Characterization of the 92,000-dalton glycoprotein induced by herpes simplex virus type 2

Abstract

Evidence is presented showing that the 92,000-dalton glycoprotein (g92K) induced by herpes simplex virus (HSV) type 2 has properties distinct from those assigned to any other HSV glycoprotein. First, the carbohydrate composition and extent of sulfation differ from those of glycoproteins D and E. Second, two clonally unrelated monoclonal antibodies, AP1 and LP5, shown in this paper to specifically immunoprecipitate g92K, do not react with any of the known processed forms of glycoproteins B, C, D, and E. Third, by using HSV type 1/HSV type 2 intertypic recombinants and a simple radioimmunoassay, the target antigen of the two monoclonal antibodies was shown to map in the same region as g92K (0.846 to 0.924). Fourth, the intertypic recombinant R12-3 was shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of infected cells to induce the HSV type 2 g92K and HSV type 1 gD and gE, whereas R12-1, which did not induce g92K, induced HSV-2 gE and an altered gD, providing genetic evidence that g92K is encoded, at least in part, by a different region of the genome from that encoding gD and gE.

Oligomeric structure of glycoproteins in herpes simplex virus type 1

“…The conclusion was that gB, gC, and gD are present in virions in three distinct structures. These investigators and others have pointed out that their findings were consistent with the lack of evidence for stable associations between or among these protein species (16,20,24). Subsequent examination of the structure of the envelope with chemical cross-linkers did identify gB multimers and dimers of gC (38).…”

Identification of an immunodominant sequential epitope in glycoprotein G of herpes simplex virus type 2 that is useful for serotype-specific diagnosis

“…We speculate that the type 2 linear sequence may be conformationally constrained by other parts of gG2 to form a type 2-specific structure. Additionally, the heavy N-and O-glycosylation of gG2 [Marsden et al, 1984;Balachandran and Hutt-Fletcher, 1985;Olofsson et al, 1986] may mask epitopes within its unique region. These speculations remain to be investigated.…”

“…Progress toward a type-specific serodiagnostic test has been facilitated by the identification of an HSV-2 glycoprotein, designated gG2 [Marsden et al, 1978[Marsden et al, , 1984Roizman et al, 1984] and its HSV-1 counterpart, gG1 [McGeoch et al, 1985;Ackerman et al, 1986;Frame et al, 1986]. Determination and comparison of the DNA sequence of the genes encoding gG1 and gG2 showed the two proteins to have diverged considerably [McGeoch et al, 1985[McGeoch et al, , 1987.…”

Inhibitors of protein glycosylation and glycoprotein processing in viral systems

“…Several mechanisms have been proposed for the viral egress through the cytoplasm and cell surface (Roizman and Furlong, 1974;Spear, 1985). An active role *Morphological and biochemical aspects on HSV infection of permissive cells are reviewed by Roizman andFurlong, 1974, andRoizman, 1978. Spear, 1976;Morse et al, 1978;Reuchan et al, 1979;Frink et al, 1983;Para et al, 1983;Marsden et al, 1984;Roizman et al, 1984;Buckmaster et al, 1984;Spear, 1985;McGeoch et al, 1985;Swain et al, 1985;Ackermann et al, 1986;Richman et al, 1986. of the Golgi apparatus seems required, as this egress is arrested by monensin, an ionophore disturbing the Golgi-mediated intracellular traffic (Johnson and Spear, 1982).…”