An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase

J Virol. 1991 Jul;65(7):3681-92. doi: 10.1128/JVI.65.7.3681-3692.1991.


Epstein-Barr virus (EBV) encodes two integral membrane proteins in latently infected growth-transformed cells. One of these, LMP1, can transform rodent fibroblasts and induce markers of B-lymphocyte activation. The second, LMP2, colocalizes with LMP1 in a constitutive patch in the EBV-transformed B-lymphocyte plasma membrane. The experiments reported here demonstrate that LMP2 may biochemically interact with LMP1 and that LMP2 closely associates with and is an important substrate for a B-lymphocyte tyrosine kinase in EBV-transformed B lymphocytes or in B-lymphoma cells in which LMP2 is expressed by gene transfer. LMP2 is also serine and threonine phosphorylated. LMP2 localizes to a peripheral membrane (presumably plasma membrane) patch in transfected B-lymphoma cells and colocalizes with much of the cellular tyrosine-phosphorylated proteins. LMP2 undergoes tyrosine phosphorylation in anti-LMP2 or antiphosphotyrosine immunoprecipitates from transfected B-lymphoma cells or EBV-transformed B lymphocytes. The first 167 of the 497 amino acids of LMP2 retain full ability to associate with and act as a substrate for a tyrosine kinase. A 70-kDa phosphotyrosine cell protein associates with LMP2 in transfected cells or in EBV-transformed B lymphocytes and could be a mediator of the effects of LMP2.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / immunology
  • Antigens, Viral / metabolism*
  • Cell Line
  • Cell Transformation, Viral*
  • Cloning, Molecular
  • DNA Mutational Analysis
  • Fluorescent Antibody Technique
  • Herpesvirus 4, Human / metabolism*
  • Humans
  • In Vitro Techniques
  • Membrane Proteins / immunology
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Phosphorylation
  • Phosphotyrosine
  • Protein-Tyrosine Kinases / metabolism*
  • Structure-Activity Relationship
  • Transfection
  • Tyrosine / analogs & derivatives
  • Tyrosine / metabolism
  • Viral Matrix Proteins*
  • Viral Proteins / immunology
  • Viral Proteins / metabolism*


  • Antigens, Viral
  • EBV-associated membrane antigen, Epstein-Barr virus
  • Membrane Proteins
  • Phosphoproteins
  • Viral Matrix Proteins
  • Viral Proteins
  • Phosphotyrosine
  • Tyrosine
  • Protein-Tyrosine Kinases