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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張麗冠 | zh_TW |
dc.contributor.advisor | Li-Kwan Chang | en |
dc.contributor.author | 林杰昌 | zh_TW |
dc.contributor.author | Chieh-Chang Lin | en |
dc.date.accessioned | 2023-03-19T23:50:15Z | - |
dc.date.available | 2023-12-26 | - |
dc.date.copyright | 2022-09-02 | - |
dc.date.issued | 2022 | - |
dc.date.submitted | 2002-01-01 | - |
dc.identifier.citation | 王頂立 (2021) Influence of TRIM5α on Epstein-Barr virus BFRF3. 臺灣大學生化科技學系碩士論文. 林俐岑 (2020) Role of TRIM5α in the regulation of Epstein-Barr virus minor capsid protein BORF1. 臺灣大學生化科技學系碩士論文. 徐詩媁 (2013) Role of TRIM5α in the lytic progression of Epstein-Barr virus. 臺灣大學生化科技學系碩士論文. 陳則堯 (2016) Role of autophagy in the regulation of BORF1 of Epstein-Barr virus by TRIM5α. 臺灣大學生化科技學系碩士論文. 陳建炘(2011) TRIM5α restrains Epstein-Barr virus lytic cycle by mediating ubiquitination of Rta. 臺灣大學生化科技學系碩士論文. 黃翔弘 (2020) Role of Rta in the late stage of Epstein-Barr virus life cycle. 臺灣大學生化科技學系博士論文. 廖博弘 (2019) Role of Epstein-Barr virus BFRF3 in nuclear translocation of VCA. 臺灣大學生化科技學系碩士論文. Adams, A. (1987) Replication of latent Epstein-Barr virus genomes in Raji cells. Journal of Virology 61, 1743-1746. Akutsu, M., Dikic, I., and Bremm, A. (2016) Ubiquitin chain diversity at a glance. Journal of Cell Science 129, 875-880. Ambrose, Z., and Aiken, C. (2014) HIV-1 uncoating: connection to nuclear entry and regulation by host proteins. Virology 454-455, 371-379. Ambrose, Z., Lee, K., Ndjomou, J., Xu, H., Oztop, I., Matous, J., Takemura, T., Unutmaz, D., Engelman, A., Hughes, S.H., et al. (2012) Human immunodeficiency virus type 1 capsid mutation N74D alters cyclophilin A dependence and impairs macrophage infection. Journal of Virology 86, 4708-4714. Andersson-Anvret, M., Forsby, N., Klein, G., Henle, W., and Biörklund, A. (1979) Relationship between the Epstein-Barr virus genome and nasopharyngeal carcinoma in Caucasian patients. International Journal of Cancer 23, 762-767. Babcock, G.J., Decker, L.L., Volk, M., and Thorley-Lawson, D.A. (1998) EBV Persistence in Memory B Cells In Vivo. Immunity 9, 395-404. Baer, R., Bankier, A.T., Biggin, M.D., Deininger, P.L., Farrell, P.J., Gibson, T.J., Hatfull, G., Hudson, G.S., Satchwell, S.C., Séguin, C., et al. (1984) DNA sequence and expression of the B95-8 Epstein—Barr virus genome. Nature 310, 207-211. Bajaj, B.G., Murakami, M., and Robertson, E.S. (2007) Molecular biology of EBV in relationship to AIDS-associated oncogenesis. Cancer Treatment and Research 133, 141-162. Battivelli, E., Migraine, J., Lecossier, D., Matsuoka, S., Perez-Bercoff, D., Saragosti, S., Clavel, F., and Hance Allan, J. (2011) Modulation of TRIM5α Activity in Human Cells by Alternatively Spliced TRIM5 Isoforms. Journal of Virology 85, 7828-7835. Beaulaton, J., and Lockshin, R.A. (1977) Ultrastructural study of the normal degeneration of the intersegmental muscles of Antheraea polyphemus and Manduca sexta (Insecta, lepidoptera) with particular reference to cellular autophagy. Journal of Morphology 154, 39-57. Bertani, G. (1951) Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. Journal of Bacteriology 62, 293-300. Black, L.R., and Aiken, C. (2010) TRIM5alpha disrupts the structure of assembled HIV-1 capsid complexes in vitro. Journal of Virology 84, 6564-6569. Bloss, T.A., and Sugden, B. (1994) Optimal lengths for DNAs encapsidated by Epstein-Barr virus. Journal of Virology 68, 8217-8222. Brown, J.C., and Newcomb, W.W. (2011) Herpesvirus capsid assembly: insights from structural analysis. Current Opinion in Virology 1, 142-149. Burke, A.P., Yen, T.S., Shekitka, K.M., and Sobin, L.H. (1990) Lymphoepithelial carcinoma of the stomach with Epstein-Barr virus demonstrated by polymerase chain reaction. Modern Pathology 3, 377-380. Burkitt, D. (1958) A sarcoma involving the jaws in African children. British Journal of Surgery 46, 218-223. Callis, J. (2014) The ubiquitination machinery of the ubiquitin system. Arabidopsis Book 12, e0174. Campbell, E.M., Dodding, M.P., Yap, M.W., Wu, X., Gallois-Montbrun, S., Malim, M.H., Stoye, J.P., and Hope, T.J. (2007) TRIM5 alpha cytoplasmic bodies are highly dynamic structures. Molecular Biology of the Cell 18, 2102-2111. Campbell, E.M., and Hope, T.J. (2015) HIV-1 capsid: the multifaceted key player in HIV-1 infection. Nature Reviews: Microbiology 13, 471-483. Campbell, E.M., Weingart, J., Sette, P., Opp, S., Sastri, J., O'Connor, S.K., Talley, S., Diaz-Griffero, F., Hirsch, V., and Bouamr, F. (2016) TRIM5α-Mediated Ubiquitin Chain Conjugation Is Required for Inhibition of HIV-1 Reverse Transcription and Capsid Destabilization. Journal of Virology 90, 1849-1857. Carter, S.D., Mamede, J.I., Hope, T.J., and Jensen, G.J. (2020) Correlated cryogenic fluorescence microscopy and electron cryo-tomography shows that exogenous TRIM5α can form hexagonal lattices or autophagy aggregates in vivo. Proceedings of the National Academy of Sciences of the United States of America 117, 29702-29711. Chang, L.-K., and Liu, S.