Effect of monoclonal antibodies on limited proteolysis of native glycoprotein gD of herpes simplex virus type 1

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Abstract
The properties of 17 rabbit monoclonal antibodies to glycoprotein gD of herpes simplex type 1 (HSV-1) (gD-1) and HSV-2 (gD-2) were examined. The antibodies recognized 8 separate determinants of gD based on differences in radioimmuno-precipitation and neutralization assays. The determinants were distributed as follows: 3 were gD-1 specific, 1 was gD-2 specific and 4 were type common. Several type-specific and type-common determinants appeared to be involved in neutralization. A procedure was developed for examining the effect that binding of monoclonal antibody has on proteolysis of native gD-1 by Staphylococcus aureus V8 protease. Several different patterns of protease V8 cleavage were obtained depending on the monoclonal antibody used. The proteolysis patterns were generally consistent with the immunological groupings. With 4 groups of antibodies, fragments of gD-1 remained bound to antibody after V8 treatment. A 38,000-dalton fragment remained bound to antibodies in 3 different groups of monoclonal antibodies. This fragment appeared to contain 1 type-common and 2 type-specific determinants. A 12,000-dalton fragment remained bound to antibodies belonging to 1 type-common group of monoclonal antibodies. Tryptic peptide analysis revealed that the 12,000-dalton fragment represented a portion of the 38,000-dalton fragment and was enriched in a type-common arginine tryptic peptide.