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Herpes simplex virus types 1 and 2 (HSV-1 and HSV-2, respectively) specify five major glycoproteins designated as gA, gB, gC, gD, and gE. Previous studies have shown that gA and gB differ in electrophoretic mobility but not in reactivity with antisera prepared to each of these glycoproteins. Moreover, gA and gB of HSV-1 crossreact in serologic tests with the corresponding glycoproteins of HSV-2. In this paper, we report on the reactivities of gA and gB of HSV-1 and HSV-2 with 24 independently derived monoclonal antibodies reactive with these antigens. Our results show the following: (i) Electrophoretic mobilities of HSV-1 and HSV-2 glycoproteins gA and gB made in HEp-2 cells are significantly less than those made in Vero cells. (ii) All monoclonal antibodies precipitated both gA and gB made in infected HEp-2 cells. These include 12 monoclonal antibodies that neutralized virus and 12 that did not. (iii) HSV-2 glycoproteins gA and gB made in HEp-2 cells contain type-specific domains. However, monoclonal antibodies produced by one clone directed to these domains did not react with glycoproteins made in Vero cells. (iv) Lysates of infected Vero cells contain three lower molecular weight polypeptides that also reacted with monoclonal antibodies directed to glycoproteins gA and gB. These polypeptides are virus specific inasmuch as those specified by HSV-1 differ in electrophoretic mobilities from those specified by HSV-2. these polypeptides are absent in lysates of HEp-2 cells.

Differential immunologic reactivity and processing of glycoproteins gA and gB of herpes simplex virus types 1 and 2 made in Vero and HEp-2 cells.