-T. (2000) Activation of the BRLF1 promoter and lytic cycle of Epstein–Barr virus by histone acetylation. Nucleic Acids Research 28, 3918-3925. Chang, L.K., Lee, Y.H., Cheng, T.S., Hong, Y.R., Lu, P.J., Wang, J.J., Wang, W.H., Kuo, C.W., Li, S.S., and Liu, S.T. (2004) Post-translational modification of Rta of Epstein-Barr virus by SUMO-1. Journal of Biological Chemistry 279, 38803-38812. Chang, P.J., Chang, Y.S., and Liu, S.T. (1998) Characterization of the BcLF1 promoter in Epstein-Barr virus. Journal of General Virology 79 ( Pt 8), 2003-2006. Chesnokova, L.S., Nishimura, S.L., and Hutt-Fletcher, L.M. (2009) Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8. Proceedings of the National Academy of Sciences of the United States of America 106, 20464-20469. Chiramel, A.I., Meyerson, N.R., McNally, K.L., Broeckel, R.M., Montoya, V.R., Méndez-Solís, O., Robertson, S.J., Sturdevant, G.L., Lubick, K.J., Nair, V., et al. (2019) TRIM5α restricts flavivirus replication by targeting the viral protease for proteasomal degradation. bioRxiv, 605345. Chiu, Y.F., Tung, C.P., Lee, Y.H., Wang, W.H., Li, C., Hung, J.Y., Wang, C.Y., Kawaguchi, Y., and Liu, S.T. (2007) A comprehensive library of mutations of Epstein Barr virus. Journal of General Virology 88, 2463-2472. Cloherty, A.P.M., Rader, A.G., Compeer, B., and Ribeiro, C.M.S. (2021) Human TRIM5α: Autophagy Connects Cell-Intrinsic HIV-1 Restriction and Innate Immune Sensor Functioning. Viruses 13. Cohen, J.I. (2000) Epstein–Barr Virus Infection. New England Journal of Medicine 343, 481-492. Connolly, S.A., Jackson, J.O., Jardetzky, T.S., and Longnecker, R. (2011) Fusing structure and function: a structural view of the herpesvirus entry machinery. Nature Reviews: Microbiology 9, 369-381. Crawford, D.H. (2001) Biology and disease associations of Epstein-Barr virus. Philosophical Transactions of the Royal Society of London Series B: Biological Sciences 356, 461-473. Dambaugh, T., Beisel, C., Hummel, M., King, W., Fennewald, S., Cheung, A., Heller, M., Raab-Traub, N., and Kieff, E. (1980) Epstein-Barr virus (B95-8) DNA VII: molecular cloning and detailed mapping. Proceedings of the National Academy of Sciences of the United States of America 77, 2999-3003. De Leo, A., Colavita, F., Ciccosanti, F., Fimia, G.M., Lieberman, P.M., and Mattia, E. (2015) Inhibition of autophagy in EBV-positive Burkitt's lymphoma cells enhances EBV lytic genes expression and replication. Cell Death & Disease 6, e1876. de Witte, L., Nabatov, A., Pion, M., Fluitsma, D., de Jong, M.A., de Gruijl, T., Piguet, V., van Kooyk, Y., and Geijtenbeek, T.B. (2007) Langerin is a natural barrier to HIV-1 transmission by Langerhans cells. Nature Medicine 13, 367-371. Deretic, V., Kimura, T., Timmins, G., Moseley, P., Chauhan, S., and Mandell, M. (2015) Immunologic manifestations of autophagy. Journal of Clinical Investigation 125, 75-84. Diaz-Griffero, F., Gallo, D.E., Hope, T.J., and Sodroski, J. (2011) Trafficking of some old world primate TRIM5α proteins through the nucleus. Retrovirology 8, 38. Diaz-Griffero, F., Kar, A., Perron, M., Xiang, S.H., Javanbakht, H., Li, X., and Sodroski, J. (2007) Modulation of retroviral restriction and proteasome inhibitor-resistant turnover by changes in the TRIM5alpha B-box 2 domain. Journal of Virology 81, 10362-10378. Diaz-Griffero, F., Li, X., Javanbakht, H., Song, B., Welikala, S., Stremlau, M., and Sodroski, J. (2006) Rapid turnover and polyubiquitylation of the retroviral restriction factor TRIM5. Virology 349, 300-315. Diaz-Griffero, F., Qin, X.-r., Hayashi, F., Kigawa, T., Finzi, A., Sarnak, Z., Lienlaf, M., Yokoyama, S., and Sodroski, J. (2009) A B-Box 2 surface patch important for TRIM5α self-association, capsid binding avidity, and retrovirus restriction. Journal of Virology 83, 10737-10751. Dolyniuk, M., Pritchett, R., and Kieff, E. (1976) Proteins of Epstein-Barr virus. I. Analysis of the polypeptides of purified enveloped Epstein-Barr virus. Journal of Virology 17, 935-949. Donaghy, G., and Jupp, R. (1995) Characterization of the Epstein-Barr virus proteinase and comparison with the human cytomegalovirus proteinase. Journal of Virology 69, 1265-1270. Epstein, M.A., Achong, B.G., and Barr, Y.M. (1964) Virus particles in cultured lymphoblasts from Burkitt's lymphoma. The Lancet 283, 702-703. Finley, D. (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annual Review of Biochemistry 78, 477-513. Fixman, E.D., Hayward, G.S., and Hayward, S.D. (1995) Replication of Epstein-Barr virus oriLyt: lack of a dedicated virally encoded origin-binding protein and dependence on Zta in cotransfection assays. Journal of Virology 69, 2998-3006. Fletcher, A.J., Vaysburd, M., Maslen, S., Zeng, J., Skehel, J.M., Towers, G.J., and James, L.C. (2018) Trivalent RING Assembly on Retroviral Capsids Activates TRIM5 Ubiquitination and Innate Immune Signaling. Cell Host & Microbe 24, 761-775.e766. Foot, N., Henshall, T., and Kumar, S. (2017) Ubiquitination and the Regulation of Membrane Proteins. Physiological Reviews 97, 253-281. Forshey, B.M., von Schwedler, U., Sundquist, W.I., and Aiken, C. (2002) Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. Journal of Virology 76, 5667-5677. Fujii, K., Yokoyama, N., Kiyono, T., Kuzushima, K., Homma, M., Nishiyama, Y., Fujita, M., and Tsurumi, T. (2000) The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1-BBLF2/3 complex. Journal of Virology 74, 2550-2557. Ganser-Pornillos, B.K., Chandrasekaran, V., Pornillos, O., Sodroski, J.G., Sundquist, W.I., and Yeager, M. (2011) Hexagonal assembly of a restricting TRIM5alpha protein. Proceedings of the National Academy of Sciences of the United States of America 108, 534-539. Ganser-Pornillos, B.K., and Pornillos, O. (2019) Restriction of HIV-1 and other retroviruses by TRIM5. Nature Reviews: Microbiology 17, 546-556. Gardella, T., Medveczky, P., Sairenji, T., and Mulder, C. (1984) Detection of circular and linear