{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["96(12)"],"submitter":["Li Z"],"funding":["This work was supported by NIH grants R35GM138283 to Majid Kazemian, DK044533 and AI17712 to Ourania Andrisani, GM119785 to Fang Huang, and NIH grant P30CA023168 to the Purdue Institute for Cancer Research."],"pubmed_abstract":["RNA helicase DDX5 is a host restriction factor for hepatitis B virus (HBV) biosynthesis. Mass spectrometry (LC-MS/MS) identified significant DDX5-interacting partners, including interferon-inducible protein 16 (IFI16) and RBBP4/7, an auxiliary subunit of polycomb repressive complex 2 (PRC2). DDX5 co-eluted with IFI16, RBBP4/7, and core PRC2 subunits in size exclusion chromatography fractions derived from native nuclear extracts. Native gel electrophoresis of DDX5 immunoprecipitants revealed a 750 kDa DDX5/IFI16/PRC2 complex, validated by nanoscale co-localization via super-resolution microscopy. Prior studies demonstrated that IFI16 suppresses HBV transcription by binding to the interferon-sensitive response element of covalently closed circular DNA (cccDNA), reducing H3 acetylation and in"],"journal":["Journal of medical virology"],"pagination":["e70118"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11648352"],"repository":["biostudies-literature"],"pubmed_title":["RNA Helicase DDX5 in Association With IFI16 and the Polycomb Repressive Complex 2 Silences Transcription of the Hepatitis B Virus by Interferon."],"pmcid":["PMC11648352"],"pubmed_authors":["Huang F","Andrisani O","Li Z","Mohallem R","Bi C","Aryal UK","Kazemian M","Rahman N","Pattnaik A"],"additional_accession":[]},"is_claimable":false,"name":"RNA Helicase DDX5 in Association With IFI16 and the Polycomb Repressive Complex 2 Silences Transcription of the Hepatitis B Virus by Interferon.","description":"RNA helicase DDX5 is a host restriction factor for hepatitis B virus (HBV) biosynthesis. Mass spectrometry (LC-MS/MS) identified significant DDX5-interacting partners, including interferon-inducible protein 16 (IFI16) and RBBP4/7, an auxiliary subunit of polycomb repressive complex 2 (PRC2). DDX5 co-eluted with IFI16, RBBP4/7, and core PRC2 subunits in size exclusion chromatography fractions derived from native nuclear extracts. Native gel electrophoresis of DDX5 immunoprecipitants revealed a 750 kDa DDX5/IFI16/PRC2 complex, validated by nanoscale co-localization via super-resolution microscopy. Prior studies demonstrated that IFI16 suppresses HBV transcription by binding to the interferon-sensitive response element of covalently closed circular DNA (cccDNA), reducing H3 acetylation and in","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2025-04-04T01:31:30.873Z","creation":"2025-04-04T01:31:30.873Z"},"accession":"S-EPMC11648352","cross_references":{"pubmed":["39679735"],"doi":["10.1002/jmv.70118"]}}