Expression of Herpes simplex virus type 1 glycoprotein C antigens in Escherichia coli.

DNA fragments encoding structural information of the Herpes simplex virus type 1 (HSV-1) glycoprotein C (gC) gene were cloned into pUC plasmids [Vieira and Messing, Gene 19 (1982) 259-268]. None of the hybrid plasmids were able to direct the synthesis of significant amounts of gC related peptides. Several of the plasmid-bearing strains, however, exhibited inhibition characteristics which can be correlated with the presence on the plasmid of specific gC gene sequences. After insertion of gC DNA fragments into expression vector pMF2 between phage lambda repressor gene cI and lacZ, significant amounts of cI::gC::beta-galactosidase fusion proteins are synthesized. These tripartite fusion proteins are immunologically reactive with anti-HSV-1 antisera. The expression system based on pMF2 can be generally used to identify and express foreign antigens in Escherichia coli.