herpesvirus DNA molecules in mammalian cells by gel electrophoresis. Journal of Virology 50, 248-254. Gatica, D., Lahiri, V., and Klionsky, D.J. (2018) Cargo recognition and degradation by selective autophagy. Nature Cell Biology 20, 233-242. Giot, J.F., Mikaelian, I., Buisson, M., Manet, E., Joab, I., Nicolas, J.C., and Sergeant, A. (1991) Transcriptional interference between the EBV transcription factors EB1 and R: both DNA-binding and activation domains of EB1 are required. Nucleic Acids Research 19, 1251-1258. Goldstone, D.C., Walker, P.A., Calder, L.J., Coombs, P.J., Kirkpatrick, J., Ball, N.J., Hilditch, L., Yap, M.W., Rosenthal, P.B., Stoye, J.P., et al. (2014) Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice. Proceedings of the National Academy of Sciences of the United States of America 111, 9609-9614. Graham, F.L., Smiley, J., Russell, W.C., and Nairn, R. (1977) Characteristics of a human cell line transformed by DNA from human adenovirus type 5. Journal of General Virology 36, 59-74. Green, D.R., Galluzzi, L., and Kroemer, G. (2011) Mitochondria and the autophagy-inflammation-cell death axis in organismal aging. Science 333, 1109-1112. Groettrup, M., Pelzer, C., Schmidtke, G., and Hofmann, K. (2008) Activating the ubiquitin family: UBA6 challenges the field. Trends in Biochemical Sciences 33, 230-237. Grumati, P., and Dikic, I. (2018) Ubiquitin signaling and autophagy. Journal of Biological Chemistry 293, 5404-5413. Ha, S.-W., Ju, D., and Xie, Y. (2012) The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits. Biochemical and Biophysical Research Communications 419, 226-231. Hammerschmidt, W., and Sugden, B. (1988) Identification and characterization of oriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55, 427-433. Hampar, B., Tanaka, A., Nonoyama, M., and Derge, J.G. (1974) Replication of the resident repressed Epstein-Barr virus genome during the early S phase (S-1 period) of nonproducer Raji cells. Proceedings of the National Academy of Sciences of the United States of America 71, 631-633. Harbury, P.B., Tidor, B., and Kim, P.S. (1995) Repacking protein cores with backbone freedom: structure prediction for coiled coils. Proceedings of the National Academy of Sciences of the United States of America 92, 8408-8412. Harbury, P.B., Zhang, T., Kim, P.S., and Alber, T. (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407. Hardie, D.G. (2014) AMPK--sensing energy while talking to other signaling pathways. Cell Metabolism 20, 939-952. Hardwick, J.M., Lieberman, P.M., and Hayward, S.D. (1988) A new Epstein-Barr virus transactivator, R, induces expression of a cytoplasmic early antigen. Journal of Virology 62, 2274-2284. Hatakeyama, S. (2011) TRIM proteins and cancer. Nature Reviews Cancer 11, 792-804. Hatakeyama, S. (2017) TRIM Family Proteins: Roles in Autophagy, Immunity, and Carcinogenesis. Trends in Biochemical Sciences 42, 297-311. Hausen, H.Z., O'Neill, F.J., Freese, U.K., and Hecker, E. (1978) Persisting oncogenic herpesvirus induced by the tumour promoter TPA. Nature 272, 373-375. He, C., and Klionsky, D.J. (2009) Regulation mechanisms and signaling pathways of autophagy. Annual Review of Genetics 43, 67-93. Henderson, E.E., and Long, W.K. (1981) Host cell reactivation of uv- and X-ray-damaged herpes simplex virus by epstein-barr virus (EBV)-transformed lymphoblastoid cell lines. Virology 115, 237-248. Henle, G., and Henle, W. (1966) Immunofluorescence in cells derived from Burkitt's lymphoma. Journal of Bacteriology 91, 1248-1256. Henson, B.W., Perkins, E.M., Cothran, J.E., and Desai, P. (2009) Self-assembly of Epstein-Barr virus capsids. Journal of Virology 83, 3877-3890. Himathongkham, S., and Luciw, P.A. (1996) Restriction of HIV-1 (Subtype B) Replication at the Entry Step in Rhesus Macaque Cells. Virology 219, 485-488. Hofmann, W., Schubert, D., LaBonte, J., Munson, L., Gibson, S., Scammell, J., Ferrigno, P., and Sodroski, J. (1999) Species-specific, postentry barriers to primate immunodeficiency virus infection. Journal of Virology 73, 10020-10028. Homa, F.L., and Brown, J.C. (1997) Capsid assembly and DNA packaging in herpes simplex virus. Reviews in Medical Virology 7, 107-122. Hu, H., and Sun, S.-C. (2016) Ubiquitin signaling in immune responses. Cell Research 26, 457-483. Huang, H.H., Chen, C.S., Wang, W.H., Hsu, S.W., Tsai, H.H., Liu, S.T., and Chang, L.K. (2016) TRIM5α Promotes Ubiquitination of Rta from Epstein-Barr Virus to Attenuate Lytic Progression. Frontiers in Microbiology 7, 2129. Huang, H.H., Wang, W.H., Feng, T.H., and Chang, L.K. (2020) Rta is an Epstein-Barr virus tegument protein that improves the stability of capsid protein BORF1. Biochemical and Biophysical Research Communications 523, 773-779. Hughes, M.A., Brennan, P.M., Bunting, A.S., Cameron, K., Murray, A.F., and Shipston, M.J. (2014) Patterning human neuronal networks on photolithographically engineered silicon dioxide substrates functionalized with glial analogues. Journal of Biomedical Materials Research, Part A 102, 1350-1360. Hutt-Fletcher, L.M. (2007) Epstein-Barr virus entry. Journal of Virology 81, 7825-7832. Imai, S., Nishikawa, J., and Takada, K. (1998) Cell-to-Cell Contact as an Efficient Mode of Epstein-Barr Virus Infection of Diverse Human Epithelial Cells. Journal of Virology 72, 4371-4378. James Leo, C., Keeble Anthony, H., Khan, Z., Rhodes David, A., and Trowsdale, J. (2007) Structural basis for PRYSPRY-mediated tripartite motif (TRIM) protein function. Proceedings of the