Individual herpes simplex virus 1 glycoproteins display characteristic rates of maturation from precursor to mature form both in infected cells and in cells that constitutively express the glycoproteins.
Pulse-chase experiments in conjunction with quantitative immunoprecipitation have been used to study the time-course of conversion from precursor to mature form of herpes simplex virus 1 glycoproteins C, D and B (gC, gD, and gB). The experimental systems employed were two infected cell lines and cells that constitutively express gD or gB. The relative rates of conversion among the glycoproteins did not vary in the systems used; the rate of maturation of gC was about two-fold higher than that of gD which, in turn, was about one and a half-fold higher than that of gB. Treatment with phosphonoacetate which inhibits viral DNA synthesis and hence virion morphogenesis induced a striking increase in the time course of conversion of immature gC, gD, and gB to fully glycosylated forms when measured late in the infection. The model of HSV glycoproteins maturation as integral components of the virion envelope is discussed.
Campadelli-Fiume
G
G
Section of Microbiology and Virology, University of Bologna, Italy.
Lombardo
M T
MT
Foà-Tomasi
L
L
Avitabile
E
E
Serafini-Cessi
F
F
D000818:Animals; D002294:Carcinoma, Squamous Cell / Q000473:pathology; D002460:Cell Line; D006224:Cricetinae; D005347:Fibroblasts / Q000378:metabolism; D006023:Glycoproteins / Q000096:biosynthesis*; D006801:Humans; D007668:Kidney; D007822:Laryngeal Neoplasms / Q000473:pathology; D008647:Mesocricetus; D009024:Morphogenesis; D010746:Phosphonoacetic Acid / Q000494:pharmacology; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D018139:Simplexvirus / Q000378:metabolism*; D014407:Tumor Cells, Cultured / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000096:biosynthesis*
D006023:Glycoproteins; D011498:Protein Precursors; D014759:Viral Envelope Proteins; D010746:Phosphonoacetic Acid