請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/41710
完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 陳美如(Mei-Ru Chen) | |
dc.contributor.author | Jiin-Tarng Wang | en |
dc.contributor.author | 王錦堂 | zh_TW |
dc.date.accessioned | 2021-06-15T00:28:28Z | - |
dc.date.available | 2009-02-10 | |
dc.date.copyright | 2009-02-10 | |
dc.date.issued | 2009 | |
dc.date.submitted | 2009-01-20 | |
dc.identifier.citation | Abate, D.A., Watanabe, S. and Mocarski, E.S. (2004) Major human cytomegalovirus structural protein pp65 (ppUL83) prevents interferon response factor 3 activation in the interferon response. J Virol, 78, 10995-11006.
Alexopoulou, L., Holt, A.C., Medzhitov, R. and Flavell, R.A. (2001) Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature, 413, 732-738. Andrejeva, J., Childs, K.S., Young, D.F., Carlos, T.S., Stock, N., Goodbourn, S. and Randall, R.E. (2004) The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. Proc Natl Acad Sci U S A, 101, 17264-17269. Asai, R., Kato, A., Kato, K., Kanamori-Koyama, M., Sugimoto, K., Sairenji, T., Nishiyama, Y. and Kawaguchi, Y. (2006) Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1. J Virol, 80, 5125-5134. Au, W.C., Moore, P.A., Lowther, W., Juang, Y.T. and Pitha, P.M. (1995) Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes. Proc Natl Acad Sci U S A, 92, 11657-11661. 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., Seguin, C. and et al. (1984) DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature, 310, 207-211. Balachandran, S., Roberts, P.C., Brown, L.E., Truong, H., Pattnaik, A.K., Archer, D.R. and Barber, G.N. (2000) Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection. Immunity, 13, 129-141. Berger, M., Stahl, N., Del Sal, G. and Haupt, Y. (2005) Mutations in proline 82 of p53 impair its activation by Pin1 and Chk2 in response to DNA damage. Mol Cell Biol, 25, 5380-5388. Boehme, K.W., Guerrero, M. and Compton, T. (2006) Human cytomegalovirus envelope glycoproteins B and H are necessary for TLR2 activation in permissive cells. J Immunol, 177, 7094-7102. Boehme, K.W., Singh, J., Perry, S.T. and Compton, T. (2004) Human cytomegalovirus elicits a coordinated cellular antiviral response via envelope glycoprotein B. J Virol, 78, 1202-1211. Browne, E.P. and Shenk, T. (2003) Human cytomegalovirus UL83-coded pp65 virion protein inhibits antiviral gene expression in infected cells. Proc Natl Acad Sci U S A, 100, 11439-11444. Brzozka, K., Finke, S. and Conzelmann, K.K. (2005) Identification of the rabies virus alpha/beta interferon antagonist: phosphoprotein P interferes with phosphorylation of interferon regulatory factor 3. J Virol, 79, 7673-7681. Chang, T.H., Liao, C.L. and Lin, Y.L. (2006) Flavivirus induces interferon-beta gene expression through a pathway involving RIG-I-dependent IRF-3 and PI3K-dependent NF-kappaB activation. Microbes Infect, 8, 157-171. Chang, Y., Tung, C.H., Huang, Y.T., Lu, J., Chen, J.Y. and Tsai, C.H. (1999) Requirement for cell-to-cell contact in Epstein-Barr virus infection of nasopharyngeal carcinoma cells and keratinocytes. J Virol, 73, 8857-8866. Chee, A.V. and Roizman, B. (2004) Herpes simplex virus 1 gene products occlude the interferon signaling pathway at multiple sites. J Virol, 78, 4185-4196. Chen, C. and Okayama, H. (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol, 7, 2745-2752. Chen, M.R., Chang, S.J., Huang, H. and Chen, J.Y. (2000a) A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro. J Virol, 74, 3093-3104. Chen, M.R., Huang, H., Fen, C.Y. and Chen, J.Y. (2000b) A novel EBNA-1 tag system for high level expression and efficient detection of fusion proteins in vitro and in vivo. J Virol Methods, 85, 35-41. Chen, M.R., Tsai, C.H., Wu, F.F., Kan, S.H., Yang, C.S. and Chen, J.Y. (1999) The major immunogenic epitopes of Epstein-Barr virus (EBV) nuclear antigen 1 are encoded by sequence domains which vary among nasopharyngeal carcinoma biopsies and EBV-associated cell lines. J Gen Virol, 80 ( Pt 2), 447-455. Clement, J.F., Bibeau-Poirier, A., Gravel, S.P., Grandvaux, N., Bonneil, E., Thibault, P., Meloche, S. and Servant, M.J. (2008) Phosphorylation of IRF-3 on Ser 339 generates a hyperactive form of IRF-3 through regulation of dimerization and CBP association. J Virol, 82, 3984-3996. Dai, X., Sayama, K., Yamasaki, K., Tohyama, M., Shirakata, Y., Hanakawa, Y., Tokumaru, S., Yahata, Y., Yang, L., Yoshimura, A. and Hashimoto, K. (2006) SOCS1-negative