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Cheragh, Mahboobeh, Sadeghizadeh, Majid, Pouriayevali, Mohammad Hasan, Parsania, Masoud. (1402). Dendrosomal nanocurcumin prevents EBV-associated cell transformation by targeting the lytic cycle genes of the Epstein-Barr virus in the generation of lymphoblastoid cell line. , 26(10), 1220-1226. doi: 10.22038/ijbms.2023.69839.15199
Mahboobeh Cheragh; Majid Sadeghizadeh; Mohammad Hasan Pouriayevali; Masoud Parsania. "Dendrosomal nanocurcumin prevents EBV-associated cell transformation by targeting the lytic cycle genes of the Epstein-Barr virus in the generation of lymphoblastoid cell line". , 26, 10, 1402, 1220-1226. doi: 10.22038/ijbms.2023.69839.15199
Cheragh, Mahboobeh, Sadeghizadeh, Majid, Pouriayevali, Mohammad Hasan, Parsania, Masoud. (1402). 'Dendrosomal nanocurcumin prevents EBV-associated cell transformation by targeting the lytic cycle genes of the Epstein-Barr virus in the generation of lymphoblastoid cell line', , 26(10), pp. 1220-1226. doi: 10.22038/ijbms.2023.69839.15199
Cheragh, Mahboobeh, Sadeghizadeh, Majid, Pouriayevali, Mohammad Hasan, Parsania, Masoud. Dendrosomal nanocurcumin prevents EBV-associated cell transformation by targeting the lytic cycle genes of the Epstein-Barr virus in the generation of lymphoblastoid cell line. , 1402; 26(10): 1220-1226. doi: 10.22038/ijbms.2023.69839.15199

Dendrosomal nanocurcumin prevents EBV-associated cell transformation by targeting the lytic cycle genes of the Epstein-Barr virus in the generation of lymphoblastoid cell line

Iranian Journal of Basic Medical Sciences
مقاله 13، دوره 26، شماره 10، دی 2023، صفحه 1220-1226    اصل مقاله (717.83 K)
نوع مقاله: Original Article
شناسه دیجیتال (DOI): 10.22038/ijbms.2023.69839.15199
نویسندگان
Mahboobeh Cheragh1؛ Majid Sadeghizadeh2؛ Mohammad Hasan Pouriayevali3؛ Masoud Parsania* 4، 5
1Department of Microbiology, Faculty of Advanced Science and Technology, Tehran Medical Sciences, Islamic Azad University, Tehran, Iran
2Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran
3Department of Arboviruses and Viral Hemorrhagic Fevers (National Reference Laboratory), Pasteur Institute of Iran, Tehran, Iran
4Department of Microbiology, Faculty of Medicine, Tehran Medical Sciences, Islamic Azad University, Tehran, Iran
5Medical Genomics Research Center, Tehran Medical Sciences, Islamic Azad University, Tehran, Iran
چکیده
Objective(s): Targeting the lytic cycle of the Epstein-Barr virus (EBV) has been considered a new treatment strategy for malignancies caused by this virus.  This study aimed to investigate the effect of Dendrosomal NanoCurcumin (DNC) to prevent cell transformation and inhibit the expression of viral lytic gene expression in the generation of lymphoblastoid cell line (LCL).
Materials and Methods: Cell viability of LCLs and PBMCs was performed by MTT assay, and flow cytometry (Annexin/PI) was used for evaluation of apoptosis. CD markers on the surface of generated LCL (CD19) cells were examined for cell validation. The effect of DNC on transformation was evaluated by examining cell morphology and determining the expression level of lytic genes BZLF1, Zta, BHRF1, and BRLF1 of EBV using Real-time PCR. Student’s t-test was used for statistical analysis.
Results: The MTT assay showed that DNC can inhibit the proliferation of LCL in a dose-dependent manner. The 50% cytotoxic concentration (CC50) of DNC and curcumin for LCL was determined 38.8 µg/ml and 75 µg/ml, respectively after 72 hr. Also, Real-time PCR data analysis showed that DNC in 30 µg/ml concentration significantly inhibited cell transformation in the LCL and significantly reduced viral lytic genes such as BZLF1, Zta, BHRF1, and BRLF1expression compared to control.
Conclusion: Overall, these findings show that DNC reduces the expression of the viral lytic cycle genes and also the induction of cell apoptosis and finally prevents the generation of LCL.
کلیدواژه‌ها
Cell transformation؛ Curcumin؛ Epstein-Barr virus؛ Lymphoma؛ Viral genes
مراجع
1. Khan G, Hashim MJ. Global burden of deaths from Epstein-Barr virus attributable malignancies 1990-2010. Infect Agent Cancer 2014; 9:1-11.
