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Journal of Virology, January 2000, p. 1057-1060, Vol. 74, No. 2
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Late Lytic LMP-1 Protein of Epstein-Barr Virus Can Negatively Regulate LMP-1 Signaling

Kimberly D. Erickson and Jennifer M. Martin*

Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309

Received 16 August 1999/Accepted 8 October 1999

The BNLF-1 open reading frame of Epstein-Barr virus (EBV) encodes two related proteins, latent membrane protein-1 (LMP-1) and lytic LMP-1 (lyLMP-1). LMP-1 is a latent protein required for immortalization of human B cells by EBV, whereas lyLMP-1 is expressed during the lytic cycle and is found in the EBV virion. We show here that, in contrast to LMP-1, lyLMP-1 is stable, with a half-life of >20 h in tetradecanoyl phorbol acetate- and butyrate-treated B95-8 cells. Although lyLMP-1 itself has negligible effects on NF-kappa B activity, it inhibits NF-kappa B activation by LMP-1 in a dose-dependent manner. The lyLMP-1 protein does not oligomerize with LMP-1, and the negative effect of lyLMP-1 on NF-kappa B activation by LMP-1 does not result from lyLMP-1-mediated disruption of LMP-1 oligomers. Modulation of LMP-1-activated signaling pathways is the first identified biological activity associated with lyLMP-1, and this activity may contribute to the progression of EBV's lytic cycle.

* Corresponding author. Mailing address: Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Box 347, Boulder, CO 80309. Phone: (303) 492-6346. Fax: (303) 492-1587. E-mail: jm{at}stripe.colorado.edu.

Journal of Virology, January 2000, p. 1057-1060, Vol. 74, No. 2
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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