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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 張麗冠(Li-kwan Chang) | |
| dc.contributor.author | Shih-Wei Jing | en |
| dc.contributor.author | 荊士瑋 | zh_TW |
| dc.date.accessioned | 2021-06-17T03:25:38Z | - |
| dc.date.available | 2023-05-31 | |
| dc.date.copyright | 2018-05-31 | |
| dc.date.issued | 2017 | |
| dc.date.submitted | 2018-05-18 | |
| dc.identifier.citation | Ali, A. S., M. Al-Shraim, A. M. Al-Hakami & I. M. Jones (2015) Epstein- Barr Virus: Clinical and Epidemiological Revisits and Genetic Basis of Oncogenesis. Open Virol J, 9, 7-28.
Baczyk, D., M. C. Audette, S. Drewlo, K. Levytska & J. C. Kingdom (2017) SUMO-4: A novel functional candidate in the human placental protein SUMOylation machinery. PLoS One, 12, e0178056. Baker, T. S., W. W. Newcomb, F. P. Booy, J. C. Brown & A. C. Steven (1990) Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy. J Virol, 64, 563-73. Bayer, P., A. Arndt, S. Metzger, R. Mahajan, F. Melchior, R. Jaenicke & J. Becker (1998) Structure determination of the small ubiquitin-related modifier SUMO-1. J Mol Biol, 280, 275-86. Bernier-Villamor, V., D. A. Sampson, M. J. Matunis & C. D. Lima (2002) Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell, 108, 345-56. Bertani, G. (1951) Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol, 62, 293-300. Chang, L. K., Y. H. Lee, T. S. Cheng, Y. R. Hong, P. J. Lu, J. J. Wang, W. H. Wang, C. W. Kuo, S. S. Li & S. T. Liu (2004) Post-translational modification of Rta of Epstein-Barr virus by SUMO-1. J Biol Chem, 279, 38803-12. Chang, L. K. & S. T. Liu (2000) Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation. Nucleic Acids Res, 28, 3918-25. Chang, T. H., T. Kubota, M. Matsuoka, S. Jones, S. B. Bradfute, M. Bray & K. Ozato (2009) Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PLoS Pathog, 5, e1000493. Collier, R. J. & H. A. Cole (1969) Diphtheria toxin subunit active in vitro. Science, 164, 1179-81. Countryman, J. & G. Miller (1985) Activation of expression of latent Epstein-Barr herpesvirus after gene transfer with a small cloned subfragment of heterogeneous viral DNA. Proc Natl Acad Sci U S A, 82, 4085-9. Deckman, I. C., M. Hagen & P. J. McCann, 3rd (1992) Herpes simplex virus type 1 protease expressed in Escherichia coli exhibits autoprocessing and specific cleavage of the ICP35 assembly protein. J Virol, 66, 7362-7. Desterro, J. M., M. S. Rodriguez & R. T. Hay (1998) SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell, 2, 233-9. Desterro, J. M., M. S. Rodriguez, G. D. Kemp & R. T. Hay (1999) Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J Biol Chem, 274, 10618-24. Desterro, J. M., J. Thomson & R. T. Hay (1997) Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett, 417, 297-300. Elia, A. E., A. P. Boardman, D. C. Wang, E. L. Huttlin, R. A. Everley, N. Dephoure, C. Zhou, I. Koren, S. P. Gygi & S. J. Elledge (2015) Quantitative Proteomic Atlas of Ubiquitination and Acetylation in the DNA Damage Response. Mol Cell, 59, 867-81. Epstein, M. A., B. G. Achong & Y. M. Barr (1964) Virus Particles in Cultured Lymphoblasts from Burkitt's Lymphoma. Lancet, 1, 702-3. Feederle, R., M. Kost, M. Baumann, A. Janz, E. Drouet, W. Hammerschmidt & H. J. Delecluse (2000) The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J, 19, 3080-9. Feng, W. H., G. Hong, H. J. Delecluse & S. C. Kenney (2004) Lytic induction therapy for Epstein-Barr virus-positive B-cell lymphomas. J Virol, 78, 1893-902. Fingeroth, J. D., J. J. Weis, T. F. Tedder, J. L. Strominger, P. A. Biro & D. T. Fearon (1984) Epstein-Barr virus receptor of human B lymphocytes is the C3d receptor CR2. Proc Natl Acad Sci U S A, 81, 4510-4. Fixman, E. D., G. S. Hayward & S. D. Hayward (1992) trans-acting requirements for replication of Epstein-Barr virus ori-Lyt. J Virol, 66, 5030-9. Froger, A. & J. E. Hall (2007) Transformation of plasmid DNA into E. coli using the heat shock method. J Vis Exp, 253. Fukayama, M., J. M. Chong & H. Uozaki (2001) Pathology and molecular pathology of Epstein-Barr virus-associated gastric carcinoma. Curr Top Microbiol Immunol, 258, 91-102. Gandhi, M. K., J. T. Tellam & R. Khanna (2004) Epstein-Barr virus-associated Hodgkin's lymphoma. Br J Haematol, 125, 267-81. Goffard, A., N. Callens, B. Bartosch, C. Wychowski, F. L. Cosset, C. Montpellier & J. Dubuisson (2005) Role of N-linked glycans in the functions of hepatitis C virus envelope glycoproteins. J Virol, 79, 8400-9. Gong, M. & E. Kieff (1990) Intracellular trafficking of two major Epstein-Barr virus glycoproteins, gp350/220 and gp110. J Virol, 64, 1507-16. Graham, F. L., J. Smiley, W. C. Russell & R. Nairn (1977) Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J Gen Virol, 36, 59-74. Guo, D., M. Li, Y. Zhang, P. Yang, S. Eckenrode, D. Hopkins, W. Zheng, S. Purohit, R. H. Podolsky, A. Muir, J. Wang, Z. Dong, T. Brusko, M. Atkinson, P. Pozzilli, A. Zeidler, L. J. Raffel, C. O. Jacob, Y. Park, M. Serrano-Rios, M. T. Larrad, Z. Zhang, H. J. Garchon, J. F. Bach, J. I. Rotter, J. X. She & C. Y. Wang (2004) A functional variant of SUMO4, a new I kappa B alpha modifier, is associated with type 1 diabetes. Nat Genet, 36, 837-41. Hadari, T., J. V. Warms, I. A. Rose & A. Hershko (1992) A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation. J Biol Chem, 267, 719-27. Han, Q., C. Chang, L. Li, C. Klenk, J. Cheng, Y. Chen, N. Xia, Y. Shu, Z. Chen, G. Gabriel, B. Sun & K. Xu (2014) Sumoylation of influenza A virus nucleoprotein is essential for intracellular trafficking and virus growth. J Virol, 88, 9379-90. Hannich, J. T., A. Lewis, M. B. Kroetz, S. J. Li, H. Heide, A. Emili & M. Hochstrasser (2005) Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J Biol Chem, 280, 4102-10. Hecker, C. M., M. Rabiller, K. Haglund, P. Bayer & I. Dikic (2006) Specification of SUMO1- and SUMO2-interacting motifs. J Biol Chem, 281, 16117-27. Henson, B. W., E. M. Perkins, J. E. Cothran & P. Desai (2009) Self-assembly of Epstein-Barr virus capsids. J Virol, 83, 3877-90. Herrold, R. E., A. Marchini, S. Fruehling & R. Longnecker (1996) Glycoprotein 