Localization of epitopes of herpes simplex virus type 1 glycoprotein D

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Abstract
Eight groups of monoclonal antibodies which react with distinct epitopes of herpes simplex virus glycoprotein D (gD) were defined. One of these, group VII antibody, was shown to react with a type-common continuous epitope within residues 11-19 of the mature glycoprotein (residues 36-44 of the predicted sequence of gD). In the current investigation, the sites of binding of .apprx. additional antibody groups which recognize continuous epitopes of gD were localized. The use of truncated forms of gD as well as computer predictions of secondary structure and hydrophilicity were instrumental in locating these epitopes and choosing synthetic peptides to mimic their reactivity. Group II antibodies, which are type common, react with an epitope within residues 268-287 of the mature glycoprotein (residues 293-312 of the predicted sequence). Group V antibodies, which are gD-1 specific, react with an epitope within residues 340 to 356 of the mature protein (residues 365-381 of the predicted sequence). Four additional groups of monoclonal antibodies appear to react with discontinuous epitopes of gD-1, since the reactivity of these antibodies was lost when the glycoprotein was denatured by reduction and alkylation. Truncated forms of gD were used to localize these 4 epitopes to the first 260 amino acids of the mature protein. Competition experiments were used to assess the relative positions of binding of various pairs of monoclonal antibodies. In several cases, when 1 antibody was bound, there was no interference with the binding of an antibody from another group, indicating that the epitopes were distinct. In other cases, there was competition, indicating that these epitopes might share some common amino acids.