Dissociation of patching by latent membrane protein-1 of Epstein-Barr virus from its stimulation of NF-kappaB activity

J Gen Virol. 1999 Dec:80 ( Pt 12):3227-3232. doi: 10.1099/0022-1317-80-12-3227.

Abstract

Alterations were made in the amino terminus and the first two transmembrane-spanning regions of the latent membrane protein-1 (LMP-1) of Epstein-Barr virus. These mutant proteins were tested for their abilities to patch and to stimulate NF-kappaB activity. A subset of these derivatives retains the wild-type topology of LMP-1 in the plasma membrane, but has lost the ability to patch. Deletion of residues 9-20 of LMP-1, which contain potential SH3-binding motifs, abrogates patching of LMP-1. However, mutation of the prolines within these motifs, which eliminates binding of LMP-1 to SH3 domains in vitro, does not prevent patching by LMP-1. Deletion of the first two transmembrane regions of LMP-1 does prevent it patching. Some of the derivatives of LMP-1 which do not patch do stimulate NF-kappaB activity. Patching by LMP-1 appears to be a higher-order assemblage of protein that is compatible with the stimulation of NF-kappaB activity but is not necessary for this signalling.

MeSH terms

  • Cell Line
  • Cell Membrane / metabolism
  • Fluorescent Antibody Technique
  • Herpesvirus 4, Human / genetics
  • Herpesvirus 4, Human / metabolism*
  • Humans
  • NF-kappa B / genetics
  • NF-kappa B / metabolism*
  • Sequence Deletion
  • Signal Transduction*
  • Transfection
  • Viral Matrix Proteins / chemistry
  • Viral Matrix Proteins / genetics
  • Viral Matrix Proteins / metabolism*
  • src Homology Domains

Substances

  • EBV-associated membrane antigen, Epstein-Barr virus
  • NF-kappa B
  • Viral Matrix Proteins