urinary Tract Infections Involving Escherichia coli. Journal of Clinical Cellular Immunology, 2014. 05. 22.Wullt, B., et al., The host response to urinary tract infection. Infectious Disease Clinics of North America, 2003. 17(2): p. 279-301. 23.Flores-Kim, J. and A.J. Darwin, Regulation of bacterial virulence gene expression by cell envelope stress responses. Virulence, 2014. 5(8): p. 835-851. 24.Silhavy, T.J., D. Kahne, and S. Walker, The bacterial cell envelope. Cold Spring Harb Perspect Biol, 2010. 2(5): p. a000414. 25.Asmar, A.T. and J.-F. Collet, Lpp, the Braun lipoprotein, turns 50—major achievements and remaining issues. FEMS Microbiology Letters, 2018. 365(18). 26.Nakamura, K. and M. Inouye, DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an extremely AT-rich promoter. Cell, 1979. 18(4): p. 1109-1117. 27.Cohen, E.J., et al., Nanoscale-length control of the flagellar driveshaft requires hitting the tethered outer membrane. Science, 2017. 356(6334): p. 197-200. 28.Kikuchi, S., I. Shibuya, and K. Matsumoto, Viability of an Escherichia coli pgsA null mutant lacking detectable phosphatidylglycerol and cardiolipin. J Bacteriol, 2000. 182(2): p. 371-6. 29.Cascales, E., et al., Pal lipoprotein of Escherichia coli plays a major role in outer membrane integrity. J Bacteriol, 2002. 184(3): p. 754-9. 30.Uhlich, G.A., et al., The CsgA and Lpp proteins of an Escherichia coli O157:H7 strain affect HEp-2 cell invasion, motility, and biofilm formation. Infection and immunity, 2009. 77(4): p. 1543-1552. 31.Dorel, C., P. Lejeune, and A. Rodrigue, The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities? Res Microbiol, 2006. 157(4): p. 306-14. 32.Sha, J., et al., The two murein lipoproteins of Salmonella enterica serovar Typhimurium contribute to the virulence of the organism. Infect Immun, 2004. 72(7): p. 3987-4003. 33.Diao, J., et al., Peptidoglycan Association of Murein Lipoprotein Is Required for KpsD-Dependent Group 2 Capsular Polysaccharide Expression and Serum Resistance in a Uropathogenic Escherichia coli Isolate. mBio. 8(3): p. e00603-17. 34.Sha, J., et al., Braun lipoprotein (Lpp) contributes to virulence of yersiniae: potential role of Lpp in inducing bubonic and pneumonic plague. Infect Immun, 2008. 76(4): p. 1390-409. 35.Liu, T., et al., Immunological responses against Salmonella enterica serovar Typhimurium Braun lipoprotein and lipid A mutant strains in Swiss-Webster mice: potential use as live-attenuated vaccines. Microb Pathog, 2008. 44(3): p. 224-37. 36.Erova, T.E., et al., Protective Immunity Elicited by Oral Immunization of Mice with Salmonella enterica Serovar Typhimurium Braun Lipoprotein (Lpp) and Acetyltransferase (MsbB) Mutants. Front Cell Infect Microbiol, 2016. 6: p. 148. 37.Skirrow, M.B., The Dienes (Mutual Inhibition) Test In The Investigation Of Proteus Infections. Journal of Medical Microbiology, 1969. 2(4): p. 471-477. 38.de Lorenzo, V., et al., Mini-Tn5 transposon derivatives for insertion mutagenesis, promoter probing, and chromosomal insertion of cloned DNA in gram-negative eubacteria. J Bacteriol, 1990. 172(11): p. 6568-72. 39.Wu, Y. and F.W. Outten, IscR controls iron-dependent biofilm formation in Escherichia coli by regulating type I fimbria expression. J Bacteriol, 2009. 191(4): p. 1248-57. 40.Wu, J., et al., Pyruvate-associated acid resistance in bacteria. Appl Environ Microbiol, 2014. 80(14): p. 4108-13. 41.Chiang, M.