biostudies-literatureRen LBLRD VANCRR NIH HHSHHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin DiseasesNIAID NIH HHSThrasher Research FundNCI NIH HHSHHS | NIH | National Institute of Allergy and Infectious DiseasesNIAMS NIH HHS5993-6006https://www.ebi.ac.uk/biostudies/studies/S-EPMC6463704biostudies-literatureUnknown294(15)Genome replication and virion assembly of segmented RNA viruses are highly coordinated events, tightly regulated by sequence and structural elements in the UTRs of viral RNA. This process is poorly defined and likely requires the participation of host proteins in concert with viral proteins. In this study, we employed a proteomics-based approach, named RNA-protein interaction detection (RaPID), to comprehensively screen for host proteins that bind to a conserved motif within the rotavirus (RV) 3' terminus. Using this assay, we identified ATP5B, a core subunit of the mitochondrial ATP synthase, as having high affinity to the RV 3'UTR consensus sequences. During RV infection, ATP5B bound to the RV 3'UTR and co-localized with viral RNA and viroplasm. Functionally, siRNA-mediated genetic depleThe Journal of biological chemistryProfiling of rotavirus 3'UTR-binding proteins reveals the ATP synthase subunit ATP5B as a host factor that supports late-stage virus replication.PMC6463704U19 AI116484S10 RR027425R01 AR43799R01 AR49737R56 AI021362I01 BX000158R01 AR043799R01 AI021362K99 AI135031P30 CA124435R01 AR049737R01 AI125249Early Career AwardAmieva MRRen LKhavari PADing SCo JGreenberg HBLi BRamanathan MSong YfalseProfiling of rotavirus 3'UTR-binding proteins reveals the ATP synthase subunit ATP5B as a host factor that supports late-stage virus replication.Genome replication and virion assembly of segmented RNA viruses are highly coordinated events, tightly regulated by sequence and structural elements in the UTRs of viral RNA. This process is poorly defined and likely requires the participation of host proteins in concert with viral proteins. In this study, we employed a proteomics-based approach, named RNA-protein interaction detection (RaPID), to comprehensively screen for host proteins that bind to a conserved motif within the rotavirus (RV) 3' terminus. Using this assay, we identified ATP5B, a core subunit of the mitochondrial ATP synthase, as having high affinity to the RV 3'UTR consensus sequences. During RV infection, ATP5B bound to the RV 3'UTR and co-localized with viral RNA and viroplasm. Functionally, siRNA-mediated genetic deple2019-01-01T00:00:00Z2019 Apr2026-04-29T22:54:39.089Z2020-05-22T16:34:15ZS-EPMC64637043077047210.1074/jbc.RA118.00600410.1074/jbc.ra118.006004