Protease 2A induces stress granule formation during coxsackievirus B3 and enterovirus 71 infections

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• 作者：Shuo Wu (1)
  Yan Wang (1)
  Lexun Lin (1)
  Xiaoning Si (1)
  Tianying Wang (1)
  Xiaoyan Zhong (1)
  Lei Tong (1)
  Ying Luan (1)
  Yang Chen (1)
  Xiaoyu Li (3)
  Fengmin Zhang (1)
  Wenran Zhao (2)
  Zhaohua Zhong (1)
  
  1. Department of Microbiology ; Harbin Medical University ; Harbin ; 150081 ; China
  3. Division of Gastroenterology and Hepatology ; Department of Medicine ; University of Florida-Jacksonville ; Jacksonville ; FL ; 32206 ; USA
  2. Department of Cell Biology ; Harbin Medical University ; Harbin ; 150081 ; China
  
• 关键词：Stress granule ; 2A protease ; Coxsackievirus B ; Enterovirus 71
• 刊名：Virology Journal
• 出版年：2014
• 出版时间：December 2014
• 年：2014
• 卷：11
• 期：1
• 全文大小：1,628 KB
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• 刊物主题：Virology;
• 出版者：BioMed Central
• ISSN：1743-422X

文摘

Background Stress granules (SGs) are granular aggregates in the cytoplasm that are formed under a variety of stress situations including viral infection. Previous studies indicate that poliovirus, a member of Picornaviridae, can induce SG formation. However, the exact mechanism by which the picornaviruses induce SG formation is unknown. Method The localization of SG markers in cells infected with coxsackievirus B3 (CVB3) or enterovirus 71 (EV71) and in cells expressing each viral protein was determined via immunofluorescence assays or plasmid transfection. Eight plasmids expressing mutants of the 2A protease (2Apro) of CVB3 were generated using a site-directed mutagenesis strategy. The cleavage efficiencies of eIF4G by CVB3 2Apro and its mutants were determined via western blotting assays. Results In this study, we found that CVB3 infection induced SG formation, as evidenced by the co-localization of some accepted SG markers in viral infection-induced granules. Furthermore, we identified that 2Apro of CVB3 was the key viral component that triggered SG formation. A 2Apro mutant with the G122E mutation, which exhibited very low cleavage efficiency toward eIF4G, significantly attenuated its capacity for SG induction, indicating that the protease activity was required for 2Apro to initiate SG formation. Finally, we observed that SGs also formed in EV71-infected cells. Expression of EV71 2Apro alone was also sufficient to cause SG formation. Conclusion Both CVB3 and EV71 infections can induce SG formation, and 2Apro plays a crucial role in the induction of SG formation during these infections. This finding may help us to better understand how picornaviruses initiate the SG response.