EXPRESSION OF THE EPSTEIN-BARR-VIRUS TERMINAL REPEAT PROTEIN-1 IN ESCHERICHIA-COLI

A pMAL(c)-based plasmid clone with a synthetic tac promoter was constr ucted to efficiently express the full-length terminal repeat protein 1 (TP1) of Epstein-Barr virus in Escherichia coli. The N-terminal part of the recombinant protein is represented by a maltose-binding protein , permitting thereby its isolation from bacterial lysates by affinity chromatography. Subsequent treatment with proteolytic factor Xa yields the target protein in discrete form. A tryptophan-regulated vector pA TH-11 was used to construct several plasmid clones capable of expressi ng various N- and C-proximal fragments of TP1. This collection can be used to obtain corresponding antisera and for preliminary immunologica l mapping of the TP1 molecule.