National Academy of Sciences 104, 6200-6205. Javanbakht, H., Diaz-Griffero, F., Stremlau, M., Si, Z., and Sodroski, J. (2005) The contribution of RING and B-box 2 domains to retroviral restriction mediated by monkey TRIM5alpha. Journal of Biological Chemistry 280, 26933-26940. Javanbakht, H., Yuan, W., Yeung, D.F., Song, B., Diaz-Griffero, F., Li, Y., Li, X., Stremlau, M., and Sodroski, J. (2006) Characterization of TRIM5alpha trimerization and its contribution to human immunodeficiency virus capsid binding. Virology 353, 234-246. Jin, M., Liu, X., and Klionsky, D.J. (2013) SnapShot: Selective autophagy. Cell 152, 368-368.e362. Johannsen, E., Luftig, M., Chase, M.R., Weicksel, S., Cahir-McFarland, E., Illanes, D., Sarracino, D., and Kieff, E. (2004) Proteins of purified Epstein-Barr virus. Proceedings of the National Academy of Sciences of the United States of America 101, 16286-16291. Kanda, T. (2018) EBV-Encoded Latent Genes. Advances in Experimental Medicine and Biology 1045, 377-394. Kang, M.-S., and Kieff, E. (2015) Epstein–Barr virus latent genes. Experimental & Molecular Medicine 47, e131-e131. Keown, J.R., Black, M.M., Ferron, A., Yap, M., Barnett, M.J., Pearce, F.G., Stoye, J.P., and Goldstone, D.C. (2018) A helical LC3-interacting region mediates the interaction between the retroviral restriction factor Trim5α and mammalian autophagy-related ATG8 proteins. Journal of Biological Chemistry 293, 18378-18386. Keown, J.R., Yang, J.X., Douglas, J., and Goldstone, D.C. (2016) Characterisation of assembly and ubiquitylation by the RBCC motif of Trim5α. Scientific Reports 6, 26837. Khammissa, R.A.G., Fourie, J., Chandran, R., Lemmer, J., and Feller, L. (2016) Epstein-Barr Virus and Its Association with Oral Hairy Leukoplakia: A Short Review. International Journal of Dentistry 2016, 4941783-4941783. Khan, M.M., Strack, S., Wild, F., Hanashima, A., Gasch, A., Brohm, K., Reischl, M., Carnio, S., Labeit, D., Sandri, M., et al. (2014) Role of autophagy, SQSTM1, SH3GLB1, and TRIM63 in the turnover of nicotinic acetylcholine receptors. Autophagy 10, 123-136. Kim, J., Kundu, M., Viollet, B., and Guan, K.-L. (2011a) AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nature Cell Biology 13, 132-141. Kim, J., Tipper, C., and Sodroski, J. (2011b) Role of TRIM5α RING domain E3 ubiquitin ligase activity in capsid disassembly, reverse transcription blockade, and restriction of simian immunodeficiency virus. Journal of Virology 85, 8116-8132. Kimura, T., Jain, A., Choi, S.W., Mandell, M.A., Johansen, T., and Deretic, V. (2017) TRIM-directed selective autophagy regulates immune activation. Autophagy 13, 989-990. Kimura, T., Jain, A., Choi, S.W., Mandell, M.A., Schroder, K., Johansen, T., and Deretic, V. (2015) TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity. Journal of Cell Biology 210, 973-989. Kimura, T., Mandell, M., and Deretic, V. (2016) Precision autophagy directed by receptor regulators - emerging examples within the TRIM family. Journal of Cell Science 129, 881-891. Ko, A., Lee, E.W., Yeh, J.Y., Yang, M.R., Oh, W., Moon, J.S., and Song, J. (2010) MKRN1 induces degradation of West Nile virus capsid protein by functioning as an E3 ligase. Journal of Virology 84, 426-436. Kobayashi, R., Kato, A., Sagara, H., Watanabe, M., Maruzuru, Y., Koyanagi, N., Arii, J., and Kawaguchi, Y. (2017) Herpes Simplex Virus 1 Small Capsomere-Interacting Protein VP26 Regulates Nucleocapsid Maturation. Journal of Virology 91. Komatsu, M., Waguri, S., Koike, M., Sou, Y.S., Ueno, T., Hara, T., Mizushima, N., Iwata, J., Ezaki, J., Murata, S., et al. (2007) Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-1163. Lamark, T., and Johansen, T. (2012) Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy. International Journal of Cell Biology 2012, 736905. Lee, J., Giordano, S., and Zhang, J. (2012) Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling. Biochemical Journal 441, 523-540. Li, X., and Sodroski, J. (2008) The TRIM5alpha B-box 2 domain promotes cooperative binding to the retroviral capsid by mediating higher-order self-association. Journal of Virology 82, 11495-11502. Li, X., Yeung, D.F., Fiegen, A.M., and Sodroski, J. (2011) Determinants of the higher order association of the restriction factor TRIM5alpha and other tripartite motif (TRIM) proteins. Journal of Biological Chemistry 286, 27959-27970. Li, Y., Li, X., Stremlau, M., Lee, M., and Sodroski, J. (2006) Removal of arginine 332 allows human TRIM5alpha to bind human immunodeficiency virus capsids and to restrict infection. Journal of Virology 80, 6738-6744. Li, Y.L., Chandrasekaran, V., Carter, S.D., Woodward, C.L., Christensen, D.E., Dryden, K.A., Pornillos, O., Yeager, M., Ganser-Pornillos, B.K., Jensen, G.J., et al. (2016) Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids. Elife 5. Liao, G., Wu, F.Y., and Hayward, S.D. (2001) Interaction with the Epstein-Barr virus helicase targets Zta to DNA replication compartments. Journal of Virology 75, 8792-8802. Lindahl, T., Adams, A., Bjursell, G., Bornkamm, G.W., Kaschka-Dierich, C., and Jehn, U. (1976) Covalently closed circular duplex DNA of Epstein-Barr virus in a human lymphoid cell line. Journal of Molecular Biology 102, 511-530. Liu, W., Cui, Y., Wang, C., Li, Z., Gong, D., Dai, X., Bi, G.