feedback of STAT1 activation is a key pathway in the dsRNA-induced innate immune response of human keratinocytes. J Invest Dermatol, 126, 1574-1581. de Jesus, O., Smith, P.R., Spender, L.C., Elgueta Karstegl, C., Niller, H.H., Huang, D. and Farrell, P.J. (2003) Updated Epstein-Barr virus (EBV) DNA sequence and analysis of a promoter for the BART (CST, BARF0) RNAs of EBV. J Gen Virol, 84, 1443-1450. Delhaye, S., van Pesch, V. and Michiels, T. (2004) The leader protein of Theiler's virus interferes with nucleocytoplasmic trafficking of cellular proteins. J Virol, 78, 4357-4362. Dragan, A.I., Hargreaves, V.V., Makeyeva, E.N. and Privalov, P.L. (2007) Mechanisms of activation of interferon regulator factor 3: the role of C-terminal domain phosphorylation in IRF-3 dimerization and DNA binding. Nucleic Acids Res, 35, 3525-3534. Duguay, D., Mercier, F., Stagg, J., Martineau, D., Bramson, J., Servant, M., Lin, R., Galipeau, J. and Hiscott, J. (2002) In vivo interferon regulatory factor 3 tumor suppressor activity in B16 melanoma tumors. Cancer Res, 62, 5148-5152. Epstein, M.A., Henle, G., Achong, B.G. and Barr, Y.M. (1965) Morphological and Biological Studies on a Virus in Cultured Lymphoblasts from Burkitt's Lymphoma. J Exp Med, 121, 761-770. Evans, A.S., Niederman, J.C. and McCollum, R.W. (1968) Seroepidemiologic studies of infectious mononucleosis with EB virus. N Engl J Med, 279, 1121-1127. Fitzgerald, K.A., McWhirter, S.M., Faia, K.L., Rowe, D.C., Latz, E., Golenbock, D.T., Coyle, A.J., Liao, S.M. and Maniatis, T. (2003) IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. Nat Immunol, 4, 491-496. Fuld, S., Cunningham, C., Klucher, K., Davison, A.J. and Blackbourn, D.J. (2006) Inhibition of interferon signaling by the Kaposi's sarcoma-associated herpesvirus full-length viral interferon regulatory factor 2 protein. J Virol, 80, 3092-3097. Gao, S.J., Boshoff, C., Jayachandra, S., Weiss, R.A., Chang, Y. and Moore, P.S. (1997) KSHV ORF K9 (vIRF) is an oncogene which inhibits the interferon signaling pathway. Oncogene, 15, 1979-1985. Georgel, P., Jiang, Z., Kunz, S., Janssen, E., Mols, J., Hoebe, K., Bahram, S., Oldstone, M.B. and Beutler, B. (2007) Vesicular stomatitis virus glycoprotein G activates a specific antiviral Toll-like receptor 4-dependent pathway. Virology, 362, 304-313. Gershburg, E. and Pagano, J.S. (2002) Phosphorylation of the Epstein-Barr virus (EBV) DNA polymerase processivity factor EA-D by the EBV-encoded protein kinase and effects of the L-riboside benzimidazole 1263W94. J Virol, 76, 998-1003. Gershburg, E. and Pagano, J.S. (2008) Conserved herpesvirus protein kinases. Biochim Biophys Acta, 1784, 203-212. Gershburg, E., Raffa, S., Torrisi, M.R. and Pagano, J.S. (2007) Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J Virol, 81, 5407-5412. Gitlin, L., Barchet, W., Gilfillan, S., Cella, M., Beutler, B., Flavell, R.A., Diamond, M.S. and Colonna, M. (2006) Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus. Proc Natl Acad Sci U S A, 103, 8459-8464. Grogan, E., Jenson, H., Countryman, J., Heston, L., Gradoville, L. and Miller, G. (1987) Transfection of a rearranged viral DNA fragment, WZhet, stably converts latent Epstein-Barr viral infection to productive infection in lymphoid cells. Proc Natl Acad Sci U S A, 84, 1332-1336. Hahn, A.M., Huye, L.E., Ning, S., Webster-Cyriaque, J. and Pagano, J.S. (2005) Interferon regulatory factor 7 is negatively regulated by the Epstein-Barr virus immediate-early gene, BZLF-1. J Virol, 79, 10040-10052. Hanks, S.K. and Hunter, T. (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. Faseb J, 9, 576-596. Hannon, G.J., Demetrick, D. and Beach, D. (1993) Isolation of the Rb-related p130 through its interaction with CDK2 and cyclins. Genes Dev, 7, 2378-2391. Harmon, M.A., Boehm, M.F., Heyman, R.A. and Mangelsdorf, D.J. (1995) Activation of mammalian retinoid X receptors by the insect growth regulator methoprene. Proc Natl Acad Sci U S A, 92, 6157-6160. Hato, S.V., Ricour, C., Schulte, B.M., Lanke, K.H., de Bruijni, M., Zoll, J., Melchers, W.J., Michiels, T. and van Kuppeveld, F.J. (2007) The mengovirus leader protein blocks interferon-alpha/beta gene transcription and inhibits activation of interferon regulatory factor 3. Cell Microbiol, 9, 2921-2930. Heil, F., Hemmi, H., Hochrein, H., Ampenberger, F., Kirschning, C., Akira, S., Lipford, G., Wagner, H. and Bauer, S. (2004) Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science, 