Characterization of the gene encoding herpes simplex virus type 2 glycoprotein C and comparison with the type 1 counterpart

Abstract

The gene encoding the glycoprotein C (gC) of herpes simplex virus type 1 maps to the region of the viral genome from 0.62 to 0.64. Recently, a herpes simplex virus type 2 glycoprotein previously designated gF and now designated gC was mapped to a homologous location. Analysis of the herpes simplex virus type 2 mRNA species encoded in this region revealed a major transcript of 2.5 kilobases, a 0.73-kilobase transcript (the 5' ends of which were mapped by primer extension), and several minor species, all nearly identical to the herpes simplex virus type 1 pattern. A polypeptide of ca. 60,000 daltons was identified by in vitro translation of hybrid-selected mRNA. A smaller protein of ca. 20,000 daltons was also mapped to this region. The nucleotide sequence of a 3.4-kilobase segment of DNA encompassing gC was determined, and an open reading frame of 1,440 nucleotides specifying a 480-amino acid protein with properties consistent with that of a glycoprotein was identified. Comparative DNA sequence analysis showed regions of limited homology within the coding sequences for gC and a deletion which results in 31 fewer amino acids in the gC-2 near the amino terminus of the protein. The carboxy termini of gC-1 and gC-2 are very similar, as are the 20,000-dalton proteins. 561 on July 6, 2020 by guest

Mapping of linear antigenic determinants on glycoprotein C of herpes simplex virus type 1 and type 2 recognized by human serum immunoglobulin G antibodies

“…Using the SPOTs system (IC-Chemicals, Ismaning, Germany), overlapping dekapeptides (9 amino acids overlapping) representing the entire coding region of gC-1 (strain KOS, 511 amino acids, 502 dekapeptides) [Frink et al, 1983] and gC-2 (strain 333, 480 amino acids, 471 dekapeptides) [Swain et al, 1985] were synthesized on derivatized cellulose membranes in an 8 × 12 matrix of small circular dots according to the manufacturer's instructions. For analysis by immunodot assay, peptides identified as reactive by pep scan were resynthesized on strips of cellulose membranes.…”

“…In addition, gC-1 and gC-2 share only limited sequence homology within their N-terminal part. The Nterminus of gC-1 contains a stretch of 28 amino acid residues that is absent from gC-2 [Frink et al, 1983;Swain et al, 1985].…”

Herpes simplex virus glycoproteins gC-1 and gC-2 bind to the third component of complement and provide protection against complement-mediated neutralization of viral infectivity.

“…In the studies herein, gC-2 from two viral strains, a lowpassage clinical isolate [HSV-2(G)] and gC-2, derived from a laboratory strain [HSV-2(333)] both bound to iC3-Sepharose. The genes for gC-1 and gC-2 occupy colinear positions on their respective viral genomes (10) and are homologous in sequence (26,27). The glycoproteins specified by these genes are quite different in size, however, in part because gC-1 contains a stretch of 27 amino acids near its NH2-terminus that are not present in gC-2 (26,27).…”

“…The genes for gC-1 and gC-2 occupy colinear positions on their respective viral genomes (10) and are homologous in sequence (26,27). The glycoproteins specified by these genes are quite different in size, however, in part because gC-1 contains a stretch of 27 amino acids near its NH2-terminus that are not present in gC-2 (26,27). Moreover, the number of antigenic determinants shared by the two glycoproteins seems to be limited in comparison with the unique antigenic determinants (14,19,28,29).…”

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).…”