-Q., Sun, R., and Zhou, Z.H. (2020a) Structures of capsid and capsid-associated tegument complex inside the Epstein–Barr virus. Nature Microbiology 5, 1285-1298. Liu, X., and Cohen, J.I. (2016) Epstein-Barr Virus (EBV) Tegument Protein BGLF2 Promotes EBV Reactivation through Activation of the p38 Mitogen-Activated Protein Kinase. Journal of Virology 90, 1129-1138. Liu, X., Sadaoka, T., Krogmann, T., and Cohen, J.I. (2020b) Epstein-Barr Virus (EBV) Tegument Protein BGLF2 Suppresses Type I Interferon Signaling To Promote EBV Reactivation. Journal of Virology 94. Lorick, K.L., Jensen, J.P., Fang, S., Ong, A.M., Hatakeyama, S., and Weissman, A.M. (1999) RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proceedings of the National Academy of Sciences of the United States of America 96, 11364-11369. Lu, K., den Brave, F., and Jentsch, S. (2017) Receptor oligomerization guides pathway choice between proteasomal and autophagic degradation. Nature Cell Biology 19, 732-739. Luka, J., Kallin, B., and Klein, G. (1979) Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate. Virology 94, 228-231. Lumb, K.J., and Kim, P.S. (1995) A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry 34, 8642-8648. Luo, H. (2016) Interplay between the virus and the ubiquitin-proteasome system: molecular mechanism of viral pathogenesis. Current Opinion in Virology 17, 1-10. Lupas, A., Van Dyke, M., and Stock, J. (1991) Predicting Coiled Coils from Protein Sequences. Science 252, 1162-1164. Mandell, M.A., Jain, A., Arko-Mensah, J., Chauhan, S., Kimura, T., Dinkins, C., Silvestri, G., Münch, J., Kirchhoff, F., Simonsen, A., et al. (2014) TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition. Developmental Cell 30, 394-409. Mauthe, M., Orhon, I., Rocchi, C., Zhou, X., Luhr, M., Hijlkema, K.J., Coppes, R.P., Engedal, N., Mari, M., and Reggiori, F. (2018) Chloroquine inhibits autophagic flux by decreasing autophagosome-lysosome fusion. Autophagy 14, 1435-1455. Meroni, G., and Diez-Roux, G. (2005) TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases. Bioessays 27, 1147-1157. Mettenleiter Thomas, C. (2002) Herpesvirus Assembly and Egress. Journal of Virology 76, 1537-1547. Meyer, H.-J., and Rape, M. (2014) Enhanced Protein Degradation by Branched Ubiquitin Chains. Cell 157, 910-921. Miller, N., and Hutt-Fletcher, L.M. (1992) Epstein-Barr virus enters B cells and epithelial cells by different routes. Journal of Virology 66, 3409-3414. Mische, C.C., Javanbakht, H., Song, B., Diaz-Griffero, F., Stremlau, M., Strack, B., Si, Z., and Sodroski, J. (2005) Retroviral restriction factor TRIM5alpha is a trimer. Journal of Virology 79, 14446-14450. Murphy, G., Pfeiffer, R., Camargo, M.C., and Rabkin, C.S. (2009) Meta-analysis shows that prevalence of Epstein-Barr virus-positive gastric cancer differs based on sex and anatomic location. Gastroenterology 137, 824-833. Nemerow, G.R., and Cooper, N.R. (1984) Early events in the infection of human B lymphocytes by Epstein-Barr virus: the internalization process. Virology 132, 186-198. Nemerow, G.R., Mold, C., Schwend, V.K., Tollefson, V., and Cooper, N.R. (1987) Identification of gp350 as the viral glycoprotein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: sequence homology of gp350 and C3 complement fragment C3d. Journal of Virology 61, 1416-1420. Niedobitek, G., Meru, N., and Delecluse, H.J. (2001) Epstein-Barr virus infection and human malignancies. International Journal of Experimental Pathology 82, 149-170. Nonoyama, M., Huang, C.H., Pagano, J.S., Klein, G., and Singh, S. (1973) DNA of Epstein-Barr virus detected in tissue of Burkitt's lymphoma and nasopharyngeal carcinoma. Proceedings of the National Academy of Sciences of the United States of America 70, 3265-3268. Odumade, O.A., Hogquist, K.A., and Balfour, H.H., Jr. (2011) Progress and problems in understanding and managing primary Epstein-Barr virus infections. Clinical Microbiology Reviews 24, 193-209. Oyama, T., Ichimura, K., Suzuki, R., Suzumiya, J., Ohshima, K., Yatabe, Y., Yokoi, T., Kojima, M., Kamiya, Y., Taji, H., et al. (2003) Senile EBV+ B-cell lymphoproliferative disorders: a clinicopathologic study of 22 patients. American Journal of Surgical Pathology 27, 16-26. Ozato, K., Shin, D.M., Chang, T.H., and Morse, H.C., 3rd (2008) TRIM family proteins and their emerging roles in innate immunity. Nature Reviews: Immunology 8, 849-860. Peña, Maria Marjorette O., Xing, Yang Y., Koli, S., and Berger, Franklin G. (2006) Role of N-terminal residues in the ubiquitin-independent degradation of human thymidylate synthase. Biochemical Journal 394, 355-363. Perez-Caballero, D., Hatziioannou, T., Zhang, F., Cowan, S., and Bieniasz, P.D. (2005) Restriction of human immunodeficiency virus type 1 by TRIM-CypA occurs with rapid kinetics and independently of cytoplasmic bodies, ubiquitin, and proteasome activity. Journal of Virology 79, 15567-15572. Perkins, E.M., Anacker, D., Davis, A., Sankar, V., Ambinder, R.F., and Desai, P. (2008) Small capsid protein pORF65 is essential for assembly of Kaposi's sarcoma-associated herpesvirus capsids. Journal of Virology 82, 7201-7211. Pertel, T., Hausmann, S., Morger, D., Züger, S., Guerra, J., Lascano, J., Reinhard, C., Santoni, F.A., Uchil, P.D., Chatel, L., et al. (2011) TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature 472, 361-365. Pfüller, R., and Hammerschmidt, W. (1996) Plasmid-like replicative intermediates of the Epstein-Barr virus lytic origin of DNA replication. Journal of Virology 70, 3423-3431. Pfoh, R., Lacdao, I.K., and Saridakis, V. (2015) Deubiquitinases and the new therapeutic opportunities offered to cancer. Endocrine-Related Cancer 22, T35-54. Pham, Q.T., Bouchard, A., Grütter, M.G., and