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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張淑媛 | |
| dc.contributor.author | Yu-Kai Chao | en |
| dc.contributor.author | 趙昱凱 | zh_TW |
| dc.date.accessioned | 2021-05-20T21:34:19Z | - |
| dc.date.available | 2015-09-13 | |
| dc.date.available | 2021-05-20T21:34:19Z | - |
| dc.date.copyright | 2010-09-13 | |
| dc.date.issued | 2010 | |
| dc.date.submitted | 2010-08-17 | |
| dc.identifier.citation | 1. Ali, S. M., M. J. Geisow, and R. D. Burgoyne. 1989. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature 340:313-5.
2. Alwine, J. C., W. L. Steinhart, and C. W. Hill. 1974. Transcription of herpes simplex type 1 DNA in nuclei isolated from infected HEp-2 and KB cells. Virology 60:302-7. 3. Backes, P., D. Quinkert, S. Reiss, M. Binder, M. Zayas, U. Rescher, V. Gerke, R. Bartenschlager, and V. Lohmann. Role of annexin A2 in the production of infectious hepatitis C virus particles. J Virol. 4. Batterson, W., and B. Roizman. 1983. Characterization of the herpes simplex virion-associated factor responsible for the induction of alpha genes. J Virol 46:371-7. 5. Bowzard, J. B., R. J. Visalli, C. B. Wilson, J. S. Loomis, E. M. Callahan, R. J. Courtney, and J. W. Wills. 2000. Membrane targeting properties of a herpesvirus tegument protein-retrovirus Gag chimera. J Virol 74:8692-9. 6. Calistri, A., P. Sette, C. Salata, E. Cancellotti, C. Forghieri, A. Comin, H. Gottlinger, G. Campadelli-Fiume, G. Palu, and C. Parolin. 2007. Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies. J Virol 81:11468-78. 7. Campadelli-Fiume, G., F. Cocchi, L. Menotti, and M. Lopez. 2000. The novel receptors that mediate the entry of herpes simplex viruses and animal alphaherpesviruses into cells. Rev Med Virol 10:305-19. 8. Chasserot-Golaz, S., N. Vitale, I. Sagot, B. Delouche, S. Dirrig, L. A. Pradel, J. P. Henry, D. Aunis, and M. F. Bader. 1996. Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells. J Cell Biol 133:1217-36. 9. Chiang, Y., A. Rizzino, Z. A. Sibenaller, M. S. Wold, and J. K. Vishwanatha. 1999. Specific down-regulation of annexin II expression in human cells interferes with cell proliferation. Mol Cell Biochem 199:139-47. 10. Cocchi, F., L. Menotti, P. Dubreuil, M. Lopez, and G. Campadelli-Fiume. 2000. Cell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB). J Virol 74:3909-17. 11. Conley, A. J., D. M. Knipe, P. C. Jones, and B. Roizman. 1981. Molecular genetics of herpes simplex virus. VII. Characterization of a temperature-sensitive mutant produced by in vitro mutagenesis and defective in DNA synthesis and accumulation of gamma polypeptides. J Virol 37:191-206. 12. Costa, R. H., B. G. Devi, K. P. Anderson, B. H. Gaylord, and E. K. Wagner. 1981. Characterization of a major late herpes simplex virus type 1 mRNA. J Virol 38:483-96. 13. Costanzo, F., G. Campadelli-Fiume, L. Foa-Tomasi, and E. Cassai. 1977. Evidence that herpes simplex virus DNA is transcribed by cellular RNA polymerase B. J Virol 21:996-1001. 14. Creutz, C. E., L. G. Dowling, J. J. Sando, C. Villar-Palasi, J. H. Whipple, and W. J. Zaks. 1983. Characterization of the chromobindins. Soluble proteins that bind to the chromaffin granule membrane in the presence of Ca2+. J Biol Chem 258:14664-74. 15. Crump, C. M., B. Bruun, S. Bell, L. E. Pomeranz, T. Minson, and H. M. Browne. 