{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vladimirova O"],"funding":["National Cancer Institute","NCI NIH HHS"],"pagination":["e1009231"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7943007"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["Liquid-liquid phase separation (LLPS) can drive formation of diverse and essential macromolecular structures, including those specified by viruses. Kaposi's Sarcoma-Associated Herpesvirus (KSHV) genomes associate with the viral encoded Latency-Associated Nuclear Antigen (LANA) to form stable nuclear bodies (NBs) during latent infection. Here, we show that LANA-NB formation and KSHV genome conformation involves LLPS. Using LLPS disrupting solvents, we show that LANA-NBs are partially disrupted, while DAXX and PML foci are highly resistant. LLPS disruption altered the LANA-dependent KSHV chromosome conformation but did not stimulate lytic reactivation. We found that LANA-NBs undergo major morphological transformation during KSHV lytic reactivation to form LANA-associated replication compartm"],"journal":["PLoS pathogens"],"pubmed_title":["Phase separation and DAXX redistribution contribute to LANA nuclear body and KSHV genome dynamics during latency and reactivation."],"pmcid":["PMC7943007"],"funding_grant_id":["P30 CA010815","R01 CA186775","RO1 CA186775","P30 CA0101815","R01 CA117830","P01 CA174439","RO1 CA117830","PO1 CA174439"],"pubmed_authors":["De Leo A","Lieberman PM","Deng Z","Vladimirova O","Hayden J","Wiedmer A"],"additional_accession":[]},"is_claimable":false,"name":"Phase separation and DAXX redistribution contribute to LANA nuclear body and KSHV genome dynamics during latency and reactivation.","description":"Liquid-liquid phase separation (LLPS) can drive formation of diverse and essential macromolecular structures, including those specified by viruses. Kaposi's Sarcoma-Associated Herpesvirus (KSHV) genomes associate with the viral encoded Latency-Associated Nuclear Antigen (LANA) to form stable nuclear bodies (NBs) during latent infection. Here, we show that LANA-NB formation and KSHV genome conformation involves LLPS. Using LLPS disrupting solvents, we show that LANA-NBs are partially disrupted, while DAXX and PML foci are highly resistant. LLPS disruption altered the LANA-dependent KSHV chromosome conformation but did not stimulate lytic reactivation. We found that LANA-NBs undergo major morphological transformation during KSHV lytic reactivation to form LANA-associated replication compartm","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jan","modification":"2025-04-18T13:29:01.591Z","creation":"2025-04-06T23:16:07.753Z"},"accession":"S-EPMC7943007","cross_references":{"pubmed":["33471863"],"doi":["10.1371/journal.ppat.1009231"]}}