An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases

A. L. Burkhardt, J. B. Bolen, E. Kieff, R. Longnecker*

*Corresponding author for this work

Research output: Contribution to journalComment/debatepeer-review

113 Scopus citations

Abstract

In latently infected growth-transformed human lymphocytes, Epstein-Barr virus (EBV) encodes two integral plasma membrane proteins: LMP1, which constitutively induces B-lymphocyte activation and intercellular adhesion, and LMP2A, which associates with LMP1 and is a tyrosine kinase substrate. We now demonstrate that LMP2A associates with src family protein tyrosine kinases, particularly lyn kinase, in nonionic detergent extracts of transfected B lymphoma cells or in extracts of EBV-transformed B lymphocytes. The LMP2A and tyrosine kinase association is stable in nonionic detergents and includes a 70-kDa cell protein which is also an in vitro or in vivo kinase substrate. This LMP2A association with B-lymphocyte src family tyrosine kinases is likely to be an important pathway in EBV's effects on cell growth.

Original languageEnglish (US)
Pages (from-to)5161-5167
Number of pages7
JournalJournal of virology
Volume66
Issue number8
DOIs
StatePublished - 1992

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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