-K., et al., Impact of Hfq on Global Gene Expression and Virulence in Klebsiella pneumoniae. PLOS ONE, 2011. 6(7): p. e22248. 42.Alamuri, P., et al., Adhesion, Invasion, and Agglutination Mediated by Two Trimeric Autotransporters in the Human Uropathogen Proteus mirabilis. Infection and Immunity, 2010. 78(11): p. 4882-4894. 43.Peerbooms, P.G., A.M. Verweij, and D.M. MacLaren, Vero cell invasiveness of Proteus mirabilis. Infect Immun, 1984. 43(3): p. 1068-71. 44.Giulietti, A., et al., An Overview of Real-Time Quantitative PCR: Applications to Quantify Cytokine Gene Expression. Methods, 2001. 25(4): p. 386-401. 45.Del Porto, P., et al., Dysfunctional CFTR alters the bactericidal activity of human macrophages against Pseudomonas aeruginosa. PloS one, 2011. 6(5): p. e19970-e19970. 46.Tsai, Y.-L., et al., cAMP receptor protein regulates mouse colonization, motility, fimbria-mediated adhesion, and stress tolerance in uropathogenic Proteus mirabilis. Scientific Reports, 2017. 7(1): p. 7282. 47.Armbruster, C.E., et al., Genome-wide transposon mutagenesis of Proteus mirabilis: Essential genes, fitness factors for catheter-associated urinary tract infection, and the impact of polymicrobial infection on fitness requirements. PLoS pathogens, 2017. 13(6): p. e1006434-e1006434. 48.Devi, K.P., et al., Eugenol (an essential oil of clove) acts as an antibacterial agent against Salmonella typhi by disrupting the cellular membrane. J Ethnopharmacol, 2010. 130(1): p. 107-15. 49.Fukuoka, T., et al., Increase in susceptibility of Pseudomonas aeruginosa to carbapenem antibiotics in low-amino-acid media. Antimicrob Agents Chemother, 1991. 35(3): p. 529-32. 50.Schweizer, H.P. and T.T. Hoang, An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosa. Gene, 1995. 158(1): p. 15-22. 51.Jiang, S.S., et al., Characterization of UDP-glucose dehydrogenase and UDP-glucose pyrophosphorylase mutants of Proteus mirabilis: defectiveness in polymyxin B resistance, swarming, and virulence. Antimicrob Agents Chemother, 2010. 54(5): p. 2000-9. 52.Morgenstein, R.M., K.M. Clemmer, and P.N. Rather, Loss of the waaL O-antigen ligase prevents surface activation of the flagellar gene cascade in Proteus mirabilis. J Bacteriol, 2010. 192(12): p. 3213-21. 53.McLean, R.J., et al., Histochemical and biochemical urease localization in the periplasm and outer membrane of two Proteus mirabilis strains. Can J Microbiol, 1986. 32(10): p. 772-8. 54.Hirayama, D., T. Iida, and H. Nakase, The Phagocytic Function of Macrophage-Enforcing Innate Immunity and Tissue Homeostasis. Int J Mol Sci, 2017. 19(1). 55.Wilson, M., R. Seymour, and B. Henderson, Bacterial perturbation of cytokine networks. Infection and immunity, 1998. 66(6): p. 2401-2409. 56.Zhang, J.M. and J. An, Cytokines, inflammation, and pain. Int Anesthesiol Clin, 2007. 45(2): p. 27-37. 57.Foster, J.R., The functions of cytokines and their uses in toxicology. International journal of experimental pathology, 2001. 82(3): p. 171-192. 58.Feghali, C.A. and T.M. Wright, Cytokines in acute and chronic inflammation. Front Biosci, 1997. 2: p. d12-26. 59.Fossum, C., Cytokines as markers for infections and their effect on growth performance and well-being in the pig. Domestic Animal Endocrinology, 1998. 15(5): p. 439-444. 60.Ni, Y., J. Reye, and R.R. Chen, lpp deletion as a permeabilization method. Biotechnology and Bioengineering, 2007. 97(6): p. 1347-1356. 61.Mathelié-Guinlet, M., et al., Lipoprotein Lpp regulates the mechanical properties of the E. coli cell envelope. Nature Communications, 2020. 