Document Actions
The late lytic LMP-1 protein of Epstein- ... tively regulate LMP-1 signaling
The late lytic LMP-1 protein of Epstein-Barr virus can negatively regulate LMP-1 signaling.
26
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-kappaB activity, it inhibits NF-kappaB 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-kappaB 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.
Erickson KD, Martin JM
Journal of virology
2000-01-01 00:00
74
2
1057-60
Animals,Butyrates,Cell Line, Transformed,Herpesvirus 4, Human,Humans,NF-kappa B,Signal Transduction,Tetradecanoylphorbol Acetate,Viral Matrix Proteins,Butyrates,EBV-associated membrane antigen, Epstein-Barr virus,NF-kappa B,Viral Matrix Proteins,Tetradecanoylphorbol Acetate
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309, USA
J. Virol.
NIAID AI-01537-02, NCI CA-64610-06
0022-538X
829
True
10623774
