{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8(7)"],"submitter":["Monette A"],"funding":["Canadian Institutes of Health Research"],"pubmed_abstract":["The precursor group-specific antigen (pr55(Gag)) is central to HIV-1 assembly. Its expression alone is sufficient to assemble into virus-like particles. It also selects the genomic RNA for encapsidation and is involved in several important virus-host interactions for viral assembly and restriction, making its synthesis essential for aspects of viral replication. Here, we show that the initiation of translation of the HIV-1 genomic RNA is mediated through both a cap-dependent and an internal ribosome entry site (IRES)-mediated mechanisms. In support of this notion, pr55(Gag) synthesis was maintained at 70% when cap-dependent translation initiation was blocked by the expression of eIF4G- and PABP targeting viral proteases in two in vitro systems and in HIV-1-expressing cells directly infecte"],"journal":["PloS one"],"pagination":["e68108"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3702555"],"repository":["biostudies-literature"],"pubmed_title":["Dual mechanisms of translation initiation of the full-length HIV-1 mRNA contribute to gag synthesis."],"pmcid":["PMC3702555"],"pubmed_authors":["Lopez-Lastra M","Mouland AJ","Valiente-Echeverria F","Monette A","Cohen EA","Rivero M"],"additional_accession":[]},"is_claimable":false,"name":"Dual mechanisms of translation initiation of the full-length HIV-1 mRNA contribute to gag synthesis.","description":"The precursor group-specific antigen (pr55(Gag)) is central to HIV-1 assembly. Its expression alone is sufficient to assemble into virus-like particles. It also selects the genomic RNA for encapsidation and is involved in several important virus-host interactions for viral assembly and restriction, making its synthesis essential for aspects of viral replication. Here, we show that the initiation of translation of the HIV-1 genomic RNA is mediated through both a cap-dependent and an internal ribosome entry site (IRES)-mediated mechanisms. In support of this notion, pr55(Gag) synthesis was maintained at 70% when cap-dependent translation initiation was blocked by the expression of eIF4G- and PABP targeting viral proteases in two in vitro systems and in HIV-1-expressing cells directly infecte","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2026-04-08T16:33:23.485Z","creation":"2026-04-08T06:33:58.991Z"},"accession":"S-EPMC3702555","cross_references":{"pubmed":["23861855"],"doi":["10.1371/journal.pone.0068108"]}}