A herpesvirus saimiri membrane protein required for interleukin-2 independence forms a stable complex with p56lck

Troy Lund, Maria M. Medveczky, Peter J. Neame, Peter G. Medveczky

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

ORF-2, a 32-kDa viral protein expressed by herpesvirus saimiri-transformed lymphocytes, is essential for transformation and is expressed on the plasma membrane of transformed cells. The current work now shows that most (approximately 80%) of ORF-2 resides in the cytoplasm, while only a small portion protrudes from the cell surface. Expressed as a glutathione S-transferase fusion protein, ORF-2 was found to interact with a 56-kDa cellular protein in untransformed, herpesvirus saimiri-transformed, and Jurkat lymphocytes. Micro-sequencing proved that this protein is the lymphocyte-specific tyrosine protein kinase p56lck. Two regions of ORF-2 were found to be required for p56lck interaction. Current evidence suggests that the interaction of ORF-2 with p56lck plays a key role in the specific transformation of T lymphocytes to an interleukin-2-independent phenotype.

Original languageEnglish (US)
Pages (from-to)600-606
Number of pages7
JournalJournal of virology
Volume70
Issue number1
DOIs
StatePublished - 1996

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