Characterization of the gene and an antigenic determinant of equine herpesvirus type-1 glycoprotein 14 with homology to gB-equivalent glycoproteins of other herpesviruses.

The gene encoding glycoprotein 14 (gp14) of equine herpesvirus type 1 was sequenced. Nucleotide sequence analysis revealed a complete transcription unit composed of a CAT box, a TATA box, a ribosome-binding sequence, a polyadenylation signal and an open reading frame (ORF) of 2940 bp transcribed from left to right. The amino acid (aa) sequence deduced from this ORF corresponded to that of a protein with 979 aa and had the characteristic features of membrane gp including a 20-aa signal sequence at the N terminus, a 743-aa surface domain, a 40-aa membrane anchoring region, a 108-aa hydrophilic cytoplasmic domain at the C terminus and eleven potential sites for N-linked glycosylation. An unusual feature of this protein was an exceptionally long (66aa) sequence, with a preponderance of hydrophilic residues, preceding the hydrophobic signal core. An antigenic determinant recognized by an anti-gp14 monoclonal antibody was present in the N terminus of the postulated surface domain. Comparison of gp 14 with the gp of other herpesviruses indicated that gp14 was highly homologous to corresponding gp of pseudorabies (gII), bovine herpesvirus (gI), varicella-zoster virus (gII), as well as of herpes simplex virus, Epstein-Barr virus and human cytomegalovirus (gB).