Abstract
Glycoprotein D (gD) of herpes simplex virus type 2 (HSV-2) was excreted from infected cells into the medium. Peptide mapping analysis and lectin binding assays suggested that the gD in the medium is secreted after full glycosylation and cleavage at its C terminus. Release of HSV-2 gD was inhibited by addition of either tunicamycin or brefeldin A, suggesting that the gD in the medium was secreted through the endoplasmic reticulum and Golgi apparatus.
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