The glycoproteins of cells infected with herpes simplex virus 1 or 2 (HSV-1 or HSV-2) were solubilized with non-ionic detergent NP-40 and electrophoresed in acrylamide gels. At least 12 bands containing virus glycoproteins were formed. The HSV-1 glycoproteins correspond in electrophoretic mobility to structural proteins in the HSV virions and to the virus proteins in plasma membranes of infected cells. All virus glycoproteins were bound to immunoadsorbent columns made by cross-linking either homologous or heterologous antibody. Immunoadsorbent columns readily discriminated between host and virus glycoproteins. The differentiation between HSV-1 and HSV-2 glycoproteins varied; the degree of specificity of the immunoadsorbent gels was related to the specificity exhibited by the antisera in neutralization tests. All immunoadsorbent antibody gels tested bound homologous glycoproteins in proportions similar to those in the input extract. Immunoadsorbent antibody gels of high specificity bound disproportionate amounts of only a few heterologous glycoproteins. Immunoadsorbent antibody gels of low specificity reacted with heterologous glycoprotein preparations as if they were a homologous preparation.


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