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PMID: 1710288 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Journal of virology ·Vol. 65 ·No. 7 ·1991-07-00 ·Pages 3681-92

Longnecker R, Druker B, Roberts TM, Kieff E

Abstract

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.

MeSH Terms
Amino Acid Sequence Antigens, Viral/immunology,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,metabolism Molecular Sequence Data Phosphoproteins/chemistry,metabolism Phosphorylation Phosphotyrosine Protein-Tyrosine Kinases/metabolism Structure-Activity Relationship Transfection Tyrosine/analogs & derivatives,metabolism Viral Matrix Proteins Viral Proteins/immunology,metabolism
Chemicals
Antigens, Viral EBV-associated membrane antigen, Epstein-Barr virus Membrane Proteins Phosphoproteins Viral Matrix Proteins Viral Proteins Phosphotyrosine Tyrosine Protein-Tyrosine Kinases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Longnecker R
Department of Microbiology and Molecular Genetics and Medicine, Harvard Medical School, Boston, Massachusetts.
Druker B
Roberts T M
Kieff E
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1991-07-00
Pages
3681-92
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC241385
Subset
IM
Grants
NCI NIH HHS · CA47006 · United States
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