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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 張麗冠(Chang Li-Kwan) | |
dc.contributor.author | Tzu-Hui Feng | en |
dc.contributor.author | 馮資惠 | zh_TW |
dc.date.accessioned | 2021-06-16T06:47:16Z | - |
dc.date.available | 2019-08-14 | |
dc.date.copyright | 2014-08-14 | |
dc.date.issued | 2014 | |
dc.date.submitted | 2014-07-25 | |
dc.identifier.citation | Abaitua F, Hollinshead M, Bolstad M, Crump CM, O'Hare P (2012) A Nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore. J Virol 86: 8998-9014
Adams A (1987) Replication of latent Epstein-Barr virus genomes in Raji cells. J Virol 61: 1743-1746 Adams A, Pozos TC, Purvey HV (1989) Replication of latent Epstein-Barr virus genomes in normal and malignant lymphoid cells. Int J Cancer 44: 560-564 Amon W, Farrell PJ (2005) Reactivation of Epstein-Barr virus from latency. Rev Med Virol 15: 149-156 Andersson-Anvret M, Forsby N, Klein G, Henle W, Biorklund A (1979) Relationship between the Epstein-Barr virus genome and nasopharyngeal carcinoma in Caucasian patients. Int J Cancer 23: 762-767 Asai R, Kato A, Kato K, Kanamori-Koyama M, Sugimoto K, Sairenji T, Nishiyama Y, 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 Baer R, Bankier AT, Biggin MD, Deininger PL, Farrell PJ, Gibson TJ, Hatfull G, Hudson GS, Satchwell SC, Seguin C, et al. (1984) DNA sequence and expression of the B95-8 Epstein-Barr virus genome. Nature 310: 207-211 Bajaj BG, Murakami M, Robertson ES (2007) Molecular biology of EBV in relationship to AIDS-associated oncogenesis. Cancer Treat Res 133: 141-162 Batisse J, Manet E, Middeldorp J, Sergeant A, Gruffat H (2005) Epstein-Barr virus mRNA export factor EB2 is essential for intranuclear capsid assembly and production of gp350. J Virol 79: 14102-14111 Batterson W, Roizman B (1983) Characterization of the herpes simplex virion-associated factor responsible for the induction of alpha genes. J Virol 46: 371-377 Biggin M, Bodescot M, Perricaudet M, Farrell P (1987) Epstein-Barr virus gene expression in P3HR1-superinfected Raji cells. J Virol 61: 3120-3132 Booy FP, Trus BL, Newcomb WW, Brown JC, Conway JF, Steven AC (1994) Finding a needle in a haystack: detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of herpes simplex virus). Proc Natl Acad Sci U S A 91: 5652-5656 Boutell C, Everett RD (2013) Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J Gen Virol 94: 465-481 Burke AP, Yen TS, Shekitka KM, Sobin LH (1990) Lymphoepithelial carcinoma of the stomach with Epstein-Barr virus demonstrated by polymerase chain reaction. Mod Pathol 3: 377-380 Burkitt D (1958) A sarcoma involving the jaws in African children. Br J Surg 46: 218-223 Burkitt D (1962) A children's cancer dependent on climatic factors. Nature 194: 232-234 Calderwood MA, Holthaus AM, Johannsen E (2008) The Epstein-Barr virus LF2 protein inhibits viral replication. J Virol 82: 8509-8519 Calderwood MA, Venkatesan K, Xing L, Chase MR, Vazquez A, Holthaus AM, Ewence AE, Li N, Hirozane-Kishikawa T, Hill DE, Vidal M, Kieff E, Johannsen E (2007) Epstein-Barr virus and virus human protein interaction maps. Proc Natl Acad Sci U S A 104: 7606-7611 Campbell ME, Palfreyman JW, Preston CM (1984) Identification of herpes simplex virus DNA sequences which encode a trans-acting polypeptide responsible for stimulation of immediate early transcription. J Mol Biol 180: 1-19 Chang FR, Hsieh YC, Chang YF, Lee KH, Wu YC, Chang LK (2010a) Inhibition of the Epstein-Barr virus lytic cycle by moronic acid. Antiviral Res 85: 490-495 Chang LK, Chuang JY, Nakao M, Liu ST (2010b) MCAF1 and synergistic activation of the transcription of Epstein-Barr virus lytic genes by Rta and Zta. Nucleic Acids Res 38: 4687-4700 Chang LK, Chung JY, Hong YR, Ichimura T, Nakao M, Liu ST (2005) Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus via an interaction with MCAF1. Nucleic Acids Res 33: 6528-6539 Chang LK, Lee YH, Cheng TS, Hong YR, Lu PJ, Wang JJ, Wang WH, Kuo CW, Li SS, Liu ST (2004a) Post-translational modification of Rta of Epstein-Barr virus by SUMO-1. J Biol Chem 279: 38803-38812 Chang LK, Liu ST (2000) Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation. Nucleic Acids Res 28: 3918-3925 Chang LK, Liu ST, Kuo CW, Wang WH, Chuang