110, the Epstein-Barr virus homolog of herpes simplex virus glycoprotein B, is essential for Epstein-Barr virus replication in vivo. J Virol, 70, 2049-54. Hershko, A. & A. Ciechanover (1998) The ubiquitin system. Annu Rev Biochem, 67, 425-79. Heymann, J. B., N. Cheng, W. W. Newcomb, B. L. Trus, J. C. Brown & A. C. Steven (2003) Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat Struct Biol, 10, 334-41. Hofmann, H., S. Floss & T. Stamminger (2000) Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b. J Virol, 74, 2510-24. Jarrett, R. F., G. L. Stark, J. White, B. Angus, F. E. Alexander, A. S. Krajewski, J. Freeland, G. M. Taylor, P. R. Taylor, Scotland & G. Newcastle Epidemiology of Hodgkin Disease Study (2005) Impact of tumor Epstein-Barr virus status on presenting features and outcome in age-defined subgroups of patients with classic Hodgkin lymphoma: a population-based study. Blood, 106, 2444-51. Jayabalan, A. K., A. Sanchez, R. Y. Park, S. P. Yoon, G. Y. Kang, J. H. Baek, P. Anderson, Y. Kee & T. Ohn (2016) NEDDylation promotes stress granule assembly. Nat Commun, 7, 12125. Jenkins, P. J., U. K. Binne & P. J. Farrell (2000) Histone acetylation and reactivation of Epstein-Barr virus from latency. J Virol, 74, 710-20. Jentsch, S. & I. Psakhye (2013) Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annu Rev Genet, 47, 167-86. Jimeno, S., M. J. Fernandez-Avila, A. Cruz-Garcia, C. Cepeda-Garcia, D. Gomez-Cabello & P. Huertas (2015) Neddylation inhibits CtIP-mediated resection and regulates DNA double strand break repair pathway choice. Nucleic Acids Res, 43, 987-99. Johannsen, E., M. Luftig, M. R. Chase, S. Weicksel, E. Cahir-McFarland, D. Illanes, D. Sarracino & E. Kieff (2004) Proteins of purified Epstein-Barr virus. Proc Natl Acad Sci U S A, 101, 16286-91. Kolesar, P., P. Sarangi, V. Altmannova, X. Zhao & L. Krejci (2012) Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation. Nucleic Acids Res, 40, 7831-43. Kumar, S., Y. Yoshida & M. Noda (1993) Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem Biophys Res Commun, 195, 393-9. Kuppers, R. (2003) B cells under influence: transformation of B cells by Epstein-Barr virus. Nat Rev Immunol, 3, 801-12. Lake, C. M. & L. M. Hutt-Fletcher (2000) Epstein-Barr virus that lacks glycoprotein gN is impaired in assembly and infection. J Virol, 74, 11162-72. Li, Z., Q. Cui, X. Wang, B. Li, D. Zhao, Q. Xia & P. Zhao (2017) Functions and substrates of NEDDylation during cell cycle in the silkworm, Bombyx mori. Insect Biochem Mol Biol. Liang, Y. C., C. C. Lee, Y. L. Yao, C. C. Lai, M. L. Schmitz & W. M. Yang (2016) SUMO5, a Novel Poly-SUMO Isoform, Regulates PML Nuclear Bodies. Sci Rep, 6, 26509. Lieberman, P. M. & A. J. Berk (1990) In vitro transcriptional activation, dimerization, and DNA-binding specificity of the Epstein-Barr virus Zta protein. J Virol, 64, 2560-8. Liu, X. & J. I. Cohen (2015) Epstein-Barr Virus (EBV) Tegument Protein BGLF2 Promotes EBV Reactivation through Activation of the p38 Mitogen-Activated Protein Kinase. J Virol, 