Fig. 6
The cleavage of an interior proteolytic site of ATF6 was induced by virus rather than by 3Cpro. a HEK293T cells were transfected with p90ATF6, a 512/517 double mutant, and a truncation mutant of amino acids 1–516 in AS3w-HA-FLAG for 24 h. After that, cells were infected with EV-A71 at an MOI of 200 and cell lysates were harvested at 16 h p.i. Equal amounts of protein lysates (30 μg) were analyzed by 10% SDS-PAGE followed by western blotting. The results shown here are representative of at least four independent experiments. b Schematic representation of the predicted cleavage of full-length ATF6 and amino acids 1–516 of ATF6. The arrows indicate the sites cleaved by 3Cpro and by an unknown protease induced by EV-A71 infection. The numbers indicate the predicted molecular weights of the products based on gel electrophoresis, and their relative positions are matched to the functional domains of ATF6