JY, Bianchi E, Hong YR (2008) Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM. J Mol Biol 379: 231-242 Chang LK, Wei TT, Chiu YF, Tung CP, Chuang JY, Hung SK, Li C, Liu ST (2003) Inhibition of Epstein-Barr virus lytic cycle by (-)-epigallocatechin gallate. Biochem Biophys Res Commun 301: 1062-1068 Chang PJ, Chang YS, Liu ST (1998a) Characterization of the BcLF1 promoter in Epstein-Barr virus. J Gen Virol 79: 2003-2006 Chang PJ, Chang YS, Liu ST (1998b) Role of Rta in the translation of bicistronic BZLF1 of Epstein-Barr virus. J Virol 72: 5128-5136 Chang Y, Lee HH, Chang SS, Hsu TY, Wang PW, Chang YS, Takada K, Tsai CH (2004b) Induction of Epstein-Barr virus latent membrane protein 1 by a lytic transactivator Rta. J Virol 78: 13028-13036 Chang YN, Dong DL, Hayward GS, Hayward SD (1990) The Epstein-Barr virus Zta transactivator: a member of the bZIP family with unique DNA-binding specificity and a dimerization domain that lacks the characteristic heptad leucine zipper motif. J Virol 64: 3358-3369 Chen LW, Chang PJ, Delecluse HJ, Miller G (2005) Marked variation in response of consensus binding elements for the Rta protein of Epstein-Barr virus. J Virol 79: 9635-9650 Chen LW, Raghavan V, Chang PJ, Shedd D, Heston L, Delecluse HJ, Miller G (2009) Two phenylalanines in the C-terminus of Epstein-Barr virus Rta protein reciprocally modulate its DNA binding and transactivation function. Virology 386: 448-461 Chen YJ, Tsai WH, Chen YL, Ko YC, Chou SP, Chen JY, Lin SF (2011) Epstein-Barr virus (EBV) Rta-mediated EBV and Kaposi's sarcoma-associated herpesvirus lytic reactivations in 293 cells. PLoS One 6: e17809 Chevallier-Greco A, Gruffat H, Manet E, Calender A, Sergeant A (1989) The Epstein-Barr virus (EBV) DR enhancer contains two functionally different domains: domain A is constitutive and cell specific, domain B is transactivated by the EBV early protein R. J Virol 63: 615-623 Chiu YF, Tung CP, Lee YH, Wang WH, Li C, Hung JY, Wang CY, Kawaguchi Y, Liu ST (2007) A comprehensive library of mutations of Epstein Barr virus. J Gen Virol 88: 2463-2472 Copeland AM, Newcomb WW, Brown JC (2009) Herpes simplex virus replication: roles of viral proteins and nucleoporins in capsid-nucleus attachment. J Virol 83: 1660-1668 Countryman J, Gradoville L, Bhaduri-McIntosh S, Ye J, Heston L, Himmelfarb S, Shedd D, Miller G (2009) Stimulus duration and response time independently influence the kinetics of lytic cycle reactivation of Epstein-Barr virus. J Virol 83: 10694-10709 Countryman J, Miller G (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: 4085-4089 Cox MA, Leahy J, Hardwick JM (1990) An enhancer within the divergent promoter of Epstein-Barr virus responds synergistically to the R and Z transactivators. J Virol 64: 313-321 Crawford DH (2001) Biology and disease associations of Epstein-Barr virus. Philos Trans R Soc Lond B Biol Sci 356: 461-473 Dambaugh T, Beisel C, Hummel M, King W, Fennewald S, Cheung A, Heller M, Raab-Traub N, Kieff E (1980) Epstein-Barr virus (B95-8) DNA VII: molecular cloning and detailed mapping. Proc Natl Acad Sci U S A 77: 2999-3003 Darr CD, Mauser A, Kenney S (2001) Epstein-Barr virus immediate-early protein BRLF1 induces the lytic form of viral replication through a mechanism involving phosphatidylinositol-3 kinase activation. J Virol 75: 6135-6142 Delboy MG, Nicola AV (2011) A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virus. J Virol 85: 5910-5918 Delboy MG, Siekavizza-Robles CR, Nicola AV (2010) Herpes simplex virus tegument ICP0 is capsid associated, and its E3 ubiquitin ligase domain is important for incorporation into virions. J Virol 84: 1637-1640 Deutsch MJ, Ott E, Papior P, Schepers A (2010) The latent origin of replication of Epstein-Barr virus directs viral genomes to active regions of the nucleus. J Virol 84: 2533-2546 Doepker RC, Hsu WL, Saffran HA, Smiley JR (2004) Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H. J Virol 78: 4684-4699 Dolyniuk M, Pritchett R, Kieff E (1976a) Proteins of Epstein-Barr virus. I. Analysis of the polypeptides of purified enveloped Epstein-Barr virus. J Virol 17: 935-949 Dolyniuk M, Wolff E, Kieff E (1976b) Proteins of Epstein-Barr Virus. II. Electrophoretic analysis of the polypeptides of the nucleocapsid and the