Similarities and differences in the Fc-binding glycoprotein (gE) of herpes simplex virus types 1 and 2 and tentative mapping of the viral gene for this glycoprotein

Abstract

Affinity chromatography and immunoprecipitation experiments were performed to determine whether cells infected with herpes simplex virus type 2 (HSV-2) expressed a glycoprotein that was functionally and antigenically related to the HSV-1 Fc-binding glycoprotein designated gE. A protein from extracts of HSV-2-infected [human laryngeal carcinoma] HEp-2 cells bound specifically to an Fc affinity column and the electrophoretic mobility of this protein in sodium dodecyl sulfate-acrylamide gels was slightly less than the mobility of HSV-1 gE. Immunoprecipitation experiments performed with a rabbit antiserum prepared against HSV-1 gE revealed that extracts from HSV-2-infected cells contained a glycoprotein that was antigenically related to HSV-1 gE; the electrophoretic mobility of the HSV-2 gE was indistinguishable from the mobility of the HSV-2 Fc-binding protein; the antiserum reacted with both newly synthesized transient forms and stable fully processed forms of both HSV-1 gE and HSV-2 gE; and the transient and stable forms of HSV-2 gE all had lower electrophoretic mobilities than their HSV-1 counterparts. Electrophoretic analyses of gE precipitated from extracts of HEp-2 cells infected with 2 sets of HSV-1 .times. HSV-2 intertypic recombinant viruses suggested that the gene for gE is located at the right end of the HSV genome (0.85-0.97 map units) in the unique portion of the S component.