Herpes simplex virus type 2 glycoprotein gF and type 1 glycoprotein gC have related antigenic determinants

Abstract

The 104-S monoclonal antibody immunoprecipitated from herpes simplex virus type 2 (HSV-2)-infected cell extracts the 75,000-molecular-weight glycoprotein gF and its 65,000-molecular-weight precursor (pgF). The precursor pgF was sensitive to endoglycosidase H digestion, indicating the presence of high mannose-type oligosaccharides, whereas the stable gF product was sensitive to neuraminidase digestion, indicating the presence of sialic acid residues. The 104-S antibody also weakly precipitated the 130,000-molecular-weight herpes simplex virus type 1 (HSV-1) glycoprotein gC from both infected cell extracts and purified preparations obtained through the use of monoclonal antibody-containing immunoadsorbent columns. Immunofluorescence tests demonstrated that the 104-S antibody reacted with antigen present in cells infected with HSV-2 strain 333 and HSV-1 strain 14012 but not with antigen present in cells infected with HSV-1 strain MP, a strain deficient in HSV-1 gC production. These findings indicate that HSV-1 gC and HSV-2 gF have antigenic determinants that are related.

Humoral immune response to HSV‐1 and HSV‐2 viral proteins in patients with primary genital herpes

“…Antibodies that precipitated proteins of the heterotype virus were most readily detected in convalescent-phase sera: Antibodies to HSV-2 gB and p148 were detected in early sera from all patients with HSV-1 infections, and antibodies to HSV-1 p148, gC, and gB were detected in early sera from most HSV-2 patients (Table ID). The early human antibodies that recognize both HSV-1 and HSV-2 glycoprotein antigens are consistent with reports of type common epitopes on gB [Pereira et al, 19811 and also with the report of cross-reactivity and genetic relatedness of HSV-1 gC and one of the components of the HSV-2 g80 complex [Zweig et al, 1983;Zezulak et al, 19831. In summary, our data indicates that in both genital HSV-1 and HSV-2 infections, a sequential immune response to HSV-specific polypeptides can be identified. In both primary HSV-1 and HSV-2 infections precipitating antibodies to several glycosylated and nonglycosylated proteins appear early in the course of infection.…”

Antibody response to type‐common and type‐unique epitopes of herpes simplex virus polypeptides

“…The immunological relatedness of HSVl and HSV2 can be demonstrated using the neutralizing activity of immune sera [Vestergaard, 19801; a correlate of typecommon neutralizing antibody at the molecular level is the fact that glycoproteins gB, and gD have type-common epitopes [Vestergaard, 19801. Glycoprotein gC in contrast, was until recently thought to have only serotype-specific epitopes. Two reports [Zweig et al, 1983;Zezulak et al, 19831, however, have suggested that this polypeptide may also have cross-reacting antigenic determinants. The identification of polypeptides with type-specific epitopes is becoming even more important as the use of monoclonal antibodies as diagnostic reagents increases.…”

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.

“…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). Although these two homologous glycoproteins have diverged with time more than some of the other homologous HSV-1 and HSV-2 glycoproteins, it appears that they retain a common affinity for C3b and very likely also retain common activities associated with this binding activity .…”