Phospholipase A2 Activity Is Copurified Together with Herpes simplex Virus-Specified Fc Receptor Proteins

Abstract
We purified Fc-binding proteins from herpes simplex virus (HSV)-infected Vero cells by using an inverse immunoaffínity column chromatography. Polyacrylamide gel electrophoresis analysis revealed a single, virus-specific 65-kd polypeptide both in HSV type 1- and HSV type 2-infected cell-derived preparations. A Ca2+-dependent phospholipase A2 activity was demonstrated to be associated with the viral Fc-binding proteins.
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