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. 1992 Aug;66(8):5161–5167. doi: 10.1128/jvi.66.8.5161-5167.1992

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

A L Burkhardt 1, J B Bolen 1, E Kieff 1, R Longnecker 1
PMCID: PMC241398  PMID: 1321296

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.

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Selected References

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