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Gene Review

LMP-2B  -  LMP-2B

Human herpesvirus 4

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Disease relevance of LMP-2B

  • Since these mRNAs are readily detected in largely latently infected cells and do not increase in abundance with EBV replication, these putative latent-infection membrane proteins are tentatively designated LMP-2A and LMP-2B, respectively [1].
  • Coupled transcription of Epstein-Barr virus latent membrane protein (LMP)-1 and LMP-2B genes in nasopharyngeal carcinomas [2].
  • As a strategy for stimulating immunity against EBV for the treatment of EBV-associated tumors, we have genetically engineered dendritic cells (DC) to express EBV antigens, such as latent membrane protein 2B (LMP2B), using recombinant adenovirus vectors [3].
  • 1. We found that in vitro-reactivated CTL preparations from several A2.1-positive virus-immune donors contained detectable reactivity against A2.1-bearing target cells expressing either LMP2A or the smaller LMP2B protein from recombinant vaccinia virus vectors [4].

High impact information on LMP-2B


Chemical compound and disease context of LMP-2B


Biological context of LMP-2B

  • Two species of the Epstein-Barr virus-encoded latent membrane protein 2, LMP2A and LMP2B, are generated by alternative splicing, each species having a distinct first exon [9].
  • A panel of fusion proteins was constructed in which the fluorescent enhanced green fluorescent protein and DsRed protein domains were fused to the N- and C-termini of LMP2A and LMP2B [10].

Anatomical context of LMP-2B

  • The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessential [11].
  • Lymphoblastoid cell lines generated by virus-induced transformation of normal B cells in vitro, express the full spectrum of six EBNAs and three latent membrane proteins (LMP1, LMP2A, and LMP2B); furthermore, these lines often contain a small fraction of cells spontaneously entering the lytic cycle [12].
  • No evidence of co-localization of LMP2B with endosomes or surface expression was obtained [10].

Co-localisations of LMP-2B


Regulatory relationships of LMP-2B

  • These results indicate that EBNA-3C directly activates the expression of LMP-1 and LMP-2B but is unlikely to significantly regulate EBNA expression via Cp under normal growth conditions [7].
  • Interestingly, when LMP2B was expressed in conjunction with LMP2A, there was a restoration of normal BCR signal transduction upon BCR cross-linking [6].

Other interactions of LMP-2B

  • YT cells express the EBV-associated nuclear antigen (EBNA)-1, the latent membrane protein (LMP)-1, and LMP-2A, but not EBNA-2 and LMP-2B genes [13].


  1. Two related Epstein-Barr virus membrane proteins are encoded by separate genes. Sample, J., Liebowitz, D., Kieff, E. J. Virol. (1989) [Pubmed]
  2. Coupled transcription of Epstein-Barr virus latent membrane protein (LMP)-1 and LMP-2B genes in nasopharyngeal carcinomas. Chen, F., Hu, L.F., Ernberg, I., Klein, G., Winberg, G. J. Gen. Virol. (1995) [Pubmed]
  3. Dendritic cells transduced with an adenovirus vector encoding Epstein-Barr virus latent membrane protein 2B: a new modality for vaccination. Ranieri, E., Herr, W., Gambotto, A., Olson, W., Rowe, D., Robbins, P.D., Kierstead, L.S., Watkins, S.C., Gesualdo, L., Storkus, W.J. J. Virol. (1999) [Pubmed]
  4. HLA A2.1-restricted cytotoxic T cells recognizing a range of Epstein-Barr virus isolates through a defined epitope in latent membrane protein LMP2. Lee, S.P., Thomas, W.A., Murray, R.J., Khanim, F., Kaur, S., Young, L.S., Rowe, M., Kurilla, M., Rickinson, A.B. J. Virol. (1993) [Pubmed]
  5. An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking. Miller, C.L., Lee, J.H., Kieff, E., Longnecker, R. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  6. Epstein-barr virus latent membrane protein 2B (LMP2B) modulates LMP2A activity. Rovedo, M., Longnecker, R. J. Virol. (2007) [Pubmed]
  7. Epstein-Barr Virus EBNA-3C Is Targeted to and Regulates Expression from the Bidirectional LMP-1/2B Promoter. Jim??nez-Ram??rez, C., Brooks, A.J., Forshell, L.P., Yakimchuk, K., Zhao, B., Fulgham, T.Z., Sample, C.E. J. Virol. (2006) [Pubmed]
  8. Zebularine reactivates silenced E-cadherin but unlike 5-Azacytidine does not induce switching from latent to lytic Epstein-Barr virus infection in Burkitt's lymphoma Akata cells. Rao, S.P., Rechsteiner, M.P., Berger, C., Sigrist, J.A., Nadal, D., Bernasconi, M. Mol. Cancer (2007) [Pubmed]
  9. Consistent transcription of the Epstein-Barr virus LMP2 gene in nasopharyngeal carcinoma. Busson, P., McCoy, R., Sadler, R., Gilligan, K., Tursz, T., Raab-Traub, N. J. Virol. (1992) [Pubmed]
  10. Epstein-Barr virus latent membrane protein 2B (LMP2B) co-localizes with LMP2A in perinuclear regions in transiently transfected cells. Lynch, D.T., Zimmerman, J.S., Rowe, D.T. J. Gen. Virol. (2002) [Pubmed]
  11. The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessential. Longnecker, R., Miller, C.L., Miao, X.Q., Marchini, A., Kieff, E. J. Virol. (1992) [Pubmed]
  12. Three pathways of Epstein-Barr virus gene activation from EBNA1-positive latency in B lymphocytes. Rowe, M., Lear, A.L., Croom-Carter, D., Davies, A.H., Rickinson, A.B. J. Virol. (1992) [Pubmed]
  13. EBV-NK cells interactions and lymphoproliferative disorders. Kanegane, H., Yachie, A., Miyawaki, T., Tosato, G. Leuk. Lymphoma (1998) [Pubmed]
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