11(1): p. 1789. 62.Lima, S., et al., Dual Molecular Signals Mediate the Bacterial Response to Outer-Membrane Stress. Science, 2013. 340(6134): p. 837. 63.Chao, Y. and J. Vogel, A 3′ UTR-Derived Small RNA Provides the Regulatory Noncoding Arm of the Inner Membrane Stress Response. Molecular Cell, 2016. 61(3): p. 352-363. 64.Guisbert, E., et al., Hfq modulates the sigmaE-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli. J Bacteriol, 2007. 189(5): p. 1963-73. 65.Guo, M.S., et al., MicL, a new σE-dependent sRNA, combats envelope stress by repressing synthesis of Lpp, the major outer membrane lipoprotein. Genes Dev, 2014. 28(14): p. 1620-34. 66.Samsudin, F., et al., Braun's Lipoprotein Facilitates OmpA Interaction with the Escherichia coli Cell Wall. Biophysical journal, 2017. 113(7): p. 1496-1504. 67.Morgenstein, R.M., B. Szostek, and P.N. Rather, Regulation of gene expression during swarmer cell differentiation in Proteus mirabilis. FEMS Microbiology Reviews, 2010. 34(5): p. 753-763. 68.Belas, R. and R. Suvanasuthi, The ability of Proteus mirabilis to sense surfaces and regulate virulence gene expression involves FliL, a flagellar basal body protein. J Bacteriol, 2005. 187(19): p. 6789-803. 69.Asmar, A.T., et al., Communication across the bacterial cell envelope depends on the size of the periplasm. PLOS Biology, 2017. 15(12): p. e2004303. 70.Kearns, D.B., A field guide to bacterial swarming motility. Nature reviews. Microbiology, 2010. 8(9): p. 634-644. 71.Imlay, J.A., The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium. Nat Rev Microbiol, 2013. 11(7): p. 443-54. 72.Arts, I.S., A. Gennaris, and J.-F. Collet, Reducing systems protecting the bacterial cell envelope from oxidative damage. FEBS Letters, 2015. 589(14): p. 1559-1568. 73.Flannagan, R.S., B. Heit, and D.E. Heinrichs, Antimicrobial Mechanisms of Macrophages and the Immune Evasion Strategies of Staphylococcus aureus. Pathogens (Basel, Switzerland), 2015. 4(4): p. 826-868. 74.Tisoncik, J.R., et al., Into the eye of the cytokine storm. Microbiol Mol Biol Rev, 2012. 76(1): p. 16-32. 75.Fadl, A.A., et al., Murein lipoprotein is a critical outer membrane component involved in Salmonella enterica serovar typhimurium systemic infection. Infection and immunity, 2005. 73(2): p. 1081-1096. 76.Hews, C.L., et al., Maintaining Integrity Under Stress: Envelope Stress Response Regulation of Pathogenesis in Gram-Negative Bacteria. Frontiers in Cellular and Infection Microbiology, 2019. 9(313). 77.Klein, G. and S. Raina, Small regulatory bacterial RNAs regulating the envelope stress response. Biochemical Society transactions, 2017. 45(2): p. 417-425. 78.De Lay, N., D.J. Schu, and S. Gottesman, Bacterial small RNA-based negative regulation: Hfq and its accomplices. The Journal of biological chemistry, 2013. 288(12): p. 7996-8003. 79.Guest, R.L. and T.L. Raivio, The Cpx Inner Membrane Stress Response, in Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria. 2016. p. 1015-1024. 80.Cui, G., et al., Reduced expression of microenvironmental Th1 cytokines accompanies adenomas-carcinomas sequence of colorectum. Cancer Immunol Immunother, 2007. 56(7): p. 985-95. 81.Lee, M.R., et al., Differed IL-1 Beta Response between Active TB and LTBI Cases by Ex Vivo Stimulation of Human Monocyte-Derived Macrophage with TB-Specific Antigen. Dis Markers, 2019. 2019: p. 7869576. 82.Gao, H., et al., Human IL-6, IL-17, IL-1β, and TNF-α differently regulate the expression of pro-inflammatory related genes, tissue factor, and swine leukocyte antigen class I in porcine aortic endothelial cells. Xenotransplantation, 2017. 24(2). | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/79745 | - |
