NIRF, a novel ubiquitin ligase, inhibits hepatitis B virus replication through effect on HBV core protein and H3 histones

DNA and Cell Biology

Volumn 34, Issue 5, 2015, Pages 327-332

  Qian, Guanhua ^a,b   Hu, Bin ^a   Zhou, Danlin ^a   Xuan, Yanyan ^a   Bai, Lu ^a   Duan, Changzhu ^a  

^a CHONGQING MEDICAL UNIVERSITY   (China)

^b THE SECOND AFFILIATED HOSPITAL OF CHONGQING MEDICAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; HEPATITIS B SURFACE ANTIGEN; HEPATITIS B(E) ANTIGEN; HISTONE H3; MESSENGER RNA; NIRF PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VIRUS DNA; HISTONE; UBIQUITIN; UHRF2 PROTEIN, HUMAN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DRUG INHIBITION; EMBRYO; GENETIC TRANSFECTION; HEPATITIS B VIRUS; HEPG2 CELL LINE; HUMAN; HUMAN CELL; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ACETYLATION; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; RANDOMIZED CONTROLLED TRIAL; VIRUS INHIBITION; VIRUS REPLICATION; ACETYLATION; ANIMAL; BAGG ALBINO MOUSE; ENZYME IMMUNOASSAY; GENETICS; HEPATITIS B; METABOLISM; PHYSIOLOGY; PROTEIN PROCESSING; REAL TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; VIROLOGY; WESTERN BLOTTING;

HEPATITIS B VIRUS;

ACETYLATION; ANIMALS; BLOTTING, WESTERN; DNA, VIRAL; HEP G2 CELLS; HEPATITIS B; HEPATITIS B E ANTIGENS; HEPATITIS B SURFACE ANTIGENS; HEPATITIS B VIRUS; HISTONES; HUMANS; IMMUNOENZYME TECHNIQUES; MALE; MICE; MICE, INBRED BALB C; PROTEIN PROCESSING, POST-TRANSLATIONAL; REAL-TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; VIRUS REPLICATION;

EID: 84928987613     PISSN: 10445498     EISSN: 15577430     Source Type: Journal    
DOI: 10.1089/dna.2014.2714     Document Type: Article

References (21)

1. Bronner, C., Achour, M., Arima, Y., Chataigneau, T., Saya, H., and Schini-Kerth, V. B. (2007). The UHRF family: oncogenes that are drugable targets for cancer therapy in the near future. Pharmacol Ther 115, 419-434
2. Chisari, F. V. (2000). Viruses, immunity, and cancer: lessons from hepatitis B. Am J Pathol 156, 1117-1132
3. Gerle, B., Koroknai, A., Fejer, G., Bakos, A., Banati, F., Szenthe, K., Wolf, H., Niller, H. H., Minarovits, J., and Salamon. (2007). Acetylated histone H3 and H4 mark the upregulated LMP2A promoter of Epstein-Barr virus in lymphoid cells. J Virol 81, 13242-13247
4. Jackson, P. K., Eldridge, A. G., Freed, E., Furstenthal, L., Hsu, J. Y., Kaiser, B. K., and Reimann, J. D. (2000). The lore of the RINGs-substrate recognition and catalysis by ubiquitin ligases. Trends Cell Biol 10, 429-439
5. Jeong, H., Cho, M. H., Park, S. G., and Jung, G. (2014). Interaction between nucleophosmin and HBV core protein increases HBV capsid assembly. FEBS Lett 588, 851-858
6. Kang, H., Yu, J., and Jung, G. (2008). Phosphorylation of hepatitis B virus core Cterminally truncated protein (Cp149) by PKC increases capsid assembly andstability. Biochem J 416, 47-54
7. Lee, S. J., Shim, H. Y., Hsieh, A., Min, J. Y., and Jung, G. (2009). Hepatitis B virus core interacts with the host cell nucleolar protein, nucleophosmin 1. J Microbiol 47, 746-752
8. Liu, F., Song, Y., and Liu, D. (1999). Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA. Gene Ther 6, 1258-1266
9. Moolla, N., Kew, M., and Arbuthnot, P. (2002). Regulatory elements of hepatitis B virus transcription. J Viral Hepat 9, 323-331
10. Mori, T., Ikeda, D. D., Fukushima, T., Takenoshita, S., and Kochi, H. (2011). NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor. Cell Cycle 10, 3284-3299
11. Mori, T., Ikeda, D. D., Yoshiki, Y., Unoki, M.; NIRF Project. (2012). NIRF/UHRF2 occupies a central position in the cell cycle network and allows coupling with the epigenetic landscape. FEBS Lett 586, 1570-1583
12. Mori, T., Li, Y., Hata, H., and Kochi, H. (2004). NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein. FEBS Lett 557, 209-214
13. Mori, T., Li, Y., Hata, H., Ono, K., and Kochi, H. (2002). NIRF, a novel RING finger protein, isinvolved in cell-cycle regulation. Biochem Biophys Res Commun 296, 530-536
14. Nassal, M. (2008). Hepatitis B viruses: reverse transcription a different way. Virus Res 134, 235-249
15. Ott, J. J., Stevens, G. A., Groeger, J., and Wiersma, S. T. (2012). Global epidemiology of hepatitis B virus infection: new estimates of age-specific HBsAg seroprevalence and endemicity. Vaccine 30, 2212-2219
16. Porterfield, J. Z., Dhason, M. S., Loeb, D. D., Nassal, M., Stray, S. J., and Zlotnick, A. (2010). Full-length hepatitis B virus core protein packages viral and heterologous RNA with similarly high levels of cooperativity. J Virol 84, 7174-7184
17. Qian, G., Jin, F., Chang, L., Yang, Y., Peng, H., and Duan, C. (2012). NIRF, a novel ubiquitin ligase, interacts with hepatitis B virus core protein and promotes its degradation. Biotechnol Lett 34, 29-36
18. Shim, H. Y., Quan, X., Yi, Y. S, and Jung, G. (2011). Heat shock protein 90 facilitates formation of theHBVcapsid via interacting with the HBV core protein dimers. Virology 410, 161-169
19. Teresa, P., Laura, B., Giusepeppina, R., Natalia, P., Giovanni, S., Giovanni, R., and Massimo, L. (2006). Hepatitis B virus replication is regulated by the acetylation status of hepatitis B virus cccDNA-bound H3 and H4 histones. Gastroenterology 130, 823-837
20. Xu, W. S., Zhao, K. K., Miao, X. H., Wu, N., Cai, X., Zhang, R. Q., and Wan, J. (2010). Effect of oxymatrine on the replication cycle ofhepatitis B virus in vitro. World J Gastroenterol 16, 2028-2037
21. Zhang, G., Budker, V., and Wolff, J. A. (1999). High levels of foreign gene expression in hepatocytes after tail vein injections of naked plasmid DNA. Hum Gene Ther 10, 1735-1737