{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tsai K"],"funding":["NIDCR NIH HHS","NCI NIH HHS","NIH"],"pagination":["30-40"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4628856"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14"],"pubmed_abstract":["All known gammaherpesviruses encode at least one conserved tegument protein that contains sequence homology to the cellular purine biosynthesis enzyme: phosphoribosylformylglycineamide amidotransferase (FGARAT, or PFAS). While no enzymatic activity have been found on these viral FGARAT-homology proteins (vFGARAT), they are important for disarming host intrinsic antiviral machinery. Most vFGARAT proteins disrupt the intrinsic antiviral response-associated cellular subnuclear structure: ProMyelocytic Leukemia (PML) associated nuclear body (PML-NB). vFGARATs from different viruses target different components of PML-NB to prevent cellular repression of viral infection. In addition, vFGARATs of rhadinoviruses were recently found to oligomerize with the cellular FGARAT to deamidate RIG-I and rep"],"journal":["Current opinion in virology"],"pubmed_title":["Disruption of host antiviral resistances by gammaherpesvirus tegument proteins with homology to the FGARAT purine biosynthesis enzyme."],"pmcid":["PMC4628856"],"funding_grant_id":["R01 CA093606","T32 CA115299","CA 093606","DE 017336","P30 CA010815","R01 DE017336","P01 CA174439","R01 CA117830"],"pubmed_authors":["Messick TE","Lieberman PM","Tsai K"],"additional_accession":[]},"is_claimable":false,"name":"Disruption of host antiviral resistances by gammaherpesvirus tegument proteins with homology to the FGARAT purine biosynthesis enzyme.","description":"All known gammaherpesviruses encode at least one conserved tegument protein that contains sequence homology to the cellular purine biosynthesis enzyme: phosphoribosylformylglycineamide amidotransferase (FGARAT, or PFAS). While no enzymatic activity have been found on these viral FGARAT-homology proteins (vFGARAT), they are important for disarming host intrinsic antiviral machinery. Most vFGARAT proteins disrupt the intrinsic antiviral response-associated cellular subnuclear structure: ProMyelocytic Leukemia (PML) associated nuclear body (PML-NB). vFGARATs from different viruses target different components of PML-NB to prevent cellular repression of viral infection. In addition, vFGARATs of rhadinoviruses were recently found to oligomerize with the cellular FGARAT to deamidate RIG-I and rep","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2025-04-18T18:28:58.874Z","creation":"2019-03-27T02:01:08Z"},"accession":"S-EPMC4628856","cross_references":{"pubmed":["26256000"],"doi":["10.1016/j.coviro.2015.07.008"]}}