2. Young LS, Rickinson AB. Epstein–Barr virus: 40 years on. Nat Rev Cancer 2004; 4:757-768.
3. Hernández Durán A, Grünewald K, Topf M. Conserved Central Intraviral Protein Interactome of the Herpesviridae Family. Msystems 2019; 4:e00295-00219.
4. Dunmire SK, Verghese PS, Balfour Jr HH. Primary epstein-barr virus infection. J Clin Virol 2018; 102:84-92.
5. Houldcroft CJ, Kellam P. Host genetics of Epstein–Barr virus infection, latency and disease. Rev Med Virol 2015; 25:71-84.
6. Kang M-S, Kieff E. Epstein–Barr virus latent genes. Exp Mol Med 2015; 47:e131-e131.
7. Hong GK, Kumar P, Wang L, Damania B, Gulley ML, Delecluse H-J, et al. Epstein-Barr virus lytic infection is required for efficient production of the angiogenesis factor vascular endothelial growth factor in lymphoblastoid cell lines. J Virol 2005; 79:13984-13992.
8. Hui-Yuen J, McAllister S, Koganti S, Hill E, Bhaduri-McIntosh S. Establishment of Epstein-Barr virus growth-transformed lymphoblastoid cell lines. J Vis Exp 2011:e3321.
9. Amoli M, Carthy D, Platt H, Ollier W. EBV Immortalization of human B lymphocytes separated from small volumes of cryo-preserved whole blood. Int J Epidemiol 2008; 37:i41-i45.
10. Li H, Liu S, Hu J, Luo X, Li N, Bode AM, et al. Epstein-Barr virus lytic reactivation regulation and its pathogenic role in carcinogenesis. Int J Biol Sci 2016; 12:1309.
11. Tsai S-C, Lin S-J, Chen P-W, Luo W-Y, Yeh T-H, Wang H-W, et al. EBV Zta protein induces the expression of interleukin-13, promoting the proliferation of EBV-infected B cells and lymphoblastoid cell lines. Blood 2009; 114:109-118.
12. Morrison TE, Mauser A, Klingelhutz A, Kenney SC. Epstein-Barr virus immediate-early protein BZLF1 inhibits tumor necrosis factor alpha-induced signaling and apoptosis by downregulating tumor necrosis factor receptor 1. J Virol 2004; 78:544-549.
13. Milián E, Prats E, Cairó JJ, Gòdia F, Vives J. BHRF1 exerts an antiapoptotic effect and cell cycle arrest via Bcl-2 in murine hybridomas. J Biotechnol 2015; 209:58-67.
14. Xu F-H, Xiong D, Xu Y-F, Cao S-M, Xue W-Q, Qin H-D, et al. An epidemiological and molecular study of the relationship between smoking, risk of nasopharyngeal carcinoma, and Epstein–Barr virus activation. J Natl Cancer Inst 2012; 104:1396-1410.
15. Gargouri B, Nasr R, Mseddi M, Benmansour R, Lassoued s. Induction of Epstein-Barr virus (EBV) lytic cycle in vitro causes lipid peroxidation, protein oxidation and DNA damage in lymphoblastoid B cell lines. Lipids Health Dis 2011; 10:1-8.
16. Frisan T, Levitsky V, Masucci M. Generation of lymphoblastoid cell lines (LCLs). Epstein-Barr Virus Protocols Methods Mol Biol 2001:125-127.
17. Darlington GJ. Epstein-Barr virus transformation of lymphoblasts. CSH Protoc 2006; 2006:pdb. prot4481.
18. Jagetia GC, Aggarwal BB. “Spicing up” of the immune system by curcumin. J Clin Immunol 2007; 27:19-35.
19. Wilken R, Veena MS, Wang MB, Srivatsan ES. Curcumin: A review of anti-cancer properties and therapeutic activity in head and neck squamous cell carcinoma. Mol Cancer 2011; 10:1-19.
20. Zhou X, Wang W, Li P, Zheng Z, Tu Y, Zhang Y, et al. Curcumin enhances the effects of 5-fluorouracil and oxaliplatin in inducing gastric cancer cell apoptosis both in vitro and in vivo. Oncol Res 2016; 23:29.
21. Maheshwari RK, Singh AK, Gaddipati J, Srimal RC. Multiple biological activities of curcumin: a short review. Life Sci 2006; 78:2081-2087.
22. Aggarwal BB, Sung B. Pharmacological basis for the role of curcumin in chronic diseases: an age-old spice with modern targets. Trends Pharmacol Sci 2009; 30:85-94.