303, 1526-1529. Hemmi, H., Takeuchi, O., Kawai, T., Kaisho, T., Sato, S., Sanjo, H., Matsumoto, M., Hoshino, K., Wagner, H., Takeda, K. and Akira, S. (2000) A Toll-like receptor recognizes bacterial DNA. Nature, 408, 740-745. Henle, G., Henle, W., Clifford, P., Diehl, V., Kafuko, G.W., Kirya, B.G., Klein, G., Morrow, R.H., Munube, G.M., Pike, P., Tukei, P.M. and Ziegler, J.L. (1969) Antibodies to Epstein-Barr virus in Burkitt's lymphoma and control groups. J Natl Cancer Inst, 43, 1147-1157. Henle, G., Henle, W. and Diehl, V. (1968) Relation of Burkitt's tumor-associated herpes-ytpe virus to infectious mononucleosis. Proc Natl Acad Sci U S A, 59, 94-101. Henle, W., Diehl, V., Kohn, G., Zur Hausen, H. and Henle, G. (1967) Herpes-type 69 virus and chromosome marker in normal leukocytes after growth with irradiated Burkitt cells. Science, 157, 1064-1065. Heylbroeck, C., Balachandran, S., Servant, M.J., DeLuca, C., Barber, G.N., Lin, R. and Hiscott, J. (2000) The IRF-3 transcription factor mediates Sendai virus-induced apoptosis. J Virol, 74, 3781-3792. Hiscott, J. (2007) Triggering the innate antiviral response through IRF-3 activation. J Biol Chem, 282, 15325-15329. Honda, K., Takaoka, A. and Taniguchi, T. (2006) Type I interferon [corrected] gene induction by the interferon regulatory factor family of transcription factors. Immunity, 25, 349-360. Honda, K. and Taniguchi, T. (2006) IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors. Nat Rev Immunol, 6, 644-658. Hopp, T.P. and Woods, K.R. (1981) Prediction of protein antigenic determinants from amino acid sequences. Proc Natl Acad Sci U S A, 78, 3824-3828. Hudewentz, J., Bornkamm, G.W. and Zur Hausen, H. (1980) Effect of the diterpene ester TPA on Epstein-Barr virus antigen- and DNA synthesis in producer and nonproducer cell lines. Virology, 100, 175-178. 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. J Virol, 72, 4371-4378. Ishii, K.J. and Akira, S. (2006) Innate immune recognition of, and regulation by, DNA. Trends Immunol, 27, 525-532. Iwamura, T., Yoneyama, M., Yamaguchi, K., Suhara, W., Mori, W., Shiota, K., Okabe, Y., Namiki, H. and Fujita, T. (2001) Induction of IRF-3/-7 kinase and NF-kappaB in response to double-stranded RNA and virus infection: common and unique pathways. Genes Cells, 6, 375-388. James, P., Halladay, J. and Craig, E.A. (1996) Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics, 144, 1425-1436. Jaworska, J., Gravel, A., Fink, K., Grandvaux, N. and Flamand, L. (2007) Inhibition of transcription of the beta interferon gene by the human herpesvirus 6 immediate-early 1 protein. J Virol, 81, 5737-5748. 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. Proc Natl Acad Sci U S A, 101, 16286-16291. Karpova, A.Y., Trost, M., Murray, J.M., Cantley, L.C. and Howley, P.M. (2002) Interferon regulatory factor-3 is an in vivo target of DNA-PK. Proc Natl Acad Sci U S A, 99, 2818-2823. Kato, H., Takeuchi, O., Sato, S., Yoneyama, M., Yamamoto, M., Matsui, K., Uematsu, S., Jung, A., Kawai, T., Ishii, K.J., Yamaguchi, O., Otsu, K., Tsujimura, T., Koh, C.S., Reis e Sousa, C., Matsuura, Y., Fujita, T. and Akira, S. (2006) Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature, 441, 101-105. Kato, K., Kawaguchi, Y., Tanaka, M., Igarashi, M., Yokoyama, A., Matsuda, G., Kanamori, M., Nakajima, K., Nishimura, Y., Shimojima, M., Phung, H.T., Takahashi, E. and Hirai, K. (2001) Epstein-Barr virus-encoded protein kinase BGLF4 mediates hyperphosphorylation of cellular elongation factor 1delta (EF-1delta): EF-1delta is universally modified by conserved protein kinases of herpesviruses in mammalian cells. J Gen Virol, 82, 1457-1463. Kato, K., Yokoyama, A., Tohya, Y., Akashi, H., Nishiyama, Y. and Kawaguchi, Y. (2003) Identification of protein kinases responsible for phosphorylation of Epstein-Barr virus nuclear antigen leader protein at serine-35, which regulates its coactivator function. J Gen Virol, 84, 3381-3392. Kim, T.K., Lee, J.S., Oh, S.Y., Jin, X., Choi, Y.J., Lee, T.H., Lee, E., Choi, Y.K., You, S., Chung, Y.G., Lee, J.B., DePinho, R.A., Chin, L. and Kim, H. (2007) Direct transcriptional activation of promyelocytic leukemia protein by IFN regulatory factor 3 induces the p53-dependent growth inhibition of cancer cells. Cancer Res, 67, 11133-11140. Kolaskar, A.S. and Tongaonkar, P.C. (1990) A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett, 276, 172-174. Krosky, P.M., Baek, M.C. and