glucosamine- and polysaccharide-containing components of enveloped virus. J Virol 18: 289-297 Duffy C, Mbong EF, Baines JD (2009) VP22 of herpes simplex virus 1 promotes protein synthesis at late times in infection and accumulation of a subset of viral mRNAs at early times in infection. J Virol 83: 1009-1017 El-Guindy A, Ghiassi-Nejad M, Golden S, Delecluse HJ, Miller G (2013) Essential role of Rta in lytic DNA replication of Epstein-Barr virus. J Virol 87: 208-223 Elliott GD, Meredith DM (1992) The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49. J Gen Virol 73: 723-726 Epstein MA, Achong BG, Barr YM (1964) Virus Particles in Cultured Lymphoblasts from Burkitt's Lymphoma. Lancet 1: 702-703 Everett R, Chelbi Alix M (2007) PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89: 819-830 Everett RD (2000) ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioessays 22: 761-770 Everett RD, Parsy ML, Orr A (2009) Analysis of the functions of herpes simplex virus type 1 regulatory protein ICP0 that are critical for lytic infection and derepression of quiescent viral genomes. J Virol 83: 4963-4977 Fafeur V, O'Hara B, Bohlen P (1993) A glycosylation-deficient endothelial cell mutant with modified responses to transforming growth factor-beta and other growth inhibitory cytokines: evidence for multiple growth inhibitory signal transduction pathways. Mol Biol Cell 4: 135-144 Farrell PJ, Rowe DT, Rooney CM, Kouzarides T (1989) Epstein-Barr virus BZLF1 trans-activator specifically binds to a consensus AP-1 site and is related to c-fos. EMBO J 8: 127-132 Feederle R, Kost M, Baumann M, Janz A, Drouet E, Hammerschmidt W, Delecluse HJ (2000) The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators. EMBO J 19: 3080-3089 Feng P, Everly DN, Jr., Read GS (2005) mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A. J Virol 79: 9651-9664 Flemington E, Speck SH (1990a) Autoregulation of Epstein-Barr virus putative lytic switch gene BZLF1. J Virol 64: 1227-1232 Flemington E, Speck SH (1990b) Identification of phorbol ester response elements in the promoter of Epstein-Barr virus putative lytic switch gene BZLF1. J Virol 64: 1217-1226 Flemington EK, Goldfeld AE, Speck SH (1991) Efficient transcription of the Epstein-Barr virus immediate-early BZLF1 and BRLF1 genes requires protein synthesis. J Virol 65: 7073-7077 Geiss-Friedlander R, Melchior F (2007) Concepts in sumoylation: a decade on. Nat Rev Mol Cell Biol 8: 947-956 Goding CR, O'Hare P (1989) Herpes simplex virus Vmw65-octamer binding protein interaction: a paradigm for combinatorial control of transcription. Virology 173: 363-367 Graham FL, Smiley J, Russell WC, Nairn R (1977) Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J Gen Virol 36: 59-74 Gray JJ (1995) Avidity of EBV VCA-specific IgG antibodies: distinction between recent primary infection, past infection and reactivation. J Virol Methods 52: 95-104 Greenspan JS, Greenspan D, Lennette ET, Abrams DI, Conant MA, Petersen V, Freese UK (1985) Replication of Epstein-Barr virus within the epithelial cells of oral 'hairy' leukoplakia, an AIDS-associated lesion. N Engl J Med 313: 1564-1571 Gross S, Catez F, Masumoto H, Lomonte P (2012) Centromere architecture breakdown induced by the viral E3 ubiquitin ligase ICP0 protein of herpes simplex virus type 1. PLoS One 7: e44227 Gruffat H, Duran N, Buisson M, Wild F, Buckland R, Sergeant A (1992) Characterization of an R-binding site mediating the R-induced activation of the Epstein-Barr virus BMLF1 promoter. J Virol 66: 46-52 Gruffat H, Manet E, Rigolet A, Sergeant A (1990) The enhancer factor R of Epstein-Barr virus (EBV) is a sequence-specific DNA binding protein. Nucleic Acids Res 18: 6835-6843 Gutsch DE, Marcu KB, Kenney SC (1994) The Epstein-Barr virus BRLF1 gene product transactivates the murine and human c-myc promoters. Cell Mol Biol (Noisy-le-grand) 40: 747-760 Hagglund R, Roizman B (2004) Role of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1. J Virol 78: 2169-2178 Hardwick JM, Lieberman PM, Hayward SD (1988) A new Epstein-Barr virus transactivator, R, induces expression of a cytoplasmic early antigen. J Virol 62: 2274-2284 Heilmann AM, Calderwood MA, Portal D, Lu Y, Johannsen E (2012) Genome-wide analysis of Epstein-Barr virus Rta DNA