90, 1129-38. Lucero, P., E. Penalver, L. Vela & R. Lagunas (2000) Monoubiquitination is sufficient to signal internalization of the maltose transporter in Saccharomyces cerevisiae. J Bacteriol, 182, 241-3. Marusic, M. B., N. Mencin, M. Licen, L. Banks & H. S. Grm (2010) Modification of human papillomavirus minor capsid protein L2 by sumoylation. J Virol, 84, 11585-9. Mattiroli, F. & T. K. Sixma (2014) Lysine-targeting specificity in ubiquitin and ubiquitin-like modification pathways. Nat Struct Mol Biol, 21, 308-16. Minty, A., X. Dumont, M. Kaghad & D. Caput (2000) Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem, 275, 36316-23. Munz, C. (2017) The Autophagic Machinery in Viral Exocytosis. Front Microbiol, 8, 269. Nemerow, G. R. & N. R. Cooper (1984) Early events in the infection of human B lymphocytes by Epstein-Barr virus: the internalization process. Virology, 132, 186-98. Nemerow, G. R., R. A. Houghten, M. D. Moore & N. R. Cooper (1989) Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2). Cell, 56, 369-77. Newcomb, W. W., R. M. Juhas, D. R. Thomsen, F. L. Homa, A. D. Burch, S. K. Weller & J. C. Brown (2001) The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid. J Virol, 75, 10923-32. Newcomb, W. W., D. R. Thomsen, F. L. Homa & J. C. Brown (2003) Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids. J Virol, 77, 9862-71. Newcomb, W. W., B. L. Trus, F. P. Booy, A. C. Steven, J. S. Wall & J. C. Brown (1993) Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes. J Mol Biol, 232, 499-511. Nicholson, P., C. Addison, A. M. Cross, J. Kennard, V. G. Preston & F. J. Rixon (1994) Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a. J Gen Virol, 75 ( Pt 5), 1091-9. Okuma, T., R. Honda, G. Ichikawa, N. Tsumagari & H. Yasuda (1999) In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2. Biochem Biophys Res Commun, 254, 693-8. Pegtel, D. M., J. Middeldorp & D. A. Thorley-Lawson (2004) Epstein-Barr virus infection in ex vivo tonsil epithelial cell cultures of asymptomatic carriers. J Virol, 78, 12613-24. Preston, V. G., F. J. Rixon, I. M. McDougall, M. McGregor & M. F. al Kobaisi (1992) Processing of the herpes simplex virus assembly protein ICP35 near its carboxy terminal end requires the product of the whole of the UL26 reading frame. Virology, 186, 87-98. Ragoczy, T. & G. Miller (1999) Role of the epstein-barr virus RTA protein in activation of distinct classes of viral lytic cycle genes. J Virol, 73, 9858-66. Rangasamy, D., K. Woytek, S. A. Khan & V. G. Wilson (2000) SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation. J Biol Chem, 275, 37999-8004. Rixon, F. J., C. Addison, A. McGregor, S. J. Macnab, P. Nicholson, V. G. Preston & J. D. Tatman (1996) Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins. J Gen Virol, 77 ( Pt 9), 2251-60. Rooney, C. M., D. T. Rowe, T. Ragot & P. J. Farrell (1989) The spliced BZLF1 gene of Epstein-Barr virus (EBV) transactivates an early EBV promoter and induces the virus productive cycle. J Virol, 63, 