Coen, D.M. (2003) The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress. J Virol, 77, 905-914. Krug, A., Luker, G.D., Barchet, W., Leib, D.A., Akira, S. and Colonna, M. (2004) Herpes simplex virus type 1 activates murine natural interferon-producing cells through toll-like receptor 9. Blood, 103, 1433-1437. Kudoh, A., Daikoku, T., Ishimi, Y., Kawaguchi, Y., Shirata, N., Iwahori, S., Isomura, H. and Tsurumi, T. (2006) Phosphorylation of MCM4 at sites inactivating DNA helicase activity of the MCM4-MCM6-MCM7 complex during Epstein-Barr virus productive replication. J Virol, 80, 10064-10072. Kumar, K.P., McBride, K.M., Weaver, B.K., Dingwall, C. and Reich, N.C. (2000) Regulated nuclear-cytoplasmic localization of interferon regulatory factor 3, a subunit of double-stranded RNA-activated factor 1. Mol Cell Biol, 20, 4159-4168. Latz, E., Schoenemeyer, A., Visintin, A., Fitzgerald, K.A., Monks, B.G., Knetter, C.F., 71 Lien, E., Nilsen, N.J., Espevik, T. and Golenbock, D.T. (2004) TLR9 signals after translocating from the ER to CpG DNA in the lysosome. Nat Immunol, 5, 190-198. Lee, C.P., Chen, J.Y., Wang, J.T., Kimura, K., Takemoto, A., Lu, C.C. and Chen, M.R. (2007) Epstein-Barr virus BGLF4 kinase induces premature chromosome condensation through activation of condensin and topoisomerase II. J Virol, 81, 5166-5180. Lee, C.P., Huang, Y.H., Lin, S.F., Chang, Y., Chang, Y.H., Takada, K. and Chen, M.R. (2008) Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production. J Virol, 82, 11913-11926. Lefort, S., Soucy-Faulkner, A., Grandvaux, N. and Flamand, L. (2007) Binding of Kaposi's sarcoma-associated herpesvirus K-bZIP to interferon-responsive factor 3 elements modulates antiviral gene expression. J Virol, 81, 10950-10960. Lemaire, P.A., Lary, J. and Cole, J.L. (2005) Mechanism of PKR activation: dimerization and kinase activation in the absence of double-stranded RNA. J Mol Biol, 345, 81-90. Lin, R., Genin, P., Mamane, Y., Sgarbanti, M., Battistini, A., Harrington, W.J., Jr., Barber, G.N. and Hiscott, J. (2001) HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators. Oncogene, 20, 800-811. Lu, C.C., Chen, Y.C., Wang, J.T., Yang, P.W. and Chen, M.R. (2007) Xeroderma pigmentosum C is involved in Epstein Barr virus DNA replication. J Gen Virol, 88, 3234-3243. 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. Lund, J., Sato, A., Akira, S., Medzhitov, R. and Iwasaki, A. (2003) Toll-like receptor 9-mediated recognition of Herpes simplex virus-2 by plasmacytoid dendritic cells. J Exp Med, 198, 513-520. Makarova, O., Kamberov, E. and Margolis, B. (2000) Generation of deletion and point mutations with one primer in a single cloning step. Biotechniques, 29, 970-972. Mantovani, F., Tocco, F., Girardini, J., Smith, P., Gasco, M., Lu, X., Crook, T. and Del Sal, G. (2007) The prolyl isomerase Pin1 orchestrates p53 acetylation and dissociation from the apoptosis inhibitor iASPP. Nat Struct Mol Biol, 14,912-920. Marschall, M., Marzi, A., aus dem Siepen, P., Jochmann, R., Kalmer, M., Auerochs, S., Lischka, P., Leis, M. and Stamminger, T. (2005) Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina. J Biol Chem, 280, 33357-33367. Melroe, G.T., DeLuca, N.A. and Knipe, D.M. (2004) Herpes simplex virus 1 hasmultiple mechanisms for blocking virus-induced interferon production. J Virol, 78, 8411-8420. Miller, D.M., Zhang, Y., Rahill, B.M., Waldman, W.J. and Sedmak, D.D. (1999) Human cytomegalovirus inhibits IFN-alpha-stimulated antiviral and immunoregulatory responses by blocking multiple levels of IFN-alpha signal transduction. J Immunol, 162, 6107-6113. Mori, M., Yoneyama, M., Ito, T., Takahashi, K., Inagaki, F. and Fujita, T. (2004)Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation. J Biol Chem, 279,9698-9702. Morin, P., Braganca, J., Bandu, M.T., Lin, R., Hiscott, J., Doly, J. and Civas, A. (2002) Preferential binding sites for interferon regulatory factors 3 and 7 involved in interferon-A gene transcription. J Mol Biol, 316, 1009-1022. Morrison, E.E., Wang, Y.F. and Meredith, D.M. (1998) Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument.J Virol, 72, 7108-7114. Netterwald, J.R., Jones, T.R., Britt, W.J., Yang, S.J., McCrone, I.P. and Zhu, H. (2004) Postattachment events associated with viral entry are necessary for induction of interferon-stimulated genes by human cytomegalovirus. J Virol, 78, 6688-6691. Okabe, Y., Kawane, K., Akira, S., Taniguchi, T. and Nagata, S. (2005) Toll-like