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To facilitate detection of glycoprotein K (gK) specified by herpes simplex virus, a 12-amino-acid epitope tag was inserted within gK domain III. Recombinant virus gKprotC-DIII, expressing the tagged gK, was isolated. This virus formed wild-type plaques and replicated as efficiently as the wild-type KOS virus in Vero cells. Anti-protein C MAb detected high-mannose and Golgi complex-dependent glycosylated gK within cells as well as on purified virions. The gK-null virus ΔgK (gK-/-) entered Vero cells substantially more slowly than the wild-type KOS (gK+/+), while ΔgK virus grown in complementing VK302 cells (gK-/+) entered with entry kinetics similar to those of the KOS virus.

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Journal of Virology

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