3109-16. Schneider-Poetsch, T., J. Ju, D. E. Eyler, Y. Dang, S. Bhat, W. C. Merrick, R. Green, B. Shen & J. O. Liu (2010) Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat Chem Biol, 6, 209-217. Shaw, G., S. Morse, M. Ararat & F. L. Graham (2002) Preferential transformation of human neuronal cells by human adenoviruses and the origin of HEK 293 cells. FASEB J, 16, 869-71. Song, J., Z. Zhang, W. Hu & Y. Chen (2005) Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J Biol Chem, 280, 40122-9. Steinacher, R. & P. Schar (2005) Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr Biol, 15, 616-23. Stuart, A. D., J. P. Stewart, J. R. Arrand & M. Mackett (1995) The Epstein-Barr virus encoded cytokine viral interleukin-10 enhances transformation of human B lymphocytes. Oncogene, 11, 1711-9. Su, C. I., C. H. Tseng, C. Y. Yu & M. M. Lai (2016) SUMO Modification Stabilizes Dengue Virus Nonstructural Protein 5 To Support Virus Replication. J Virol, 90, 4308-19. Sun, H., J. D. Leverson & T. Hunter (2007) Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J, 26, 4102-12. Swaminathan, S., R. Hesselton, J. Sullivan & E. Kieff (1993) Epstein-Barr virus recombinants with specifically mutated BCRF1 genes. J Virol, 67, 7406-13. Tan, J. M., E. S. Wong, D. S. Kirkpatrick, O. Pletnikova, H. S. Ko, S. P. Tay, M. W. Ho, J. Troncoso, S. P. Gygi, M. K. Lee, V. L. Dawson, T. M. Dawson & K. L. Lim (2008) Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet, 17, 431-9. Tatham, M. H., E. Jaffray, O. A. Vaughan, J. M. Desterro, C. H. Botting, J. H. Naismith & R. T. Hay (2001) Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem, 276, 35368-74. Terrell, J., S. Shih, R. Dunn & L. Hicke (1998) A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol Cell, 1, 193-202. Thrower, J. S., L. Hoffman, M. Rechsteiner & C. M. Pickart (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J, 19, 94-102. Tsai, K., N. Thikmyanova, J. A. Wojcechowskyj, H. J. Delecluse & P. M. Lieberman (2011) EBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcription. PLoS Pathog, 7, e1002376. van Gent, M., S. G. Braem, A. de Jong, N. Delagic, J. G. Peeters, I. G. Boer, P. N. Moynagh, E. Kremmer, E. J. Wiertz, H. Ovaa, B. D. Griffin & M. E. Ressing (2014) Epstein-Barr virus large tegument protein BPLF1 contributes to innate immune evasion through interference with toll-like receptor signaling. PLoS Pathog, 10, e1003960. Walsh, C. T., S. Garneau-Tsodikova & G. J. Gatto, Jr. (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed Engl, 44, 7342-72. Wang, W. H., L. K. Chang & S. T. Liu (2011) Molecular interactions of Epstein-Barr virus capsid proteins. J Virol, 85, 1615-24. Wang, W. H., C. W. Kuo, L. K. Chang, C. C. Hung, T. H. Chang & S. T. Liu (2015) Assembly of Epstein-Barr Virus Capsid in Promyelocytic Leukemia Nuclear Bodies. J Virol, 89, 8922-31. Wang, Y. E., A. Park, M. Lake, M. Pentecost, B. Torres, T. E. Yun, M. C. Wolf, M. R. Holbrook, A. N. Freiberg & B. Lee (2010) Ubiquitin-regulated nuclear-cytoplasmic trafficking of the Nipah virus matrix protein is important for viral budding. PLoS