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Gene Review

EBNA-LP  -  EBNA-LP protein

Human herpesvirus 4

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Disease relevance of EBNA-LP


High impact information on EBNA-LP

  • The Epstein-Barr virus (EBV) EBNA-LP protein is important for EBV-mediated B-cell immortalization and is a potent gene-specific coactivator of the viral transcriptional activator, EBNA2 [1].
  • The mechanism(s) by which EBNA-LP functions as a coactivator remains an important question in the biology of EBV-induced B-cell immortalization [1].
  • Protein kinase A catalytic subunit alpha (PKAcsalpha) is significantly associated with HA95 in the presence or absence of EBNA-LP [6].
  • Marked decreases in the levels of EBV nuclear antigen-1 (EBNA-1), EBNA-2, and EBNA-LP antibodies correlated with the increase in EBV-infected PBL [7].
  • However, previous studies have indicated that EBNA-LP may contribute to immortalization by enhancing EBNA2-mediated transcriptional activation of the LMP-1 gene [8].

Biological context of EBNA-LP


Anatomical context of EBNA-LP

  • Several lymphoblastoid cell lines infected with the EBNA-LP mutant recombinant viruses had a high percentage of cells with bright cytoplasmic immunoglobulin staining, as is characteristic of cells undergoing plasmacytoid differentiation [13].
  • We report here that EBNA-LP self-associates in vivo and the domain responsible for the homotypic association is a multifunctional domain mediating nuclear localization, nuclear matrix association, and EBNA-2-dependent coactivator function of the protein [14].
  • (iii) When Flag epitope-tagged EBNA-LP with either one or two W1W2 repeats and EBNA-LP containing four W1W2 repeats were coexpressed in COS-7 cells, the latter was specifically coimmunoprecipitated with the former [14].
  • EBNA-2 is essential for lymphocyte transformation, and EBNA-LP is at least critical [15].

Associations of EBNA-LP with chemical compounds

  • Identification of evolutionarily conserved serine residues and regions in EBNA-LP homologues provides important clues for identifying the cellular cofactors and molecular mechanisms mediating these conserved viral functions [3].
  • Clustered alanine mutations were introduced into CR1 to CR3, and the conserved serines were also changed to alanine residues in an EBNA-LP with two repeats, which is the minimal protein able to cooperate with EBNA2 [5].
  • (ii) A purified chimeric protein consisting of glutathione S-transferase fused to EBNA-LP specifically formed complexes with EBNA-LP transiently expressed in COS-7 cells [14].
  • Release from nocodazole G2/M block or treatment with phosphatase caused the more slowly migrating species of EBNA-LP to disappear [16].
  • (iii) The EBNA-LP mutant with the arginine to alanine substitutions in NMTS was no longer localized not only to the nuclear matrix but also to the nucleus [17].

Physical interactions of EBNA-LP


Regulatory relationships of EBNA-LP


Other interactions of EBNA-LP

  • We have also found that the behavior of EBNA-3A in a cell fractionation procedure that distinguishes insoluble matrix from soluble cell fractions is modified by EBNA-LP, indicating a further novel level of interplay between the EBNA proteins [19].
  • Consistent with this, the EBV-encoded conserved protein kinase BGLF4 specifically mediated the phosphorylation of EBNA-LP at Ser-35 [20].

