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Epstein-Barr virus lytic cycle activation alters proteasome subunit expression in Burkitt's lymphoma cells
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Alessandra De Leo
Published/Copyright:
June 11, 2010
Abstract
We have shown that Epstein-Barr virus (EBV) lytic cycle activation in Burkitt's lymphoma (BL) cells down-regulates chymotrypsin- and caspase-like activities of the proteasome. The aim of the present study was to evaluate whether EBV activation might also affect proteasome subunit composition. Our results indicate that, independently of the latency program established in the host cells, induction of the EBV lytic cycle reduces the expression of the proteasomal components β5, β1 and β2i, whereas it increases that of β2, β1i, PA28α and PA28β. The modulation of the composition and enzymatic activities of the proteolytic complex are indicative of a less efficient generation of viral immunoepitopes.
Keywords: Burkitt's lymphoma cells; Epstein-Barr virus activation; immunoproteasome; MHC-class I epitopes
Received: 2010-2-4
Accepted: 2010-5-17
Published Online: 2010-06-11
Published in Print: 2010-09-01
©2010 by Walter de Gruyter Berlin New York
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Keywords for this article
Burkitt's lymphoma cells;
Epstein-Barr virus activation;
immunoproteasome;
MHC-class I epitopes
Articles in the same Issue
- Review
- Molecular mechanisms of signal transduction via adiponectin and adiponectin receptors
- Genes and Nucleic Acids
- Isolation of genes involved in pancreas regeneration by subtractive hybridization
- Wild type p53-dependent transcriptional upregulation of cathepsin L expression is mediated by C/EBPα in human glioblastoma cells
- Protein Structure and Function
- Epstein-Barr virus lytic cycle activation alters proteasome subunit expression in Burkitt's lymphoma cells
- Dentipain, a Streptococcus pyogenes IdeS protease homolog, is a novel virulence factor of Treponema denticola
- Membranes, Lipids, Glycobiology
- Resveratrol treatment induces redox stress in red blood cells: a possible role of caspase 3 in metabolism and anion transport
- Cell Biology and Signaling
- Activation of the plasma kallikrein-kinin system on human lung epithelial cells
- Antiproliferative effects induced by guanine-based purines require hypoxanthine-guanine phosphoribosyltransferase activity
- Phosphorylation of caldesmon by myosin light chain kinase increases its binding affinity for phosphorylated myosin filaments
- Proteolysis
- Effects of magnesium ions on recombinant human furin: selective activation of hydrolytic activity upon substrates derived from virus envelope glycoprotein