2004. Alphaherpesvirus glycoprotein M causes the relocalization of plasma membrane proteins. J Gen Virol 85:3517-27. 16. Elliott, G., and P. O'Hare. 1997. Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88:223-33. 17. Emans, N., J. P. Gorvel, C. Walter, V. Gerke, R. Kellner, G. Griffiths, and J. Gruenberg. 1993. Annexin II is a major component of fusogenic endosomal vesicles. J Cell Biol 120:1357-69. 18. Forest, T., S. Barnard, and J. D. Baines. 2005. Active intranuclear movement of herpesvirus capsids. Nat Cell Biol 7:429-31. 19. Geisow, M. J. 1986. Common domain structure of Ca2+ and lipid-binding proteins. FEBS Lett 203:99-103. 20. Geraghty, R. J., C. Krummenacher, G. H. Cohen, R. J. Eisenberg, and P. G. Spear. 1998. Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280:1618-20. 21. Gerke, V., C. E. Creutz, and S. E. Moss. 2005. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 6:449-61. 22. Gerke, V., and S. E. Moss. 2002. Annexins: from structure to function. Physiol Rev 82:331-71. 23. Gibson, W., and B. Roizman. 1971. Compartmentalization of spermine and spermidine in the herpes simplex virion. Proc Natl Acad Sci U S A 68:2818-21. 24. Goto, H., and Y. Kawaoka. 1998. A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc Natl Acad Sci U S A 95:10224-8. 25. Goto, H., K. Wells, A. Takada, and Y. Kawaoka. 2001. Plasminogen-binding activity of neuraminidase determines the pathogenicity of influenza A virus. J Virol 75:9297-301. 26. Graham, M. E., V. Gerke, and R. D. Burgoyne. 1997. Modification of annexin II expression in PC12 cell lines does not affect Ca(2+)-dependent exocytosis. Mol Biol Cell 8:431-42. 27. Gruenberg, J., and H. Stenmark. 2004. The biogenesis of multivesicular endosomes. Nat Rev Mol Cell Biol 5:317-23. 28. Hajjar, K. A., and S. Krishnan. 1999. Annexin II: a mediator of the plasmin/plasminogen activator system. Trends Cardiovasc Med 9:128-38. 29. Harder, T., and V. Gerke. 1993. The subcellular distribution of early endosomes is affected by the annexin II2p11(2) complex. J Cell Biol 123:1119-32. 30. Harrist, A. V., E. V. Ryzhova, T. Harvey, and F. Gonzalez-Scarano. 2009. Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells. PLoS One 4:e5020. 31. Hayes, M. J., C. J. Merrifield, D. Shao, J. Ayala-Sanmartin, C. D. Schorey, T. P. Levine, J. Proust, J. Curran, M. Bailly, and S. E. Moss. 2004. Annexin 2 binding to phosphatidylinositol 4,5-bisphosphate on endocytic vesicles is regulated by the stress response pathway. J Biol Chem 279:14157-64. 32. Hayes, M. J., D. M. Shao, A. Grieve, T. Levine, M. Bailly, and S. E. Moss. 2009. Annexin A2 at the interface between F-actin and membranes enriched in phosphatidylinositol 4,5,-bisphosphate. Biochim Biophys Acta 1793:1086-95. 33. Herold, B. C., D. WuDunn, N. Soltys, and P. G. Spear. 1991. Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity. J Virol 65:1090-8. 34. Homa, F. L., and J. C. Brown. 1997. Capsid assembly and DNA packaging in herpes simplex virus. Rev Med Virol 7:107-122. 35. Honess, R. W., and B. Roizman. 1974. Regulation of herpesvirus macromolecular synthesis. I. Cascade regulation of the synthesis of three groups of viral proteins. J Virol 14:8-19. 36. Jones, P. C., and B. Roizman. 