Glycoprotein gE of herpes simplex virus type 1: effects of anti-gE on virion infectivity and on virus-induced fc-binding receptors

Abstract

An Fc-binding glycoprotein, designated gE, was detected previously in cells infected with herpes simplex virus type 1 (HSV-1) and in virion preparations isolated from infected cells. gE from HSV-1 strain HFEM(syn) was purified by affinity chromatography and preparative electrophoresis and then a rabbit was immunized to produce an antiserum to glycoprotein gE. This antiserum selectively precipitated gE and its precursors from detergent-solubilized extracts of HSV-1 strain HFEM(syn)-infected human laryngeal carcinoma HEp-2 cells, from extracts of other cell lines infected with the same virus and from extracts of HEp-2 cells infected with several other HSV-1 strains. The antiserum did not precipitate any proteins from uninfected cells. The several forms of gE detected by immunoprecipitation accumulated in variable quantities in different cells infected with the different virus strains and also varied slightly with respect to electrophoretic mobility, suggesting some differences in the gE from different HSV-1 strains and some effects of the host cell on the nature and extent of posttranslational processing. One of the electrophoretic forms of gE previously detected in purified preparations of virions could be precipitated by anti-gE from extracts of purified HSV-1 strain HFEM(syn) virions. Anti-gE neutralized HSV-1 infectivity but only in the presence of complement. F(ab'')2 fragments of the anti-gE Ig partially inhibited the binding of 125I-labeled IgG to the Fc receptors on HSV-1-infected cells. [African green monkey kidney Vero, hamster kidney BHK-21 and human embryo lung HEL cells were also used in this study.].