23. Sarbolouki MN, Sadeghizadeh M, Yaghoobi MM, Karami A, Lohrasbi T. Dendrosomes: a novel family of vehicles for transfection and therapy. J Chem Technol Biotechnol 2000; 75:919-922.
24. Tahmasebi BM, Erfani MV, Babaei E, Najafi F, Zamani M, Shariati M, et al. Dendrosomal Nano-Curcumin, the Novel Formulation to Improve the Anticancer Properties of Curcumin.  progress s in biological sciences 2015;5: 143-158.
25. Mirgani MT, Isacchi B, Sadeghizadeh M, Marra F, Bilia AR, Mowla SJ, et al. Dendrosomal curcumin nanoformulation downregulates pluripotency genes via miR-145 activation in U87MG glioblastoma cells. Int J Nanomedicine 2014; 9:403.
26. Babaei E, Sadeghizadeh M, Hassan ZM, Feizi MAH, Najafi F, Hashemi SM. Dendrosomal curcumin significantly suppresses cancer cell proliferation in vitro and in vivo. Int Immunopharmacol 2012; 12:226-234.
27. Farhangi B, Alizadeh AM, Khodayari H, Khodayari S, Dehghan MJ, Khori V, et al. Protective effects of dendrosomal curcumin on an animal metastatic breast tumor. Eur J Pharmacol 2015; 758:188-196.
28. Ranji N, Sadeghizadeh M. Investigation of free and dendrosomal curcumin effects on apoptosis induction in stem cells and cancer cell lines. Pathobiology Research 2011; 14:37-49.
29. Sadeghizadeh M, Ranjbar B, Damaghi M, Khaki L, Sarbolouki MN, Najafi F, et al. Dendrosomes as novel gene porters‐III. J Chem Technol Biotechnol: International Research in Process, Environmental & Clean Technology 2008; 83:912-920.
30. Ghahari SMM, Ajami A, Sadeghizadeh M, Rastaghi ARE, Mahdavi M. Nanocurcumin as an adjuvant in killed Toxoplasma gondii vaccine formulation: An experience in BALB/c mice. Exp Parasitol 2022; 243:108404.
31. Farsani SSM, Sadeghizadeh M, Gholampour MA, Safari Z, Najafi F. Nanocurcumin as a novel stimulator of megakaryopoiesis that ameliorates chemotherapy-induced thrombocytopenia in mice. Life Sci 2020; 256:117840.
32. Esmatabadi MJD, Farhangi B, Montazeri M, Monfared H, Sistani RN, Sadeghizadeh M. Up-regulation of miR-21 decreases chemotherapeutic effect of dendrosomal curcumin in breast cancer cells. Iran J Basic Med Sci 2017; 20:350.
33. Gou M, Men K, Shi H, Xiang M, Zhang J, Song J, et al. Curcumin-loaded biodegradable polymeric micelles for colon cancer therapy in vitro and in vivo. Nanoscale 2011; 3:1558-1567.
34. Baghi N, Bakhshinejad B, Keshavarz R, Babashah S, Sadeghizadeh M. Dendrosomal nanocurcumin and exogenous p53 can act synergistically to elicit anticancer effects on breast cancer cells. Gene 2018; 670:55-62.
35. Esmatabadi MJD, Farhangi B, Safari Z, Kazerooni H, Shirzad H, Zolghadr F, et al. Dendrosomal curcumin inhibits metastatic potential of human SW480 colon cancer cells through Down-regulation of Claudin1, Zeb1 and Hef1-1 gene expression. Asian Pac J Cancer Prev 2015; 16:2473-2481.
36. Chaiwongkot A, Kitkumthorn N, Srisuttee R, Buranapraditkun S. Cellular expression profiles of Epstein-Barr virus-transformed B-lymphoblastoid cell lines Corrigendum in/10.3892/br. 2020.1379. Biomed Rep 2020; 13:1-1.
37. Londin ER, Keller MA, D’Andrea MR, Delgrosso K, Ertel A, Surrey S, et al. Whole-exome sequencing of DNA from peripheral blood mononuclear cells (PBMC) and EBV-transformed lymphocytes from the same donor. BMC genomics 2011; 12:1-9.
38. Frisan T, Levitsky V, Masucci M. Generation of lymphoblastoid cell lines (LCLs).  Epstein-Barr Virus Protocols: Springer; Methods Mol Biol 2001. p. 125-127.
