Generation and properties of the glycoprotein E-related 32K/34K/35K and 55K/57K polypeptides encoded by herpes simplex virus type 1.
A hybridoma line was isolated which produced antibody reacting with polypeptides of apparent molecular weights 32,000, 34,000 and 35,000 (32K/34K/35K) and 55,000 and 57,000 (55K/57K). These were sulphated glycoproteins that have previously been found in the medium of herpes simplex virus type 1 (HSV-1)-infected cells. By tryptic peptide mapping and serological cross-reactions the polypeptides were shown to be related to HSV-1 glycoprotein E (gE-1) but they lacked the Fc binding function. The 32K/34K/35K and 55K/57K polypeptides were not found in the medium of HSV-1-infected cells incubated in serum-free medium. They could be generated in vitro from purified gE-1 in the presence of serum. It is likely that 32K/34K/35K and 55K/57K are derived from gE-1 by the action of serum proteases.
D000818:Animals; D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D002460:Cell Line; D003429:Cross Reactions; D006825:Hybridomas / Q000276:immunology; D007141:Immunoglobulin Fc Fragments; D008970:Molecular Weight; D010449:Peptide Mapping; D018139:Simplexvirus / Q000235:genetics*; D014357:Trypsin; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000302:isolation & purification
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D007141:Immunoglobulin Fc Fragments; D014759:Viral Envelope Proteins; C044768:glycoprotein E, herpes simplex virus type 1; D014357:Trypsin