Epstein-Barr virus lytic cycle activation alters proteasome subunit expression in Burkitt's lymphoma cells

Biological Chemistry

Volumn 391, Issue 9, 2010, Pages 1041-1046

  De Leo, Alessandra ^a   Matusali, Giulia ^a   Arena, Giuseppe ^a   Di Renzo, Livia ^a   Mattia, Elena ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

Burkitt's lymphoma cells; Epstein Barr virus activation; immunoproteasome; MHC class I epitopes

Indexed keywords

CASPASE; CHYMOTRYPSIN; EPITOPE; GAMMA INTERFERON; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME;

ANTIGEN EXPRESSION; ARTICLE; BURKITT LYMPHOMA; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBUNIT; EPSTEIN BARR VIRUS; HUMAN; HUMAN CELL; LYMPHOMA CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; VIRUS CELL INTERACTION;

BURKITT LYMPHOMA; HERPESVIRUS 4, HUMAN; HUMANS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN SUBUNITS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; VIRUS ACTIVATION;

HUMAN HERPESVIRUS 4;

EID: 77957557667     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2010.107     Document Type: Article

References (27)

1. Dantuma, N.P. and Masucci, M.G. (2003). The ubiquitin/proteasome system in Epstein-Barr virus latency and associated malignan-cies. Semin. Cancer Biol. 13, 69-76.
2. Frisan, T., Levitsky, V, Polack, A., and Masucci, M.G. (1998). Phe-notype-dependent differences in proteasome subunit composi-tion and cleavage specificity in B cell lines. J. Immunol. 160, 3281-3289.
3. Gaczynska, M., Rock, K.L., and Goldberg, A.L. (1993). Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365, 264-267.
4. Gavioli, R., Gallerani, E., Fortini, C., Fabris, M., Bottoni, A., Canel-la, A., Bonaccorsi, A., Marastoni, M., Micheletti, F., Cafaro, A., et al. (2004). HIV-1 tat protein modulates the generation ofcyto-toxic T cell epitopes by modifying proteasome composition and enzymatic activity. J. Immunol. 173, 3838-3843.
5. Griffin, T.A., Nandi, D., Cruz, M., Fehling, HJ., Kaer, L.V., Mon-aco, JJ., and Colbert, R.A. (1998). Immunoproteasome assem-bly: cooperative incorporation of interferon 7 (IFN-7)-inducible subunits. J. Exp. Med. 187, 97-104.
6. Groettrup, M., Khan, S., Schwarz, K., and Schmidtke, G. (2001). Interferon-7 inducible exchanges of 20S proteasome active site subunits: why? Biochimie 83, 367-372.
7. Hirano, Y., Kaneko, T., Okamoto, K., Bai, M., Yashiroda, H., Furuyama, K., Kato, K., Tanaka, K., and Murata, S. (2008). Dis-secting β-ring assembly pathway of the mammalian 20S protea-some. EMBO J. 27, 2204-2213.
8. + T cell immune evasion protein specific to Epstein-Barr virus and its close relatives in Old World primates. J. Exp. Med. 204, 1863-1873.
9. Huang, X., Seifert, U., Salzmann, U., Henklein, P., Preissner, R., Henke, W., Sijts, AJ., Kloetzel, P.M., and Dubiel, W. (2002). The RTP site shared by the HIV-1 Tat protein and the 11S reg-ulator subunit α is crucial for their effects on proteasome func-tion including antigen processing. J. Mol. Biol. 323, 771-782.
10. Lupas, A., Koster, AJ., and Baumeister, W. (1993). Structural fea-tures of 26S and 20S proteasomes. Enzyme Protein 47, 252-273.
11. Mattia, E., Ceridono, M., Chichiarelli, S., and D'Erme, M. (1999). Interactions of Epstein-Barr virus origins of replication with nuclear matrix in the latent and in the lytic phases of viral infec-tion. Virology 262, 9-17.
12. Matusali, G., Leo, A.D., Gavioli, R., Bertelli, L., Renzo, L.D., and Mattia, E. (2007). Down-regulation of proteolytic complexes following EBV activation in BL cells. Biochem. Biophys. Res. Commun. 352, 947-952.
13. Ragoczy, T. and Miller, G. (1999). Role of the Epstein-Barr virus Rta protein in activation of distinct classes of viral lytic cycle genes. J. Virol. 73, 9858-9866.
14. Rechsteiner, M., Realini, C., and Ustrell, V. (2000). The proteasome activator 11 S REG (PA28) and class I antigen presentation. Biochem. J. 345, 1-15.
15. Rickinson, A.B. and Kieff, E.B. (2001). Epstein-Barr Virus, Vol. 2 (Philadelphia, PA, USA: Lippincott Williams & Wilkins).
16. Ritz, U., Momburg, F., Pilch, H., Huber, C., Maeurer, M.J., and Seliger, B. (2001). Deficient expression of components of the MHC class I antigen processing machinery in human cervical carcinoma. Int. J. Oncol. 19, 1211-1220.
17. Rowe, M., Glaunsinger, B., van Leeuwen, D., Zuo, J., Sweetman, D., Ganem, D., Middeldorp, J., Wiertz, EJ.HJ., and Ressing, M.E. (2007). Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion. Proc. Natl. Acad. Sci. USA 104, 3366-3371.
18. Sijts, AJ., Ruppert, T., Rehermann, B., Schmidt, M., Koszinowski, U., and Kloetzel, P.M. (2000). Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features ofimmunoproteasomes. J. Exp. Med. 191, 503-514.
19. Steers, NJ., Peachman, K.K., McClain, S.R., Alving, C.R., andRao, M. (2009). HIV-1 Gag p24 alters the composition of immuno-proteasomes and affects antigen presentation. J. Virol. 29, 29.
20. Stohwasser, R., Holzhutter, H.G., Lehmann, U., Henklein, P., and Kloetzel, P.M. (2003). Hepatitis B virus HBx peptide 116-138 and proteasome activator PA28 compete for binding to the pro-teasome α4/MC6 subunit. Biol. Chem. 384, 39-49.
21. Tanaka, K. and Kasahara, M. (1998). The MHC class I ligand-generating system: roles of immunoproteasomes and the inter-feron-gamma-inducible proteasome activator PA28. Immunol. Rev. 163, 161-176.
22. Thorley-Lawson, D.A. (2001). Epstein-Barr virus: exploiting the immune system. Nat. Rev. Immunol. 1, 75-82.
23. Van den Eynde, B.J. and Morel, S. (2001). Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome. Curr. Opin. Immunol. 13, 147-153.
24. Whitby, F.G., Masters, E.I., Kramer, L., Knowlton, J.R., Yao, Y., Wang, C.C., and Hill, C.P. (2000). Structural basis for the acti-vation of 20S proteasomes by 11S regulators. Nature 408, 115-120.
25. Yuan, J., Cahir-McFarland, E., Zhao, B., and Kieff, E. (2006). Virus and cell RNAs expressed during Epstein-Barr virus replication. J. Virol. 80, 2548-2565.
26. + T cells through an additional host shutoff function. J. Virol. 82, 2385-2393.
27. Zuo, J., Currin, A., Griffin, B.D., Shannon-Lowe, C., Thomas, W.A., Ressing, M.E., Wiertz, E.J., and Rowe, M. (2009). The Epstein-Barr virus G-protein-coupled receptor contributes to immune evasion by targeting MHC class I molecules for degradation. PLoS Pathog. 5, e1000255.