39. Ruitenberg JJ, Mulder CB, Maino VC, Landay AL, Ghanekar SA. VACUTAINER® CPT™ and Ficoll density gradient separation perform equivalently in maintaining the quality and function of PBMC from HIV seropositive blood samples. BMC Immunol 2006; 7:1-8.
40. Thorley-Lawson DA, Gross A. Persistence of the Epstein–Barr virus and the origins of associated lymphomas. N Engl J Med 2004; 350:1328-1337.
41. Meerloo JV, Kaspers GJ, Cloos J. Cell sensitivity assays: the MTT assay.  Cancer cell culture: Springer 2011. p. 237-245.
42. Tolosa L, Donato MT, Gómez-Lechón MJ. General cytotoxicity assessment by means of the MTT assay.  Protocols in in vitro hepatocyte research: Springer 2015. p. 333-348.
43. Amon W, Binné UK, Bryant H, Jenkins PJ, Karstegl CE, Farrell PJ. Lytic cycle gene regulation of Epstein-Barr virus. J Virol 2004; 78:13460-13469.
44. Bhende PM, Seaman WT, Delecluse H-J, Kenney SC. BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186. J Virol 2005; 79:7338-7348.
45. Bhende PM, Dickerson SJ, Sun X, Feng W-H, Kenney SC. X-box-binding protein 1 activates lytic Epstein-Barr virus gene expression in combination with protein kinase D. J Virol 2007; 81:7363-7370.
46. Chang Y, Lee H-H, Chen Y-T, Lu J, Wu S-Y, Chen C-W, et al. Induction of the early growth response 1 gene by Epstein-Barr virus lytic transactivator Zta. J Virol 2006; 80:7748-7755.
47. Bristol JA, Djavadian R, Albright ER, Coleman CB, Ohashi M, Hayes M, et al. A cancer-associated Epstein-Barr virus BZLF1 promoter variant enhances lytic infection. PLoS Pathog 2018; 14:e1007179.
48. Lee C-H, Yeh T-H, Lai H-C, Wu S-Y, Su I-J, Takada K, et al. Epstein-Barr virus Zta-induced immunomodulators from nasopharyngeal carcinoma cells upregulate interleukin-10 production from monocytes. J Virol 2011; 85:7333-7342.
49. Guenther JF, Cameron JE, Nguyen HT, Wang Y, Sullivan DE, Shan B, et al. Modulation of lung inflammation by the Epstein-Barr virus protein Zta. Am J Physiol Lung Cell Mol Physiol 2010; 299:L771-L784.
50. Murata T, Sato Y, Kimura H. Modes of infection and oncogenesis by the Epstein–Barr virus. Rev Med Virol 2014; 24:242-253.
51. Stanfield BA, Luftig MA. Recent advances in understanding Epstein-Barr virus. F1000Res 2017; 6:386.
52. Morrison TE, Kenney SC. BZLF1, an Epstein–Barr virus immediate–early protein, induces p65 nuclear translocation while inhibiting p65 transcriptional function. J Virol 2004; 328:219-232.
53. Fitzsimmons L, Cartlidge R, Chang C, Sejic N, Galbraith LC, Suraweera CD, et al. EBV BCL-2 homologue BHRF1 drives chemoresistance and lymphomagenesis by inhibiting multiple cellular pro-apoptotic proteins. Cell Death Differ 2020; 27:1554-1568.
54. Li H, Hu J, Luo X, Bode AM, Dong Z, Cao Y. Therapies based on targeting Epstein‐Barr virus lytic replication for EBV‐associated malignancies. Cancer Sci 2018; 109:2101-2108.
55. Yap H-Y, Siow T-S, Chow S-K, Teow S-Y. Epstein-Barr Virus-(EBV-) immortalized lymphoblastoid cell lines (LCLs) express high level of CD23 but low CD27 to support their growth. Adv Virol 2019; 2019:6464521.
56. Hur D, Lee M, Kim J, Kim JH, Shin Y, Rho J, et al. CD19 signalling improves the Epstein–Barr virus‐induced immortalization of human B cell. Cell Prolif 2005; 38:35-45.
57. Shakeri A, Panahi Y, Johnston TP, Sahebkar A. Biological properties of metal complexes of curcumin. BioFactors 2019; 45:304-317.
58. Šudomová M, Hassan ST. Nutraceutical curcumin with promising protection against herpesvirus infections and their associated inflammation: mechanisms and pathways. Microorganisms 2021; 9:292.
59. Liu L, Yang J, Ji W, Wang C. Curcumin inhibits proliferation of epstein–barr virus-associated human nasopharyngeal carcinoma cells by inhibiting EBV nuclear antigen 1 expression. Biomed Res Int 2019; 2019:8592921.

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