EXPRESSION OF HERPES-SIMPLEX VIRUS TYPE-1 GLYCOPROTEIN-L (GL) IN TRANSFECTED MAMMALIAN-CELLS - EVIDENCE THAT GL IS NOT INDEPENDENTLY ANCHORED TO CELL-MEMBRANES

We expressed herpes simplex virus type 1 glycoprotein L (gL) in transf ected cells to investigate whether it is independently anchored to pla sma membranes or is membrane associated as a result of complex formati on with gH. gL was detected by immunofluorescence microscopy at the su rfaces of cotransfected cells when it was expressed with gH but not wh en it was expressed in the absence of gH or with a truncated form of g H, gH(Trunc)(792), which lacks the membrane-spanning region and termin ates at amino acid 792. Immunoprecipitation studies of transfected-cel l culture media revealed that gL was secreted from cells when expresse d in the absence of gH and was secreted from cotransfected cells compl exed with gH(Trunc)(792). These observations demonstrate that gL is no t independently anchored to plasma membranes but is membrane associate d as a result of complex formation with gH.