SUMO Modification Stabilizes Dengue Virus Nonstructural Protein 5 To Support Virus Replication.
Bottom Line: By expressing various NS5 mutants, we found that the SUMO acceptor sites are located in the N-terminal domain of NS5 and that a putative SUMO-interacting motif (SIM) of this domain is crucial for its SUMOylation.SUMOylation-defective mutants also failed to suppress the induction of STAT2-mediated host antiviral interferon signaling.Here, we found that the replicase of DENV, nonstructural protein 5 (NS5), can be SUMOylated.
Affiliation: Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.Show MeSH
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Mentions: Since Ubc9 previously has been shown to interact with several DENV proteins (32, 34, 38), we asked whether any viral protein could be modified by SUMO. To this end, all 10 of the DENV proteins each were cloned with an HA tag and used in an in vivo SUMOylation assay to screen the potential SUMOylated DENV proteins. By cotransfection with EGFP-tagged SUMO1, each HA-tagged viral protein was immunoprecipitated by anti-HA agarose and separated by SDS-PAGE to reveal any additional protein bands showing a higher molecular mass than those expected of each viral protein. Among all of the viral proteins we examined, a higher-molecular-mass band was found only with NS5 (Fig. 2A), which suggested that DENV NS5 can be SUMOylated. E and NS4A also showed several higher-molecular-mass bands, both in the absence and in the presence of SUMO. The nature of these proteins is not known. For the current study, we focused on NS5.
Affiliation: Department of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.