IRAK4 is essential for TLR9-induced suppression of Epstein-Barr virus BZLF1 transcription in Akata Burkitt’s lymphoma cells

PLoS ONE

Volumn 12, Issue 10, 2017, Pages

  Jordi, Marc ^a   Marty, Jeannine ^a   Mordasini, Vanessa ^a   Lünemann, Anna ^a   McComb, Scott ^a   Bernasconi, Michele ^a   Nadal, David ^a  

^a UNIVERSITY CHILDREN S HOSPITAL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 9; CRISPR ASSOCIATED PROTEIN; IMMEDIATE EARLY PROTEIN BZLF1; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 1; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE 4; MYELOID DIFFERENTIATION FACTOR 88; TOLL LIKE RECEPTOR 9; BZLF1 PROTEIN, HERPESVIRUS 4, HUMAN; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE; IRAK1 PROTEIN, HUMAN; IRAK4 PROTEIN, HUMAN; MYD88 PROTEIN, HUMAN; TLR9 PROTEIN, HUMAN; TRANSACTIVATOR PROTEIN;

AKATA CELL LINE; ARTICLE; B LYMPHOCYTE; CELL DEATH; CELL VIABILITY; CONTROLLED STUDY; CROSS LINKING; ENZYME INACTIVATION; EPSTEIN BARR VIRUS; PROTEIN EXPRESSION; PROTEIN SYNTHESIS; PROTEIN TARGETING; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; BURKITT LYMPHOMA; CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEAT; GENETICS; HUMAN; METABOLISM; PATHOLOGY; PHYSIOLOGY; TUMOR CELL LINE; VIROLOGY; VIRUS ACTIVATION;

BURKITT LYMPHOMA; CELL LINE, TUMOR; CLUSTERED REGULARLY INTERSPACED SHORT PALINDROMIC REPEATS; HERPESVIRUS 4, HUMAN; HUMANS; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASES; MYELOID DIFFERENTIATION FACTOR 88; TOLL-LIKE RECEPTOR 9; TRANS-ACTIVATORS; VIRUS ACTIVATION;

EID: 85032936526     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0186614     Document Type: Article

References (39)