Pathog, 6, e1001186. Weinheimer, S. P., P. J. McCann, 3rd, D. R. O'Boyle, 2nd, J. T. Stevens, B. A. Boyd, D. A. Drier, G. A. Yamanaka, C. L. DiIanni, I. C. Deckman & M. G. Cordingley (1993) Autoproteolysis of herpes simplex virus type 1 protease releases an active catalytic domain found in intermediate capsid particles. J Virol, 67, 5813-22. Westphal, E. M., W. Blackstock, W. Feng, B. Israel & S. C. Kenney (2000) Activation of lytic Epstein-Barr virus (EBV) infection by radiation and sodium butyrate in vitro and in vivo: a potential method for treating EBV-positive malignancies. Cancer Res, 60, 5781-8. Wodrich, H., D. Henaff, B. Jammart, C. Segura-Morales, S. Seelmeir, O. Coux, Z. Ruzsics, C. M. Wiethoff & E. J. Kremer (2010) A capsid-encoded PPxY-motif facilitates adenovirus entry. PLoS Pathog, 6, e1000808. Wu, C. Y., K. S. Jeng & M. M. Lai (2011) The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus. J Virol, 85, 6618-28. Yang, S. H., A. Galanis, J. Witty & A. D. Sharrocks (2006) An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J, 25, 5083-93. Yang, Y. C., Y. Yoshikai, S. W. Hsu, H. Saitoh & L. K. Chang (2013) Role of RNF4 in the ubiquitination of Rta of Epstein-Barr virus. J Biol Chem, 288, 12866-79. Young, K. A., A. P. Herbert, P. N. Barlow, V. M. Holers & J. P. Hannan (2008) Molecular basis of the interaction between complement receptor type 2 (CR2/CD21) and Epstein-Barr virus glycoprotein gp350. J Virol, 82, 11217-27. zur Hausen, H., F. J. O'Neill, U. K. Freese & E. Hecker (1978) Persisting oncogenic herpesvirus induced by the tumour promotor TPA. Nature, 272, 373-5. 陳菡亭 (2011) Regulation of Epstein-Barr Virus Capsid Protein BDLF1 by Ubiquitin-like Modifier Proteins. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/69732 | - |
| dc.description.abstract | 人類第四型皰疹病毒(Epstein-Barr virus, EBV)是第一個被發現的人類致癌病毒，並且能夠長期潛伏於人體的B淋巴球細胞中。EB病毒外殼為一個正二十面體，由VCA組成的12個五聚體與150個六聚體，以及320個由2個BDLF1與1個BORF1所組成的三聚體組裝而成。目前已知BDLF1會被BORF1帶入細胞核中，並於PML nuclear body附近進行組裝。另外先前的研究指出SUMO-1會修飾BDLF1，本研究進一步證明SUMO-2與Ub同樣也會對BDLF1進行修飾。其中，BDLF1的胺基酸K124位置為Ub以及SUMO-2的主要修飾位置，而且BDLF1會藉由SUMO-interacting motifs (SIMs)促進SUMO-2對K124的修飾並與Ub競爭，以提升BDLF1的穩定性。除此之外，BDLF1的SIMs也具有增強與BORF1間結合力的能力。綜合以上結果推論，EB病毒外鞘蛋白質BDLF1上的SIMs對於K124的類泛素化是必要的，並且減少K124的泛素化，以增加BDLF1的半衰期。除此之外，BDLF1的SIMs能夠加強與BORF1的結合。因此，BDLF1可能會透過這兩種策略來提升病毒顆粒的組裝量，進而促進病毒的增殖。 | zh_TW |
| dc.description.abstract | Epstein-Barr virus (EBV) is the first discovered oncogenic virus and infect human B cells. EBV contains an icosahedral nucleocapsid which is composed by 12 pentameric, 150 hexameric capsomers and 320 triplexes. These capsomers are composed by the major capsid protein, VCA, and connected by triplexes forming by two minor capsid proteins, BORF1 and BDLF1. A previous study indicated that BDLF1interacts with BORF1, and then the proteins were transported to the PML nuclear bodies in the nucleus for the capsid assembly. BDLF1 has also been shown to be modified by SUMO-1. This study further demonstrated that BDLF1 is modified by SUMO-2 and ubiquitin. The BDLF1 K124 is the main modification site of SUMO-2 and ubiquitin. Moreover, the SUMO-interacting motifs (SIMs) of BDLF1 are required for the sumoylation of BDLF1, but not the ubiquitination of BDLF1, which thereby increases the stability of BDLF1. Additionally, BDLF1 SIMs promote the interaction of BDLF1 with BORF1, which may facilitate capsid assembly and virus proliferation. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-17T03:25:38Z (GMT). No. of bitstreams: 1 ntu-106-R04b22026-1.pdf: 1928710 bytes, checksum: b9dd45e58022c924b0d63c033695d10f (MD5) Previous issue date: 2017 | en |
| dc.description.tableofcontents | 目錄
中文摘要 i Abstract ii 縮寫表 iii 目錄 iv 圖目錄 vii 表目錄 viii 前言 1 一、 後轉譯修飾作用 (Post-translational modification) 1 1. 泛素化修飾 (Ubiquitination) 1 2. 類泛素化修飾 (Sumoylation) 2 3. Neddylation 4 二、 Epstein Barr virus (EBV) 5 1. EB病毒的生活史 5 2. EB病毒溶裂期的晚期蛋白質 6 3. 皰疹病毒顆粒的組裝 7 4. EB病毒顆粒組裝 8 三、 病毒與宿主的後轉譯修飾 9 研究目的 11 實驗材料與方法 12 一、 細菌株與細胞株 12 二、 質體與質體DNA萃取 12 三、 抗體 12 四、 E. coli的轉型作用 (Transformation) 13 五、 細胞轉染 (Transfection) 13 六、 西方墨點法 (Western blotting) 13 七、 變性免疫沉澱法 14 八、 免疫沉澱反應 (Immunoprecipitation) 15 九、 E. coli的蛋白質表現誘導 15 十、 Glutathione S-transferase pull down assay 16 十一、 蛋白質穩定性的測試 16 結果 17 一、BDLF1會受到泛素的修飾 17 二、BDLF1會受到類泛素的修飾 17 三、泛素與類泛素會互相競爭對BDLF1的共價鍵修飾 18 四、BDLF1的K124為主要的泛素與類泛素修飾位 19 五、BDLF1-K124R點突變提高蛋白質穩定性 20 六、BDLF1的SIM影響蛋白質的穩定性 20 七、BDLF1-K124R點突變不影響蛋白質的結合能力 21 八、BDLF1的 SIMs序列對BDLF1與BORF1結合的影響 22 九、SUMO-2不會增強BDLF1與BORF1間的結合 23 討論 24 Ub與SUMO-2會互相競爭對BDLF1 K124位的修飾 24 BDLF1 SIMs調控K124上的修飾並提高蛋白質穩定性 25 BDLF1 SIMs藉由SUMO-1加強與BORF1間的結合 26 BDLF1的SIM可能參與後轉譯修飾的調控 28 BDLF1的後轉譯修飾作用可能會影響病毒顆粒組裝 28 附錄 46 附錄1、EB病毒外鞘蛋白質 46 參考文獻 47 圖目錄 圖1、BDLF1會受到泛素化修飾。 33 圖2、BDLF1會受到SUMO-2的共價鍵修飾。 35 圖3、Ub與SUMO-2會互相競爭對BDLF1的共價鍵修飾。 36 圖4、BDLF1的胺基酸序列K124位置為Ub與SUMO-2的主要修飾位。 38 圖5、K124R點突變會增加BDLF1的穩定性。 39 圖6、SIM突變影響BDLF1穩定性。 40 圖7、BDLF1 K124R點突變與其二聚體的形成。 41 圖8、BDLF1 K124R點突變不影響其與BORF1的結合。 42 圖9、BDLF1 SIMs會影響BDLF1 N端與BORF1之間的結合 43 圖10、SUMO-2不會增強BDLF1與BORF1間的結合 44 圖11、 BDLF1與後轉譯修飾模型圖 45 表目錄 表1、本研究中所用到的質體 30 表2、本研究使用的抗體 32 | |
| dc.language.iso | zh-TW | |
| dc.subject | 人類皰疹病毒第四型 | zh_TW |
| dc.subject | 類泛素化 | zh_TW |
| dc.subject | 泛素化 | zh_TW |
| dc.subject | BDLF1 | zh_TW |
| dc.subject | Epstein-Barr virus | en |
| dc.subject | BDLF1 | en |
| dc.subject | ubiquitination | en |
| dc.subject | sumoylation | en |
| dc.title | 泛素化與類泛素化對Epstein-Barr病毒外鞘蛋白質BDLF1的調控 | zh_TW |
| dc.title | Regulation of the Epstein-Barr virus capsid protein BDLF1 by ubiquitination and sumoylation | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 106-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 劉世東(Shih-Tung Liu),張世宗(Shih-chung Chang),廖憶純,張沛鈞 | |
| dc.subject.keyword | 人類皰疹病毒第四型,BDLF1,泛素化,類泛素化, | zh_TW |
| dc.subject.keyword | Epstein-Barr virus,BDLF1,ubiquitination,sumoylation, | en |
| dc.relation.page | 62 | |
| dc.identifier.doi | 10.6342/NTU201800827 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2018-05-21 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 生化科技學系 | zh_TW |
| 顯示於系所單位： | 生化科技學系 | |
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