binding. J Virol 86: 5151-5164 Heine JW, Honess RW, Cassai E, Roizman B (1974) Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J Virol 14: 640-651 Henaff D, Remillard-Labrosse G, Loret S, Lippe R (2013) Analysis of the early steps of herpes simplex virus 1 capsid tegumentation. J Virol 87: 4895-4906 Henderson EE, Long WK (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, Henle W (1966) Studies on cell lines derived from Burkitt's lymphoma. Trans N Y Acad Sci 29: 71-79 Henson BW, Perkins EM, Cothran JE, Desai P (2009) Self-assembly of Epstein-Barr virus capsids. J Virol 83: 3877-3890 Hinuma Y, Konn M, Yamaguchi J, Grace JT, Jr. (1967) Replication of herpes-type virus in a Burkitt lymphoma cell line. J Virol 1: 1203-1206 Ho CH, Chen CL, Li WY, Chen CJ (2009) Decoy receptor 3, upregulated by Epstein-Barr virus latent membrane protein 1, enhances nasopharyngeal carcinoma cell migration and invasion. Carcinogenesis 30: 1443-1451 Ho CH, Hsu CF, Fong PF, Tai SK, Hsieh SL, Chen CJ (2007) Epstein-Barr virus transcription activator Rta upregulates decoy receptor 3 expression by binding to its promoter. J Virol 81: 4837-4847 Holley-Guthrie EA, Quinlivan EB, Mar EC, Kenney S (1990) The Epstein-Barr virus (EBV) BMRF1 promoter for early antigen (EA-D) is regulated by the EBV transactivators, BRLF1 and BZLF1, in a cell-specific manner. J Virol 64: 3753-3759 Homa FL, Brown JC (1997) Capsid assembly and DNA packaging in herpes simplex virus. Rev Med Virol 7: 107-122 Hsu TY, Chang Y, Wang PW, Liu MY, Chen MR, Chen JY, Tsai CH (2005) Reactivation of Epstein-Barr virus can be triggered by an Rta protein mutated at the nuclear localization signal. J Gen Virol 86: 317-322 Hung CH, Liu ST (1999) Characterization of the Epstein-Barr virus BALF2 promoter. J Gen Virol 80 ( Pt 10): 2747-2750 Imai S, Koizumi S, Sugiura M, Tokunaga M, Uemura Y, Yamamoto N, Tanaka S, Sato E, Osato T (1994) Gastric carcinoma: monoclonal epithelial malignant cells expressing Epstein-Barr virus latent infection protein. Proc Natl Acad Sci U S A 91: 9131-9135 Jacob RJ, Morse LS, Roizman B (1979) Anatomy of herpes simplex virus DNA. XII. Accumulation of head-to-tail concatemers in nuclei of infected cells and their role in the generation of the four isomeric arrangements of viral DNA. J Virol 29: 448-457 Jiang JH, Wang N, Li A, Liao WT, Pan ZG, Mai SJ, Li DJ, Zeng MS, Wen JM, Zeng YX (2006) Hypoxia can contribute to the induction of the Epstein-Barr virus (EBV) lytic cycle. J Clin Virol 37: 98-103 Johannsen E, Luftig M, Chase MR, Weicksel S, Cahir-McFarland E, Illanes D, Sarracino D, Kieff E (2004) Proteins of purified Epstein-Barr virus. Proc Natl Acad Sci U S A 101: 16286-16291 Johnson DC, Baines JD (2011) Herpesviruses remodel host membranes for virus egress. Nat Rev Microbiol 9: 382-394 Jones JF, Shurin S, Abramowsky C, Tubbs RR, Sciotto CG, Wahl R, Sands J, Gottman D, Katz BZ, Sklar J (1988) T-cell lymphomas containing Epstein-Barr viral DNA in patients with chronic Epstein-Barr virus infections. N Engl J Med 318: 733-741 Jurak I, Silverstein LB, Sharma M, Coen DM (2012) Herpes simplex virus is equipped with RNA- and protein-based mechanisms to repress expression of ATRX, an effector of intrinsic immunity. J Virol 86: 10093-10102 Kallin B, Luka J, Klein G (1979) Immunochemical characterization of Epstein-Barr virus-associated early and late antigens in n-butyrate-treated P3HR-1 cells. J Virol 32: 710-716 Kato A, Yamamoto M, Ohno T, Kodaira H, Nishiyama Y, Kawaguchi Y (2005) Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1. J Virol 79: 9325-9331 Kawanishi M (1995) Nitric oxide inhibits Epstein-Barr virus DNA replication and activation of latent EBV. Intervirology 38: 206-213 Kelly BJ, Fraefel C, Cunningham AL, Diefenbach RJ (2009) Functional roles of the tegument proteins of herpes simplex virus type 1. Virus Res 145: 173-186 Kenney S, Kamine J, Holley-Guthrie E, Mar EC, Lin JC, Markovitz D, Pagano J (1989) The Epstein-Barr virus immediate-early gene product, BMLF1, acts in trans by a posttranscriptional mechanism which is reporter gene dependent. J Virol 63: 3870-3877 Kirchmaier AL, Sugden B (1995) Plasmid maintenance of derivatives of oriP of Epstein-Barr virus. J Virol 69: 1280-1283 Kirkitadze MD, Barlow PN, Price NC, Kelly SM, Boutell CJ, Rixon FJ, McClelland DA (1998) The herpes simplex virus triplex protein, VP23, exists as a molten globule. J Virol 72: 10066-10072 Klein G, Giovanella B, Westman A, Stehlin JS, Mumford D (1975) An EBV-genome-negative cell line established from an American Burkitt lymphoma; receptor characteristics. EBV infectibility and permanent conversion into EBV-positive sublines by in vitro infection. Intervirology 5: 319-334 Klupp BG, Granzow H, Mettenleiter TC (2000) Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product. J Virol 74: 10063-10073 Klupp BG, Granzow H, Mettenleiter TC (2001) Effect of the pseudorabies virus US3 protein on nuclear membrane localization of the UL34 protein and virus egress from the nucleus. J Gen Virol 82: 2363-2371 Kolman JL, Taylor N, Gradoville L, Countryman J, Miller G (1996) Comparing transcriptional activation and autostimulation by ZEBRA and ZEBRA/c-Fos chimeras. J Virol 70: 1493-1504 Konturek PC, Konturek SJ, Brzozowski T (2006) Gastric cancer and Helicobacter pylori infection. J Physiol Pharmacol 57 Suppl 3: 51-65 Kumar R, Whitehurst CB, Pagano JS (2014) The Rad6/18 Ubiquitin Complex Interacts with the Epstein-Barr Virus Deubiquitinating Enzyme, BPLF1, and Contributes to Virus Infectivity. J Virol 88: 6411-6422 Kurilla MG, Heineman T, Davenport LC, Kieff E, Hutt-Fletcher LM (1995) A novel Epstein-Barr virus glycoprotein gp150 expressed from the BDLF3 open reading frame. Virology 209: 108-121 Kwong AD, Frenkel N (1987) Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs. Proc Natl Acad Sci U S A 84: 1926-1930 Lam Q, Smibert CA, Koop KE, Lavery C, Capone JP, Weinheimer SP, Smiley JR (1996) Herpes simplex virus VP16 rescues viral mRNA from destruction by the virion host shutoff function. EMBO J 15: 2575-2581 Le Roux F, Sergeant A, Corbo L (1996) Epstein-Barr virus (EBV) EB1/Zta protein provided in trans and competent for the activation of productive cycle genes does not activate the BZLF1 gene in the EBV genome. J Gen Virol 77: 501-509 Lee GE, Murray JW, Wolkoff AW, Wilson DW (2006) Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro. J Virol 80: 4264-4275 Lee YH, Chiu YF, Wang WH, Chang LK, Liu ST (2008) Activation of the ERK signal transduction pathway by Epstein-Barr virus immediate-early protein Rta. J Gen Virol 89: 2437-2446 Leslie J, Rixon FJ, McLauchlan J (1996) Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles. Virology 220: 60-68 Levy JA, Henle G (1966) Indirect immunofluorescence tests with sera from African children and cultured Burkitt lymphoma cells. J Bacteriol 92: 275-276 Li Y, Mahajan NP, Webster-Cyriaque J, Bhende P, Hong GK, Earp HS, Kenney S (2004a) The C-mer gene is induced by Epstein-Barr virus immediate-early protein BRLF1. J Virol 78: 11778-11785 Li Y, Webster-Cyriaque J, Tomlinson CC, Yohe M, Kenney S (2004b) Fatty acid synthase expression is induced by the Epstein-Barr virus immediate-early protein BRLF1 and is required for lytic viral gene expression. J Virol 78: 4197-4206 Liashkovich I, Hafezi W, Kuhn JM, Oberleithner H, Shahin V (2011) Nuclear delivery mechanism of herpes simplex virus type 1 genome. J Mol Recognit 24: 414-421 Lieberman PM, Hardwick JM, Hayward SD (1989) Responsiveness of the Epstein-Barr virus NotI repeat promoter to the Z transactivator is mediated in a cell-type-specific manner by two independent signal regions. J Virol 63: 3040-3050 Lieberman PM, Hardwick JM, Sample J, Hayward GS, Hayward SD (1990) The zta transactivator involved in induction of lytic cycle gene expression in Epstein-Barr virus-infected lymphocytes binds to both AP-1 and ZRE sites in target promoter and enhancer regions. J Virol 64: 1143-1155 Lima VP, de Lima MA, Andre AR, Ferreira MV, Barros MA, Rabenhorst SH (2008) H pylori (CagA) and Epstein-Barr virus infection in gastric carcinomas: correlation with p53 mutation and c-Myc, Bcl-2 and Bax expression. World J Gastroenterol 14: 884-891 Lin TP, Chen SY, Duh PD, Chang LK, Liu YN (2008) Inhibition of the epstein-barr virus lytic cycle by andrographolide. Biol Pharm Bull 31: 2018-2023 Lindner SE, Sugden B (2007) The plasmid replicon of Epstein-Barr virus: mechanistic insights into efficient, licensed, extrachromosomal replication in human cells. Plasmid 58: 1-12 Liu C, Sista ND, Pagano JS (1996) Activation of the Epstein-Barr virus DNA polymerase promoter by the BRLF1 immediate-early protein is mediated through USF and E2F. J Virol 70: 2545-2555 Liu FY, Roizman B (1991) The herpes simplex virus 1 gene encoding a protease also contains within its coding domain the gene encoding the more abundant substrate. J Virol 65: 5149-5156 Liu P, Speck SH (2003) Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta. Virology 310: 199-206 Loret S, Guay G, Lippe R (2008) Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol 82: 8605-8618 Loret S, Lippe R (2012) Biochemical analysis of infected cell polypeptide (ICP)0, ICP4, UL7 and UL23 incorporated into extracellular herpes simplex virus type 1 virions. J Gen Virol 93: 624-634 Luka J, Kallin B, Klein G (1979) Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate. Virology 94: 228-231 Maeda E, Akahane M, Kiryu S, Kato N, Yoshikawa T, Hayashi N, Aoki S, Minami M, Uozaki H, Fukayama M, Ohtomo K (2009) Spectrum of Epstein-Barr virus-related diseases: a pictorial review. Jpn J Radiol 27: 4-19 Manet E, Gruffat H, Trescol-Biemont MC, Moreno N, Chambard P, Giot JF, Sergeant A (1989) Epstein-Barr virus bicistronic mRNAs generated by facultative splicing code for two transcriptional trans-activators. EMBO J 8: 1819-1826 Manet E, Rigolet A, Gruffat H, Giot JF, Sergeant A (1991) Domains of the Epstein-Barr virus (EBV) transcription factor R required for dimerization, DNA binding and activation. Nucleic Acids Res 19: 2661-2667 Mannick JB, Asano K, Izumi K, Kieff E, Stamler JS (1994) Nitric oxide produced by human B lymphocytes inhibits apoptosis and Epstein-Barr virus reactivation. Cell 79: 1137-1146 Maruzuru Y, Shindo K, Liu Z, Oyama M, Kozuka-Hata H, Arii J, Kato A, Kawaguchi Y (2014) Role of Herpes Simplex Virus 1 Immediate Early Protein ICP22 in Viral Nuclear Egress. J Virol 88: 7445-7454 Maurer BA, Wilbert SM, Imamura T (1970) Incidence of EB virus-containing cells in primary and secondary clones of several Burkitt lymphoma cell lines. Cancer Res 30: 2870-2875 Mayhew TM (2009) Quantifying immunogold localization patterns on electron microscopic thin sections of placenta: recent developments. Placenta 30: 565-570 Mbong EF, Woodley L, Dunkerley E, Schrimpf JE, Morrison LA, Duffy C (2012) Deletion of the herpes simplex virus 1 UL49 gene results in mRNA and protein translation defects that are complemented by secondary mutations in UL41. J Virol 86: 12351-12361 Mecocci P, Mariani E, Cornacchiola V, Polidori MC (2004) Antioxidants for the treatment of mild cognitive impairment. Neurol Res 26: 598-602 Mettenleiter TC, Klupp BG, Granzow H (2009) Herpesvirus assembly: an update. Virus Res 143: 222-234 Mossman KL, Smiley JR (2002) Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication. J Virol 76: 1995-1998 Mou F, Wills E, Baines JD (2009) Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids. J Virol 83: 5181-5191 Newcomb WW, Homa FL, Thomsen DR, Booy FP, Trus BL, Steven AC, Spencer JV, Brown JC (1996) Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation. J Mol Biol 263: 432-446 Newcomb WW, Thomsen DR, Homa FL, Brown JC (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: 9862-9871 Nolan LA, Morgan AJ (1995) The Epstein-Barr virus open reading frame BDLF3 codes for a 100-150 kDa glycoprotein. J Gen Virol 76 ( Pt 6): 1381-1392 Nutter LM, Grill SP, Li JS, Tan RS, Cheng YC (1987) Induction of virus enzymes by phorbol esters and n-butyrate in Epstein-Barr virus genome-carrying Raji cells. Cancer Res 47: 4407-4412 Ojala PM, Sodeik B, Ebersold MW, Kutay U, Helenius A (2000) Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol Cell Biol 20: 4922-4931 Okoye ME, Sexton GL, Huang E, McCaffery JM, Desai P (2006) Functional analysis of the triplex proteins (VP19C and VP23) of herpes simplex virus type 1. J Virol 80: 929-940 Oroskar AA, Read GS (1989) Control of mRNA stability by the virion host shutoff function of herpes simplex virus. J Virol 63: 1897-1906 Padula ME, Sydnor ML, Wilson DW (2009) Isolation and preliminary characterization of herpes simplex virus 1 primary enveloped virions from the perinuclear space. J Virol 83: 4757-4765 Page HG, Read GS (2010) The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F. J Virol 84: 6886-6890 Paladino P, Collins SE, Mossman KL (2010) Cellular localization of the herpes simplex virus ICP0 protein dictates its ability to block IRF3-mediated innate immune responses. PLoS One 5: e10428 Pasdeloup D, Blondel D, Isidro AL, Rixon FJ (2009) Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J Virol 83: 6610-6623 Pattle SB, Farrell PJ (2006) The role of Epstein-Barr virus in cancer. Expert Opin Biol Ther 6: 1193-1205 Pfeffer S, Zavolan M, Grasser FA, Chien M, Russo JJ, Ju J, John B, Enright AJ, Marks D, Sander C, Tuschl T (2004) Identification of virus-encoded microRNAs. Science 304: 734-736 Pfuller R, Hammerschmidt W (1996) Plasmid-like replicative intermediates of the Epstein-Barr virus lytic origin of DNA replication. J Virol 70: 3423-3431 Preston VG, al-Kobaisi MF, McDougall IM, Rixon FJ (1994) The herpes simplex virus gene UL26 proteinase in the presence of the UL26.5 gene product promotes the formation of scaffold-like structures. J Gen Virol 75 ( Pt 9): 2355-2366 Purves FC, Spector D, Roizman B (1991) The herpes simplex virus 1 protein kinase encoded by the US3 gene mediates posttranslational modification of the phosphoprotein encoded by the UL34 gene. J Virol 65: 5757-5764 Quinlivan EB, Holley-Guthrie EA, Norris M, Gutsch D, Bachenheimer SL, Kenney SC (1993) Direct BRLF1 binding is required for cooperative BZLF1/BRLF1 activation of the Epstein-Barr virus early promoter, BMRF1. Nucleic Acids Res 21: 1999-2007 Ragoczy T, Heston L, 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 Ragoczy T, Miller G (2001) Autostimulation of the Epstein-Barr virus BRLF1 promoter is mediated through consensus Sp1 and Sp3 binding sites. J Virol 75: 5240-5251 Rajcani J, Andrea V, Ingeborg R (2004) Peculiarities of herpes simplex virus (HSV) transcription: an overview. Virus Genes 28: 293-310 Read GS, Patterson M (2007) Packaging of the virion host shutoff (Vhs) protein of herpes simplex virus: two forms of the Vhs polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions. J Virol 81: 1148-1161 Reynolds AE, Wills EG, Roller RJ, Ryckman BJ, Baines JD (2002) Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. J Virol 76: 8939-8952 Rixon FJ, Addison C, McGregor A, Macnab SJ, Nicholson P, Preston VG, Tatman JD (1996) Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins. J Gen Virol 77: 2251-2260 Roller RJ, Bjerke SL, Haugo AC, Hanson S (2010) Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids. J Virol 84: 3921-3934 Roller RJ, Haugo AC, Kopping NJ (2011) Intragenic and extragenic suppression of a mutation in herpes simplex virus 1 UL34 that affects both nuclear envelope targeting and membrane budding. J Virol 85: 11615-11625 Ryckman BJ, Roller RJ (2004) Herpes simplex virus type 1 primary envelopment: UL34 protein modification and the US3-UL34 catalytic relationship. J Virol 78: 399-412 Sapetschnig A, Rischitor G, Braun H, Doll A, Schergaut M, Melchior F, Suske G (2002) Transcription factor Sp3 is silenced through SUMO modification by PIAS1. EMBO J 21: 5206-5215 Sato H, Takimoto T, Tanaka S, Tanaka J, Raab-Traub N (1990) Concatameric replication of Epstein-Barr virus: structure of the termini in virus-producer and newly transformed cell lines. J Virol 64: 5295-5300 Schipke J, Pohlmann A, | |
dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/57465 | - |
dc.description.abstract | Epstein-Barr virus (EBV),簡稱 EB 病毒,是人類第四型皰疹病毒,與許多腫瘤疾病相關。當病毒進入溶裂期時,會最先表現極早期蛋白質 (immediate early protein),Zta 與 Rta,以活化早期蛋白質 (early protein),協助遺傳物質大量複製,進而活化晚期蛋白質,主要與病毒組裝相關。病毒的外鞘含有主要外鞘蛋白質 (major capsid protein; VCA),兩種次要外鞘蛋白質 (minor capsid protein; BORF1 and BDLF1),以及小外鞘蛋白質 (small capsid protein; BFRF3) 等,共同組裝成正二十面體的病毒外鞘,組裝完成後,病毒顆粒釋出 (egress) 感染其它細胞開啟下一個生活史,而外鞘的組裝在晚期是十分重要的一環。目前對於 Rta 的研究著重於極早期以及早期的調控,但在晚期的角色仍不清楚。本篇研究主要探討 Rta 與外鞘蛋白質之間的關係。首先發現,Rta 會與 BORF1 以及 BDLF1 在細胞內結合,並利用 GST-pull down 證明,Rta 能與 BORF1、BDLF1、VCA 以及 BFRF3 等外鞘蛋白質直接結合。接著,以免疫螢光法觀察到 Rta 在溶裂晚期會與 BORF1、 BDLF1,以及 BFRF3 等外鞘蛋白質共同分布於細胞核內。並以蔗糖梯度分離、脫殼實驗以及電子顯微鏡的觀察,證實 Rta 會做為鞘間蛋白質存在於病毒顆粒中。最後,透過變性免疫沈澱法發現 Rta 會降低 BORF1 的去泛素化修飾,穩定外鞘蛋白質,另一方面,藉由冷光報導基因分析,觀察到 BORF1 會降低 Rta 活化早期基因的能力。本研究揭露了極早期蛋白質 Rta 會與外鞘蛋白質會相互結合,且首度提出 Rta 是 EB 病毒的鞘間蛋白質,會提升外鞘蛋白質的穩定性,並受外鞘蛋白質調控 Rta 活化早期基因。 | zh_TW |
dc.description.abstract | Epstein-Barr virus (EBV) is also called human herpesvirus 4 (HHV-4), which is associated with many neoplastic diseases. When the virus enters to lytic stage, it expresses two immediate early (IE) proteins, Rta and Zta, which are required to promote the transcription of early genes, to help the replication of viral DNA. Then, the late proteins are activated, which are required for nucleocapsid assembly and egress. The icosahedron capsid of EBV contains major capsid protein, VCA, two minor capsid proteins, BORF1 and BDLF1, and small capsid protein, BFRF3. After virion assembly, they egress to infect other cells and continue the next life cycle. To date, the functional analysis of Rta focuses on the regulation during the immediate early stage and early stage. However, the role of Rta in the late stage is still unclear. The purpose of this study is to elucidate the relationship between Rta and capsid proteins. First, coimmunoprecipitation assay reveals that Rta colocalizes with BORF1, and BDLF1. And GST pull down assay shows that Rta interacts directly with BORF1, BDLF1, VCA, and BFRF3. Moreover, immunofluorescence reveals that Rta colocalizes with three capsid proteins, including BORF1, BDLF1, and BFRF3 during the late stage of the lytic cycle. Furthermore, Rta is also present in the virions and served as a tegument protein. Finally, denature immunoprecipetation reveals Rta decreesed the ubiquitination of BORF1, stabilizing BORF1; luciferase assay provides BORF1 decreased the transactivation of early genes by Rta. Taken together, this study demonstrated that Rta interacts with EBV capsid, exists in the virions as a tegument protein, increases the stability of capsid proteins, and the activation of erly genes by Rta is regulated by capsid proteins. | en |
dc.description.provenance | Made available in DSpace on 2021-06-16T06:47:16Z (GMT). No. of bitstreams: 1 ntu-103-R01b22045-1.pdf: 58404404 bytes, checksum: 690805ef6bf4a72f3197c95c5bf1aca2 (MD5) Previous issue date: 2014 | en |
dc.description.tableofcontents | 誌謝 i
摘要 ii Abstract iii 目錄 iv 圖目錄 vi 表目錄 vii 前言 1 1. EB 病毒與疾病 1 2. EB 病毒的遺傳物質 1 3. EB 病毒的生活史 2 4. EB 病毒的極早期蛋白質 Zta 與 Rta 4 5. 皰疹病毒的組裝與出核 7 6. EB 病毒的病毒顆粒組裝 9 7. 溶裂期極早期蛋白質在晚期的角色 10 研究目的 12 材料與方法 13 1. 細胞株 13 2. EB 病毒的溶裂期誘導 13 3. 質體與抗體 13 4. 細菌 13 5. 細胞轉染 (Transfection) 14 6. SDS-PAGE 蛋白質膠體電泳以及西方點墨法 (Western blot analysis) 14 7. 免疫沉澱分析 (Immunoprecipitation) 14 8. 蛋白質的誘導表現 15 9. Glutathione-S-transferase (GST) pull-down assay 15 10. 共免疫螢光顯微鏡分析 (Immunofluorescence analysis) 15 11. 病毒顆粒的取得與純化 16 12. 脫殼試驗(detegumentation assay) 16 13. 電子顯微鏡 ( Transmission Electron Microscopy) 16 14. 變性免疫沈澱法 ( Denature immunoprecipitation, denature IP) 17 15. 冷光報導基因分析 17 結果 19 1. Rta 與外鞘蛋白質 BORF1 以及 BDLF1 在細胞中結合 19 2. Rta 於胞外會與病毒外鞘蛋白質直接結合 19 3. Rta 與病毒外鞘蛋白質共同分布 20 4. Rta 被包覆於病毒顆粒中 21 5. Rta 為鞘間蛋白質 23 6. Rta 降低 BORF1 受泛素化修飾 24 討論 25 圖表 32 附錄 55 附錄1、EB 病毒的結構 55 附錄2、HSV-1 的外鞘組裝 56 附錄3、EB病毒的外鞘蛋白質同源體對照表 57 附錄4、EB 病毒的外鞘殼體 58 附錄5、Rta 在細胞核內結合於病毒外鞘之上 59 參考文獻 60 圖目錄 圖 1、EB 病毒的生活史 35 圖 2、Rta 與 BORF1 以及 BDLF1 在細胞內結合 36 圖 3、Rta 與 BORF1、BDLF1、VCA、BFRF3 在細胞體外直接結合 37 圖 4、Rta 不與 BdRF1 在細胞體外直接結合 38 圖 5、Rta 與 BORF1 在 293T 細胞中的免疫螢光分析 39 圖 6、Rta 與BORF1在P3HR1細胞中的免疫螢光分析 40 圖 7、Rta 與 BDLF1、BFRF3 在 P3HR1 細胞的免疫螢光分析 41 圖 8、Rta 與 BDLF1、BFRF3 在 P3HR1 細胞的免疫螢光分析 42 圖 9、Rta 與 BORF1、BFRF3 在 P3HR1 細胞的免疫螢光分析 43 圖 10、Rta 存在病毒顆粒之中 45 圖 11、Rta 存在於抗 gp350 抗體膠體沈澱的病毒顆粒中 46 圖 12、Rta 是鞘間蛋白質 47 圖 13、Rta 存在於病毒顆粒外鞘上 48 圖 14、Rta 會降低 BORF1 受泛素化修飾 49 圖 15、Rta 與 BORF1 片段刪除株在 293T 細胞中的免疫螢光分析 51 圖 16、Rta 與 BDLF1 在 P3HR1 細胞中的結合 52 圖 17、BORF1 會抑制 Rta 活化早期基因 pBMRF1-ZRERRE 53 圖 18、Rta 在病毒外鞘組裝的角色 54 表目錄 表 1、本研究使用的質體 32 表 2、本研究使用的抗體 34 | |
dc.language.iso | zh-TW | |
dc.title | EB 病毒的 Rta 蛋白質參與在外鞘組裝的研究 | zh_TW |
dc.title | Involvement of Rta in the capsid assembly of Epstein-Barr virus | en |
dc.type | Thesis | |
dc.date.schoolyear | 102-2 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 劉世東(Shih-Tung Liu),張沛鈞(Pey-Jium Chang),張世宗(Shih-Chung Chang),莊健盈(Jian-Ying Chuang) | |
dc.subject.keyword | Epstein- Barr Virus (EB 病毒),Rta 蛋白質,外鞘蛋白質,病毒顆粒,鞘間蛋白質, | zh_TW |
dc.subject.keyword | Epstein- Barr Virus,Rta,capsid proteins,tegument proteins, | en |
dc.relation.page | 76 | |
dc.rights.note | 有償授權 | |
dc.date.accepted | 2014-07-25 | |
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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