Berthoux, L. (2010) Generation of human TRIM5alpha mutants with high HIV-1 restriction activity. Gene Therapy 17, 859-871. Pham, Q.T., Veillette, M., Brandariz-Nuñez, A., Pawlica, P., Thibert-Lefebvre, C., Chandonnet, N., Diaz-Griffero, F., and Berthoux, L. (2013) A novel aminoacid determinant of HIV-1 restriction in the TRIM5α variable 1 region isolated in a random mutagenic screen. Virus Research 173, 306-314. Pohl, C., and Dikic, I. (2019) Cellular quality control by the ubiquitin-proteasome system and autophagy. Science 366, 818-822. Raab-Traub, N., and Flynn, K. (1986) The structure of the termini of the Epstein-Barr virus as a marker of clonal cellular proliferation. Cell 47, 883-889. Reszka, N., Zhou, C., Song, B., Sodroski, J.G., and Knipe, D.M. (2010) Simian TRIM5alpha proteins reduce replication of herpes simplex virus. Virology 398, 243-250. Reymond, A., Meroni, G., Fantozzi, A., Merla, G., Cairo, S., Luzi, L., Riganelli, D., Zanaria, E., Messali, S., Cainarca, S., et al. (2001) The tripartite motif family identifies cell compartments. EMBO Journal 20, 2140-2151. Ribeiro, C.M., Sarrami-Forooshani, R., Setiawan, L.C., Zijlstra-Willems, E.M., van Hamme, J.L., Tigchelaar, W., van der Wel, N.N., Kootstra, N.A., Gringhuis, S.I., and Geijtenbeek, T.B. (2016) Receptor usage dictates HIV-1 restriction by human TRIM5α in dendritic cell subsets. Nature 540, 448-452. Riley, B.E., Lougheed, J.C., Callaway, K., Velasquez, M., Brecht, E., Nguyen, L., Shaler, T., Walker, D., Yang, Y., Regnstrom, K., et al. (2013) Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. Nature Communications 4, 1982. Rixon, F.J., Addison, C., McGregor, A., Macnab, S.J., Nicholson, P., Preston, V.G., and Tatman, J.D. (1996) Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins. Journal of General Virology 77 ( Pt 9), 2251-2260. Robinson William, H., and Steinman, L. (2022) Epstein-Barr virus and multiple sclerosis. Science 375, 264-265. Roganowicz, M.D., Komurlu, S., Mukherjee, S., Plewka, J., Alam, S.L., Skorupka, K.A., Wan, Y., Dawidowski, D., Cafiso, D.S., Ganser-Pornillos, B.K., et al. (2017) TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition. PLoS Pathogens 13, e1006686. Rold, C.J., and Aiken, C. (2008) Proteasomal degradation of TRIM5alpha during retrovirus restriction. PLoS Pathogens 4, e1000074. Saha, B., and Mandell, M.A. (2022) The retroviral restriction factor TRIM5/TRIM5α regulates mitochondrial quality control. Autophagy, 1-2. Saha, B., Salemi, M., Williams, G.L., Oh, S., Paffett, M.L., Phinney, B., and Mandell, M.A. (2022) Interactomic analysis reveals a homeostatic role for the HIV restriction factor TRIM5α in mitophagy. Cell Reports 39, 110797. Sanchez, J.G., Okreglicka, K., Chandrasekaran, V., Welker, J.M., Sundquist, W.I., and Pornillos, O. (2014) The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer. Proceedings of the National Academy of Sciences of the United States of America 111, 2494-2499. Scheffner, M., Nuber, U., and Huibregtse, J.M. (1995) Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 373, 81-83. Serio, T.R., Kolman, J.L., and Miller, G. (1997) Late gene expression from the Epstein-Barr virus BcLF1 and BFRF3 promoters does not require DNA replication in cis. Journal of Virology 71, 8726-8734. Shaid, S., Brandts, C.H., Serve, H., and Dikic, I. (2013) Ubiquitination and selective autophagy. Cell Death and Differentiation 20, 21-30. Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels. Analytical Chemistry 68, 850-858. Shibata, R., Sakai, H., Kawamura, M., Tokunaga, K., and Adachi, A. (1995) Early replication block of human immunodeficiency virus type 1 in monkey cells. Journal of General Virology 76 ( Pt 11), 2723-2730. Shin, J. (1998) P62 and the sequestosome, a novel mechanism for protein metabolism. Archives of Pharmacal Research 21, 629-633. Short, K.M., and Cox, T.C. (2006) Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding. Journal of Biological Chemistry 281, 8970-8980. Singh, R., and Cuervo, A.M. (2012) Lipophagy: connecting autophagy and lipid metabolism. International Journal of Cell Biology 2012, 282041. Slobodkin, M.R., and Elazar, Z. (2013) The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy. Essays in Biochemistry 55, 51-64. Speck, P., Haan, K.M., and Longnecker, R. (2000) Epstein-Barr virus entry into cells. Virology 277, 1-5. Stewart, M.D., Ritterhoff, T., Klevit, R.E., and Brzovic, P.S. (2016) E2 enzymes: more than just middle men. Cell Research 26, 423-440. Stremlau, M., Owens, C.M., Perron, M.J., Kiessling, M., Autissier, P., and Sodroski, J. (2004) The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys. Nature 427, 848-853. Suzuki, R., Moriishi, K., Fukuda, K., Shirakura, M., Ishii, K., Shoji, I., Wakita, T., Miyamura, T., Matsuura, Y., and Suzuki, T. (2009) Proteasomal turnover of hepatitis C virus core protein is regulated by two distinct mechanisms: a ubiquitin-dependent mechanism and a ubiquitin-independent but PA28gamma-dependent mechanism. Journal of Virology 83, 2389-2392. Takada, K. (1984) Cross-linking of cell surface immunoglobulins induces Epstein-Barr virus in Burkitt lymphoma lines. International Journal of Cancer 33, 27-32. Tomar, D., Singh, R., Singh, A.K., Pandya, C.D., and Singh, R. (2012) TRIM13 regulates ER stress induced autophagy and clonogenic ability of the cells. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1823, 316-326. Torok, M., and Etkin, L.D. (2001) Two B or not two B? Overview of the rapidly expanding B-box family of proteins. Differentiation 67, 63-71. Tovey, M.G., Lenoir, G., and Begon-Lours, J. (1978) Activation of latent Epstein-Barr virus by antibody to human IgM. Nature 276, 270-272. Trus, B.L., Heymann, J.B., Nealon, K., Cheng, N., Newcomb, W.W., Brown, J.C., Kedes, D.H., and Steven, A.C. (2001) Capsid structure of Kaposi's sarcoma-associated herpesvirus, a gammaherpesvirus, compared to those of an alphaherpesvirus, herpes simplex virus type 1, and a betaherpesvirus, cytomegalovirus. Journal of Virology 75, 2879-2890. Tsao, S.W., Tsang, C.M., Pang, P.S., Zhang, G., Chen, H., and Lo, K.W. (2012) The biology of EBV infection in human epithelial cells. Seminars in Cancer Biology 22, 137-143. Tsukada, M., and Ohsumi, Y. (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Letters 333, 169-174. Tsurumi, T., Fujita, M., and Kudoh, A. (2005) Latent and lytic Epstein-Barr virus replication strategies. Reviews in Medical Virology 15, 3-15. Tugizov, S.M., Berline, J.W., and Palefsky, J.M. (2003) Epstein-Barr virus infection of polarized tongue and nasopharyngeal epithelial cells. Nature Medicine 9, 307-314. Valimberti, I., Tiberti, M., Lambrughi, M., Sarcevic, B., and Papaleo, E. (2015) E2 superfamily of ubiquitin-conjugating enzymes: constitutively active or activated through phosphorylation in the catalytic cleft. Scientific Reports 5, 14849. Valladeau, J., Ravel, O., Dezutter-Dambuyant, C., Moore, K., Kleijmeer, M., Liu, Y., Duvert-Frances, V., Vincent, C., Schmitt, D., Davoust, J., et al. (2000) Langerin, a novel C-type lectin specific to Langerhans cells, is an endocytic receptor that induces the formation of Birbeck granules. Immunity 12, 71-81. van Gent, M., Braem, S.G.E., de Jong, A., Delagic, N., Peeters, J.G.C., Boer, I.G.J., Moynagh, P.N., Kremmer, E., Wiertz, E.J., Ovaa, H., et al. (2014) Epstein-Barr Virus Large Tegument Protein BPLF1 Contributes to Innate Immune Evasion through Interference with Toll-Like Receptor Signaling. PLOS Pathogens 10, e1003960. Vergne, I., and Deretic, V. (2010) The role of PI3P phosphatases in the regulation of autophagy. FEBS Letters 584, 1313-1318. von Schwedler, U.K., Stray, K.M., Garrus, J.E., and Sundquist, W.I. (2003) Functional surfaces of the human immunodeficiency virus type 1 capsid protein. Journal of Virology 77, 5439-5450. Walczak, M., and Martens, S. (2013) Dissecting the role of the Atg12-Atg5-Atg16 complex during autophagosome formation. Autophagy 9, 424-425. Wang, L., Howell, M.E.A., Sparks-Wallace, A., Hawkins, C., Nicksic, C.A., Kohne, C., Hall, K.H., Moorman, J.P., Yao, Z.Q., and Ning, S. (2019) p62-mediated Selective autophagy endows virus-transformed cells with insusceptibility to DNA damage under oxidative stress. PLoS Pathogens 15, e1007541. Wang, W.-H., Chang, L.-K., and Liu, S.-T. (2011) Molecular Interactions of Epstein-Barr Virus Capsid Proteins. Journal of Virology 85, 1615-1624. Wang, W.H., Kuo, C.W., Chang, L.K., Hung, C.C., Chang, T.H., and Liu, S.T. (2015) Assembly of Epstein-Barr Virus Capsid in Promyelocytic Leukemia Nuclear Bodies. Journal of Virology 89, 8922-8931. Wei, Y., Chen, S., Wang, M., and Cheng, A. (2018) Tripartite motif-containing proteins precisely and positively affect host antiviral immune response. Scandinavian Journal of Immunology 87, e12669. Wong, P.M., Puente, C., Ganley, I.G., and Jiang, X. (2013) The ULK1 complex: sensing nutrient signals for autophagy activation. Autophagy 9, 124-137. Wu, X., Anderson, J.L., Campbell, E.M., Joseph, A.M., and Hope, T.J. (2006) Proteasome inhibitors uncouple rhesus TRIM5alpha restriction of HIV-1 reverse transcription and infection. Proceedings of the National Academy of Sciences of the United States of America 103, 7465-7470. Yamauchi, K., Wada, K., Tanji, K., Tanaka, M., and Kamitani, T. (2008) Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential role. FEBS Journal 275, 1540-1555. Yang, Y., Brandariz-Nuñez, A., Fricke, T., Ivanov, D.N., Sarnak, Z., and Diaz-Griffero, F. (2014) Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction. Virology 448, 217-228. Yap, M.W., Nisole, S., Lynch, C., and Stoye, J.P. (2004) Trim5alpha protein restricts both HIV-1 and murine leukemia virus. Proceedings of the National Academy of Sciences of the United States of America 101, 10786-10791. Yap, M.W., Nisole, S., and Stoye, J.P. (2005) A Single Amino Acid Change in the SPRY Domain of Human Trim5α Leads to HIV-1 Restriction. Current Biology 15, 73-78. Yau, R.G., Doerner, K., Castellanos, E.R., Haakonsen, D.L., Werner, A., Wang, N., Yang, X.W., Martinez-Martin, N., Matsumoto, M.L., Dixit, V.M., et al. (2017) Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control. Cell 171, 918-933.e920. Ylä-Anttila, P., Gupta, S., and Masucci, M.G. (2021) The Epstein-Barr virus deubiquitinase BPLF1 targets SQSTM1/p62 to inhibit selective autophagy. Autophagy 17, 3461-3474. Young, L., and Murray, P. (2003) Young LS, Murray PG.. Epstein-Barr virus and oncogenesis: from latent genes to tumours. Oncogene 22: 5108-5121. Oncogene 22, 5108-5121. Yudina, Z., Roa, A., Johnson, R., Biris, N., de Souza Aranha Vieira, Daniel A., Tsiperson, V., Reszka, N., Taylor, Alexander B., Hart, P.J., Demeler, B., et al. (2015) RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin. Cell Reports 12, 788-797. Zhang, P., Zhang, Z., Fu, Y., Zhang, Y., Washburn, M.P., Florens, L., Wu, M., Huang, C., Hou, Z., and Mohan, M. (2021) K63-linked ubiquitination of DYRK1A by TRAF2 alleviates Sprouty 2-mediated degradation of EGFR. Cell Death & Disease 12, 608. Zhao, G., Ke, D., Vu, T., Ahn, J., Shah, V.B., Yang, R., Aiken, C., Charlton, L.M., Gronenborn, A.M., and Zhang, P. (2011) Rhesus TRIM5α Disrupts the HIV-1 Capsid at the InterHexamer Interfaces. PLOS Pathogens 7, e1002009. Zheng, N., and Shabek, N. (2017) Ubiquitin Ligases: Structure, Function, and Regulation. Annual Review of Biochemistry 86, 129-157. | - |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/86343 | - |
