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Nucleic Acids Research, 1989, Vol. 17, No. 19 7609-7622
© 1989

MOLECULAR BIOLOGY

The characterization of the EBV alkaline deoxyribonuclease cloned and expressed in E.coli

Sally A. Baylis, Dorothy J.M. Purifoy1 and Edward Littler

Department of Molecular Biology, Paterson Institute for Cancer Research, Christic Hospital and Holt Radium Institute Wilmslow Road, Manchester M20 9BX 1Department of Molecular Science, Wellcome Research Laboratories Beckenham, Kent BR3 3BS, UK

Received July 19, 1989. Revised September 4, 1989. Accepted September 4, 1989.

Studies of nucleic acid homology suggest the BGLF5 open reading frame of Epstein-Barr virus (EBV) encodes an alkaline deoxyribonuclease (DNase) sharing some homology with that of herpes simplex virus. We report here the expression of the BGLF5 open reading frame in E. coli and the expression of high levels of a novel alkaline DNase activity in induced cells. This alkaline DNase has been purified to apparent homogeneity as a single protein species. This is the first report of the expression of a herpesvirus coded DNase in a prokaryotic system and of the purification of the EBV DNase to demonstrable purity. It has the biochemical characteristics of a typical herpesvirus alkaline exonuclease showing a high pH optimum, an absolute requirement for Mg2+ for activity and sensitivity to high salt concentrations and polyamines. The enzyme activity was neutralized by sera from patients with nasopharyngeal carcinoma and was reactive with these sera in Western blot analysis. Thus the prokaryotic expression system described here provides an economical and efficient source of the EBV DNase for biochemical and seroepidemiological analysis.


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