Abstract

The envelope glycoprotein B (gB) coded for by the herpes simplex virus type 1 (HSV-1) UL27 gene is similar to the amino acid (aa) sequence of the gB coded by a homologous gene in HSV-2 DNA. The putative antigenic domains in HSV-1 and HSV-2 gB glycoproteins were analyzed on a comparative basis by suitable computer programs, which allowed the prediction of putative antigenic and topogenic domains. The computer-derived domains were compared to experimentally reported antigenic domains in HSV-1 gB glycoprotein. The computer-predicted antigenic domains in the HSV-1 gB glycoprotein matched well with the reported experimentally derived antigenic domains. The aa sequence of antigenic domain 1 was noted to resemble the amino acid sequence in ApoE that is involved in the attachment of this protein to LDL receptors. The clusters of hydrophobic aa domains are conserved in the two viral glycoproteins and are signals for transfer of the viral proteins through the cellular membrane.

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