Herpes simplex virus type‐1‐induced stimulation of ribosomal protein S6 phosphorylation is inhibited in neomycin‐treated human epidermoid carcinoma 2 cells and in ras‐transformed cells

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Abstract
Neomycin, an inhibitor of inositol phospholipid turnover, prevents Herpes-simplex-virus-type-1(HSV-1)-induced stimulation of ribosomal protein S6 phosphorylation, but does not impair the S6 phosphorylation induced by serum. Long-term treatment with phorbol 12-myristate 13-acetate, which down-regulates protein kinase C activity, does not inhibit virus-induced S6 phosphorylation. In ras-transformed cells, S6 phosphorylation is not stimulated after HSV-1 infection. These results suggest that activation of the inositol phospholipid pathway is involved in the HSV-1-induced stimulation of S6 phosphorylation. However, protein kinase C activation does not appear to be necessary for HSV-1-induced S6 phosphorylation.