Defective glycoprotein C of the syncytial strain of herpes simplex virus type 1

Abstract

Glycoproteins of the herpes simplex virus type 1 (HSV-1) non-syncytial strain Kupka showed two times higher affinity for the Helix pomatia (HP) lectin than glycoproteins of the syncytial strain HSZP. As revealed by the results of immunoprecipitation test and by the comparison of the synthesis of virus glycoproteins, glycoprotein C (gC) was synthesized in sufficient amounts in the HSZP strain-infected cells. The difference in the binding to HP lectin was found to be caused by decreased affinity of gC of the strain HSZP for HP lectin. The decreased affinity for HP lectin was brought about by lower proportion of O-linked oligosaccharides in the gC molecule. The glycoproteins of either HSV-1 strain under study synthesized in BHK cells displayed higher affinity for HP lectin than those synthesized in VERO cells.