Abstract

Herpes viral glycoproteins are considered likely to be important targets of virus-specific immunity because they are expressed on the membranes of infected cells and because monoclonal antibodies to the surface glycoproteins of human herpes viruses often have neutralizing activity (Corey and Spear, 1986; Friedrichs and Grose, 1984; Keller et al. 1984; Rasmussen et al. 1985). Recent studies in viral immunology also demonstrate a host response to the nonglycosylated, internal or nucleoproteins of several viruses (Townsend et al. 1984; Yewdell et al. 1986). The investigation of immunity to proteins of both herpes simplex virus (HSV) and varicella-zoster virus (VZV) has progressed over the past few years in parallel with the expansion of knowledge about the molecular virology of these herpes viruses. These advances have allowed the mapping of gene sequences for many of the major viral proteins and their expression in plasmids and by transfection of mammalian cells (Davison and Scott, 1986; Pachl et al. 1987). Similarities between HSV and VZV have been defined at the molecular level with the identification of homologies between several gene sequences and, in the case of the HSV gB and VZV gp II, the demonstration of antigenic crossreactivity.

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