receptor-independent gene induction program activated by mammalian DNA escaped from apoptotic DNA degradation. J Exp Med, 202, 1333-1339. Parekh, B.S. and Maniatis, T. (1999) Virus infection leads to localized hyperacetylation of histones H3 and H4 at the IFN-beta promoter. Mol Cell, 3, 125-129. Pope, J.H., Horne, M.K. and Scott, W. (1968) Transformation of foetal human keukocytes in vitro by filtrates of a human leukaemic cell line containing herpes-like virus. Int J Cancer, 3, 857-866. Preston, C.M., Harman, A.N. and Nicholl, M.J. (2001) Activation of interferon response factor-3 in human cells infected with herpes simplex virus type 1 or human cytomegalovirus. J Virol, 75, 8909-8916. Qualtiere, L.F. and Pearson, G.R. (1979) Epstein-Barr virus-induced membrane antigens: immunochemical characterization of Triton X-100 solubilized viral membrane antigens from EBV-superinfected Raji cells. Int J Cancer, 23,808-817. Ragoczy, T., Heston, L. and Miller, G. (1998) The Epstein-Barr virus Rta protein activates lytic cycle genes and can disrupt latency in B lymphocytes. J Virol, 72, 7978-7984. Rickinson, A.B. and Kieff, E.D. (2007) Epstein-Barr Virus. In D. M. a. P. M Howley (ed) Fields Virology (fifth ed), 2, 2656-2700. Lippincott Williams& Wilkins. Saira, K., Zhou, Y. and Jones, C. (2007) The infected cell protein 0 encoded by bovine herpesvirus 1 (bICP0) induces degradation of interferon response factor 3 and, consequently, inhibits beta interferon promoter activity. J Virol, 81, 3077-3086. Saitoh, T., Tun-Kyi, A., Ryo, A., Yamamoto, M., Finn, G., Fujita, T., Akira, S., Yamamoto, N., Lu, K.P. and Yamaoka, S. (2006) Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the proly isomerase Pin1. Nat Immunol, 7, 598-605. Samanta, M., Iwakiri, D., Kanda, T., Imaizumi, T. and Takada, K. (2006) EB virus-encoded RNAs are recognized by RIG-I and activate signaling to induce type I IFN. Embo J, 25, 4207-4214. Sarkar, S.N., Peters, K.L., Elco, C.P., Sakamoto, S., Pal, S. and Sen, G.C. (2004) Novel roles of TLR3 tyrosine phosphorylation and PI3 kinase in double-stranded RNA signaling. Nat Struct Mol Biol, 11, 1060-1067. Schroder, M. and Bowie, A.G. (2005) TLR3 in antiviral immunity: key player or bystander? Trends Immunol, 26, 462-468.Sen, G.C. (2001) Viruses and interferons. Annu Rev Microbiol, 55, 255-281. Servant, M.J., Grandvaux, N., tenOever, B.R., Duguay, D., Lin, R. and Hiscott, J. (2003) Identification of the minimal phosphoacceptor site required for in vivo activation of interferon regulatory factor 3 in response to virus and double-stranded RNA. J Biol Chem, 278, 9441-9447. Servant, M.J., ten Oever, B., LePage, C., Conti, L., Gessani, S., Julkunen, I., Lin, R. and Hiscott, J. (2001) Identification of distinct signaling pathways leading to the phosphorylation of interferon regulatory factor 3. J Biol Chem, 276, 355-363. Sharma, S., tenOever, B.R., Grandvaux, N., Zhou, G.P., Lin, R. and Hiscott, J. (2003) Triggering the interferon antiviral response through an IKK-related pathway. Science, 300, 1148-1151. Shibaki, T., Suzutani, T., Yoshida, I., Ogasawara, M. and Azuma, M. (2001) Participation of type I interferon in the decreased virulence of the UL13 gene-deleted mutant of herpes simplex virus type 1. J Interferon Cytokine Res, 21, 279-285. Suhara, W., Yoneyama, M., Kitabayashi, I. and Fujita, T. (2002) Direct involvement of CREB-binding protein/p300 in sequence-specific DNA binding of virus-activated interferon regulatory factor-3 holocomplex. J Biol Chem, 277, 22304-22313. Takada, K. (1984) Cross-linking of cell surface immunoglobulins induces Epstein-Barr virus in Burkitt lymphoma lines. Int J Cancer, 33, 27-32. Takada, K., Horinouchi, K., Ono, Y., Aya, T., Osato, T., Takahashi, M. and Hayasaka, S. (1991) An Epstein-Barr virus-producer line Akata: establishment of the cell line and analysis of viral DNA. Virus Genes, 5, 147-156. Takaoka, A., Wang, Z., Choi, M.K., Yanai, H., Negishi, H., Ban, T., Lu, Y., Miyagishi, M., Kodama, T., Honda, K., Ohba, Y. and Taniguchi, T. (2007) DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature, 448, 501-505. Tsai, C.H., Williams, M.V. and Glaser, R. (1991) Characterization of two monoclonal antibodies to Epstein-Barr virus diffuse early antigen which react to two different epitopes and have different biological function. J Virol Methods, 33, 47-52. Tseng, S.F., Chang, C.Y., Wu, K.J. and Teng, S.C. (2005) Importin KPNA2 is required for