1979. Regulation of herpesvirus macromolecular synthesis. VIII. The transcription program consists of three phases during which both extent of transcription and accumulation of RNA in the cytoplasm are regulated. J Virol 31:299-314. 37. Jost, M., D. Zeuschner, J. Seemann, K. Weber, and V. Gerke. 1997. Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes. J Cell Sci 110 ( Pt 2):221-8. 38. Knipe, D. M., and A. Cliffe. 2008. Chromatin control of herpes simplex virus lytic and latent infection. Nat Rev Microbiol 6:211-21. 39. Knop, M., E. Aareskjold, G. Bode, and V. Gerke. 2004. Rab3D and annexin A2 play a role in regulated secretion of vWF, but not tPA, from endothelial cells. EMBO J 23:2982-92. 40. Konig, J., J. Prenen, B. Nilius, and V. Gerke. 1998. The annexin II-p11 complex is involved in regulated exocytosis in bovine pulmonary artery endothelial cells. J Biol Chem 273:19679-84. 41. Lambert, O., N. Cavusoglu, J. Gallay, M. Vincent, J. L. Rigaud, J. P. Henry, and J. Ayala-Sanmartin. 2004. Novel organization and properties of annexin 2-membrane complexes. J Biol Chem 279:10872-82. 42. LeBouder, F., E. Morello, G. F. Rimmelzwaan, F. Bosse, C. Pechoux, B. Delmas, and B. Riteau. 2008. Annexin II incorporated into influenza virus particles supports virus replication by converting plasminogen into plasmin. J Virol 82:6820-8. 43. Leuzinger, H., U. Ziegler, E. M. Schraner, C. Fraefel, D. L. Glauser, I. Heid, M. Ackermann, M. Mueller, and P. Wild. 2005. Herpes simplex virus 1 envelopment follows two diverse pathways. J Virol 79:13047-59. 44. Loomis, J. S., R. J. Courtney, and J. W. Wills. 2003. Binding partners for the UL11 tegument protein of herpes simplex virus type 1. J Virol 77:11417-24. 45. Loret, S., G. Guay, and R. Lippe. 2008. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol 82:8605-18. 46. Mayran, N., R. G. Parton, and J. Gruenberg. 2003. Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells. EMBO J 22:3242-53. 47. Merrifield, C. J., S. E. Moss, C. Ballestrem, B. A. Imhof, G. Giese, I. Wunderlich, and W. Almers. 1999. Endocytic vesicles move at the tips of actin tails in cultured mast cells. Nat Cell Biol 1:72-4. 48. Merrifield, C. J., U. Rescher, W. Almers, J. Proust, V. Gerke, A. S. Sechi, and S. E. Moss. 2001. Annexin 2 has an essential role in actin-based macropinocytic rocketing. Curr Biol 11:1136-41. 49. Mettenleiter, T. C. 2002. Herpesvirus assembly and egress. J Virol 76:1537-47. 50. Mettenleiter, T. C. 2006. Intriguing interplay between viral proteins during herpesvirus assembly or: the herpesvirus assembly puzzle. Vet Microbiol 113:163-9. 51. Mettenleiter, T. C., B. G. Klupp, and H. Granzow. 2006. Herpesvirus assembly: a tale of two membranes. Curr Opin Microbiol 9:423-9. 52. Mettenleiter, T. C., and T. Minson. 2006. Egress of alphaherpesviruses. J Virol 80:1610-1; author reply 1611-2. 53. Montgomery, R. I., M. S. Warner, B. J. Lum, and P. G. Spear. 1996. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87:427-36. 54. Ojala, P. M., B. Sodeik, M. W. Ebersold, U. Kutay, and A. Helenius. 2000. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol Cell Biol 20:4922-31. 55. Padula, M. E., M. L. Sydnor, and D. W. Wilson. 2009. Isolation and preliminary characterization of herpes simplex virus 1 primary enveloped virions from the perinuclear space. J Virol 83:4757-65. 56. Pawliczek, T., and C. M. Crump. 