Membrane proteins specified by herpes simplex viruses. V. Identification of an Fc-binding glycoprotein

Abstract

A glycoprotein with affinity for the Fc region of immunoglobulin [Ig] was isolated from extracts of cultured cells [human epidermoid carcinoma HEp-2 and baby hamster kidney BHK-21] infected with herpes simplex virus type 1. Experiments were done to characterize its properties and to investigate whether it could account for the Fc-binding activity previously demonstrated on the surfaces of intact herpes simplex virus-infected cells. Affinity chromatography was used to identify and isolate the Fc-binding glycoprotein and to demonstrate the specificity of its interaction with IgG-Fc. Three electrophoretically distinguishable Fc-binding polypeptides were identified by affinity chromatography, and appear to be different forms of the same translation product, based on comparisons of proteolytic digestion products and on the kinetics of appearance of each form after a brief pulse with radioactive amino acids. Apparently 1 polypeptide, designated pE, is processed to yield gE1, which is in turn processed to yield gE2. gE1 and gE2 are glycosylated membrane proteins and both can be labeled by the lactoperoxidase-catalyzed radioiodination of intact infected cells, indicating the presence of these proteins in surface membranes of the cells. Increases in the amounts of gE1 and gE2 at the cell surface paralleled the increase in Fc-binding activity of intact infected cells.