1. Young LS, Rickinson AB. Epstein-Barr virus: 40 years on. Nat Rev Cancer. 2004; 4: 757–68. https://doi.org/10.1038/nrc1452 PMID: 15510157
2. Speck SH, Ganem D. Viral latency and its regulation: lessons from the gamma-herpesviruses. Cell Host Microbe. Elsevier Inc.; 2010; 8: 100–15. https://doi.org/10.1016/j.chom.2010.06.014 PMID: 20638646
3. Klein G. Epstein-Barr virus strategy in normal and neoplastic B cells. Cell. 1994; 77: 791–3. PMID: 8004668
4. Brady G, Macarthur GJ, Farrell PJ. Epstein-Barr virus and Burkitt lymphoma. Postgrad Med J. 2008; 84: 372–7. https://doi.org/10.1136/jcp.2007.047977 PMID: 18716017
5. Nemerow GR, Mold C, Schwend VK, Tollefson V, Cooper NR. Identification of gp350 as the viral glyco-protein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: sequence homology of gp350 and C3 complement fragment C3d. J Virol. 1987; 61: 1416–20. PMID: 3033269
6. Rowe DT, Rowe M, Evan GI, Wallace LE, Farrell PJ, Rickinson AB. Restricted expression of EBV latent genes and T-lymphocyte-detected membrane antigen in Burkitt’s lymphoma cells. EMBO J. 1986; 5: 2599–607. PMID: 3023050
7. Rowe M, Kelly GL, Bell AI, Rickinson AB. Burkitt’s lymphoma: the Rosetta Stone deciphering Epstein-Barr virus biology. Semin Cancer Biol. 2009; 19: 377–88. https://doi.org/10.1016/j.semcancer.2009.07.004 PMID: 19619657
8. Countryman J, Jenson H, Seibl R, Wolf H, Miller G. Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency. J Virol. 1987; 61: 3672–9. PMID: 2824806
9. Tovey MG, Lenoir G, Begon-Lours J. Activation of latent Epstein-Barr virus by antibody to human IgM. Nature. 1978; 276: 270–2. https://doi.org/10.1038/276270a0 PMID: 213727
10. zur Hausen H, O’Neill FJ, Freese UK, Hecker E. Persisting oncogenic herpesvirus induced by the tumour promotor TPA. Nature. Nature Publishing Group; 1978; 272: 373–5. https://doi.org/10.1038/272373a0 PMID: 204874
11. Luka J, Kallin B, Klein G. Induction of the Epstein-Barr virus (EBV) cycle in latently infected cells by n-butyrate. Virology. 1979; 94: 228–31. PMID: 220786
12. Takada K. Cross-linking of cell surface immunoglobulins induces Epstein-Barr virus in Burkitt lymphoma lines. Int J Cancer. 1984; 33: 27–32. PMID: 6319296
13. di Renzo L, Altiok A, Klein G, Klein E. Endogenous TGF-beta contributes to the induction of the EBV lytic cycle in two Burkitt lymphoma cell lines. Int J Cancer. 1994; 57: 914–9. PMID: 8206684
14. Lünemann A, Rowe M, Nadal D. Epstein Barr Virus Volume 2: One Herpes Virus: Many Diseases. In: Münz C, editor. Cham: Springer International Publishing; 2015. pp. 265–287. https://doi.org/10.1007/978-3-319-22834-1_9
15. Middeldorp JM. Epstein Barr Virus Volume 2: One Herpes Virus: Many Diseases. In: Münz C, editor. Cham: Springer International Publishing; 2015. pp. 289–323. https://doi.org/10.1007/978-3-319-22834-1_10
16. Hislop AD, Taylor GS. Epstein Barr Virus Volume 2: One Herpes Virus: Many Diseases. In: Münz C, editor. Cham: Springer International Publishing; 2015. pp. 325–353. https://doi.org/10.1007/978-3-319-22834-1_11
17. Murata T, Kondo Y, Sugimoto A, Kawashima D, Saito S, Isomura H, et al. Epigenetic histone modification of Epstein-Barr virus BZLF1 promoter during latency and reactivation in Raji cells. J Virol. 2012; 86: 4752–61. https://doi.org/10.1128/JVI.06768-11 PMID: 22357272
18. Ramasubramanyan S, Osborn K, Flower K, Sinclair AJ. Dynamic chromatin environment of key lytic cycle regulatory regions of the Epstein-Barr virus genome. J Virol. 2012; 86: 1809–19. https://doi.org/10.1128/JVI.06334-11 PMID: 22090141
19. Bryant H, Farrell PJ. Signal Transduction and Transcription Factor Modification during Reactivation of Epstein-Barr Virus from Latency. J Virol. 2002; 76: 10290–8. https://doi.org/10.1128/JVI.76.20.1029010298.2002 PMID: 12239305
20. Ladell K, Dorner M, Zauner L, Berger C, Zucol F, Bernasconi M, et al. Immune activation suppresses initiation of lytic Epstein-Barr virus infection. Cell Microbiol. 2007; 9: 2055–69. https://doi.org/10.1111/j.1462-5822.2007.00937.x PMID: 17419714
21. Zauner L, Melroe GT, Sigrist J a, Rechsteiner MP, Dorner M, Arnold M, et al. TLR9 triggering in Burkitt’s lymphoma cell lines suppresses the EBV BZLF1 transcription via histone modification. Oncogene. Nature Publishing Group; 2010; 29: 4588–4598. https://doi.org/10.1038/onc.2010.203 PMID: 20514021