| dc.description.abstract | "奇異變形桿菌(Proteus mirabilis)為一臨床重要尿道致病菌，尤其常見感染長期使用尿導管的病人。其為革蘭氏陰性菌，具有外膜、肽聚醣、內膜的三層包膜(envelope)結構。Lpp存在於外膜蛋白且以共價鍵連接肽聚醣，能夠維持細胞形狀以及膜間腔(periplasm)的距離。於陰性菌，Lpp是含量最豐富的外膜蛋白之一。目前已有眾多研究表明Lpp參與細菌對於外膜壓力的抵抗機制，且影響外膜的通透性。本篇研究欲探討Lpp對於Proteus mirabilis的重要性以及對毒力因子的影響。首先建構並確認lpp突變株，並分析其外膜組成，再分析lpp突變株對於Proteus mirabilis的表現型，發現lpp突變株的表面移行能力下降，且對於氧化壓力的抵抗能力，及巨噬細胞內存活能力皆不如野生株。以最小抑制濃度實驗分析lpp突變株，則發現其對於某些藥物以及SDS的感受性上升。另外也發現，lpp突變株的外膜通透性相較於野生株高。lpp突變株的細胞入侵能力及細胞毒性相較於野生株顯著下降，所引起的促發炎細胞因子表現也相較野生株弱。而以小鼠模型分析其膀胱和腎臟的定殖能力，發現lpp缺失導致P. mirabilis膀胱定殖能力顯著降低。其後探討了lpp突變株的基因調控，發現lpp缺失引起調控外膜壓力的rpoE, cpxP表現量提升。在缺失hfq及rpoE的情況下，lpp表現量則下降，表明hfq及rpoE參與Lpp的調控路徑。由上述可得知，Lpp在Proteus mirabilis中於外膜組成、壓力抵禦機制及泌尿道感染上扮演重要角色，具備作為抗感染藥物標的的潛力。" | zh_TW |
| dc.description.provenance | Made available in DSpace on 2022-11-23T09:09:38Z (GMT). No. of bitstreams: 1 U0001-1808202116470200.pdf: 3682987 bytes, checksum: c19f9de8564b37660968ea75e0b45e21 (MD5) Previous issue date: 2021 | en |
| dc.description.tableofcontents | 致謝……………………………………………………………………………… i 中文摘要………………………………………………………………………… ii 英文摘要………………………………………………………………………… iii 目錄……………………………………………………………………………… v 圖目錄…………………………………………………………………………… vii 表目錄…….……………………………………………………………………… viii 第一章 緒論…………………………………………………………………… 1 第一節 奇異變形桿菌(Proteus mirabilis)的基本介紹…………………… 1 第二節 P. mirabilis的致病因子……………………………………… 1 第三節 泌尿道感染引起之先天性免疫反應…………………………… 3 第四節 Braun’s lipoprotein (Lpp)簡介…………………………………… 4 第五節 Lpp對於革蘭氏陰性菌致病力影響…………………………… 5 第六節 研究動機與目的………………………………………………… 5 第二章 實驗設計、材料與方法……………………………………………… 7 第一節 實驗設計……………………………………………………… 7 第二節 實驗材料………………………………………………………… 7 第三節 構築突變株及質體……………………………………………… 8 第四節 分析毒力因子(virulence factors)及表現型(phenotypes) ……… 26 第五節 基因表達………………………………………………………… 45 第三章 實驗結果……………………………………………………………… 50 第一節 lpp 突變株之建構及確認……………………………………… 50 第二節 Proteus mirabilis lpp突變株表現型分析……………………… 53 第三節 分析lpp之調控………………………………………………… 70 第四章 討論與結論…………………………………………………………… 73 第一節 討論……………………………………………………………… 73 第二節 結論……………………………………………………………… 76 參考文獻………………………………………………………………………… 77 表………………………………………………………………………………… 84 附錄……………………………………………………………………………… 89 | |
| dc.language.iso | zh-TW | |
| dc.subject | 毒力因子 | zh_TW |
| dc.subject | 奇異變形桿菌 | zh_TW |
| dc.subject | lpp | zh_TW |
| dc.subject | 外膜蛋白 | zh_TW |
| dc.subject | 壓力抵抗 | zh_TW |
| dc.subject | outer membrane protein | en |
| dc.subject | lpp | en |
| dc.subject | Proteus mirabilis | en |
| dc.subject | stress resistance | en |
| dc.subject | virulence factor | en |
| dc.title | 探討Lpp在尿道致病性奇異變形桿菌中扮演之角色 | zh_TW |
| dc.title | The role of Lpp in Uropathogenic Proteus mirabilis | en |
| dc.date.schoolyear | 109-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 賴信志(Hsin-Tsai Liu),邱浩傑(Chih-Yang Tseng) | |
| dc.subject.keyword | 奇異變形桿菌,lpp,外膜蛋白,壓力抵抗,毒力因子, | zh_TW |
| dc.subject.keyword | Proteus mirabilis,lpp,outer membrane protein,stress resistance,virulence factor, | en |
| dc.relation.page | 98 | |
| dc.identifier.doi | 10.6342/NTU202102481 | |
| dc.rights.note | 同意授權(全球公開) | |
| dc.date.accepted | 2021-10-28 | |
| dc.contributor.author-college | 醫學院 | zh_TW |
| dc.contributor.author-dept | 醫學檢驗暨生物技術學研究所 | zh_TW |
| 顯示於系所單位： | 醫學檢驗暨生物技術學系 | |
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