2009. Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol 83:11254-64. 57. Pietropaolo, R., and T. Compton. 1999. Interference with annexin II has no effect on entry of human cytomegalovirus into fibroblast cells. J Gen Virol 80 ( Pt 7):1807-16. 58. Pietropaolo, R. L., and T. Compton. 1997. Direct interaction between human cytomegalovirus glycoprotein B and cellular annexin II. J Virol 71:9803-7. 59. Raynor, C. M., J. F. Wright, D. M. Waisman, and E. L. Pryzdial. 1999. Annexin II enhances cytomegalovirus binding and fusion to phospholipid membranes. Biochemistry 38:5089-95. 60. Rescher, U., and V. Gerke. 2004. Annexins--unique membrane binding proteins with diverse functions. J Cell Sci 117:2631-9. 61. Rescher, U., D. Ruhe, C. Ludwig, N. Zobiack, and V. Gerke. 2004. Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 117:3473-80. 62. Reynolds, A. E., L. Liang, and J. D. Baines. 2004. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34. J Virol 78:5564-75. 63. Ryzhova, E. V., R. M. Vos, A. V. Albright, A. V. Harrist, T. Harvey, and F. Gonzalez-Scarano. 2006. Annexin 2: a novel human immunodeficiency virus type 1 Gag binding protein involved in replication in monocyte-derived macrophages. J Virol 80:2694-704. 64. Sarafian, T., L. A. Pradel, J. P. Henry, D. Aunis, and M. F. Bader. 1991. The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J Cell Biol 114:1135-47. 65. Seemann, J., K. Weber, M. Osborn, R. G. Parton, and V. Gerke. 1996. The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain. Mol Biol Cell 7:1359-74. 66. Shieh, M. T., D. WuDunn, R. I. Montgomery, J. D. Esko, and P. G. Spear. 1992. Cell surface receptors for herpes simplex virus are heparan sulfate proteoglycans. J Cell Biol 116:1273-81. 67. Shukla, D., J. Liu, P. Blaiklock, N. W. Shworak, X. Bai, J. D. Esko, G. H. Cohen, R. J. Eisenberg, R. D. Rosenberg, and P. G. Spear. 1999. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99:13-22. 68. Silver, S., and B. Roizman. 1985. gamma 2-Thymidine kinase chimeras are identically transcribed but regulated a gamma 2 genes in herpes simplex virus genomes and as beta genes in cell genomes. Mol Cell Biol 5:518-28. 69. Singer, G. P., W. W. Newcomb, D. R. Thomsen, F. L. Homa, and J. C. Brown. 2005. Identification of a region in the herpes simplex virus scaffolding protein required for interaction with the portal. J Virol 79:132-9. 70. Sodeik, B., M. W. Ebersold, and A. Helenius. 1997. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J Cell Biol 136:1007-21. 71. Spear, P. G., and R. Longnecker. 2003. Herpesvirus entry: an update. J Virol 77:10179-85. 72. Strang, B. L., and N. D. Stow. 2005. Circularization of the herpes simplex virus type 1 genome upon lytic infection. J Virol 79:12487-94. 73. Su, C. T., J. T. Hsu, H. P. Hsieh, P. H. Lin, T. C. Chen, C. L. Kao, C. N. Lee, and S. Y. Chang. 2008. Anti-HSV activity of digitoxin and its possible mechanisms. Antiviral Res 79:62-70. 74. Subramanian, R. P., and R. J. Geraghty. 2007. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B. Proc Natl Acad Sci U S A 104:2903-8. 75. Turcotte, S., J. Letellier, and R. Lippe. 2005. Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress. J Virol 79:8847-60. 76. Waisman, D. M. 1995. Annexin II tetramer: structure and function. Mol Cell Biochem 149-150:301-22. 