THE NUCLEOTIDE-SEQUENCE OF THE GLYCOPROTEIN-E GENE OF HERPES-SIMPLEX VIRUS TYPE-2 AND ITS STRUCTURAL CHARACTERISTICS IN COMPARISON WITH THEGE OF HERPES-SIMPLEX VIRUS TYPE-1

The nucleotide sequence of a 1.88-kb DNA cloned from the region of the herpes simplex virus type 2 (HSV-2) genome which maps colinearly with the HSV-1 glycoprotein E (gE1) gene has been determined. Contained wi thin this sequence is a major open reading frame of 548 amino acids fo r the glycoprotein E of HSV-2 (gE2). The gE2 protein has an amino acid sequence homology of 74% with the cognate gE1 protein. In particular, the carboxyterminal region of the gE2 protein shows a high degree of sequence homology to the gE1. Two putative N-linked glycosylation site s, a Fc binding motif, a phosphorylation site, and two clusters of cys teine residues are perfectly conserved in both the gE1 and gE2 protein s, suggesting that they may serve similar important functions in the l ife cycle of the herpesviruses in nature. An amino acid region, which is distinct from that of the gE1 protein in terms of amino acid compos ition, was found between amino acids 180 and 211 in the gE2 protein. T hat region, which appears to reside on the outer surface of the gE2 pr otein, may be an epitope to elicit a HSV-type specific antibody. In ad dition, a hydropathic analysis of the HSV-2 gE sequence demonstrates t hat the gE2 protein contains structures characteristic of membrane-bou nd glycoproteins, including an amino-terminal signal sequence and carb oxy-terminal hydrophobic transmembrane domain.