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. 2019 May 1;93(10):e00001-19. doi: 10.1128/JVI.00001-19

FIG 8.

FIG 8

The zinc finger domain of ZAP mediates the antiviral response and the interaction with Nsp9. (A) Schematic of ZAP domains. The truncations of ZAP were constructed according to the schematic. (B and C) The zinc finger domain of ZAP is necessary and sufficient for ZAP antiviral activity. Transfected Marc-145 cells were challenged with PRRSV, and then the cells and supernatant were harvested for Western blotting (B) and virus titration (C). (D) Western blot of co-IP from HA-tagged ZAP truncation- and Flag-tagged Nsp9-cotransfected 293T cells. Experiments were performed three times. Data are expressed as the means ± SD. ns, not significant; **, P < 0.01.