77. Walters, J. N., G. L. Sexton, J. M. McCaffery, and P. Desai. 2003. Mutation of single hydrophobic residue I27, L35, F39, L58, L65, L67, or L71 in the N terminus of VP5 abolishes interaction with the scaffold protein and prevents closure of herpes simplex virus type 1 capsid shells. J Virol 77:4043-59. 78. Warner, M. S., R. J. Geraghty, W. M. Martinez, R. I. Montgomery, J. C. Whitbeck, R. Xu, R. J. Eisenberg, G. H. Cohen, and P. G. Spear. 1998. A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus. Virology 246:179-89. 79. Wild, P., M. Engels, C. Senn, K. Tobler, U. Ziegler, E. M. Schraner, E. Loepfe, M. Ackermann, M. Mueller, and P. Walther. 2005. Impairment of nuclear pores in bovine herpesvirus 1-infected MDBK cells. J Virol 79:1071-83. 80. Wright, J. F., A. Kurosky, E. L. Pryzdial, and S. Wasi. 1995. Host cellular annexin II is associated with cytomegalovirus particles isolated from cultured human fibroblasts. J Virol 69:4784-91. 81. WuDunn, D., and P. G. Spear. 1989. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J Virol 63:52-8. 82. Zhang, J., and K. R. McCrae. 2005. Annexin A2 mediates endothelial cell activation by antiphospholipid/anti-beta2 glycoprotein I antibodies. Blood 105:1964-9. 83. Zhou, Z. H., D. H. Chen, J. Jakana, F. J. Rixon, and W. Chiu. 1999. Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. J Virol 73:3210-8. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/10498 | - |
| dc.description.abstract | 第一型人類單純疱疹病毒(Human herpes simplex virus type-1, HSV-1)在感染細胞的過程中需要胞吞、胞吐作用及許多細胞蛋白的參與。Annexin II蛋白質是Annexin蛋白質家族中的一員，主要功能與多種細胞行為有關，如細胞間質的交互作用及參與胞吞和胞吐作用等。根據先前的文獻，Annexin II會被包入HSV-1之初期病毒顆粒中，並且在細胞外之HSV-1病毒顆粒中也發現Annexin II的存在。因此本篇研究想探討宿主細胞中的Annexin II在HSV-1病毒產生過程中所扮演的角色。首先，我們利用siRNA - Annexin II降低VERO細胞株(非洲綠猴腎臟上皮細胞)中Annexin II mRNA的表現量，再感染HSV-1病毒，結果發現上清液中之HSV-1病毒活性效價也相對降低。進一步實驗證明，此現象並非由於細胞中Annexin II降解影響病毒侵入細胞所致；此外，HSV-1之後期病毒蛋白質表現量在Annexin II降解細胞中並無明顯改變，因此可以確認Annexin II表現量的下降並不會影響HSV病毒的複製過程。最後，經由分析受感染細胞上清液中病毒活性效價與細胞中病毒活性效價，發現細胞中Annexin II降解只會影響細胞上清液中病毒活性效價，而細胞內之病毒活性效價則沒有明顯改變；以此計算病毒之釋放效率顯示，HSV-1病毒從Annexin II降解之Vero細胞中釋放比例較正常Vero細胞低(12.5% v.s. 26%, P<0.01)。利用共軛焦顯微鏡觀察，在Annexin II降解之Vero細胞中，大部分病毒皆聚集在細胞核膜周圍；而在正常細胞，病毒則是散布在細胞質中。由以上實驗結果得知，細胞中Annexin II降解會導致單純疱疹病毒聚集在細胞核膜周圍，造成病毒從細胞中釋放的效率降低，其詳細的作用機制則須進一步的實驗來釐清。 | zh_TW |
| dc.description.abstract | The replication of human herpes simplex virus type-1 (HSV-1) involves a variety of cellular proteins and processes, such as endocytosis and exocytosis. Annexin II, a member of Annexin family, is involved in diverse cellular processes such as endocytosis, exocytosis, and cell matrix interactions. Recent studies indicated that Annexin II is incorporated into the primary HSV-1 virions in the perinuclear space and in the extracellular virus particles. In this study, we would like to define the role of Annexin II in HSV-1 virus production. First, siRNA was utilized to down-regulate Annexin II mRNA in Vero cell before HSV-1 infection. A significant reduction of supernatant virus titer in the Annexin II down-regulated cells was observed. Since the viral entry, HSV-1 late protein expression, and the intracellular virus titer were not disturbed in the Annexin II down-regulated cells, the reduction of Annexin II may directly influence the virus release. Using confocal microscopy, we observed that most HSV-1 particles localized at the perinuclear space in the Annexin II down-regulated Vero cells, while the distribution of HSV-1 particles in the untreated Vero cells was mainly in the cytoplasm. In summary, Annexin II plays a role in HSV virion release and reduction of Annexin II results in accumulation of virus particles at the perinuclear localization. Further analysis is required to elucidate the mechanism in which Annexin II is involved in HSV-1 release. | en |
