TAR DNA-Binding Protein 43 is Cleaved by the Protease 3C of Enterovirus A71 |
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Authors: | Wo Xiaoman Yuan Yuan Xu Yong Chen Yang Wang Yao Zhao Shuoxuan Lin Lexun Zhong Xiaoyan Wang Yan Zhong Zhaohua Zhao Wenran |
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Affiliation: | 1.Department of Cell Biology, Harbin Medical University, Harbin 150081, China2.Department of Microbiology, Harbin Medical University, Harbin 150081, China |
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Abstract: | Enterovirus A71(EV-A71) is one of the etiological pathogens leading to hand, foot, and mouth disease(HFMD), which can cause severe neurological complications. The neuropathogenesis of EV-A71 infection is not well understood. The mislocalization and aggregation of TAR DNA-binding protein 43(TDP-43) is the pathological hallmark of amyotrophic lateral sclerosis(ALS). However, whether TDP-43 was impacted by EV-A71 infection is unknown. This study demonstrated that TDP-43 was cleaved during EV-A71 infection. The cleavage of TDP-43 requires EV-A71 replication rather than the activated caspases due to viral infection. TDP-43 is cleaved by viral protease 3 C between the residues 331 Q and332 S, while mutated TDP-43(Q331 A) was not cleaved. In addition, mutated 3 C which lacks the protease activity failed to induce TDP-43 cleavage. We also found that TDP-43 was translocated from the nucleus to the cytoplasm, and the mislocalization of TDP-43 was induced by viral protease 2 A rather than 3 C. Taken together, we demonstrated that TDP-43 was cleaved by viral protease and translocated to the cytoplasm during EV-A71 infection, implicating the possible involvement of TDP-43 in the pathogenesis of EV-A71 infection. |
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Keywords: | Enterovirus A71 (EV-A71) TAR DNA-binding protein 43 (TDP-43) 3C protease 2A protease |
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