proper nuclear localization and multiple functions of NBS1. J Biol Chem, 280, 39594-39600. van Zeijl, M., Fairhurst, J., Baum, E.Z., Sun, L. and Jones, T.R. (1997) The human cytomegalovirus UL97 protein is phosphorylated and a component of virions. Virology, 231, 72-80. Wang, J.T., Yang, P.W., Lee, C.P., Han, C.H., Tsai, C.H. and Chen, M.R. (2005) Detection of Epstein-Barr virus BGLF4 protein kinase in virus replication compartments and virus particles. J Gen Virol, 86, 3215-3225. Wathelet, M.G., Lin, C.H., Parekh, B.S., Ronco, L.V., Howley, P.M. and Maniatis, T. (1998) Virus infection induces the assembly of coordinately activated transcription factors on the IFN-beta enhancer in vivo. Mol Cell, 1, 507-518. Wolf, D.G., Courcelle, C.T., Prichard, M.N. and Mocarski, E.S. (2001) Distinct and separate roles for herpesvirus-conserved UL97 kinase in cytomegalovirus DNA synthesis and encapsidation. Proc Natl Acad Sci U S A, 98, 1895-1900. Wolf, D.G., Honigman, A., Lazarovits, J., Tavor, E. and Panet, A. (1998) Characterization of the human cytomegalovirus UL97 gene product as a virion-associated protein kinase. Arch Virol, 143, 1223-1232. Wu, L., Fossum, E., Joo, C.H., Inn, K.S., Shin, Y.C., Johannsen, E., Hutt-Fletcher, L.M., Hass, J. and Jung, J.U. (2009) Epstein-Barr virus LF2: an antagonist to type I interferon. J Virol, 83, 1140-1146. Yang, P.W., Chang, S.S., Tsai, C.H., Chao, Y.H. and Chen, M.R. (2008) Effect of phosphorylation on the transactivation activity of Epstein-Barr virus BMRF1, a major target of the viral BGLF4 kinase. J Gen Virol, 89, 884-895. Yoneyama, M., Kikuchi, M., Matsumoto, K., Imaizumi, T., Miyagishi, M., Taira, K.,Foy, E., Loo, Y.M., Gale, M., Jr., Akira, S., Yonehara, S., Kato, A. and Fujita, T. (2005) Shared and unique functions of the DExD/H-box helicases RIG-I,MDA5, and LGP2 in antiviral innate immunity. J Immunol, 175, 2851-2858. Yoneyama, M., Kikuchi, M., Natsukawa, T., Shinobu, N., Imaizumi, T., Miyagishi, M., Taira, K., Akira, S. and Fujita, T. (2004) The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses.Nat Immunol, 5, 730-737. Yoneyama, M., Suhara, W., Fukuhara, Y., Fukuda, M., Nishida, E. and Fujita, T. (1998) Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF-3 and CBP/p300. Embo J, 17, 1087-1095. Yoshiyama, H., Imai, S., Shimizu, N. and Takada, K. (1997) Epstein-Barr virus infection of human gastric carcinoma cells: implication of the existence of a new virus receptor different from CD21. J Virol, 71, 5688-5691. Yue, W., Gershburg, E. and Pagano, J.S. (2005) Hyperphosphorylation of EBNA2 by Epstein-Barr virus protein kinase suppresses transactivation of the LMP1 promoter. J Virol, 79, 5880-5885. Zhou, Z.X., Kemppainen, J.A. and Wilson, E.M. (1995) Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol Endocrinol, 9, 605-615. Zhu, F.X., King, S.M., Smith, E.J., Levy, D.E. and Yuan, Y. (2002) A Kaposi's sarcoma-associated herpesviral protein inhibits virus-mediated induction of type I interferon by blocking IRF-7 phosphorylation and nuclear accumulation. Proc Natl Acad Sci U S A, 99, 5573-5578. | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/41710 | - |
dc.description.abstract | EB病毒感染全世界超過百分之九十的人口,而且和一些惡性腫瘤例如淋巴癌、鼻咽癌、胃癌以及移植後淋巴癌有高度相關性。為了更加了解這些疾病和病毒致病因子之間的關係,在本研究中,探討EB病毒所合成出以辨識脯胺酸絲胺酸/酥胺酸(Ser/Thr Pro)的BGLF4蛋白激酶,在病毒致病因子和宿主細胞之間的交互作用及其生物意義。為了探討BGLF4的可能功能,首先利用BGLF4的專一性單株抗體,偵測BGLF4在EB病毒複製的細胞中主要位在核內,同時也被包裹在病毒顆粒中。經由酵母雙雜交系統的篩選,發現干擾素調控因子3 (IRF3)的剪接變異體可以和BGLF4蛋白交互作用,並經短暫性轉染共同沉澱法和試管內GST-融合蛋白沉澱方法確定其交互作用。在利用報導質體分析中,BGLF4有效抑制poly(I:C)所刺激的干擾素β啟動子和IRF3反應區域的活性。而且BGLF4有效的抑制內生性干擾素βmRNA的表現以及STAT1 (Signal Transducers and Activators of Transcription protein 1)在第701個胺基酸酪氨酸的位置的磷酸化。進一步探討可能的機轉,BGLF4不影響poly(I:C)所引起IRF3形成雙聚體,轉移至核內,或是與CBP (cAMP Response Element Binding Protein)結合的能力。利用染色質免疫沉澱分析法,發現BGLF4會減少被活化的IRF3結合在帶有IRF3反應區域的之干擾素β啟動子上。BGLF4可以在試管內磷酸化GST-IRF3。利用點突變的分析發現絲胺酸339-脯胺酸340的磷酸化所引發Pin1的調控方式並不涉及BGLF4對IRF3的抑制作用;而是位於IRF3 DNA結合區域和干擾素調控因子結合區域中間的3個SP序列,包括Ser123、Ser173及Thr180的磷酸化可以加成性地反應BGLF4抑制IRF3的轉活化功能。同時發現在被活化進入溶裂期的EB病毒陽性NA細胞中,IRF3 也被活化。若送入siRNA抑制BGLF4的表現量,則帶有IRF3反應區域的報導質體活性會被提高。本研究的結果發現疱疹病毒的蛋白激酶可以透過一種新的機制抑制細胞的干擾素活化,以利病毒複製。 | zh_TW |
