The interaction of mitogen-activated protein kinases to Epstein-Barr virusactivation in Akata cells

To understand the mechanism by which Epstein-Barr virus (EBV) is activated in Akata cells by crosslinking of surface immunoglobulin, the interaction b etween mitogen-activated protein kinase (MAPK)/extracellular signal-regulat ed kinase (ERK) and EBV activation was investigated. Immunoblotting using a n anti-phosphoMAPK antibody (Ab) revealed that anti-IgG Ab induced rapid ph osphorylation of MAPK in the cells. The phosphorylation was inhibited by MA PK/ERK kinase specific inhibitor, PD98059. The expressions of the EBV immed iate early BZLF1 mRNA and its protein product ZEBRA, and early antigen were also inhibited by the inhibitor. These results indicate that MAPK is invol ved in the pathways of EBV activation.