Analytical, diagnostic and therapeutic context of EBNA-LP


  1. Mediation of Epstein-Barr virus EBNA-LP transcriptional coactivation by Sp100. Ling, P.D., Peng, R.S., Nakajima, A., Yu, J.H., Tan, J., Moses, S.M., Yang, W.H., Zhao, B., Kieff, E., Bloch, K.D., Bloch, D.B. EMBO J. (2005) [Pubmed]
  2. EBNA-5, an Epstein-Barr virus-encoded nuclear antigen, binds to the retinoblastoma and p53 proteins. Szekely, L., Selivanova, G., Magnusson, K.P., Klein, G., Wiman, K.G. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  3. Sequence and functional analysis of EBNA-LP and EBNA2 proteins from nonhuman primate lymphocryptoviruses. Peng, R., Gordadze, A.V., Fuentes Pananá, E.M., Wang, F., Zong, J., Hayward, G.S., Tan, J., Ling, P.D. J. Virol. (2000) [Pubmed]
  4. A bicistronic Epstein-Barr virus mRNA encodes two nuclear proteins in latently infected, growth-transformed lymphocytes. Wang, F., Petti, L., Braun, D., Seung, S., Kieff, E. J. Virol. (1987) [Pubmed]
  5. Conserved regions in the Epstein-Barr virus leader protein define distinct domains required for nuclear localization and transcriptional cooperation with EBNA2. Peng, R., Tan, J., Ling, P.D. J. Virol. (2000) [Pubmed]
  6. Protein kinase A associates with HA95 and affects transcriptional coactivation by Epstein-Barr virus nuclear proteins. Han, I., Xue, Y., Harada, S., Orstavik, S., Skalhegg, B., Kieff, E. Mol. Cell. Biol. (2002) [Pubmed]
  7. Increased levels of circulating Epstein-Barr virus (EBV)-infected lymphocytes and decreased EBV nuclear antigen antibody responses are associated with the development of posttransplant lymphoproliferative disease in solid-organ transplant recipients. Riddler, S.A., Breinig, M.C., McKnight, J.L. Blood (1994) [Pubmed]
  8. The Epstein-Barr virus EBNA-LP protein preferentially coactivates EBNA2-mediated stimulation of latent membrane proteins expressed from the viral divergent promoter. Peng, R., Moses, S.C., Tan, J., Kremmer, E., Ling, P.D. J. Virol. (2005) [Pubmed]
  9. EBNA-2 and EBNA-LP cooperate to cause G0 to G1 transition during immortalization of resting human B lymphocytes by Epstein-Barr virus. Sinclair, A.J., Palmero, I., Peters, G., Farrell, P.J. EMBO J. (1994) [Pubmed]
  10. Identification of major phosphorylation sites of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP): ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylation. Yokoyama, A., Tanaka, M., Matsuda, G., Kato, K., Kanamori, M., Kawasaki, H., Hirano, H., Kitabayashi, I., Ohki, M., Hirai, K., Kawaguchi, Y. J. Virol. (2001) [Pubmed]
  11. Expression of cyclin D2 in Epstein-Barr virus-positive Burkitt's lymphoma cell lines is related to methylation status of the gene. Sinclair, A.J., Palmero, I., Holder, A., Peters, G., Farrell, P.J. J. Virol. (1995) [Pubmed]
  12. Epstein-Barr virus leader protein enhances EBNA-2-mediated transactivation of latent membrane protein 1 expression: a role for the W1W2 repeat domain. Nitsche, F., Bell, A., Rickinson, A. J. Virol. (1997) [Pubmed]
  13. The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation. Mannick, J.B., Cohen, J.I., Birkenbach, M., Marchini, A., Kieff, E. J. Virol. (1991) [Pubmed]
  14. Conserved region CR2 of Epstein-Barr virus nuclear antigen leader protein is a multifunctional domain that mediates self-association as well as nuclear localization and nuclear matrix association. Tanaka, M., Yokoyama, A., Igarashi, M., Matsuda, G., Kato, K., Kanamori, M., Hirai, K., Kawaguchi, Y., Yamanashi, Y. J. Virol. (2002) [Pubmed]
  15. Epstein-Barr virus nuclear protein LP stimulates EBNA-2 acidic domain-mediated transcriptional activation. Harada, S., Kieff, E. J. Virol. (1997) [Pubmed]
  16. Cell cycle stage-specific phosphorylation of the Epstein-Barr virus immortalization protein EBNA-LP. Kitay, M.K., Rowe, D.T. J. Virol. (1996) [Pubmed]
  17. The conserved domain CR2 of Epstein-Barr virus nuclear antigen leader protein is responsible not only for nuclear matrix association but also for nuclear localization. Yokoyama, A., Kawaguchi, Y., Kitabayashi, I., Ohki, M., Hirai, K. Virology (2001) [Pubmed]
  18. Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) forms complexes with a cellular anti-apoptosis protein Bcl-2 or its EBV counterpart BHRF1 through HS1-associated protein X-1. Matsuda, G., Nakajima, K., Kawaguchi, Y., Yamanashi, Y., Hirai, K. Microbiol. Immunol. (2003) [Pubmed]
  19. Multiple functions within the Epstein-Barr virus EBNA-3A protein. Cludts, I., Farrell, P.J. J. Virol. (1998) [Pubmed]
  20. Identification of protein kinases responsible for phosphorylation of Epstein-Barr virus nuclear antigen leader protein at serine-35, which regulates its coactivator function. Kato, K., Yokoyama, A., Tohya, Y., Akashi, H., Nishiyama, Y., Kawaguchi, Y. J. Gen. Virol. (2003) [Pubmed]
  21. Interaction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: implication of cytoplasmic function of EBNA-LP. Kawaguchi, Y., Nakajima, K., Igarashi, M., Morita, T., Tanaka, M., Suzuki, M., Yokoyama, A., Matsuda, G., Kato, K., Kanamori, M., Hirai, K. J. Virol. (2000) [Pubmed]
  22. Epstein-Barr virus nuclear antigen leader protein induces expression of thymus- and activation-regulated chemokine in B cells. Kanamori, M., Watanabe, S., Honma, R., Kuroda, M., Imai, S., Takada, K., Yamamoto, N., Nishiyama, Y., Kawaguchi, Y. J. Virol. (2004) [Pubmed]
  23. Subnuclear localization and phosphorylation of Epstein-Barr virus latent infection nuclear proteins. Petti, L., Sample, C., Kieff, E. Virology (1990) [Pubmed]
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