dc.description.abstract | Epstein-Barr virus (EBV) infects more than 90% worldwide population, and is highly associated with many malignancies such as lymphoma, nasopharyngeal carcinoma (NPC), gastric carcinoma, and post-transplantation lymphoma diseases. In this study, EBV encoded proline-directed ser/thr protein kinase BGLF4 was studied for the interplay between virus virulent factors and the host factors and the biological significance of the interaction. To search for the possible functions of BGLF4, specific monoclonal antibodies (MoAbs) were generated to demonstrate that BGLF4 mainly localized in the nucleus of the EBV positive epithelial cells, and it is a virion-associated protein kinase. Moreover, through a yeast two-hybrid screening approach, a splicing variant of interferon regulatory factor 3 (IRF3) was found to interact with BGLF4 protein. This interaction was further defined by co-immunoprecipitation in transfected cells and GST pull-down in vitro. Using reporter assays, BGLF4 effectively suppressed the poly(I:C)-stimulated IFNβ promoter and IRF3 responsive element activities. Moreover, BGLF4 repressed poly(I:C)-stimulated expression of endogenous IFNβ mRNA and phosphorylation of STAT1 at Tyr701. In searching for a possible mechanism, BGLF4 did not affect dimerization, nuclear translocation, or CBP recruitment of IRF3 upon poly(I:C)treatment. Notably, BGLF4 reduced the amount of active IRF3 recruited to the IRF3 responsive element (IRE) containing the IFNβ promoter region in a ChIP assay. BGLF4 phosphorylated GST-IRF3 in vitro, but Ser339-Pro340 phosphorylationdependent, Pin1-mediated down regulation is not responsible for the repression. Most importantly, three proline-dependent phosphorylation sites at Ser123, Ser173 and Thr180, which cluster in a region between the DNA binding and IRF association domains of IRF3, contributed additively to BGLF4 mediated repression of IRF3(5D) transactivation activity. IRF3 signaling was activated in reactivated EBV positive NA cells, and knockdown of BGLF4 further stimulated IRF3 responsive reporter activity. The data presented here thus provide a novel mechanism by which herpes viral protein kinases suppress host innate immune responses and facilitate virus replication. | en |
dc.description.provenance | Made available in DSpace on 2021-06-15T00:28:28Z (GMT). No. of bitstreams: 1 ntu-98-D90445007-1.pdf: 3575389 bytes, checksum: 5f6c2abcf711d3a9cfc88e4e1773ba54 (MD5) Previous issue date: 2009 | en |
dc.description.tableofcontents | 中文摘要………………………………………………………………… I
Abstract……………………………………………………………… II Contents……………………………………………………………… IV Chapter 1: Introduction……………………………………………………… 1 1.1 Epstein-Barr virus………………………………………………1 1.1.1 The viral structure and genome of EBV………………… 1 1.1.2 The life cycle of EBV……………………………………… 1 1.1.3 EBV associated diseases…………………………………… 2 1.2 Innate immunity………………………………………………… 3 1.2.1 Interplay between virus and innate immunity………… 3 1.2.2 Herpesvirus and innate immune responses………………7 1.3 BGLF4 protein kinase………………………………………… 7 1.3.1 Regulatory function of BGLF4……………………………… 8 1.4 Interferon regulatory factor 3……………………………… 9 1.5 Aims of this study…………………………………………… 10 Chapter 2 Results………………………………………………………… 11 2.1 Generation of BGLF4 MoAbs…………………………………… 11 2.2 Characterization of the expression of BGLF4 protein kinase in EBV positive cells……………………… 12 2.2.1 Detection of BGLF4 protein in EBV replicating epithelial cells……………………………12 2.2.2 Identification of BGLF4 as the virion-associated protein kinase………………………… 13 2.3 BGLF4 suppresses interferon regulatory factor 3 transactivation activity…………… 14 2.3.1 BGLF4 interacts with a splicing variant and authentic form of IRF3……………………… 15 2.3.2 BGLF4 suppresses IRF3-dependent transcriptional activation…………………… 17 2.3.3 BGLF4 suppresses endogenous poly(I:C)-triggered signaling pathway ……………18 2.3.4 BGLF4 does not suppress poly(I:C)-triggered IRF3 dimerization, translocation, or CBP recruitment…………………………………. 19 2.3.5 BGLF4 suppresses poly(I:C)-triggered IRF3 binding to PRDIII-I of IFNβ promoter………………………………...... 20 2.3.6 BGLF4 phosphorylates IRF3 in vitro, but does not adapt a Pin1-mediated IRF3 degradation mechanism to block IRF3 signaling… 20 2.3.7 Ser123, Ser173 and Thr180 of IRF3 contribute additively to BGLF4 mediated suppression of IRF3(5D)……………………………... 