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      • Record: found
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      Epstein–Barr virus latent genes

      review-article
      Author(s): 1 , 2 , * , 3
      Publication date (Electronic):
      Journal: Experimental & Molecular Medicine
      Publisher: Nature Publishing Group

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          Abstract

          Latent Epstein–Barr virus (EBV) infection has a substantial role in causing many human disorders. The persistence of these viral genomes in all malignant cells, yet with the expression of limited latent genes, is consistent with the notion that EBV latent genes are important for malignant cell growth. While the EBV-encoded nuclear antigen-1 (EBNA-1) and latent membrane protein-2A (LMP-2A) are critical, the EBNA-leader proteins, EBNA-2, EBNA-3A, EBNA-3C and LMP-1, are individually essential for in vitro transformation of primary B cells to lymphoblastoid cell lines. EBV-encoded RNAs and EBNA-3Bs are dispensable. In this review, the roles of EBV latent genes are summarized.

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          Most cited references308

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          mda-5: An interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties.

          Eckhard Jankowsky, Qingping Wu, Rahul V Gopalkrishnan … (2002)
          Human melanoma cells can be reprogrammed to terminally differentiate and irreversibly lose proliferative capacity by appropriate pharmacological manipulation. Subtraction hybridization identified melanoma differentiation-associated gene-5 (mda-5) as a gene induced during differentiation, cancer reversion, and programmed cell death (apoptosis). This gene contains both a caspase recruitment domain and putative DExH group RNA helicase domains. Atypical helicase motifs of MDA-5 deviate from consensus sequences but are well conserved in a potentially new group of cloned and hypothetical proteins. mda-5 is an early response gene inducible by IFN and tumor necrosis factor-alpha, responding predominantly to IFN-beta. Protein kinase C activation by mezerein further augments mda-5 expression induced by IFN-beta. Expression of mda-5 is controlled transcriptionally by IFN-beta, and the MDA-5 protein localizes in the cytoplasm. mda-5 displays RNA-dependent ATPase activity, and ectopic expression of mda-5 in human melanoma cells inhibits colony formation. In these contexts, mda-5 may function as a mediator of IFN-induced growth inhibition and/or apoptosis. MDA-5 is a double-stranded RNA-dependent ATPase that contains both a caspase recruitment domain and RNA helicase motifs, with a confirmed association with growth and differentiation in human melanoma cells.
          Article 0 comments Cited 174 times – based on 0 reviews     Review now
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            Terminal differentiation into plasma cells initiates the replicative cycle of Epstein-Barr virus in vivo.

            Lauri Laichalk, David A. Thorley-Lawson (2005)
            In this paper we demonstrate that the cells which initiate replication of Epstein-Barr virus (EBV) in the tonsils of healthy carriers are plasma cells (CD38hi, CD10-, CD19+, CD20lo, surface immunoglobulin negative, and cytoplasmic immunoglobulin positive). We further conclude that differentiation into plasma cells, and not the signals that induce differentiation, initiates viral replication. This was confirmed by in vitro studies showing that the promoter for BZLF1, the gene that begins viral replication, becomes active only after memory cells differentiate into plasma cells and is also active in plasma cell lines. This differs from the reactivation of BZLF1 in vitro, which occurs acutely and is associated with apoptosis and not with differentiation. We suggest that differentiation and acute stress represent two distinct pathways of EBV reactivation in vivo. The fraction of cells replicating the virus decreases as the cells progress through the lytic cycle such that only a tiny fraction actually release infectious virus. This may reflect abortive replication or elimination of cells by the cellular immune response. Consistent with the later conclusion, the cells did not down regulate major histocompatibility complex class I molecules, suggesting that this is not an immune evasion tactic used by EBV and that the cells remain vulnerable to cytotoxic-T-lymphocyte attack.
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              Inhibition of antigen processing by the internal repeat region of the Epstein-Barr virus nuclear antigen-1.

              Sebastian G Klein, V Levitsky, S Imreh … (1995)
              The Epstein-Barr virus (EBV)-encoded nuclear antigen (EBNA1) is expressed in latently EBV-infected B lymphocytes that persist for life in healthy virus carriers, and is the only viral protein regularly detected in all malignancies associated with EBV. Major histocompatibility complex (MHC) class I-restricted, EBNA1-specific cytotoxic T lymphocyte (CTL) responses have not been demonstrated. Using recombinant vaccinia viruses encoding chimaeric proteins containing an immunodominant human leukocyte antigen A11-restricted CTL epitope, amino acids 416-424 of the EBNA4 protein, inserted within the intact EBNA1, or within an EBNA1 deletion mutant devoid of the internal Gly-Ala repetitive sequence, we demonstrate that the Gly-Ala repeats generate a cis-acting inhibitory signal that interferes with antigen processing and MHC class I-restricted presentation. Insertion of the Gly-Ala repeats downstream of the 416-424 epitope inhibited CTL recognition of a chimaeric EBNA4 protein. The results highlight a previously unknown mechanism of viral escape from CTL surveillance, and support the view that the resistance of cells expressing EBNA1 to rejection mediated by CTL is a critical requirement for EBV persistence and pathogenesis.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Exp Mol Med
                Journal ID (iso-abbrev): Exp. Mol. Med
                Title: Experimental & Molecular Medicine
                Publisher: Nature Publishing Group
                ISSN (Print): 1226-3613
                ISSN (Electronic): 2092-6413
                Publication date (Print): January 2015
                Publication date (Electronic): 23 January 2015
                Publication date PMC-release: 1 January 2015
                Volume: 47
                Issue: 1
                Page: e131
                Affiliations
                [1 ]Samsung Advanced Institute for Health Sciences and Technology (SAIHST), Samsung Medical Center, Sungkyunkwan University , Seoul, Korea
                [2 ]Samsung Biomedical Research Institute (SBRI), Samsung Medical Center, Sungkyunkwan University , Seoul, Korea
                [3 ]Department of Medicine, Brigham and Women's Hospital, Program in Virology, Department of Microbiology and Immunobiology, Harvard Medical School , Boston, MA, USA
                Author notes
                [* ]Samsung Advanced Institute for Health Sciences and Technology (SAIHST), Samsung Medical Center, Sungkyunkwan University , 50 Irwon-dong, Gangnam-gu, Seoul 135-710, Korea. E-mail: mkang@ 123456skku.edu
                Author information
                http://orcid.org/0000-0001-9940-9305
                Article
                Publisher Item ID: emm201484
                DOI: 10.1038/emm.2014.84
                PMC ID: 4314583
                PubMed ID: 25613728
                SO-VID: a3be8698-1eed-4e5f-b30d-19fd9179c0b4
                Copyright © Copyright © 2015 KSBMB.
                License:

                This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/

                History
                Date received : 16 September 2014
                Date accepted : 01 October 2014
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular medicine
                Data availability:
                ScienceOpen disciplines: Molecular medicine

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