{"database":"GEO","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Other":["ftp://ftp.ncbi.nlm.nih.gov/geo/series/GSE311nnn/GSE311667/"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"omics_type":["Genomics"],"species":["Homo sapiens"],"gds_type":["Genome binding/occupancy profiling by high throughput sequencing"],"full_dataset_link":["https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE311667"],"repository":["GEO"],"entry_type":["GSE"],"additional_accession":[]},"is_claimable":false,"name":"SUMOylation and ubiquitination reciprocally regulate SMCHD1 antiviral activity against herpes simplex virus 1","description":"Host restriction factors serve as intrinsic barriers against viral infection, and are frequently counteracted by viral antagonists. Previous studies, including our own, have identified SMCHD1 as a restriction factor that suppresses the replication of multiple viruses. Here, we reveal that the antiviral activity of SMCHD1 is dynamically regulated by two different post-translational modifications. SUMOylation of the SMCHD1 hinge domain is critical for its association with viral genome and enhances its antiviral activity. In contrast, during herpes simplex virus 1 (HSV-1) infection, the viral E3 ligase ICP0 induces SMCHD1 ubiquitination and proteasomal degradation, thereby relieving viral restriction. Loss of ICP0 stabilizes SMCHD1 and leads to marked accumulation of SUMOylated SMCHD1, rendering ICP0-deficient HSV-1 more sensitive to SMCHD1-mediated inhibition. Together, our findings uncover a reciprocal SUMO-ubiquitin regulatory mechanism that governs SMCHD1 antiviral activity and highlight a refined virus-host arms race centered on biphasic modification of a single restriction factor.","dates":{"publication":"2026/06/15"},"accession":"GSE311667","cross_references":{"GSM":["GSM9329158","GSM9329159"],"GPL":["24676"],"GSE":["311667"],"taxon":["Homo sapiens"]}}