The Epstein-Barr virus (EBV) BXLF1 fragment open reading frame (LORF), thought to encode deoxythymidine kinase (dTK) activity, and a shorter frame (SORF), starting at an internal in-frame AUG, were isolated by polymerase chain reaction from a plasmid containing the Eco R1 fragment of EBV strain FF-41. These were transfected into dTK–Escherichia coli, producing multiple SORF- or LORF-containing colonies, which expressed dTK. The 243 NH2 terminal residues of the LORF-encoded polypeptide thus are not essential for dTK activity. SORF, with 1,092 bp, is predicted to encode a 36- to 37-kD polypeptide, in the size range of other herpesviral dTKs.

Keywords:
Thymidine kinase, Epstein-Barr virus
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© 1996 S. Karger AG, Basel
1996
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