| dc.description.provenance | Made available in DSpace on 2021-05-20T21:34:19Z (GMT). No. of bitstreams: 1 ntu-99-R97424016-1.pdf: 1650332 bytes, checksum: 728ef64dde1f65512c60653af9a32f95 (MD5) Previous issue date: 2010 | en |
| dc.description.tableofcontents | 圖目錄 v
表目錄 vii 中文摘要 viii 英文摘要 ix 第一章 緒論 1 1.1. 第一型人類單純疱疹病毒 1 1.1.1. 人類單純疱疹病毒之結構及基因組成 1 1.1.2. 人類單純疱疹病毒之感染途徑 2 1.2. Annexin II蛋白質 4 1.2.1. Annexin II蛋白質之結構(圖一) 4 1.2.2. Annexin II蛋白質之功能 4 1.3. Annexin II蛋白質與病毒之關聯 6 1.3.1. Annexin II蛋白質與流感病毒之關聯 6 1.3.2. Annexin II蛋白質與人類免疫不全病毒第一型(Human immunodeficiency virus，HIV-1)之關聯 6 1.3.3. Annexin II蛋白質在C型肝炎病毒(Hepatitis C virus，HCV)產生過程中所扮演之角色 6 1.3.4. Annexin II蛋白質與Human herpes simplex virus type 1之關聯 7 1.4. 研究動機及目的 7 1.4.1. 研究動機 7 1.4.2. 實驗目的 7 第二章 實驗材料與實驗方法 9 2.1. 實驗材料 9 2.1.1. 細胞株 9 2.1.2. 病毒株 9 2.1.3. 培養基與試劑 9 2.1.4. 質體 10 2.1.5. 抗體 10 2.1.6. 商業實驗試劑套組 11 2.1.7. 核酸引子 (表一) 11 2.2. 實驗方法 12 2.2.1. 病毒與細胞培養 12 2.2.2. 病毒生長時程實驗 13 2.2.3. 病毒力價測定試驗 13 2.2.4. total RNA萃取及DNase處理 14 2.2.5. 反轉錄反應(Reverse transcription) 14 2.2.6. 即時相對定量PCR（Quantitative Real-time PCR） 15 2.2.7. 蛋白質濃度定量 15 2.2.8. 西方墨點法(Western blotting) 15 2.2.9. 濕式轉染法 16 2.2.10. 細胞轉染(Transfection) 17 2.2.11. 小量質體DNA萃取 17 2.2.12. 大量質體DNA萃取 17 2.2.13. 病毒穿膜試驗 (Entry assay) 18 2.2.14. 病毒核酸萃取 19 2.2.15. 染色體核酸萃取(Genomic DNA extraction) 19 2.2.16. 流式細胞計數 20 2.2.17. 免疫螢光染色 20 2.2.18. 實驗數據分析及統計 20 第三章 實驗結果 21 3.1. siRNA對Annexin II之降解效果測試 21 3.1.1. siRNA - Annexin II在293T細胞中對Annexin II mRNA所造成之降解效果 21 3.1.2. siRNA - Annexin II在Vero細胞中對Annexin II mRNA所造成之降解效果 21 3.2. siRNA降解Vero細胞中Annexin II對HSV-1病毒的影響 21 3.2.1. Annexin II降解對Vero細胞上清液中HSV-1病毒價數所產生的影響 21 3.2.2. 單純疱疹病毒對於Annexin II降解之Vero細胞與正常Vero細胞之感染比率 22 3.2.3. Annexin II降解對於HSV-1病毒侵入Vero細胞之效率所造成之影響 23 3.2.4. Vero細胞中Annexin II降解對HSV-1病毒複製過程所造成之影響 23 3.2.5. Vero細胞中Annexin II降解對HSV-1病毒釋放效率所造成之影響 24 3.2.6. HSV-1病毒蛋白VP22在Annexin II降解之Vero細胞及正常細胞中之分布比較 25 3.3. siRNA降解A549細胞中Annexin II表現量對HSV-1病毒之影響 26 3.4. 過度表現Annexin II對HSV-1病毒的影響 26 3.4.1. pRK5-Anx2 質體DNA之製備 27 3.4.2. pRK5-Anx2 質體DNA過度表現Annexin II基因之實驗 27 3.4.3. 在293T細胞中過度表現Annexin II蛋白對HSV-1病毒產生所造成之影響 27 第四章 討論 29 第五章 參考文獻 34 圖表 41 附表 66 | |
| dc.language.iso | zh-TW | |
| dc.subject | 疹病毒第一型 | zh_TW |
| dc.subject | 人類單純疱 | zh_TW |
| dc.subject | 病毒釋放 | zh_TW |
| dc.title | Annexin II蛋白質在第一型單純疱疹病毒產生過程中所扮演之角色 | zh_TW |
| dc.title | The Role of Annexin II in Human Herpes Simplex Virus Type 1 Production | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 98-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 高全良,李君男 | |
| dc.subject.keyword | 人類單純疱,疹病毒第一型,病毒釋放, | zh_TW |
| dc.subject.keyword | Herpes simplex virus type-1,HSV-1,Annexin II,Virus egress, | en |
| dc.relation.page | 66 | |
| dc.rights.note | 同意授權(全球公開) | |
| dc.date.accepted | 2010-08-18 | |
| 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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