22. Kawai T, Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol. Nature Publishing Group; 2010; 11: 373–84. https://doi.org/10.1038/ni.1863 PMID: 20404851
23. Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell. Elsevier Inc.; 2010; 140: 805–20. https://doi.org/10.1016/j.cell.2010.01.022 PMID: 20303872
24. Heeg K, Dalpke A, Peter M, Zimmermann S. Structural requirements for uptake and recognition of CpG oligonucleotides. Int J Med Microbiol. 2008; 298: 33–8. https://doi.org/10.1016/j.ijmm.2007.07.007PMID: 17706458
25. Takeshita F, Gursel I, Ishii KJ, Suzuki K, Gursel M, Klinman DM. Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Semin Immunol. 2004; 16: 17–22. https://doi.org/10.1016/j.smim.2003.10.009 PMID: 14751759
26. Zauner L, Melroe GT, Sigrist J a, Rechsteiner MP, Dorner M, Arnold M, et al. TLR9 triggering in Burkitt’s lymphoma cell lines suppresses the EBV BZLF1 transcription via histone modification. Oncogene. Nature Publishing Group; 2010; 29: 4588–98. https://doi.org/10.1038/onc.2010.203 PMID: 20514021
27. Rechsteiner MP, Berger C, Zauner L, Sigrist J a, Weber M, Longnecker R, et al. Latent membrane protein 2B regulates susceptibility to induction of lytic Epstein-Barr virus infection. J Virol. 2008; 82: 1739–47. https://doi.org/10.1128/JVI.01723-07 PMID: 18057232
28. Ran FA, Hsu PD, Wright J, Agarwala V, Scott DA, Zhang F. Genome engineering using the CRISPR-Cas9 system. Nat Protoc. 2013; 8: 2281–308. https://doi.org/10.1038/nprot.2013.143 PMID: 24157548
29. Aya T, Kinoshita T, Imai S, Koizumi S, Mizuno F, Osato T, et al. Chromosome translocation and c-MYC activation by Epstein-Barr virus and Euphorbia tirucalli in B lymphocytes. Lancet (London, England). 1991; 337: 1190.
30. Flemington EK, Goldfeld AE, Speck SH. Efficient transcription of the Epstein-Barr virus immediate-early BZLF1 and BRLF1 genes requires protein synthesis. J Virol. 1991; 65: 7073–7. PMID: 1658397
31. Yin Q, Jupiter K, Flemington EK. The Epstein-Barr virus transactivator Zta binds to its own promoter and is required for full promoter activity during anti-Ig and TGF-beta1 mediated reactivation. Virology. 2004; 327: 134–43. https://doi.org/10.1016/j.virol.2004.06.026 PMID: 15327904
32. Ye J, Gradoville L, Miller G. Cellular immediate-early gene expression occurs kinetically upstream of Epstein-Barr virus bzlf1 and brlf1 following cross-linking of the B cell antigen receptor in the Akata Burkitt lymphoma cell line. J Virol. 2010; 84: 12405–18. https://doi.org/10.1128/JVI.01415-10 PMID: 20861250
33. Chêne A, Donati D, Guerreiro-Cacais AO, Levitsky V, Chen Q, Falk KI, et al. A molecular link between malaria and Epstein-Barr virus reactivation. PLoS Pathog. 2007; 3: e80. https://doi.org/10.1371/journal.ppat.0030080 PMID: 17559303
34. Jenkins PJ, Binné UK, Farrell PJ. Histone acetylation and reactivation of Epstein-Barr virus from latency. J Virol. 2000; 74: 710–20. PMID: 10623733
35. Countryman JK, Gradoville L, Miller G. Histone hyperacetylation occurs on promoters of lytic cycle regulatory genes in Epstein-Barr virus-infected cell lines which are refractory to disruption of latency by histone deacetylase inhibitors. J Virol. 2008; 82: 4706–19. https://doi.org/10.1128/JVI.00116-08 PMID: 18337569
36. Haas F, Yamauchi K, Murat M, Bernasconi M, Yamanaka N, Speck RF, et al. Activation of NF-κB via endosomal Toll-like receptor 7 (TLR7) or TLR9 suppresses murine herpesvirus 68 reactivation. J Virol. 2014; 88: 10002–12. https://doi.org/10.1128/JVI.01486-14 PMID: 24942583
37. Izumiya Y, Izumiya C, Hsia D, Ellison TJ, Luciw P a, Kung H-J. NF-kappaB serves as a cellular sensor of Kaposi’s sarcoma-associated herpesvirus latency and negatively regulates K-Rta by antagonizing the RBP-Jkappa coactivator. J Virol. 2009; 83: 4435–46. https://doi.org/10.1128/JVI.01999-08 PMID: 19244329
38. Callan MFC. The immune response to Epstein-Barr virus. Microbes Infect. 2004; 6: 937–45. https://doi.org/10.1016/j.micinf.2004.04.014 PMID: 15310471
39. Duellman SJ, Thompson KL, Coon JJ, Burgess RR. Phosphorylation sites of Epstein-Barr virus EBNA1 regulate its function. J Gen Virol. 2009; 90: 2251–9. https://doi.org/10.1099/vir.0.012260-0 PMID: 19439552