Expression in bacteria of a polypeptide encoded by a transforming fragment of herpes simplex virus type 2

We have constructed a plasmid (pMD2) containing the 38,000 MW polypeptide (38K polypeptide) gene from the transforming Bg1II-N fragment of HSV-2 fused to the amino-terminal portion of the beta-galactosidase gene in plasmid pUC8. Nucleotide sequence determination around the fusion-junction confirmed that the viral gene sequences starting at its second codon is in the correct reading frame in relation to the translation initiation codon of beta-galactosidase. The lac control sequences direct the synthesis of a 39K protein. This protein was shown to be structurally related to the 38K protein from HSV-2-infected cells by partial proteolytic cleavage analysis. Furthermore, antiserum directed against HSV-2-infected cells, as well as a monoclonal antibody against the 38K viral polypeptide and antibodies raised against a synthetic peptide corresponding to the nine C-terminal amino acid residues of the 38K viral protein, detected the fusion protein in bacteria containing the recombinant plasmid pMD2 but not in Escherichia coli containing a related plasmid or no plasmid.