Mutant analysis of herpes simplex virus-induced cell surface antigens: resistance to complement-mediated immune cytolysis

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Abstract
BHK-21 [hamster kidney] cells infected with temperature-sensitive mutants of herpes simplex virus type 1 strain KOS representing 16 complementation groups were tested for susceptibility to complement-mediated immune cytolysis at permissive (34.degree. C) and nonpermissive (39.degree. C) temperarures. Only cells infected by mutants in complementation group E were resistant to immune cytolysis in a temperature-sensitive manner compared with wild-type infections. The expression of group E mutant cell surface antigens during infections at 34 and 39.degree. C was characterized by a combination of cell surface radioiodination, specific immunoprecipitation and gel electrophoretic analysis of immunoprecipitates. Resistance to immune lysis at 39.degree. C correlated with the absence of viral antigens exposed at the cell surface. Intrinsic radiolabeling of group E mutant infections with [14C]glucosamine revealed that normal glycoproteins were produced at 34.degree. C, but none were synthesized at 39.degree. C. The effect of 2-deoxy-D-glucose on glycosylation of group E mutants at 39.degree. C suggested that the viral glycoprotein precursors were not synthesized. The complementation group E mutants failed to complement herpes simplex virus type 1 mutants isolated by others. These included the group B mutants of strain KOS, the temperature-sensitive group D mutants of strain 17 and the LB2 mutant of strain HFEM. These mutants should be considered members of herpes simplex virus type 1 complementation group 1.2, in keeping with the new herpes simplex virus type 1 nomenclature.