dc.description.abstract | EB病毒 (Epstein-Barr virus) 隸屬於皰疹病毒γ亞科,不僅會感染全球近90%的人口,亦是第一個被發現具有致癌力的人類病毒。EB病毒的生活史包含潛伏期 (Latency) 以及溶裂期 (Lytic cycle),而其在溶裂期時會大量表現病毒基因,並產生病毒顆粒,在此過程中外鞘殼體 (Capsid) 的組裝扮演相當關鍵的角色,其中小外鞘殼體蛋白質 (Small capsid protein) BFRF3已被證實在EB病毒的外鞘殼體組裝過程中是不可或缺的。TRIM5α (Tripartite motif 5 alpha) 是一種反轉錄病毒的限制因子,在恆河猴中可以抑制愛滋病毒 (HIV-1)的感染,其具有泛素連接酶E3的活性以及作為自噬作用受器 (Autophagy cargo receptor) 的能力。先前本實驗室已發現TRIM5α可以作為EBV次外鞘蛋白質 (Minor capsid protein) BORF1的泛素連接酶E3,且會形成TRIMosome並以精準性自噬作用 (Precision autophagy) 將BORF1降解。本研究首先確認TRIM5α是透過PRYSPRY domain與BFRF3結合,然後以變性免疫沉澱分析證實TRIM5α為BFRF3的泛素連接酶E3,且TRIM5α的RING domian與其促進BFRF3上的泛素化修飾有關。本研究建構了BFRF3的全lysine突變株 (BFRF3-5KR),結果發現BFRF3-5KR不會被泛素化,其穩定性也比BFRF3高。接下來本研究發現TRIM5α不僅會降低BFRF3-5KR的穩定性,也會與BFRF3-5KR結合,此外TRIMosome的成員Beclin-1以及p62亦會與BFRF3-5KR結合,而在加入會抑制溶酶體 (Lysosome) 活性的氯喹 (Chloroquine, CQ) 後,會提升BFRF3與p62的結合,顯示TRIM5α可能藉由形成TRIMosome以精準性自噬作用降解BFRF3。未來將進一步探討BFRF3與TRIMosome的關係,得以更了解TRIM5α限制DNA病毒的機制。 | zh_TW |
dc.description.abstract | Epstein-Barr virus (EBV) belongs to the herpesvirus gamma subfamily, which not only infects nearly 90% individuals worldwide, but also is the first human virus found to be carcinogenic. EBV has two life cycles, latency and lytic cycle. EBV expresses a number of viral genes and produces infectious virions during lytic cycle. During this process, capsid assembly plays a crucial role. The small capsid protein BFRF3 has been shown to be indispensable in the assembly of EBV capsid. TRIM5α (Tripartite motif 5 alpha) is a restriction factor that inhibits Human immunodeficiency virus type 1 (HIV-1) infection in rhesus macaques. The protein acts as an autophagy cargo receptor with the activity of ubiquitin E3 ligase. Our laboratory has previously found that TRIM5α not only is the ubiquitin E3 ligase of BORF1, but also degrades BORF1 via precision autophagy by forming the platform named TRIMosome. In this study, we firstly found that TRIM5α binds directly to BFRF3 through the conserved PRYSPRY domain. TRIM5α is the ubiquitin E3 ligase of BFRF3, and the RING domain of TRIM5α is required for the ubiquitination on BFRF3. Moreover, a mutant of BFRF3 (BFRF3-5KR) was generated whose whole lysine residues were mutated. The mutant BFRF3-5KR is not ubiquitinated and its stability is higher than that of BFRF3. Overexpressing TRIM5α reduced the stability of BFRF3-5KR. Finally, this study demonstrated that BFRF3-5KR binds to TRIMosome members including TRIM5α, Beclin-1 and p62. The interaction between BFRF3 and p62 was enhanced in the presence with chloroquine, revealing that TRIM5α may destabilize BFRF3 through precision autophagy. Overall, this study affords the potentiality of TRIM5α-mediated antiviral strategy against EBV. We will further explore the relationship between BFRF3 and TRIMosome to understand the antiviral mechanism of TRIMosome in this study. | en |
dc.description.provenance | Made available in DSpace on 2023-03-19T23:50:15Z (GMT). No. of bitstreams: 1 U0001-2408202215433700.pdf: 3772209 bytes, checksum: bf0af58c8278b99e51bb2d41b6e72ef3 (MD5) Previous issue date: 2022 | en |
dc.description.tableofcontents | 致謝 i 中文摘要 ii Abstract iii 目錄 v 表目錄 vi 圖目錄 vi 前言 1 一、 Epstein-Barr病毒 (Epstein-Barr virus, EBV) 1 二、 泛素化修飾 (Ubiquitination) 6 三、 自噬作用 (Autophagy) 8 四、 TRIM5α (Tripartite motif-containing protein 5 alpha) 10 研究目的 15 材料與方法 16 一、 細胞株 16 二、 細菌 16 三、 質體DNA的萃取 16 四、 質體與抗體 16 五、 細胞轉染 (Transfection) 16 六、 SDS-PAGE蛋白質膠體電泳及西方墨點法分析 (Western blot analysis) 17 七、 蛋白質的誘導表現 17 八、 GST融合蛋白質沉澱分析 (GST Pull-down assay) 17 九、 免疫共沉澱分析 (Co-immunoprecipitation) 18 十、 變性免疫沉澱分析 (Denature Immunoprecipitation) 18 十一、蛋白質穩定性分析 (Protein stability analysis ) 19 結果 20 一、TRIM5α以PRYSPRY domain與BFRF3結合 20 二、TRIM5α會增加BFRF3的泛素化修飾 20 三、BFRF3的泛素化修飾會降低其穩定性 21 四、蛋白酶體及自噬作用降解途徑均會影響BFRF3及BFRF3-5KR的穩定性 22 五、TRIM5α會降低BFRF3-5KR的穩定性 23 六、TRIM5α、Beclin1和p62可以直接和BFRF3-5KR結合 24 七、抑制自噬作用會增加p62與BFRF3的結合 25 討論 26 圖表 32 參考資料 51 附錄 72 附錄一、EBV正二十面體單元上外鞘殼體蛋白質之原子模型結構及分布 72 附錄二、自噬作用的作用過程 73 附錄三、精準性自噬作用的機制 74 附錄四、TRIM5α限制HIV-1的機制 75 | - |
dc.language.iso | zh_TW | - |
dc.title | TRIM5α介導的TRIMosome對EB病毒BFRF3蛋白質的穩定性調控 | zh_TW |
dc.title | Regulation of the stability of Epstein-Barr virus BFRF3 by TRIM5α-mediated TRIMosome | en |
dc.type | Thesis | - |
dc.date.schoolyear | 110-2 | - |
dc.description.degree | 碩士 | - |
dc.contributor.oralexamcommittee | 劉世東;莊健盈;吳育騏;羅凱尹 | zh_TW |
dc.contributor.oralexamcommittee | Shih-Tung Liu;Jian-Ying Chuang;Yu-Chi Wu;Kai-Yin Lo | en |
dc.subject.keyword | EB病毒,BFRF3蛋白質,TRIM5α蛋白質,TRIMosome,泛素化,精準性自噬作用, | zh_TW |
dc.subject.keyword | Epstein-Barr virus,BFRF3,TRIM5α,TRIMosome,Ubiquitination,Precision autophagy, | en |
dc.relation.page | 75 | - |
dc.identifier.doi | 10.6342/NTU202202768 | - |
dc.rights.note | 同意授權(全球公開) | - |
dc.date.accepted | 2022-08-25 | - |
dc.contributor.author-college | 生命科學院 | - |
dc.contributor.author-dept | 生化科技學系 | - |
dc.date.embargo-lift | 2027-08-24 | - |
顯示於系所單位: | 生化科技學系 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-110-2.pdf 此日期後於網路公開 2027-08-24 | 3.68 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。