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. Author manuscript; available in PMC: 2008 May 5.
Published in final edited form as: J Neurovirol. 2007 Aug;13(4):373–383. doi: 10.1080/13550280701344983

Figure 4.

Figure 4

Phosphorylation of STAT1 at Y701 is mediated via JAK activation. Whole-brain lysates were prepared from mock- and T3A-infected (1 × 103 PFU, i.c.) mice at 8 days post infection and probed, by Western blot, for activated JAK2 (using an antibody specific for Y1007/1008-phosphorylated JAK2) and cleaved caspase-3. Phosphorylated JAK2 could only be detected in brain lysates from T3A- and not mock-infected animals (A) and this observation correlated with the presence of the apoptotic marker cleaved caspase-3. The contribution of JAK was also examined in whole-cell extracts from mock- and reovirus-infected primary cortical neurons in the presence and absence of the JAK inhibiter AG-490 (50 μM). Treatment with AG-490 at the time of infection completely blocked activation of STAT1 and up-regulation of total STAT1 protein levels (B). Blots provide representative examples of four repeat studies in brain and neuronal culture lysates.