21 2.3.8 Knockdown of BGLF4 enhances IRF3 responsive reporter activity in EBV-reactivated cells………………………………22 Chapter 3: Discussion…………………………………………… 23 3.1 Characterization of BGLF4 in EBV positive cells………23 3.2 BGLF4 suppresses IRF3 signaling pathway………………… 24 3.3 Closing remarks………………………………………………… 27 Chapter 4: Materials & Methods………………………………… 29 4.1 Plasmid construction………………………………………… 29 4.2 Cell culture, transfection, and induction of viral lytic cycle………………………………31 4.3 Purification of bacterially expressed recombinant BGLF4……………… 31 4.4 Generation of BGLF4 specific MoAbs……………………… 32 4.5 Immunoprecipitation assay…………………………………… 32 4.6 Indirect immunofluorescence………………………………… 33 4.7 Purification of EBV viral particles………………………33 4.8 Virion DNA extraction and polymerase chain reaction………………… 34 4.9 Electron microscopy………………………………………… 34 4.10 Yeast two-hybrid screening………………………………… 34 4.11 dsRNA stimulation…………………………………………… 35 4.12 Co-immunoprecipitation……………………………………… 35 4.13 Expression and purification of GST fusion proteins…………………… 35 4.14 In vitro transcription/translation………………………36 4.15 GST pull-down assays…………………………………………36 4.16 Reporter assays………………………………………………………….… 36 4.17 RNA purification and quantitative real-time RT-PCR………………….… 37 4.18 Analysis of IRF-3 dimerization by native PAGE…………………………. 37 4.19 Chromatin immunoprecipitation (ChIP) assay……………………………. 38 4.20 Immunoprecipitation kinase assay…………………………39 4.21 Reporter assay of IRF3 responsive activity in EBV positive NA cells and design of siBGLF4………………………………………………………... 40 Table Table 1 Summary of characterization of BGLF4 MoAbs……………………. 41 Table 2 Oligonucleotide primers and DNA templates used to generate site-directed mutants of IRF3(5D)………………………………… 42 Figures Fig. 1 Characterization of BGLF4 MoAbs …………………………………… 43 Fig. 2 Immunogenic epitopes of BGLF4 recognized by different MoAbs were analyzed by immunoblotting…………………………………………… 44 Fig. 3 Expression of BGLF4 protein in EBV-positive NA cells……………… 45 Fig. 4 Detection of BGLF4 protein in EBV viral particles…………………… 46 Fig. 5 BGLF4 interacts with a splicing variant and authentic form of IRF3………………47 Fig. 6 BGLF4 interacts IRF3 in transiently transfected HeLa cells…………………………………… 48 Fig. 7 BGLF4 does not interact with GFP in transiently transfected HeLa cells……………… 49 Fig. 8 BGLF4 interacts with IRF3 in vitro………………… 50 Fig. 9 Schematic diagram of DNA sequence and transcription factor binding sites VII of the IFNβ promoter (Wathelet et al., 1998)…………………… 51 Fig. 10 BGLF4 suppresses IRF3 transactivation activity in transient reporter assay 52 Fig. 11 BGLF4 suppresses endogenous poly(I:C)-triggered signaling pathway... 53 Fig. 12 BGLF4 does not suppress poly(I:C)-triggered IRF3 dimerization……… 54 Fig. 13 BGLF4 does not suppress poly(I:C)-triggered IRF3 translocation……… 55 Fig. 14 BGLF4 does not suppress poly(I:C)-triggered IRF3 to recruit CBP………56 Fig. 15 BGLF4 suppresses poly(I:C)-triggered IRF3 binding to PRDIII-I of IFNβ promoter……………………………… 57 Fig. 16 BGLF4 phosphorylates IRF3 in vitro………………… 58 Fig. 17 BGLF4 does not adapt a Pin1-mediated mechanism to block IRF3 activation…………………………………………… 59 Fig. 18 Summary of currently identified phosphorylation sites on IRF3 and IRF3(5D) based mutants used in this study……………………………… 60 Fig. 19 Ser123, Ser173 and Thr180 of IRF3 contribute additively to BGLF4 mediated suppression of IRF3(5D) in transient reporter assay………….. 61 Fig. 20 BGLF4 interacts with IRF3 in EBV reactivated EBV positive epithelial cells…………………………………. 62 Fig. 21 Knockdown of BGLF4 enhances IRF3 responsive reporter activity in EBV reactivated NPC cells……………………………………………………... 63 Fig. 22 The hypothetic model of BGLF4 function in repressing IRF3 transactivation in EBV positive cells…………………………………………………….. 64 Fig. 23 Strategies of BGLF4 to counteract cellular limitation and facilitate viral replication…………………………………………………………65 References…………………………………………………………… 66 Appendix I. Curriculum vitae…………………………………………………77 | |
dc.language.iso | en | |
dc.title | EB病毒BGLF4蛋白激酶特性及其抑制干擾素調節因子3
訊息傳遞功能之研究 | zh_TW |
dc.title | Characterization of Epstein-Barr virus BGLF4 kinase and
its effect on repressing interferon regulatory factor 3 signaling pathway | en |
dc.type | Thesis | |
dc.date.schoolyear | 97-1 | |
dc.description.degree | 博士 | |
dc.contributor.oralexamcommittee | 鄧述諄(Shu-Chun Teng),董馨蓮(Shin-Lian Doong),黃麗華(Lih-Hwa Hwang),林宜玲(Yi-Ling Lin),李建國(Chien-Kuo Lee) | |
dc.subject.keyword | 蛋白激酶,干擾素調節因子3, | zh_TW |
dc.subject.keyword | BGLF4 kinase,interferon regulatory factor 3, | en |
dc.relation.page | 78 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2009-01-21 | |
dc.contributor.author-college | 醫學院 | zh_TW |
dc.contributor.author-dept | 微生物學研究所 | zh_TW |
顯示於系所單位: | 微生物學科所 |
文件中的檔案:
檔案 | 大小 | 格式 | |
---|---|---|---|
ntu-98-1.pdf 目前未授權公開取用 | 3.49 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。