Interaction of NS2 with AIMP2 Facilitates the Switch from Ubiquitination to SUMOylation of M1 in Influenza A Virus-Infected Cells

• DOI: 10.1128/jvi.02170-14
• Publication Date: 2014-10-16T03:31:00Z
• Authors: Shijuan Gao; Jiaoxiang Wu; Ran-Yi Liu; Jiandong Li; Liping Song; Yan Teng; Chunjie Sheng; Dong Liu; Chen Yao; Huiming Chen; Wei Jiang; Shuai Chen; Wenlin Huang
• Keywords: Immunoprecipitation; Nuclear export signal

Influenza A viruses (IAVs) rely on host factors to support their life cycle, as viral proteins hijack or interact with cellular execute functions. Identification and understanding of these would increase our knowledge the molecular mechanisms manipulated by viruses. In this study, we searched for novel binding partners influenza virus NS2 protein, nuclear export protein responsible overcoming range restriction, a yeast two-hybrid screening assay glutathione S-transferase-pulldown coimmunoprecipitation assays identified AIMP2, potent tumor suppressor that usually functions regulate stability, one major NS2-binding candidates. We found presence protected AIMP2 from ubiquitin-mediated degradation in NS2-transfected cells functioned positive regulator IAV replication. Interestingly, had no significant effect but enhanced stability matrix M1. Further, provide evidence recruitment switches modification M1 ubiquitination SUMOylation, which occurs same attachment site (K242) thereby promotes M1-mediated ribonucleoprotein complex Collectively, results reveal new mechanism mediation replication.Although during infection has been observed, precise consequences remain obscure. Here, demonstrate first time ubiquitin SUMO compete lysine interaction facilitates switch thus increasing