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Journal of Virology, January 2007, p. 84-94, Vol. 81, No. 1
0022-538X/07/$08.00+0     doi:10.1128/JVI.01302-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Epstein-Barr Virus Latent Membrane Protein 2B (LMP2B) Modulates LMP2A Activity{triangledown}

Mark Rovedo and Richard Longnecker*

Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611

Received 20 June 2006/ Accepted 28 September 2006

Latent membrane protein 2A (LMP2A) and LMP2B are viral proteins expressed during Epstein-Barr virus (EBV) latency in EBV-infected B cells both in cell culture and in vivo. LMP2A has important roles in modulating B-cell receptor (BCR) signal transduction by associating with the cellular tyrosine kinases Lyn and Syk via specific phosphotyrosine motifs found within the LMP2A N-terminal tail domain. LMP2A has been shown to alter normal BCR signal transduction in B cells by reducing levels of Lyn and by blocking tyrosine phosphorylation and calcium mobilization following BCR cross-linking. Although little is currently known about the function of LMP2B in B cells, the similarity in structure between LMP2A and LMP2B suggests that they may localize to the same cellular compartments. To investigate the function of LMP2B, B-cell lines expressing LMP2A, LMP2B, LMP2A/LMP2B, and the relevant vector controls were analyzed. As was previously shown, cells expressing LMP2A had a dramatic block in normal BCR signal transduction as measured by calcium mobilization and tyrosine phosphorylation. There was no effect on BCR signal transduction in cells expressing LMP2B. Interestingly, when LMP2B was expressed in conjunction with LMP2A, there was a restoration of normal BCR signal transduction upon BCR cross-linking. The expression of LMP2B did not alter the cellular localization of LMP2A but did bind to and prevent the phosphorylation of LMP2A. A restoration of Lyn levels, but not a change in LMP2A levels, was also observed in cells coexpressing LMP2B with LMP2A. From these results, we conclude that LMP2B modulates LMP2A activity.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Ward 6-231, 303 E. Chicago Avenue, Chicago, IL 60611. Phone: (312) 530-0467. Fax: (312) 503-1339. E-mail: r-longnecker{at}northwestern.edu.

{triangledown} Published ahead of print on 11 October 2006.

Journal of Virology, January 2007, p. 84-94, Vol. 81, No. 1
0022-538X/07/$08.00+0     doi:10.1128/JVI.01302-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rechsteiner, M. P., Berger, C., Zauner, L., Sigrist, J. A., Weber, M., Longnecker, R., Bernasconi, M., Nadal, D. (2008). Latent Membrane Protein 2B Regulates Susceptibility to Induction of Lytic Epstein-Barr Virus Infection. J. Virol. 82: 1739-1747 [Abstract] [Full Text]  
  • Rechsteiner, M. P., Berger, C., Weber, M., Sigrist, J. A., Nadal, D., Bernasconi, M. (2007). Silencing of latent membrane protein 2B reduces susceptibility to activation of lytic Epstein-Barr virus in Burkitt's lymphoma Akata cells. J. Gen. Virol. 88: 1454-1459 [Abstract] [Full Text]  


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