Dual mechanisms of translation initiation of the full-length HIV-1 mRNA contribute to gag synthesis.

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

SUBMITTER: Monette A 

PROVIDER: S-EPMC3702555 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature