Epstein-Barr virus nuclear antigen 3C regulated genes in lymphoblastoid cell lines

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 1, 2011, Pages 337-342

  Zhao, Bo ^a   Mar, Jessica C ^b,c   Maruo, Seiji ^d   Lee, Sungwook ^a   Gewurz, Benjamin E ^a   Johannsen, Eric ^a   Holton, Kristina ^b,c   Rubio, Renee ^b,c   Takada, Kenzo ^d   Quackenbush, John ^b,c   Kieff, Elliott ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

^c DANA FARBER CANCER INSTITUTE   (United States)

^d HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Lymphoma; Notch

Indexed keywords

CHEMOKINE RECEPTOR CXCR4; EPSTEIN BARR VIRUS ANTIGEN; EPSTEIN BARR VIRUS ANTIGEN 2; EPSTEIN BARR VIRUS ANTIGEN 3A; EPSTEIN BARR VIRUS ANTIGEN 3C; ESTROGEN RECEPTOR; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE; RAC1 PROTEIN; RNA; STAT PROTEIN; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CELL GROWTH; CELL MIGRATION; CELL SURVIVAL; DOWN REGULATION; GENE; GENE CONTROL; LYMPHOBLASTOID CELL; LYN GENE; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANALYSIS OF VARIANCE; ANTIGENS, VIRAL; BAYES THEOREM; CELL LINE, TUMOR; CLUSTER ANALYSIS; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION, NEOPLASTIC; GENES; HUMANS; IMMUNOGLOBULIN J RECOMBINATION SIGNAL SEQUENCE-BINDING PROTEIN; LYMPHOCYTE ACTIVATION; MICROARRAY ANALYSIS; RECEPTORS, ESTROGEN; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; TRANSCRIPTION FACTORS;

HUMAN HERPESVIRUS 4;

EID: 78651099289     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1017419108     Document Type: Article

References (71)

1. Rickinson AB, Kieff ED (2007) Epstein-Barr virus. Fields Virology, eds Knipe DM, Howley PM (Lippincott Williams & Wilkins, Philadelphia), Vol Vol 2, pp 2655-2700.
2. Henle W, Diehl V, Kohn G, Zur Hausen H, Henle G (1967) Herpes-type virus and chromosome marker in normal leukocytes after growth with irradiated Burkitt cells. Science 157:1064-1065.
3. Pope JH (1967) Establishment of cell lines from peripheral leucocytes in infectious mononucleosis. Nature 216:810-811.
4. Kieff ED, Rickinson AB (2007) Epstein-Barr virus and its replication. Fields Virology, eds Knipe DM, Howley PM (Lippincott Williams & Wilkins, Philadelphia), Vol Vol 2, pp 2603-2654.
5. Robertson ES, et al. (1995) Epstein-Barr virus nuclear protein 3C modulates transcription through interaction with the sequence-specific DNA-binding protein J kappa. J Virol 69:3108-3116.
6. Robertson ES, Lin J, Kieff E (1996) The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa). J Virol 70:3068-3074.
7. Waltzer L, Perricaudet M, Sergeant A, Manet E (1996) Epstein-Barr virus EBNA3A and EBNA3C proteins both repress RBP-J kappa-EBNA2-activated transcription by inhibiting the binding of RBP-J kappa to DNA. J Virol 70:5909-5915.
8. Zhao B, Marshall DR, Sample CE (1996) A conserved domain of the Epstein-Barr virus nuclear antigens 3A and 3C binds to a discrete domain of Jkappa. J Virol 70: 4228-4236.
9. Cooper A, et al. (2003) EBNA3A association with RBP-Jkappa down-regulates c-myc and Epstein-Barr virus-transformed lymphoblast growth. J Virol 77:999-1010.
10. Gordadze AV, et al. (2001) Notch1IC partially replaces EBNA2 function in B cells immortalized by Epstein-Barr virus. J Virol 75:5899-5912.
11. Tomkinson B, Robertson E, Kieff E (1993) Epstein-Barr virus nuclear proteins EBNA-3A and EBNA-3C are essential for B-lymphocyte growth transformation. J Virol 67: 2014-2025.
12. Maruo S, Johannsen E, Illanes D, Cooper A, Kieff E (2003) Epstein-Barr Virus nuclear protein EBNA3A is critical for maintaining lymphoblastoid cell line growth. J Virol 77: 10437-10447.
13. Maruo S, et al. (2005) Epstein-Barr virus nuclear protein 3A domains essential for growth of lymphoblasts: Transcriptional regulation through RBP-Jkappa/CBF1 is critical. J Virol 79:10171-10179.
14. Maruo S, et al. (2006) Epstein-Barr virus nuclear protein EBNA3C is required for cell cycle progression and growth maintenance of lymphoblastoid cells. Proc Natl Acad Sci USA 103:19500-19505.
15. Maruo S, et al. (2009) Epstein-Barr virus nuclear protein EBNA3C residues critical for maintaining lymphoblastoid cell growth. Proc Natl Acad Sci USA 106:4419-4424.
16. Lee S, et al. (2009) Epstein-Barr virus nuclear protein 3C domains necessary for lymphoblastoid cell growth: Interaction with RBP-Jkappa regulates TCL1. J Virol 83: 12368-12377.
17. Chen A, Divisconte M, Jiang X, Quink C, Wang F (2005) Epstein-Barr virus with the latent infection nuclear antigen 3B completely deleted is still competent for B-cell growth transformation in vitro. J Virol 79:4506-4509.
18. Chen A, Zhao B, Kieff E, Aster JC, Wang F (2006) EBNA-3B- and EBNA-3C-regulated cellular genes in Epstein-Barr virus-immortalized lymphoblastoid cell lines. J Virol 80: 10139-10150.
19. Allday MJ, Farrell PJ (1994) Epstein-Barr virus nuclear antigen EBNA3C/6 expression maintains the level of latent membrane protein 1 in G1-arrested cells. J Virol 68: 3491-3498.
20. Allday MJ, Crawford DH, Thomas JA (1993) Epstein-Barr virus (EBV) nuclear antigen 6 induces expression of the EBV latent membrane protein and an activated phenotype in Raji cells. J Gen Virol 74:361-369.
21. Zhao B, Sample CE (2000) Epstein-barr virus nuclear antigen 3C activates the latent membrane protein 1 promoter in the presence of Epstein-Barr virus nuclear antigen 2 through sequences encompassing an spi-1/Spi-B binding site. J Virol 74: 5151-5160.
22. Zhao B, et al. (2003) Transcriptional regulatory properties of Epstein-Barr virus nuclear antigen 3C are conserved in simian lymphocryptoviruses. J Virol 77:5639-5648.
23. Jiménez-Ramírez C, et al. (2006) Epstein-Barr virus EBNA-3C is targeted to and regulates expression from the bidirectional LMP-1/2B promoter. J Virol 80:11200-11208.
24. Lin J, Johannsen E, Robertson E, Kieff E (2002) Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2. J Virol 76:232-242.
25. Wang F, et al. (1990) Epstein-Barr virus latent membrane protein (LMP1) and nuclear proteins 2 and 3C are effectors of phenotypic changes in B lymphocytes: EBNA-2 and LMP1 cooperatively induce CD23. J Virol 64:2309-2318.
26. Paschos K, et al. (2009) Epstein-barr virus latency in B cells leads to epigenetic repression and CpG methylation of the tumour suppressor gene Bim. PLoS Pathog 5: e1000492.
27. Marshall D, Sample C (1995) Epstein-Barr virus nuclear antigen 3C is a transcriptional regulator. J Virol 69:3624-3630.
28. Radkov SA, et al. (1997) Epstein-Barr virus EBNA3C represses Cp, the major promoter for EBNA expression, but has no effect on the promoter of the cell gene CD21. J Virol 71:8552-8562.
29. Radkov SA, et al. (1999) Epstein-Barr virus nuclear antigen 3C interacts with histone deacetylase to repress transcription. J Virol 73:5688-5697.
30. Grundhoff AT, et al. (1999) Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C. J Biol Chem 274: 19136-19144.
31. Touitou R, Hickabottom M, Parker G, Crook T, Allday MJ (2001) Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C. J Virol 75:7749-7755.
32. Subramanian C, et al. (2002) Epstein-Barr virus nuclear antigen 3C and prothymosin alpha interact with the p300 transcriptional coactivator at the CH1 and CH3/HAT domains and cooperate in regulation of transcription and histone acetylation. J Virol 76:4699-4708.
33. Kaul R, Murakami M, Lan K, Choudhuri T, Robertson ES (2009) EBNA3C can modulate the activities of the transcription factor Necdin in association with metastasis suppressor protein Nm23-H1. J Virol 83:4871-4883.
34. Knight JS, Lan K, Subramanian C, Robertson ES (2003) Epstein-Barr virus nuclear antigen 3C recruits histone deacetylase activity and associates with the corepressors mSin3A and NCoR in human B-cell lines. J Virol 77:4261-4272.
35. Subramanian C, Robertson ES (2002) The metastatic suppressor Nm23-H1 interacts with EBNA3C at sequences located between the glutamine- and proline-rich domains and can cooperate in activation of transcription. J Virol 76:8702-8709.
36. Littlewood TD, Hancock DC, Danielian PS, Parker MG, Evan GI (1995) A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins. Nucleic Acids Res 23:1686-1690.
37. Irizarry RA, et al. (2005) Multiple-laboratory comparison of microarray platforms. Nat Methods 2:345-350.
38. Irizarry RA, et al. (2003) Summaries of Affymetrix GeneChip probe level data. Nucleic Acids Res 31:e15.
39. Hochberg Y, Benjamini Y (1990) More powerful procedures for multiple significance testing. Stat Med 9:811-818.
40. Kaiser C, et al. (1999) The proto-oncogene c-myc is a direct target gene of Epstein-Barr virus nuclear antigen 2. J Virol 73:4481-4484.
41. Zhao B, et al. (2006) RNAs induced by Epstein-Barr virus nuclear antigen 2 in lymphoblastoid cell lines. Proc Natl Acad Sci USA 103:1900-1905.
42. Gualco G, Weiss LM, Barber GN, Bacchi CE (2010) T-cell leukemia 1 expression in nodal Epstein-Barr virus-negative diffuse large B-cell lymphoma and primary mediastinal B-cell lymphoma. Hum Pathol 41:1238-1244.
43. Teitell MA, et al. (2005) TCL1 expression and Epstein-Barr virus status in pediatric Burkitt lymphoma. Am J Clin Pathol 124:569-575.
44. Kauffmann-Zeh A, et al. (1997) Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB. Nature 385:544-548.
45. Ahmed NN, Grimes HL, Bellacosa A, Chan TO, Tsichlis PN (1997) Transduction of interleukin-2 antiapoptotic and proliferative signals via Akt protein kinase. Proc Natl Acad Sci USA 94:3627-3632.
46. Wang Q, et al. (1999) Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts. Mol Cell Biol 19:4008-4018.
47. Wise DR, et al. (2008) Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction. Proc Natl Acad Sci USA 105:18782-18787.
48. Djebbari A, Quackenbush J (2008) Seeded Bayesian Networks: Constructing genetic networks from microarray data. BMC Syst Biol 2:57.
49. Jiang Z, Gentleman R (2007) Extensions to gene set enrichment. Bioinformatics 23: 306-313.
50. Piovan E, et al. (2005) Chemokine receptor expression in EBV-associated lymphoproliferation in hu/SCID mice: Implications for CXCL12/CXCR4 axis in lymphoma generation. Blood 105:931-939.
51. Spender LC, et al. (2006) Cell target genes of Epstein-Barr virus transcription factor EBNA-2: Induction of the p55alpha regulatory subunit of PI3-kinase and its role in survival of EREB2.5 cells. J Gen Virol 87:2859-2867.
52. Maier S, et al. (2006) Cellular target genes of Epstein-Barr virus nuclear antigen 2. J Virol 80:9761-9771. (Pubitemid 44435650)
53. Hertle ML, et al. (2009) Differential gene expression patterns of EBV infected EBNA- 3A positive and negative human B lymphocytes. PLoS Pathog 5:e1000506.
54. Bain M, Watson RJ, Farrell PJ, Allday MJ (1996) Epstein-Barr virus nuclear antigen 3C is a powerful repressor of transcription when tethered to DNA. J Virol 70:2481-2489.
55. Hickabottom M, Parker GA, Freemont P, Crook T, Allday MJ (2002) Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP). J Biol Chem 277:47197-47204.
56. Cludts I, Farrell PJ (1998) Multiple functions within the Epstein-Barr virus EBNA-3A protein. J Virol 72:1862-1869.
57. Ma Q, et al. (2009) Antitumorigenesis of antioxidants in a transgenic Rac1 model of Kaposi's sarcoma. Proc Natl Acad Sci USA 106:8683-8688.
58. Mutlu AD, et al. (2007) In vivo-restricted and reversible malignancy induced by human herpesvirus-8 KSHV: A cell and animal model of virally induced Kaposi's sarcoma. Cancer Cell 11:245-258.
59. Petti LM, Ricciardi EC, Page HJ, Porter KA (2008) Transforming signals resulting from sustained activation of the PDGFbeta receptor in mortal human fibroblasts. J Cell Sci 121:1172-1182.
60. Doreau A, et al. (2009) Interleukin 17 acts in synergy with B cell-activating factor to influence B cell biology and the pathophysiology of systemic lupus erythematosus. Nat Immunol 10:778-785.
61. Cahir-McFarland ED, Davidson DM, Schauer SL, Duong J, Kieff E (2000) NF-kappa B inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells. Proc Natl Acad Sci USA 97:6055-6060.
62. Ahr B, Denizot M, Robert-Hebmann V, Brelot A, Biard-Piechaczyk M (2005) Identification of the cytoplasmic domains of CXCR4 involved in Jak2 and STAT3 phosphorylation. J Biol Chem 280:6692-6700.
63. Yu H, Kortylewski M, Pardoll D (2007) Crosstalk between cancer and immune cells: Role of STAT3 in the tumour microenvironment. Nat Rev Immunol 7:41-51.
64. Pello OM, et al. (2006) SOCS up-regulation mobilizes autologous stem cells through CXCR4 blockade. Blood 108:3928-3937.
65. Gonzalez SL, Stremlau M, He X, Basile JR, Münger K (2001) Degradation of the retinoblastoma tumor suppressor by the human papillomavirus type 16 E7 oncoprotein is important for functional inactivation and is separable from proteasomal degradation of E7. J Virol 75:7583-7591.
66. Parker GA, et al. (1996) Epstein-Barr virus nuclear antigen (EBNA)3C is an immortalizing oncoprotein with similar properties to adenovirus E1A and papillomavirus E7. Oncogene 13:2541-2549.
67. Knight JS, Sharma N, Robertson ES (2005) Epstein-Barr virus latent antigen 3C can mediate the degradation of the retinoblastoma protein through an SCF cellular ubiquitin ligase. Proc Natl Acad Sci USA 102:18562-18566.
68. Brazma A, et al. (2001) Minimum information about a microarray experiment (MIAME)-toward standards for microarray data. Nat Genet 29:365-371.
69. Eisen MB, Spellman PT, Brown PO, Botstein D (1998) Cluster analysis and display of genome-wide expression patterns. Proc Natl Acad Sci USA 95:14863-14868.
70. Saeed AI, et al. (2003) TM4: A free, open-source system for microarray data management and analysis. Biotechniques 34:374-378.
71. Wixon J, Kell D (2000) The Kyoto encyclopedia of genes and genomes - KEGG. Yeast 17:48-55.